|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-251 |
5.02e-175 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 481.51 E-value: 5.02e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFGRFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVTVV 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|.
gi 2385063227 241 DGPRGPLAVYY 251
Cdd:COG4604 241 EIDGKRICVYF 251
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-245 |
1.06e-98 |
|
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: 288.48 E-value: 1.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFGRFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVT 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
....*..
gi 2385063227 239 VVDGPRG 245
Cdd:COG1120 241 VIEDPVT 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-243 |
4.74e-69 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 212.95 E-value: 4.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQEnHFVTR-LTVRQLVAF 98
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH-HLTPEgITVRELVAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMR 176
Cdd:PRK11231 100 GRSPWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 177 HLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVTVVDGP 243
Cdd:PRK11231 180 LMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIHPEP 245
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-246 |
2.29e-66 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 206.12 E-value: 2.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGlDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLkLLTGELTP-SSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFGRFPHSRGRltAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQ------- 152
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGSSA--AQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 153 ETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRV 232
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250
....*....|....
gi 2385063227 233 FETPVTVVDGPRGP 246
Cdd:COG4559 237 YGADLRVLAHPEGG 250
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-245 |
2.40e-64 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 201.15 E-value: 2.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGlDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLrALSGELSP-DSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFGRFPHSRGRltAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE---- 155
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSR--AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 156 --YVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVF 233
Cdd:PRK13548 159 prWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
250
....*....|..
gi 2385063227 234 ETPVTVVDGPRG 245
Cdd:PRK13548 239 GADVLVQPHPET 250
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
1.74e-62 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 196.08 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKdlakvVSV 79
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLkAILG-LLPPTSGTVRLFGKPPRRARRR-----IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTR--LTVRQLVAFGRFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE 155
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGaVVEFGTPEEIMTGEVLTRVFET 235
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGG 237
|
....*.
gi 2385063227 236 PVTVVD 241
Cdd:COG1121 238 PVALLA 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
4.20e-62 |
|
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: 192.65 E-value: 4.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 3 TLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 enhfvtrltvrqlvafgrfphsrgrltaadeevvsrAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-245 |
3.80e-57 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 183.07 E-value: 3.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 3 TLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFVTRLTVRQLVAFGRFP-H-SRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPwHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVTVV 240
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGIL 252
|
....*
gi 2385063227 241 DGPRG 245
Cdd:PRK10575 253 PHPAG 257
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-233 |
5.74e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.48 E-value: 5.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV--- 76
Cdd:COG3638 2 MLELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFGRFPHS------RGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVL 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLGRTstwrslLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 151 SQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEImTGEVLT 230
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVLR 240
|
...
gi 2385063227 231 RVF 233
Cdd:COG3638 241 EIY 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-249 |
1.93e-53 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 173.63 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLVAFG 99
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRH 177
Cdd:PRK10253 106 RYPHQPlfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 178 LRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVTVVDGPRG--PLAV 249
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAgtPLVV 259
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-206 |
1.33e-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: 169.64 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKdlakvVSVLRQENHFVT- 88
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLkAILG-LLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSIDRd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 -RLTVRQLVAFGRFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:cd03235 83 fPISVRDVVLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2385063227 166 LDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRI 206
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRV 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
1.83e-52 |
|
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: 170.42 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKvVSVL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVA-FGRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:COG4555 80 PDERGLYDRLTVRENIRyFAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-233 |
4.38e-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: 166.59 E-value: 4.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV---V 77
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFGRFPHS------RGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLS 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 152 QETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEImTGEVLTR 231
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDE 239
|
..
gi 2385063227 232 VF 233
Cdd:cd03256 240 IY 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-233 |
1.09e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.62 E-value: 1.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDLAKvVS 78
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRM---LLGLlrpTSGEVRVLGEDVARDPAEVRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQ-LVAFGRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:COG1131 77 YVPQEPALYPDLTVREnLRFFARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMtGEVLTRVF 233
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
1.27e-50 |
|
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: 165.20 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQ--ENHFVTRlTVRQLVAFGrfPHSRGrLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFG--PENLG-LPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-243 |
7.89e-50 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 168.10 E-value: 7.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFGRFPHsRGRL---TAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPH-RSRFdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPV 237
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDART 240
|
....*.
gi 2385063227 238 TVVDGP 243
Cdd:PRK09536 241 AVGTDP 246
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-227 |
1.87e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 159.54 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEvaigPV--DLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVS 78
Cdd:COG3840 1 MLRLDDLTYRYGDF----PLrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGL--RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 159 LDEPLNNLD--MRhsAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:COG3840 153 LDEPFSALDpaLR--QEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-233 |
1.06e-47 |
|
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: 158.23 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV--- 76
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFGRF------PHSRGRLTAADEEvvsRAIDFLDLGGLENRYL---DQLSGGQRQRAYVA 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLgykptwRSLLGRFSEEDKE---RALSALERVGLADKAYqraDQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 148 MVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEImTGE 227
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDE 236
|
....*.
gi 2385063227 228 VLTRVF 233
Cdd:TIGR02315 237 VLRHIY 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
2.77e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 156.11 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 ---VSVLRQENHFVTRLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQE 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELP--LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 154 TEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAgHYADRICAVKDGAV 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
3.62e-47 |
|
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: 155.76 E-value: 3.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-212 |
3.31e-46 |
|
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: 153.01 E-value: 3.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSG--EVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLrLLNG-LLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQ--ENHFVTrLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:cd03225 81 FQnpDDQFFG-PTVEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
9.87e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.50 E-value: 9.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY-SGEV---AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKv 76
Cdd:COG1136 4 LLELRNLTKSYgTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 vsvLRQEN--------HFVTRLTVRQLVAFGRFPhsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAM 148
Cdd:COG1136 83 ---LRRRHigfvfqffNLLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 149 VLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAgHYADRICAVKDGAVVE 216
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.06e-44 |
|
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: 156.99 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE-----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAK 75
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 vvsvLRQENHFV---------TRLTVRQLVAFGrfPHSRGRLTAADEEvvSRAIDFLDLGGLENRYLD----QLSGGQRQ 142
Cdd:COG1123 340 ----LRRRVQMVfqdpysslnPRMTVGDIIAEP--LRLHGLLSRAERR--ERVAELLERVGLPPDLADryphELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 143 RAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEE 222
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
...
gi 2385063227 223 IMT 225
Cdd:COG1123 492 VFA 494
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-195 |
2.48e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 145.07 E-value: 2.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTgrllgldAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFvtRL 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------AGVLRPTSGTVRRAGGARVAYVPQRSEVPDSL--PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQLVAFGRFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDM 168
Cdd:NF040873 73 TVRDLVAMGRWARRGlwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 2385063227 169 RHSAQMMRHLRRVAEElERTVVVVLHD 195
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHD 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
3.50e-43 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 149.14 E-value: 3.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLL-GL---DAGVIEIAGHDV-ARTPSKDLAkv 76
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLL----RIIaGLetpDSGRIVLNGRDLfTNLPPRERR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQEN----HfvtrLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQ 152
Cdd:COG1118 77 VGFVFQHYalfpH----MTVAENIAFG--LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 153 ETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
1.49e-42 |
|
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: 144.30 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFGRfphSRGRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:cd03300 79 QNYALFPHLTVFENIAFGL---RLKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-238 |
2.32e-42 |
|
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: 144.02 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLR 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFG-RFPHSRGRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGlRVKPRSERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEimtgevltrVFETPVT 238
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE---------VYDHPAS 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-225 |
3.42e-42 |
|
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: 143.41 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAKV---V 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLrLIVG-LLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFGRFPHSRGrltaADEEVVSRAIDFLDLGGL---ENRYLDQLSGGQRQRAYVAMVLSQET 154
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRL----SEEEIREIVLEKLEAVGLrgaEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 155 EYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-225 |
6.09e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 143.21 E-value: 6.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFgrFPHSRGRLTAADEEVVSRAIDFLDL--GGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL--VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-245 |
6.52e-42 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 144.20 E-value: 6.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGLDA-------GVIEIAGHDVARTPSKD 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 73 LAKVVSVLRQENHFVTRLTVRQLVAFGRFPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVL 150
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 151 SQ---------ETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPE 221
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|....
gi 2385063227 222 EIMTGEVLTRVFETPVTVVDGPRG 245
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDG 264
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-206 |
1.25e-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: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARtPSKDLAkvv 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-PGPDRG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 sVLRQENHFVTRLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:cd03293 77 -YVFQQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRI 206
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRV 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
4.72e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 141.36 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDlakvv 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRM---IAGLedpTSGEILIGGRDVTDLPPKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 svlrqenhfvtR--------------LTVRQLVAFG---RfphsrgRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGG 139
Cdd:COG3839 75 -----------RniamvfqsyalyphMTVYENIAFPlklR------KVPKAEiDRRVREAAELLGLEDLLDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 140 QRQRayVAM--VLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:COG3839 138 QRQR--VALgrALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQV 215
|
....*.
gi 2385063227 218 GTPEEI 223
Cdd:COG3839 216 GTPEEL 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
5.43e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.00 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVL 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQE----NHfvtrLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:COG3842 83 FQDyalfPH----LTVAENVAFG--LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDIN--FAghYADRICAVKDGAVVEFGTPEEI 223
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGTPEEI 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
8.69e-39 |
|
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: 135.11 E-value: 8.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV---V 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFG-RFphsRGRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE 155
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPlRE---HTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 156 YVLLDEPLNNLD---MRHSAQMMRHLRrvaEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG1127 162 ILLYDEPTAGLDpitSAVIDELIRELR---DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.43e-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: 140.42 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSG--EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLL---GLDAGVIEIAGHDVARTPSKDLAK 75
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 VVSVLRQE-NHFVTRLTVRQLVAFGRFPHSRGRltaadEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAYVAMVLS 151
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIAEALENLGLSR-----AEARARVLELLEAVGLErrlDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 152 QETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-237 |
1.57e-38 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 134.58 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 18 GPVDLRIPRGGVTALVGPNGAGKSTLLT-MTGRLLGldAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLV 96
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLArMAGLLPG--QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRFPHSRgrlTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQ-------ETEYVLLDEPLNNLDMR 169
Cdd:COG4138 91 ALHQPAGAS---SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 170 HSAQMMRHLRRVAeELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPV 237
Cdd:COG4138 168 QQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKF 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-226 |
4.68e-38 |
|
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: 133.39 E-value: 4.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYS----GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDL 73
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRA---LAGLerpWSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 AKVVSVLRQENH--FVTRLTVRQLVAFGRFPHSRGrltaadeEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVA 147
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLP-------DREERIAELLEQVGLPPSFLDryphQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 148 MVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTG 226
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-224 |
7.99e-38 |
|
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: 132.86 E-value: 7.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTM-TGrLLGLDAGVIEIAGHDVARTPSKDLAKvVSV 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLiTG-FYRPTSGRILFDGRDITGLPPHRIAR-LGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LR--QENHFVTRLTVRQ--------------LVAFGRFPHSRGRLTAADEEVVsRAIDFLDLGGLENRYLDQLSGGQRQR 143
Cdd:COG0411 82 ARtfQNPRLFPELTVLEnvlvaaharlgrglLAALLRLPRARREEREARERAE-ELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
.
gi 2385063227 224 M 224
Cdd:COG0411 241 R 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
9.06e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.91 E-value: 9.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARtPSKDlakv 76
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGPD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALG--LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 157 VLLDEPLNNLD--MRhsAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRI 206
Cdd:COG1116 160 LLMDEPFGALDalTR--ERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRV 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-224 |
2.61e-37 |
|
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: 137.58 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTrLTVRQLVAFGRFPHSRGRLTAADEEVvsRAIDFLDL--GGLENRYLDQ---LSGGQRQRAYVAMVLSQETE 155
Cdd:COG4988 417 PQNPYLFA-GTIRENLRLGRPDASDEELEAALEAA--GLDEFVAAlpDGLDTPLGEGgrgLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
2.91e-37 |
|
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: 130.70 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVA---RTPSKDL 73
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 AKVVSVLRQE--NHFVTRLTVRQLVAFGRFPHSRGRLTAADEEVVsraIDFLDLGGLE----NRYLDQLSGGQRQRAYVA 147
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV---LLLLVGVGLPeevlNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 148 MVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-212 |
2.95e-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: 128.52 E-value: 2.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 3 TLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSvlrq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 enhfvtrltvrqlvafgrfphsrgrltaadeevvsraidfldlgglenrYLDQLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:cd00267 77 -------------------------------------------------YVPQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
6.48e-37 |
|
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: 128.07 E-value: 6.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVART--PSKDLAKVVSV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFGrfphsrgrltaadeevvsraidfldlgglenryldqLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-215 |
7.04e-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: 129.15 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLRQENHFVTRLTVRQLVAFGR 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 101 FPhsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRR 180
Cdd:cd03298 96 SP--GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*
gi 2385063227 181 VAEELERTVVVVLHDINFAGHYADRICAVKDGAVV 215
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-223 |
8.61e-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: 130.65 E-value: 8.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV---VSVLRQ--ENH-FVTr 89
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkkVGLVFQfpEHQlFEE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 lTVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:TIGR04521 99 -TVYKDIAFG--PKNLG---LSEEEAEERVKEALELVGLDEEYLERspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 166 LDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-225 |
1.75e-36 |
|
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: 129.69 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 7 VRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV----VSVLRQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFVTRLTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGL--EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-225 |
2.41e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 130.21 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE-VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVArtpSKDLAKvvsv 79
Cdd:COG1125 1 MIEFENVTKRYPDGtVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIR---DLDPVE---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LR-------QENhfvtrltvrqlvafGRFPHsrgrLTAAD-------------EEVVSRAIDFLDLGGLE-----NRYLD 134
Cdd:COG1125 74 LRrrigyviQQI--------------GLFPH----MTVAEniatvprllgwdkERIRARVDELLELVGLDpeeyrDRYPH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 135 QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLD--MRHSAQmmRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:COG1125 136 ELSGGQQQRVGVARALAADPPILLMDEPFGALDpiTREQLQ--DELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
250
....*....|...
gi 2385063227 213 AVVEFGTPEEIMT 225
Cdd:COG1125 214 RIVQYDTPEEILA 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
5.35e-36 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 126.99 E-value: 5.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL--KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-225 |
4.65e-35 |
|
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: 125.24 E-value: 4.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAK-------- 75
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARlgigrtfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 VVSVLRqenhfvtRLTVRQLVAFGRFPHSRGRLTAA-----DEEVVSRA---IDFLDLGGLENRYLDQLSGGQRQRAYVA 147
Cdd:cd03219 83 IPRLFP-------ELTVLENVMVAAQARTGSGLLLArarreEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 148 MVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
5.14e-35 |
|
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: 123.28 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPsKDLAKVVS 78
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKI---ILGLlkpDSGEIKVLGKDIKKEP-EEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQlvafgrfphsrgrltaadeevvsraidfldlgglenrYLDqLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:cd03230 77 YLPEEPSLYENLTVRE-------------------------------------NLK-LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
1.49e-34 |
|
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: 129.89 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV--AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENH-FVTrlTVRQ--LVAfgrfphsrgRLTAADEEVVsRAIDFLDLGGLENRY---LD--------QLSGGQRQRAY 145
Cdd:COG4987 414 VPQRPHlFDT--TLREnlRLA---------RPDATDEELW-AALERVGLGDWLAALpdgLDtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
1.88e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.74 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLR 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFG-RFPHSRGRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGlTVLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
2.53e-34 |
|
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: 122.86 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPsKDLAKVVSVLR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQ-LVAFGRFPHSRGRLTAadeEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHARLYGVPGAERR---ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
2.63e-34 |
|
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: 122.20 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSkDLAKVVSV 79
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLrILAG-LLPPSAGEVLWNGEPIRDARE-DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFgrfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2385063227 160 DEPLNNLDmRHSAQMMrhLRRVAEELER--TVVVVLHD 195
Cdd:COG4133 156 DEPFTALD-AAGVALL--AELIAAHLARggAVLLTTHQ 190
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
4.35e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 122.80 E-value: 4.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARtPSKDLAKvvsvL 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINK----L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQE-----------NHfvtrLTVRQLVAFGrfP-HSRGRltaADEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAY 145
Cdd:COG1126 76 RRKvgmvfqqfnlfPH----LTVLENVTLA--PiKVKKM---SKAEAEERAMELLERVGLAdkaDAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-241 |
7.08e-34 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 122.35 E-value: 7.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 18 GPVDLRIPRGGVTALVGPNGAGKSTLLT-MTGRLLGldAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLV 96
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLArMAGLLPG--SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRFPHSRgrlTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQ-------ETEYVLLDEPLNNLDMR 169
Cdd:PRK03695 91 TLHQPDKTR---TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 170 HSAQMMRHLRRVAEeLERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVTVVD 241
Cdd:PRK03695 168 QQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-164 |
1.72e-33 |
|
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: 118.52 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 19 PVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLVAF 98
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVAMVLSQETEYVLLDEPLN 164
Cdd:pfam00005 83 GL--LLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-228 |
2.81e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.46 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVART-PSKdlaKVVSVLRQENHFVTRLTVRQLVAFG 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTpPSR---RPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFPhsrG-RLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHL 178
Cdd:PRK10771 96 LNP---GlKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2385063227 179 RRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEV 228
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
8.55e-33 |
|
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: 119.21 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGL-----DAGVIEIAGHDVARTPSKDLA-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 75 -KVVSVLRQENHFvtRLTVRQLVAFGrfPHSRG-RLTAADEEVVSRAIDFLDLGGLENRYLD--QLSGGQRQRAYVAMVL 150
Cdd:cd03260 81 rRVGMVFQKPNPF--PGSIYDNVAYG--LRLHGiKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 151 SQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-240 |
1.09e-32 |
|
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: 119.42 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTM-TGRLLGLDAGVIEIAGHDVARTPSKDLAK---V 76
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLiTGDLPPTYGNDVRLFGERRGGEDVWELRKrigL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENhFVTRLTVRQLVAFGRFpHSRGR---LTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQE 153
Cdd:COG1119 83 VSPALQLR-FPRDETVLDVVLSGFF-DSIGLyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 154 TEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDIN-----FaghyaDRICAVKDGAVVEFGTPEEIMTGEV 228
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeippgI-----THVLLLKDGRVVAAGPKEEVLTSEN 235
|
250
....*....|..
gi 2385063227 229 LTRVFETPVTVV 240
Cdd:COG1119 236 LSEAFGLPVEVE 247
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-224 |
1.66e-32 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 121.50 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 9 KEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV----VSVLRQEN 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrrkkIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 85 HFVTRLTVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLEN---RYLDQLSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:TIGR01186 81 ALFPHMTILQNTSLG--PELLG---WPEQERKEKALELLKLVGLEEyehRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEIL 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
2.28e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 118.07 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSG----EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLGL----DAGVIEIAGHDVARTPSKD 72
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLI----RCINGlerpTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 73 LAKvvsvLRQE-----NHF--VTRLTVRQLVAFgrfPHSRGRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRA 144
Cdd:cd03258 77 LRK----ARRRigmifQHFnlLSSRTVFENVAL---PLEIAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 145 YVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-218 |
3.74e-32 |
|
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: 117.01 E-value: 3.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPrGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAG---HDVAR---TPSKDlaKVVSVLRQENHFVTRLTVR 93
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQQ--RKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 QLVAFGRFPHSRGRLTAADEEVVsraiDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQ 173
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELL----DLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2385063227 174 MMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
8.79e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.31 E-value: 8.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYS-GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKvvsv 79
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LR-------QENHFVTRLTVRQLVAfgrFP-HSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLS 151
Cdd:COG2884 77 LRrrigvvfQDFRLLPDRTVYENVA---LPlRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 152 QETEYVLLDEPLNNLDMRHSAQMMRHLRRVAeELERTVVVVLHDINFAGHYADRICAVKDGAVVE 216
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
9.92e-32 |
|
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: 115.75 E-value: 9.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGgVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKdLAKVVSVLR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAF----GRFPHSRgrltaADEEVVsRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:cd03264 79 QEFGVYPNFTVREFLDYiawlKGIPSKE-----VKARVD-EVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
1.02e-31 |
|
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: 115.81 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV--- 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPL--EVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
2.14e-31 |
|
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: 115.29 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE--VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVaRTPSKDLAKVVSV 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAF-GRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-214 |
4.10e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 114.19 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLRQENHFVTRLTVRQLVAFGR 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 101 FPHSRgrLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRR 180
Cdd:TIGR01277 96 HPGLK--LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....
gi 2385063227 181 VAEELERTVVVVLHDINFAGHYADRICAVKDGAV 214
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-240 |
1.31e-30 |
|
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: 116.36 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAG-------HDVARTPSKdlaKVVSVLRQENHFVTRLTV 92
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQLVAFGRfPHSRGRLTAADEEvvsRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSA 172
Cdd:TIGR02142 93 RGNLRYGM-KRARPSERRISFE---RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 173 QMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFETPVTVV 240
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSL 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-225 |
5.11e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVartpsKDLAKVVSVL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-----NDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFV-------TRLTVRQLVAFGrfP-HSRGrltAADEEVVSRAIDFLDLGGLENR---YLDQLSGGQRQRAYVAMV 149
Cdd:PRK09493 76 RQEAGMVfqqfylfPHLTALENVMFG--PlRVRG---ASKEEAEKQARELLAKVGLAERahhYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 150 LSQETEYVLLDEPLNNLD--MRHsaQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDpeLRH--EVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-223 |
5.17e-30 |
|
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: 112.04 E-value: 5.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVarTPSKDLAKVVSVLRQENHFVTRLTVRQLVAFG 99
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFPHSRGRLTaaDEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLR 179
Cdd:cd03299 96 LKKRKVDKKE--IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2385063227 180 RVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
8.63e-30 |
|
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: 110.99 E-value: 8.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAK--VVS 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLkTIMG-LLPPRSGSIRFDGRDITGLPPHERARagIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLrQENHFVTRLTVRQLVAFGRFPHSRGRLTAADEEVVSRaidFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:cd03224 80 VP-EGRRIFPELTVEENLLLGAYARRRAKRKARLERVYEL---FPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
1.53e-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: 116.47 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV--AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDLAKV 76
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKL---LLGLyepTSGRILIDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRlTVRQLVAFGRfphsrgrlTAADEEVVSRAIDFLDL--------GGLENRYLD---QLSGGQRQRAY 145
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLGD--------PDATDEEIIEAARLAGLhdfiealpMGYDTVVGEggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELL 697
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
2.96e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLR 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVtRLTVRQLVAFGrfphSRGRLTAADEEvvsRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYV 157
Cdd:COG4619 81 QEPALW-GGTVRDNLPFP----FQLRERKFDRE---RALELLERLGLPPDILDKpverLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 158 LLDEPLNNLDmRHSAQMM-RHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:COG4619 153 LLDEPTSALD-PENTRRVeELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-223 |
3.44e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDV-ARTPSKDL----AKVVSVLRQENHFVTRL 90
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLkplrKKVGIVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:PRK13634 102 TVEKDICFG--PMNFG---VSEEDAKQKAREMIELVGLPEELLARspfeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 167 DMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-225 |
3.89e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.50 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVArtpskDLAKVVSV---------LRQENHFVTRL 90
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ-----DSARGIFLpphrrrigyVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQLVAFGRFPHSRGRLTAADEEVVsraiDFLDLGGLENRYLDQLSGGQRQRayVAM---VLSQeTEYVLLDEPLNNLD 167
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEVV----ELLGIGHLLDRRPATLSGGERQR--VAIgraLLSS-PRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 168 MRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-215 |
7.67e-29 |
|
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: 108.11 E-value: 7.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIaghDVARTPSKDLAKVVSVLRQE-NHFVTRLTVRQLVAF 98
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL---NGKPIKAKERRKSIGYVMQDvDYQLFTDSVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRfphsrgRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHL 178
Cdd:cd03226 96 GL------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELI 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2385063227 179 RRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVV 215
Cdd:cd03226 170 RELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-233 |
1.01e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.07 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAghDVARTPSKDLAK---VV 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSLSQqkgLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRltvrqlvAFGRFPHsRGRLT-----------AADEEVVSRAIDFL---DLGGLENRYLDQLSGGQRQR 143
Cdd:PRK11264 81 RQLRQHVGFVFQ-------NFNLFPH-RTVLEniiegpvivkgEPKEEATARARELLakvGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
250
....*....|..
gi 2385063227 224 MTG--EVLTRVF 233
Cdd:PRK11264 232 FADpqQPRTRQF 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-223 |
1.26e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.19 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLR 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFGRfphsRGRLTAADE--EVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGL----RMQKTPAAEitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-232 |
3.75e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.18 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQ--ENHFVTRlTVR 93
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQnpDNQFVGA-TVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 QLVAFGRFPHSRGRltaadEEVVSRAIDFLDLGGLENrYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:PRK13635 101 DDVAFGLENIGVPR-----EEMVERVDQALRQVGMED-FLNRephrLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 170 HSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMT-GEVLTRV 232
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKsGHMLQEI 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-224 |
3.96e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENhFVTRLTVRQLVAFg 99
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDT-FLFSGTIRENIRY- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 rfphsrGRLTAADEEVV-----SRAIDFLDlgGLENRYlD--------QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:COG1132 437 ------GRPDATDEEVEeaakaAQAHEFIE--ALPDGY-DtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 167 DMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG1132 508 DTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
5.34e-28 |
|
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: 104.77 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE--VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRlTVRqlvafgrfphsrgrltaadeevvsraidfldlgglENryLdqLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:cd03228 81 VPQDPFLFSG-TIR-----------------------------------EN--I--LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDG 212
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
5.98e-28 |
|
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: 106.55 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV--AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRlTVRQLVAFGRFPHSRGRLTAADEevVSRAIDFLDlgGLENRYlD--------QLSGGQRQRAYVAMVLS 151
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPGATREEVEEAAR--AANAHEFIM--ELPEGY-DtvigergvKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 152 QETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
6.94e-28 |
|
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: 105.69 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARtPSKDLAKvvsvLR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINE----LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFV-------TRLTVRQLVAFGrfphSRGRLTAADEEVVSRAIDFLDLGGLENR---YLDQLSGGQRQRAYVAMVLS 151
Cdd:cd03262 76 QKVGMVfqqfnlfPHLTVLENITLA----PIKVKGMSKAEAEERALELLEKVGLADKadaYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 152 QETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAV 214
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-223 |
8.27e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 108.35 E-value: 8.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 32 LVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVLRQENHFVTRLTVRQLVAFGRFPHSRGRltaa 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGLKMRKVPR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 112 dEEVVSRAIDFL---DLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERT 188
Cdd:TIGR01187 75 -AEIKPRVLEALrlvQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2385063227 189 VVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-223 |
1.10e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.77 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 9 KEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSkdLAKVVSVLRQENHFVT 88
Cdd:PRK11607 27 KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 RLTVRQLVAFGRfphSRGRLTAAdeEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PRK11607 105 HMTVEQNIAFGL---KQDKLPKA--EIASRVNEMLGLVHMQefaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 166 LDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-225 |
1.21e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 13 GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVaRTPSKDLAKVVS----VLRQENHFVT 88
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKtvgiVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 RLTVRQLVAFGRFphsrgRLTAADEEVVSRAIDFL---DLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PRK13639 93 APTVEEDVAFGPL-----NLGLSKEEVEKRVKEALkavGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 166 LDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-248 |
3.30e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 106.70 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLGL----DAGVIEIAGHDVARTPSKD 72
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLlerpTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 73 LAKvvsvLRQE-----NHF--VTRLTVRQLVAfgrFPhsrgrLTAAD---EEVVSRAIDFLDLGGLE---NRYLDQLSGG 139
Cdd:COG1135 77 LRA----ARRKigmifQHFnlLSSRTVAENVA---LP-----LEIAGvpkAEIRKRVAELLELVGLSdkaDAYPSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 140 QRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGT 219
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
250 260 270
....*....|....*....|....*....|.
gi 2385063227 220 PEEIMT--GEVLTRVFETPVTVVDGPRGPLA 248
Cdd:COG1135 225 VLDVFAnpQSELTRRFLPTVLNDELPEELLA 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-223 |
3.66e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.11 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTP--SKDLAKVVSvlr 81
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRDICMVFQ--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 qenhfvtrltvrqlvAFGRFPH-SRGR--------LTAADEEVVSR---AIDFLDLGGLENRYLDQLSGGQRQRAYVAMV 149
Cdd:PRK11432 86 ---------------SYALFPHmSLGEnvgyglkmLGVPKEERKQRvkeALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 150 LSQETEYVLLDEPLNNLD--MRHSaqMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDanLRRS--MREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
1.69e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.55 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGV---IEIAGHDV------ARTPSK 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVqregrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 72 DLAKVVSVLRQENhFVTRLTVRQLV---AFGRFPHSRGRL---TAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAY 145
Cdd:PRK09984 84 SRANTGYIFQQFN-LVNRLSVLENVligALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAV 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
3.16e-26 |
|
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: 101.68 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKv 76
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVA-FGRFPHSRGR-LTAADEEVVSRaidfLDLGGLENRYLDQLSGGQRQRAYVAMVLSQET 154
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyFAGLYGLKGDeLTARLEELADR----LGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 155 EYVLLDEPLNNLDMRHSA---QMMRHLRrvaeELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRalrEFIRQLR----ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-239 |
5.34e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.77 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDV-ARTPS-KDLAKVV 77
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPAdRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 svlrQENHFVTRLTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRayVAM--VLSQETE 155
Cdd:PRK11650 83 ----QNYALYPHMSVRENMAYGL--KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgrAIVREPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEimtgevltrVFET 235
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVE---------VYEK 225
|
....
gi 2385063227 236 PVTV 239
Cdd:PRK11650 226 PAST 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
6.43e-26 |
|
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: 100.56 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV---V 77
Cdd:cd03292 1 IEFINVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFG-RFPHSRGRLTAadeEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlEVTGVPPREIR---KRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHYADRICAVKDGAV 214
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-221 |
9.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 9.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 13 GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQE-NHFVTRLT 91
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 92 VRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHS 171
Cdd:PRK13647 97 VWDDVAFG--PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2385063227 172 AQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPE 221
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
1.80e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLGL----DAGVIEIAGH--DVARTPSkdlAK 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLL----RVLNLletpDSGQLNIAGHqfDFSQKPS---EK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 VVSVLR-------QENHFVTRLTVRQlvafgrfphsrgRLTAA--------DEEVVSRAIDFLDLGGLEN---RYLDQLS 137
Cdd:COG4161 76 AIRLLRqkvgmvfQQYNLWPHLTVME------------NLIEApckvlglsKEQAREKAMKLLARLRLTDkadRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 138 GGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAeELERTVVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
250 260
....*....|....*....|.
gi 2385063227 218 GTPEeimtgevltrVFETPVT 238
Cdd:COG4161 223 GDAS----------HFTQPQT 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
2.40e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.60 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVA--IGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVS 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQ--ENHFVTRlTVRQLVAFGRFPHSrgrlTAADE--EVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQET 154
Cdd:PRK13648 87 IVFQnpDNQFVGS-IVKYDVAFGLENHA----VPYDEmhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 155 EYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMT-GEVLTRV 232
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDhAEELTRI 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-231 |
3.78e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.31 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 13 GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGH--DVARTPSKDLAKVVSVLRQE-NHFVTR 89
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 LTVRQLVAFGRFphsrgRLTAADEEV---VSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:PRK13636 98 ASVYQDVSFGAV-----NLKLPEDEVrkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 167 DMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTR 231
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-232 |
5.64e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVS-VLRQENHFVT 88
Cdd:PRK13652 13 YSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGlVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 RLTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDM 168
Cdd:PRK13652 93 SPTVEQDIAFG--PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 169 RHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT-GEVLTRV 232
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLqPDLLARV 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-223 |
1.16e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.49 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYsGEVAIGP-VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDlaKVVSVL 80
Cdd:PRK11000 4 VTLRNVTKAY-GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFGRfphsrgRLTAADEEV----VSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGL------KLAGAKKEEinqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
12-229 |
1.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.72 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDA---GVIEIAGHDVARTPSKDLAKVVSVLRQ--ENHF 86
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVGIVFQnpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRlTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDflDLGGLEnrYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:PRK13640 98 VGA-TVGDDVAFGL--ENRAVPRPEMIKIVRDVLA--DVGMLD--YIDSepanLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMTGEVL 229
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-233 |
2.07e-24 |
|
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: 96.84 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 22 LRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGhdvaRTPSKDLAKVVSV-LRQENHFVTRLTVRQLVAFGR 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG----ASPGKGWRHIGYVpQRHEFAWDFPISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 101 FPHSR--GRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHL 178
Cdd:TIGR03771 77 TGHIGwlRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 179 RRVAEElERTVVVVLHDINFAGHYADRICAVkDGAVVEFGTPEEIMTGEVLTRVF 233
Cdd:TIGR03771 157 IELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTF 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-233 |
2.26e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 98.03 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSvL 80
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFGRFPHS--RGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMGRYGHMgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKdGAVVEFGTPEEIMTGEVLTRVF 233
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-224 |
2.84e-24 |
|
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: 96.84 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENH-FVTrlTVRQLVAF 98
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVlFDG--TIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRFPhsrgrltAADEEVVSRAI-----DFLDlgGLENRYlD--------QLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:cd03249 100 GKPD-------ATDEEVEEAAKkanihDFIM--SLPDGY-DtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 166 LDMRHSAQMMRHLRRVAEelERTVVVVLHDINfAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-225 |
3.98e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 97.18 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY-SGEVAIGpVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLGL----DAGVIEIAGHDVARTPSKDLAK 75
Cdd:COG4598 8 ALEVRDLHKSFgDLEVLKG-VSLTARKGDVISIIGSSGSGKSTFL----RCINLletpDSGEIRVGGEEIRLKPDRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 VVSVLRQENHFVTRL-------------TVRQLVAFGrfP-HSRGRLTAadeEVVSRAIDFLDLGGLENR---YLDQLSG 138
Cdd:COG4598 83 VPADRRQLQRIRTRLgmvfqsfnlwshmTVLENVIEA--PvHVLGRPKA---EAIERAEALLAKVGLADKrdaYPAHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 139 GQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
....*..
gi 2385063227 219 TPEEIMT 225
Cdd:COG4598 237 PPAEVFG 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-219 |
4.73e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLGL----DAGVIEIAGH--DVARTPS----K 71
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLL----RVLNLlempRSGTLNIAGNhfDFSKTPSdkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 72 DLAKVVSVLRQENHFVTRLTVRQ-LV-AFGRFphsrgrLTAADEEVVSRAIDFLD---LGGLENRYLDQLSGGQRQRAYV 146
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQnLIeAPCRV------LGLSKDQALARAEKLLErlrLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 147 AMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGT 219
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-197 |
8.01e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.24 E-value: 8.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLT-MTGRL-LGLDA-GVIEIAGHDVARTPSkdLAKVV 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLsPAFSAsGEVLLNGRRLTALPA--EQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFGrFPHSRGRltAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPPTIGR--AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2385063227 158 LLDEPLNNLDMRHSAQmMRHLrrVAEELERT---VVVVLHDIN 197
Cdd:COG4136 156 LLDEPFSKLDAALRAQ-FREF--VFEQIRQRgipALLVTHDEE 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
9.58e-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: 92.90 E-value: 9.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrllgldagvieIAGHDVARTPSKDLAKVVSVLr 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKL-------------IAGELEPDEGIVTWGSTVKIG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 qenhfvtrltvrqlvafgrfphsrgrltaadeevvsraidfldlgglenrYLDQLSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:cd03221 67 --------------------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 162 PLNNLDMRHSAQMMRHLRrvaeELERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:cd03221 97 PTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
9.94e-24 |
|
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: 95.37 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQEnhfvTRL---TVRQLVAFgrfphsrGRLTAADEEVVsRAIDFLDLGGLENRYLDQ-----------LSGGQRQRAYV 146
Cdd:cd03253 81 PQD----TVLfndTIGYNIRY-------GRPDATDEEVI-EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 147 AMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
1.33e-23 |
|
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: 96.66 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY---SGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLL---GLDAGVIEIAGHDVARTPSKDL 73
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 AKV----VSVLRQE--NHFVTRLTVRQLVAFGRFPHSRGRLTAADEevvsRAIDFLDLGGLEN--RYLD----QLSGGQR 141
Cdd:COG0444 81 RKIrgreIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEARE----RAIELLERVGLPDpeRRLDryphELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 142 QRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRIC---AvkdGAVVEFG 218
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAvmyA---GRIVEEG 233
|
....*
gi 2385063227 219 TPEEI 223
Cdd:COG0444 234 PVEEL 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
1.33e-23 |
|
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: 94.65 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAkvvsVLR 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG----YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVR-QLVAFGRFpHSRGRLTAADEevVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:cd03269 77 EERGLYPKMKVIdQLVYLAQL-KGLKKEEARRR--IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
1.77e-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: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE-VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRlTVRQLVAFGRfphsrgrlTAADEEVVSRAIDFLDL--------GGLENRYLDQ---LSGGQRQRAYVAMV 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR--------PDASDAEIREALERAGLdefvaalpQGLDTPIGEGgagLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 150 LSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAgHYADRICAV 209
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-224 |
1.78e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 96.72 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKvvsvLRQENHFV---------TRL 90
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRMQMVfqdpyaslnPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQLVAFGRFPHsrGRLTAAdeEVVSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:COG4608 113 TVGDIIAEPLRIH--GLASKA--ERRERVAELLELVGLRpehaDRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 167 DMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRIcAVKD-GAVVEFGTPEEIM 224
Cdd:COG4608 189 DVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRV-AVMYlGKIVEIAPRDELY 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
2.41e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEV----AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVaRTPSKDLAkv 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 vsVLRQENHFVTRLTVRQLVAFG-RFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE 155
Cdd:COG4525 80 --VVFQKDALLPWLNVLDNVAFGlRL---RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDI 196
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-224 |
2.69e-23 |
|
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: 94.21 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlT 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 92 VRQLVAFgrfphsrGRLTAADEEVV--SRAIDFLDLG-GLENRYLDQ-------LSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:cd03254 93 IMENIRL-------GRPNATDEEVIeaAKEAGAHDFImKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAgHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-225 |
3.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.28 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAG-HDVARTPSKDLAKV---VSVLRQ--ENHFVTRlTVR 93
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyHITPETGNKNLKKLrkkVSLVFQfpEAQLFEN-TVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 QLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:PRK13641 105 KDVEFG--PKNFG---FSEDEAKEKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 170 HSAQMMRhLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK13641 180 GRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-244 |
3.45e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVA-RTPSKDLAKVVS 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMkILSG-VYQPDSGEILLDGEPVRfRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQLVAFGRFPHSRGRLtaADEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQrayvaMV-----L 150
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGLI--DWRAMRRRARELLARLGLDidpDTPVGDLSVAQQQ-----LVeiaraL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 151 SQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDIN--FAghYADRICAVKDGAVVEFG-----TPEEI 223
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDevFE--IADRVTVLRDGRLVGTGpvaelTEDEL 232
|
250 260
....*....|....*....|....
gi 2385063227 224 ---MTGEVLTRVFETPVTVVDGPR 244
Cdd:COG1129 233 vrlMVGRELEDLFPKRAAAPGEVV 256
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-224 |
8.26e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 8.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 22 LRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV----VSVLRQENHFVTRLTVRQLVA 97
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 98 FGRfphsrGRLTAADEEVVSRAIDFLDLGGLENR---YLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQM 174
Cdd:PRK10070 129 FGM-----ELAGINAEERREKALDALRQVGLENYahsYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2385063227 175 MRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-217 |
8.26e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 8.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRlLGLDAGVIEIaGHDVartpskdlakVVSV 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLkLLAGE-LEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENH-FVTRLTVRQLVafgrfphSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:COG0488 383 FDQHQEeLDPDKTVLDEL-------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 159 LDEPLNNLDMRhsaqmMRhlrrvaEELER-------TVVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:COG0488 456 LDEPTNHLDIE-----TL------EALEEalddfpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-244 |
1.09e-22 |
|
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: 92.53 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARtPSKDLAkvvsVLRQENHFVTRLTVRQLVAFG 99
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRM----VVFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLR 179
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 180 RVAEELERTVVVVLHDINFAGHYADRICAVKDGavvefgtPEEIMtGEVLTRVFETP---VTVVDGPR 244
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG-------PAANI-GQILEVPFPRPrdrLEVVEDPS 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-232 |
1.10e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.92 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV-----AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKdlAKV 76
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKK--IKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRL--------TVRQLVAFGRFphsrgRLTAADEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRA 144
Cdd:PRK13645 85 VKRLRKEIGLVFQFpeyqlfqeTIEKDIAFGPV-----NLGENKQEAYKKVPELLKLVQLPEDYVKrspfELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 145 YVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
....*....
gi 2385063227 225 TG-EVLTRV 232
Cdd:PRK13645 240 SNqELLTKI 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
1.12e-22 |
|
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: 91.89 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKdlAKVVSVLR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVR-QLVAFgrfphsrGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:cd03268 79 EAPGFYPNLTAReNLRLL-------ARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVE 216
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-216 |
1.13e-22 |
|
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: 92.41 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGrllGLD---AGVIEIAGHDVARTPSKDLAKvvsvLRQEN--------HFVT 88
Cdd:TIGR02211 24 VSLSIGKGEIVAIVGSSGSGKSTLLHLLG---GLDnptSGEVLFNGQSLSKLSSNERAK----LRNKKlgfiyqfhHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 RLTVRQLVAFgrfPHSRGRLTAADEEvvSRAIDFLDLGGLENR---YLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:TIGR02211 97 DFTALENVAM---PLLIGKKSVKEAK--ERAYEMLEKVGLEHRinhRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 166 LDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVE 216
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-226 |
1.15e-22 |
|
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: 92.86 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 24 IPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKvvsvlrqenhfvTRLTVRQLVafgrfpH 103
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD------------YEGTVRDLL------S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 104 SRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAE 183
Cdd:cd03237 84 SITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2385063227 184 ELERTVVVVLHDINFAGHYADRIcAVKDGAVVEFG---TPEEIMTG 226
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGvanPPQSLRSG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
1.16e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLD-----AGVIEIAGHDVARTPSKDLAKV 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFG----RFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQ 152
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 153 ETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-224 |
1.33e-22 |
|
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: 92.35 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAK--VVSVLrQENHFVTRLTVRQ-L 95
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLkAISG-LLPPRSGSIRFDGEDITGLPPHRIARlgIGYVP-EGRRIFPSLTVEEnL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 96 VAFGRFPHSRGRLTAADEEVVSRaidFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPlnnldmrhS---- 171
Cdd:COG0410 100 LLGAYARRDRAEVRADLERVYEL---FPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP--------Slgla 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 172 ----AQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG0410 169 plivEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-223 |
2.06e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPS----KDLAKVVSVLRQ--ENHFVTR 89
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 lTVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PRK13643 101 -TVLKDVAFG--PQNFG---IPKEKAEKIAAEKLEMVGLADEFWEkspfELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 166 LDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13643 175 LDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
2.26e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.46 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKE-YSGEV----AIGPVDLRIPRGGVTALVGPNGAGKSTLLTM-TGRLLgLDAGVIEIAGHDVARTPSKDLA 74
Cdd:COG1101 1 MLELKNLSKTfNPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAiAGSLP-PDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 75 KVVSVLRQENHFVT--RLTVRQ--LVAFGRfPHSRG---RLTAADEEVVSRAIDFLDLgGLENRyLDQ----LSGGQRQR 143
Cdd:COG1101 80 KYIGRVFQDPMMGTapSMTIEEnlALAYRR-GKRRGlrrGLTKKRRELFRELLATLGL-GLENR-LDTkvglLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVV 215
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-215 |
3.46e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY-SGE---VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKv 76
Cdd:PRK10535 4 LLELKDIRRSYpSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 vsvLRQEN--------HFVTRLTVRQLVAFGRFPHSRGRltaadEEVVSRAIDFLDLGGLENR---YLDQLSGGQRQRAY 145
Cdd:PRK10535 83 ---LRREHfgfifqryHLLSHLTAAQNVEVPAVYAGLER-----KQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHyADRICAVKDGAVV 215
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-224 |
3.59e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLR 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVrQLVAFGRFPHSRGR----------LTAADEEVVSRAIDFLDLGGLENR----YLDQLSGGQRQRAYVA 147
Cdd:PRK10619 86 QLRLLRTRLTM-VFQHFNLWSHMTVLenvmeapiqvLGLSKQEARERAVKYLAKVGIDERaqgkYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 148 MVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
3.76e-22 |
|
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: 91.07 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV-VSVL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQ--LVAFGRFPHSRGRLTAADEEVvsraIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:cd03218 81 PQEASIFRKLTVEEniLAVLEIRGLSKKEREEKLEEL----LEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 159 LDEPLNNLD---MRHSAQMMRHLRrvaeelERTVVVVLHDinfagHYA-------DRICAVKDGAVVEFGTPEEIMTGEV 228
Cdd:cd03218 157 LDEPFAGVDpiaVQDIQKIIKILK------DRGIGVLITD-----HNVretlsitDRAYIIYEGKVLAEGTPEEIAANEL 225
|
....*
gi 2385063227 229 LTRVF 233
Cdd:cd03218 226 VRKVY 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
8.29e-22 |
|
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: 88.25 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVA-RTPSKDLAKVVsv 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMkILSG-LYKPDSGEILVDGKEVSfASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 lrqenhfvtrltvrqlvafgrfphsrgrltaadeEVVSraidfldlgglenryldQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:cd03216 78 ----------------------------------AMVY-----------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVV 215
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-223 |
8.73e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 15 VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTpSKDlaKVVSVLRQENHFVTRLTVRQ 94
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHK-TKD--KYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 95 L--------VAFGrfPHSRGRLTaadEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:PRK13646 98 LfedtvereIIFG--PKNFKMNL---DEVKNYAHRLLMDLGFSRDVMSqspfQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-231 |
8.80e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.22 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLA---KVV 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrqQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFgrfphSRGRLTAADEEVVSR---AIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQET 154
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAF-----SLRNLGVPEAEITRRvdeALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 155 EYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT-GEVLTR 231
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQ 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-241 |
1.09e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVArTPSK--DLAKVV 77
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKlqGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQ--ENHFVTRlTVRQLVAFGrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE 155
Cdd:PRK13644 80 GIVFQnpETQFVGR-TVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINfAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFET 235
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLT 234
|
....*.
gi 2385063227 236 PVTVVD 241
Cdd:PRK13644 235 PPSLIE 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
1.19e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVartPSK-DLAKV- 76
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARM---ILGMtspDAGKITVLGVPV---PARaRLARAr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQ-LVAFGRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE 155
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVREnLLVFGRY---FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 156 YVLLDEPLNNLDmRHSaqmmRHL--RRVAEELER--TVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTR 231
Cdd:PRK13536 193 LLILDEPTTGLD-PHA----RHLiwERLRSLLARgkTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQ 267
|
...
gi 2385063227 232 VFE 234
Cdd:PRK13536 268 VIE 270
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-224 |
1.46e-21 |
|
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: 93.27 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE--VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:TIGR01846 456 ITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRlTVRQLVAFGRFPHSRGRLTAADEevVSRAIDFLDlgGLENRYLDQ-------LSGGQRQRAYVAMVLSQ 152
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNIALCNPGAPFEHVIHAAK--LAGAHDFIS--ELPQGYNTEvgekganLSGGQRQRIAIARALVG 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 153 ETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR01846 611 NPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELL 679
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
2.29e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVArTPSKDLAkvvsVL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERG----VV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFGRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGL--QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFA 199
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
2.89e-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: 89.08 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE--VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:cd03252 1 ITFEHVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRlTVRQLVAFGRFPHSRGRLTAADEevVSRAIDF-LDLG-GLENRYLDQ---LSGGQRQRAYVAMVLSQET 154
Cdd:cd03252 81 VLQENVLFNR-SIRDNIALADPGMSMERVIEAAK--LAGAHDFiSELPeGYDTIVGEQgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 155 EYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINfAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-236 |
3.45e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDA-----GVIEIAGHDVART---PSKDLAKVVSVLRQ 82
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPdvdPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFvTRLTVRQLVAFG----RFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:PRK14267 94 PNPF-PHLTIYDNVAIGvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEimtgevltrVFETP 236
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK---------VFENP 239
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-228 |
3.74e-21 |
|
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: 88.35 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 3 TLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAKV-VSVL 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLkTLMG-LLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVR---QLVAFGRfphsRGRLTAADEEVVSRaidFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:TIGR03410 81 PQGREIFPRLTVEenlLTGLAAL----PRRSRKIPDEIYEL---FPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEV 228
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-224 |
5.47e-21 |
|
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: 91.32 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQL 95
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 96 VAFGRfphsrgrLTAADEEVVSRA---------IDFLDLGglenryLDQ--------LSGGQRQRAYVAMVLSQETEYVL 158
Cdd:TIGR02203 426 IAYGR-------TEQADRAEIERAlaaayaqdfVDKLPLG------LDTpigengvlLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELL 555
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-223 |
6.37e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.86 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE----VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKv 76
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 vsvLRQE-----NHF--VTRLTVRQLVAfgrFPhsrgrLTAA---DEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQR 143
Cdd:PRK11153 80 ---ARRQigmifQHFnlLSSRTVFDNVA---LP-----LELAgtpKAEIKARVTELLELVGLSdkaDRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-223 |
1.01e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 15 VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSK--DLAKVVSVLRQ-ENHFVTRLT 91
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVGLVFQyPEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 92 VRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLE-NRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:PRK13637 101 IEKDIAFG--PINLG---LSEEEIENRVKRAMNIVGLDyEDYKDKspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 167 DMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-213 |
1.13e-20 |
|
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: 87.00 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGLDAGV----IEIAGHDVARTPSKDLAKVVSVLRQEnhF 86
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKP--W 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRLTVRQLVAFGRfPHSRGRLTAADEEV-VSRAIDFLDLGG---LENRYLDqLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:cd03290 90 LLNATVEENITFGS-PFNKQRYKAVTDACsLQPDIDLLPFGDqteIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 163 LNNLDMRHSAQMMRH-LRRVAEELERTVVVVLHDINFAGHyADRICAVKDGA 213
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-194 |
1.33e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 86.94 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 5 SGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGLDA--GVIEIAGhdVARTPSKDLaKVVSVLR 81
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdAISGRVEGGGTtsGQILFNG--QPRKPDQFQ-KCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFgrFPHSRGRLTAADEEVVSRAIDF----LDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:cd03234 88 QDDILLPGLTVRETLTY--TAILRLPRKSSDAIRKKRVEDVllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLH 194
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-238 |
1.79e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLL-GLDAGVieiAGHDVA-RTPSKDLAKVVSV 79
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLaGLETPS---AGELLAgTAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFGRFPHSRGRLTAADEEVvsraidfldlgGLENRYLD---QLSGGQRQRAYVAMVLSQETEY 156
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAV-----------GLADRANEwpaALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAV-----VEFGTPEEI-------M 224
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldltVDLPRPRRRgsarlaeL 234
|
250
....*....|....
gi 2385063227 225 TGEVLTRVFETPVT 238
Cdd:PRK11247 235 EAEVLQRVMSRGES 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.05e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.35 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEV--AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVS 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQ--ENHFVTrLTVRQLVAFG----RFPhsRGRLTAADEEVVSRAidfldlgGLENrYLDQ----LSGGQRQRAYVAM 148
Cdd:PRK13632 87 IIFQnpDNQFIG-ATVEDDIAFGlenkKVP--PKKMKDIIDDLAKKV-------GMED-YLDKepqnLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 149 VLSQETEYVLLDEPLNNLD---MRHSAQMMRHLRRVAeelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKTR---KKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
..
gi 2385063227 226 GE 227
Cdd:PRK13632 232 NK 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
2.47e-20 |
|
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: 89.34 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSG-EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVL 80
Cdd:TIGR02868 335 LELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENH-FVTrlTVRQLVAFgrfphsrGRLTAADEEV--VSRAIDFLDL-----GGLENRYLD---QLSGGQRQRAYVAMV 149
Cdd:TIGR02868 415 AQDAHlFDT--TVRENLRL-------ARPDATDEELwaALERVGLADWlralpDGLDTVLGEggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2385063227 150 LSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHD 195
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-225 |
2.62e-20 |
|
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: 89.36 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLltmtGR-LLGLDA--GVIEIAGHDVARTPSKDLAKvvsvLRQENHFV--------- 87
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTL----GLaLLRLIPseGEIRFDGQDLDGLSRRALRP----LRRRMQVVfqdpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 88 TRLTVRQLVAFGRFPHSRGrLTAADEEvvSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVA--MVLsqETEYVLLDE 161
Cdd:COG4172 377 PRMTVGQIIAEGLRVHGPG-LSAAERR--ARVAEALEEVGLDpaarHRYPHEFSGGQRQRIAIAraLIL--EPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-216 |
2.86e-20 |
|
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: 85.95 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY---SGEVAI-GPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGLD---AGVIEIAGHDVARTPSKDL 73
Cdd:COG4181 8 IIELRGLTKTVgtgAGELTIlKGISLEVEAGESVAIVGASGSGKSTLLGL---LAGLDrptSGTVRLAGQDLFALDEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 AKV----VSVLRQENHFVTRLTVRQLVA----FGRFPHSRGRLTAADEEVvsraidflDLGGLENRYLDQLSGGQRQRAY 145
Cdd:COG4181 85 ARLrarhVGFVFQSFQLLPTLTALENVMlpleLAGRRDARARARALLERV--------GLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVE 216
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-226 |
3.29e-20 |
|
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: 89.15 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV--AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:TIGR03375 464 IEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENhfvtRL---TVRQLVAFGRfPHsrgrltaADEEVVSRAIDFLDLGGLENRY---LD--------QLSGGQRQRAY 145
Cdd:TIGR03375 544 VPQDP----RLfygTLRDNIALGA-PY-------ADDEEILRAAELAGVTEFVRRHpdgLDmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLH-----DInfaghyADRICAVKDGAVVEFGTP 220
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHrtsllDL------VDRIIVMDNGRIVADGPK 683
|
....*.
gi 2385063227 221 EEIMTG 226
Cdd:TIGR03375 684 DQVLEA 689
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-230 |
3.75e-20 |
|
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: 86.40 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLltmtGRLL-GLD---AGVIEIAGHDVA---RTPSKDLAKVVSVLRQENH--FVTRL 90
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTL----ARLLlGLEkpaQGTVSFRGQDLYqldRKQRRAFRRDVQLVFQDSPsaVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQLVAfgrfpHSRGRLTAADE-EVVSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:TIGR02769 106 TVRQIIG-----EPLRHLTSLDEsEQKARIAELLDMVGLRsedaDKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 166 LDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVefgtpEEIMTGEVLT 230
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV-----EECDVAQLLS 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-207 |
4.18e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 88.84 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAghdvartpskDLAKVVS 78
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRM---ITGQeqpDSGTIEIG----------ETVKLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQLVAFGrfphsRGRLTAADEEVVSRAI--DFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:TIGR03719 390 VDQSRDALDPNKTVWEEISGG-----LDIIKLGKREIPSRAYvgRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 157 VLLDEPLNNLDMrhsaQMMRHLRRVAEELERTVVVVLHDINFaghyADRIC 207
Cdd:TIGR03719 465 LLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHDRWF----LDRIA 507
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
4.30e-20 |
|
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: 85.33 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE--VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:cd03245 3 IEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRlTVRQLVAFGRfphsrgrlTAADEEVVSRAIDFLDLGGLENRY---LD--------QLSGGQRQRAYVAM 148
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGA--------PLADDERILRAAELAGVTDFVNKHpngLDlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 149 VLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAgHYADRICAVKDGAVV 215
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
6.21e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDLAKvVS 78
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRM---LLGLthpDAGSISLCGEPVPSRARHARQR-VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQ-LVAFGRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:PRK13537 84 VVPQFDNLDPDFTVREnLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVFE 234
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIE 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-224 |
6.26e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.32 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEI-AGHD-VART-PSKDL----AKVVSVLRQEnhfvt 88
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwVDMTkPGPDGrgraKRYIGILHQE----- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 rltvrqlvaFGRFPHSR--GRLTAA------DEEVVSRAIDFLDLGGLE--------NRYLDQLSGGQRQRAYVAMVLSQ 152
Cdd:TIGR03269 374 ---------YDLYPHRTvlDNLTEAiglelpDELARMKAVITLKMVGFDeekaeeilDKYPDELSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 153 ETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-216 |
7.15e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKD-LAKVVSVLRQ 82
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFVTRLTVRQLVAFGRFPHSRGRLTaaDEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:PRK11288 87 ELHLVPEMTVAENLYLGQLPHKGGIVN--RRLLNYEAREQLEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVE 216
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
7.88e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKD----- 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRI---ILGIlapDSGEVLWDGEPLDPEDRRRigylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 73 ----LAKvvsvlrqenhfvtRLTVR-QLVAFGRFphsRGrLTAADeevVSRAIDF----LDLGGLENRYLDQLSGGQRQR 143
Cdd:COG4152 78 eergLYP-------------KMKVGeQLVYLARL---KG-LSKAE---AKRRADEwlerLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDmRHSAQMMRH-LRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEE 222
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLD-PVNVELLKDvIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
.
gi 2385063227 223 I 223
Cdd:COG4152 216 I 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-215 |
8.56e-20 |
|
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: 85.08 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 7 VRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHF 86
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRLTVRQ----LVAFGRFPHSRGRltaadeEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:cd03267 107 WWDLPVIDsfylLAAIYDLPPARFK------KRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVV 215
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-218 |
1.18e-19 |
|
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: 83.13 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVArTPSKDLAKVVSVLRQENH-FVTrl 90
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-DLEKALSSLISVLNQRPYlFDT-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQLVafgrfphsrGRltaadeevvsraidfldlgglenryldQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRH 170
Cdd:cd03247 90 TLRNNL---------GR---------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2385063227 171 SAQMMRHLRRVAEelERTVVVVLHDINfAGHYADRICAVKDGAVVEFG 218
Cdd:cd03247 134 ERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-225 |
1.52e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.21 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGLDA--GVIEIAGHDVARTPSKDLAKVVSVLRQENHFVt 88
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA---LLGFLPyqGSLKINGIELRELDPESWRKHLSWVGQNPQLP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 RLTVRQLVAFGRFPHSRGRLTAADEEvvSRAIDFLDL--GGLENRYLDQ---LSGGQRQRAYVAMVLSQETEYVLLDEPL 163
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEQLQQALEN--AWVSEFLPLlpQGLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 164 NNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHYaDRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-223 |
7.20e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.90 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLD-----AGVIEIAGHDV--ARTPSKDLAKVVS-VLRQ 82
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGmVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFvtRLTVRQLVAFGRfphsrgRLTAA-DEEVVSRAIDFLDLGG-----LENRYLDQ---LSGGQRQRAYVAMVLSQE 153
Cdd:PRK14239 95 PNPF--PMSIYENVVYGL------RLKGIkDKQVLDEAVEKSLKGAsiwdeVKDRLHDSalgLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 154 TEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-233 |
8.06e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 8.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 9 KEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLA-KVVSVLRQENHFV 87
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 88 TRLTV-RQLVAFGRFphsRGRLTAadEEVVSRAIDFLD---LGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPL 163
Cdd:PRK10895 91 RRLSVyDNLMAVLQI---RDDLSA--EQREDRANELMEefhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 164 NNLD---MRHSAQMMRHLRrvaeELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVF 233
Cdd:PRK10895 166 AGVDpisVIDIKRIIEHLR----DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-225 |
1.33e-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: 84.35 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKS-TLLTMTgRLLGLDA----GVIEIAGHDVARTPSKDLAKV----VSVLRQENhfVTRL 90
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAahpsGSILFDGQDLLGLSERELRRIrgnrIAMIFQEP--MTSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 ----TVRQLVAFGRFPHsrGRLTAADEEvvSRAIDFLDLGGLE------NRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:COG4172 106 nplhTIGKQIAEVLRLH--RGLSGAAAR--ARALELLERVGIPdperrlDAYPHQLSGGQRQRVMIAMALANEPDLLIAD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG4172 182 EPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-225 |
1.60e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.02 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGH------DVARTPSKDLAKVVSVLRQENHFVTRLTVR 93
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 QLVAFGRFPH---SRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRH 170
Cdd:PRK14246 109 DNIAYPLKSHgikEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 171 SAQMMRHLRRVAEELerTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK14246 189 SQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
4.01e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE--VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENH-FVTrlTVRQLVAFGRFPHSRGRLTAADEEVvsraidfldlgGLEN-----RYLD--------QLSGGQRQRAY 145
Cdd:PRK11160 419 VSQRVHlFSA--TLRDNLLLAAPNASDEALIEVLQQV-----------GLEKlleddKGLNawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 146 VAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHYaDRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA 562
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-206 |
4.64e-18 |
|
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: 82.91 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSG-EVAIGPVDLRipRGGVTALVGPNGAGKSTLLtmtgRLLgldAGVIEIAGHDVartpskDLAKVVSVL 80
Cdd:COG1245 342 VEYPDLTKSYGGfSLEVEGGEIR--EGEVLGIVGPNGIGKTTFA----KIL---AGVLKPDEGEV------DEDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQL---VAFGRFPHSRGRltaadEEVVSRaidfLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:COG1245 407 PQYISPDYDGTVEEFlrsANTDDFGSSYYK-----TEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRI 206
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-212 |
5.36e-18 |
|
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: 79.44 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLG---LDAGVIEIAGHD--VARTPskdlakvvsvlrqenhFVTRLTVRQ 94
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSA---LLGeleKLSGSVSVPGSIayVSQEP----------------WIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 95 LVAFGRfPHSRGRLtaadEEVVS-----RAIDFLDLGglenrylDQ---------LSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:cd03250 85 NILFGK-PFDEERY----EKVIKacalePDLEILPDG-------DLteigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAgHYADRICAVKDG 212
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLL-PHADQIVVLDNG 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-249 |
6.65e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVA-RTPSKDLAKV 76
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKI---LYGLyqpDSGEILIDGKPVRiRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQenHF--VTRLTVRQLVAFGRFPHSRGRL--TAADEEV--VSRAIDF-LDLggleNRYLDQLSGGQRQRAYVAMV 149
Cdd:COG3845 82 IGMVHQ--HFmlVPNLTVAENIVLGLEPTKGGRLdrKAARARIreLSERYGLdVDP----DAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 150 LSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVefGT-------PEE 222
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV--GTvdtaetsEEE 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2385063227 223 I---MTG-EVLTRVFETPVT-----------VVDGPRGPLAV 249
Cdd:COG3845 233 LaelMVGrEVLLRVEKAPAEpgevvlevenlSVRDDRGVPAL 274
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-224 |
7.52e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.37 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSG--EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVT 88
Cdd:PRK11176 351 YPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 RlTVRQLVAFGRFPH-SRGRLTAADEevVSRAIDFLDlgGLENRyLDQ--------LSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:PRK11176 431 D-TIANNIAYARTEQySREQIEEAAR--MAYAMDFIN--KMDNG-LDTvigengvlLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 160 DEPLNNLDMRHSaqmmRHLRRVAEELE--RTVVVVLHDINFAgHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK11176 505 DEATSALDTESE----RAIQAALDELQknRTSLVIAHRLSTI-EKADEILVVEDGEIVERGTHAELL 566
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
7.54e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV-----AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHD------------ 64
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 65 ------VARTPS------KDLAKVVSVLRQENHF-VTRLTVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLENR 131
Cdd:PRK13651 83 vleklvIQKTRFkkikkiKEIRRRVGVVFQFAEYqLFEQTIEKDIIFG--PVSMG---VSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 132 YLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRIC 207
Cdd:PRK13651 158 YLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*..
gi 2385063227 208 AVKDGAVVEFGTPEEIM 224
Cdd:PRK13651 237 FFKDGKIIKDGDTYDIL 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-223 |
8.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQ--ENHFVTRlTVRQLVA 97
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDNQFVGA-TVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 98 FGRFPHSRGRltaadEEVVSR------AIDFLDLgglENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHS 171
Cdd:PRK13642 105 FGMENQGIPR-----EEMIKRvdeallAVNMLDF---KTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 172 AQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-220 |
9.89e-18 |
|
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: 79.07 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENhFVTRLTVRQ-LVAF 98
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDP-VLFSGTIRSnLDPF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRfpHSRGRLTAADEEVVSRAIDFLDLGGLENRYLD---QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMM 175
Cdd:cd03244 102 GE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2385063227 176 RHLRrvaEEL-ERTVVVVLHDINFAGHYaDRICAVKDGAVVEFGTP 220
Cdd:cd03244 180 KTIR---EAFkDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
1.98e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLgldAGVIEIAGHDVARTPSKDLAkvvsVLRQE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL----KIL---AGELEPDSGEVSIPKGLRIG----YLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 84 NHFVTRLTVRQLV--AFGRFPHSRGRLTAA------DEEVVSRAID----FLDLG---------------GLENRYLDQ- 135
Cdd:COG0488 70 PPLDDDLTVLDTVldGDAELRALEAELEELeaklaePDEDLERLAElqeeFEALGgweaearaeeilsglGFPEEDLDRp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 136 ---LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDmrhsAQMMR----HLRRvaeeLERTVVVVLHDINFAGHYADRICA 208
Cdd:COG0488 150 vseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEwleeFLKN----YPGTVLVVSHDRYFLDRVATRILE 221
|
....*....
gi 2385063227 209 VKDGAVVEF 217
Cdd:COG0488 222 LDRGKLTLY 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-218 |
2.01e-17 |
|
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: 77.59 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLL-TMTGRLLGL-DAGVIEIAGHDVartPSKDLAKVVSVLRQENHFVTRLTVRQLVAFgrfphs 104
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLnALAGRRTGLgVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTLTVRETLMF------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 105 rgrlTAAdeevvsraidfldlgglenryLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEE 184
Cdd:cd03213 106 ----AAK---------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2385063227 185 lERTVVVVLH---DINFagHYADRICAVKDGAVVEFG 218
Cdd:cd03213 161 -GRTIICSIHqpsSEIF--ELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-223 |
2.25e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQ--ENHFVTRlTVRQLVA 97
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQnpDNQFVGA-TVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 98 FGR----FPHsrgrltaadEEVVSRAIDFLDLGGLEN---RYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRH 170
Cdd:PRK13650 105 FGLenkgIPH---------EEMKERVNEALELVGMQDfkeREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 171 SAQMMRHLRRVAEELERTVVVVLHDINFAGhYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-214 |
4.53e-17 |
|
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: 77.51 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQLVAFGRFPHSRG 106
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 107 RLTAAdeEVVSRAIDFLDlgGLENRYL-------DQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLR 179
Cdd:cd03248 119 CVKEA--AQKAHAHSFIS--ELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALY 194
|
170 180 190
....*....|....*....|....*....|....*
gi 2385063227 180 RVAEelERTVVVVLHDINFAGHyADRICAVKDGAV 214
Cdd:cd03248 195 DWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-227 |
7.42e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQLVAFGRFPHSRG 106
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDE 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 107 RLTAADEEvvSRAIDFldLGGLENRYL-------DQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDmrhsAQMMRHLR 179
Cdd:TIGR00958 586 EIMAAAKA--ANAHDF--IMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQ 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2385063227 180 RVAEELERTVVVVLHDINFAgHYADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:TIGR00958 658 ESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-237 |
7.73e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 7.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVA---RTPSKDLAKVVSVLRQE--NHFVTRLT 91
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARL---LVGLespSQGNVSWRGEPLAklnRAQRKAFRRDIQMVFQDsiSAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 92 VRQLVAfgrfPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLD 167
Cdd:PRK10419 108 VREIIR----EPLRHLLSLDKAERLARASEMLRAVDLDDSVLDkrppQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 168 MRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVefgtpEEIMTGEVLTrvFETPV 237
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV-----ETQPVGDKLT--FSSPA 246
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
8.69e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 15 VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEI----AGHDVARTPS------------KDLAKVVS 78
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELitnpyskkiknfKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHF-VTRLTVRQLVAFGRFPhsrgrLTAADEEVVSRAIDFLDLGGLENRYLD----QLSGGQRQRAYVAMVLSQE 153
Cdd:PRK13631 120 MVFQFPEYqLFKDTIEKDIMFGPVA-----LGVKKSEAKKLAKFYLNKMGLDDSYLErspfGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 154 TEYVLLDEPLNNLDMRHSAQMMRhLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-220 |
8.79e-17 |
|
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: 77.02 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 22 LRIPR-GGVTALVGPNGAGKSTLL-TMTGRL---LGL-------DAGVIEIAGHDVARTPSKDLAKVVSVLRQEnHFVTR 89
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALkILAGKLkpnLGKfddppdwDEILDEFRGSELQNYFTKLLEGDVKVIVKP-QYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 L------TVRQLvafgrfphsrgrLTAADE-EVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:cd03236 99 IpkavkgKVGEL------------LKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVkdgavveFGTP 220
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL-------YGEP 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
1.36e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEY-SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKD---LAKV 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFGRFPHSrgrltAADEEVVSRAIDFLDLGGLENR---YLDQLSGGQRQRAYVAMVLSQE 153
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAG-----ASGDDIRRRVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 154 TEYVLLDEPLNNLDMRHSAQMMrhlrRVAEELERTVVVVL---HDINFAGHYADRICAVKDG 212
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGIL----RLFEEFNRVGVTVLmatHDIGLISRRSYRMLTLSDG 213
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-225 |
1.54e-16 |
|
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: 78.54 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 22 LRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGLdAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQLVA-FG 99
Cdd:TIGR01842 339 FSLQAGEALAIIGPSGSGKSTLArLIVGIWPPT-SGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-TVAENIArFG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFPHSRGRLTAADEEVVSRAIdfldlGGLENRYlDQ--------LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHS 171
Cdd:TIGR01842 417 ENADPEKIIEAAKLAGVHELI-----LRLPDGY-DTvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 172 AQMMRHLRRVAEElERTVVVVLHDINFAGhYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:TIGR01842 491 QALANAIKALKAR-GITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVLA 542
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-223 |
1.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDV-ARTPSKDLAKV---VSVLRQ--ENHFVTR 89
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIrkkVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 lTVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PRK13649 102 -TVLKDVAFG--PQNFG---VSQEEAEALAREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 166 LDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13649 176 LDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
1.74e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKvVSVL 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 R--QENHFVTRLTVRQ--LVAFGRfpHSRGRLTA----------ADEEVVSRAIDFLD---LGGLENRYLDQLSGGQRQR 143
Cdd:PRK11300 84 RtfQHVRLFREMTVIEnlLVAQHQ--QLKTGLFSgllktpafrrAESEALDRAATWLErvgLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 AYVAMVLSQETEYVLLDEP---LNNLDMRHSAQMMRHLRRvaeELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTP 220
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPaagLNPKETKELDELIAELRN---EHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
...
gi 2385063227 221 EEI 223
Cdd:PRK11300 239 EEI 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-224 |
1.82e-16 |
|
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: 78.25 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDLAKVVSVLRQEnhfVTRL--TVRQ 94
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVwppTAGSVRLDGADLSQWDREELGRHIGYLPQD---VELFdgTIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 95 LVAfgRFPhsrgrlTAADEEVVS--RAIDFLDL-GGLENRYlD--------QLSGGQRQRAYVAMVLSQETEYVLLDEPL 163
Cdd:COG4618 425 NIA--RFG------DADPEKVVAaaKLAGVHEMiLRLPDGY-DtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 164 NNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-223 |
1.87e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGH---DVAR----TPSKdlAKVVSVLrQEnhfvTRLtv 92
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgiclPPEK--RRIGYVF-QD----ARL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 rqlvafgrFPHS--RGRLT----AADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:PRK11144 88 --------FPHYkvRGNLRygmaKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 167 DMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-218 |
2.04e-16 |
|
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: 75.65 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGhdvartpskdlaKVVSVLRQENHFVTRLTVRQLVAF- 98
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGLGGGFNPELTGRENIYLn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHL 178
Cdd:cd03220 109 GRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2385063227 179 RRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-206 |
2.59e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.93 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 24 IPRGGVTALVGPNGAGKSTLLtmtgRLLgldAGVIEIAGHDVARTPSkdlakvVSVLRQENHFVTRLTVRQLVAFgrfph 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFA----KLL---AGVLKPDEGEVDPELK------ISYKPQYIKPDYDGTVEDLLRS----- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 104 SRGRLTAA--DEEVVSRaidfLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRV 181
Cdd:PRK13409 424 ITDDLGSSyyKSEIIKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*
gi 2385063227 182 AEELERTVVVVLHDINFAGHYADRI 206
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYISDRL 524
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-223 |
4.69e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.19 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDV---ARTPSKDLAKVVSVLRQENHFVTRLTVRQLV 96
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRFPHSrgRLTAAD-EEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMM 175
Cdd:PRK11831 106 AYPLREHT--QLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2385063227 176 RHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-225 |
4.78e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGV-----IEIAGHDVaRTPSKDLAKV---VSVLRQ 82
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDI-YDPDVDVVELrrrVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 E-NHFvtRLTVRQLVAFGrfPHSRGRLTAAD-EEVVSRAI----------DFLDLGGLEnryldqLSGGQRQRAYVAMVL 150
Cdd:COG1117 100 KpNPF--PKSIYDNVAYG--LRLHGIKSKSElDEIVEESLrkaalwdevkDRLKKSALG------LSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 151 SQETEYVLLDEPLNNLDMRHSAQ---MMRHLRRvaeelERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPISTAKieeLILELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-238 |
8.23e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVAR-TPSKDLAKVVSV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFG--RFPHSRGRLTAADEEVVSRaidfLDL----GGLENryldqlsgGQRQRAYVAMVLSQE 153
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGlpKRQASMQKMKQLLAALGCQ----LDLdssaGSLEV--------ADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 154 TEYVLLDEPLNNLDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLTRVf 233
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI- 236
|
....*
gi 2385063227 234 eTPVT 238
Cdd:PRK15439 237 -TPAA 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-223 |
1.09e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.91 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLS--GVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV-V 77
Cdd:COG1137 1 MMTLEaeNLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQ-LVAFGRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:COG1137 81 GYLPQEASIFRKLTVEDnILAVLEL---RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 157 VLLDEPLNNLD------MRhsaQMMRHLRR-----------VAEELERTvvvvlhdinfaghyaDRICAVKDGAVVEFGT 219
Cdd:COG1137 158 ILLDEPFAGVDpiavadIQ---KIIRHLKErgigvlitdhnVRETLGIC---------------DRAYIISEGKVLAEGT 219
|
....
gi 2385063227 220 PEEI 223
Cdd:COG1137 220 PEEI 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-196 |
1.17e-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: 75.98 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 22 LRIPR-GGVTALVGPNGAGKSTLLTM-TGRL---LGldagvieiaghDVARTPSKDlakvvSVLRQ------ENHF---- 86
Cdd:COG1245 93 LPVPKkGKVTGILGPNGIGKSTALKIlSGELkpnLG-----------DYDEEPSWD-----EVLKRfrgtelQDYFkkla 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 ------------------VTRLTVRQLvafgrfphsrgrLTAADEE-VVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVA 147
Cdd:COG1245 157 ngeikvahkpqyvdlipkVFKGTVREL------------LEKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2385063227 148 MVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDI 196
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-206 |
1.78e-15 |
|
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: 72.53 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 10 EYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSkDLAKVVSVLRQENHFVTR 89
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 LTVRQLVAFGRFPHSRgrltaadeEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:cd03231 88 LSVLENLRFWHADHSD--------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2385063227 170 HSAQMMRHlrrVAEELERTVVVVL---HDINFAGHYADRI 206
Cdd:cd03231 160 GVARFAEA---MAGHCARGGMVVLtthQDLGLSEAGAREL 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-207 |
1.94e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIaGHDVartpskDLAkvvs 78
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM---ITGQeqpDSGTIKI-GETV------KLA---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 vlrqenhfvtrlTVRQlvafgrfphSRGRLtaADE----EVVSRAIDFLDLGGLE--NR-YL--------DQ------LS 137
Cdd:PRK11819 391 ------------YVDQ---------SRDAL--DPNktvwEEISGGLDIIKVGNREipSRaYVgrfnfkggDQqkkvgvLS 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 138 GGQRQRAYVAMVLSQETEYVLLDEPLNNLDMrhsaQMMRHLRRVAEELERTVVVVLHDINFaghyADRIC 207
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEEALLEFPGCAVVISHDRWF----LDRIA 509
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-224 |
2.15e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.19 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 3 TLSGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGhdvartpskdlaKVVSVLr 81
Cdd:COG1134 27 LLLRRRRTRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVSALL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 qE-NH-FVTRLTVRQLVAFgrfphsRGRL---TAAD-EEVVSRAIDFLDLGglenRYLDQ----LSGGQRQRAYVAMVLS 151
Cdd:COG1134 94 -ElGAgFHPELTGRENIYL------NGRLlglSRKEiDEKFDEIVEFAELG----DFIDQpvktYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 152 QETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-230 |
2.56e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKV-VSV 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFGRFPHSR--GRLTAADEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAYVAMVLSQET 154
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcGVNIIDWREMRVRAAMMLLRVGLKvdlDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 155 EYVLLDEP---LNNLDMRHSAQMMRHLRRVAeeleRTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGEVLT 230
Cdd:PRK09700 165 KVIIMDEPtssLTNKEVDYLFLIMNQLRKEG----TAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-193 |
4.26e-15 |
|
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: 71.24 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 13 GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTpSKDLAKVVSVLRQENHFVTRLTV 92
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQLVAFGRFPHSRGRLTAADeevvsrAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSA 172
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIED------ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 2385063227 173 QMMRHLRrvaEELERTVVVVL 193
Cdd:TIGR01189 165 LLAGLLR---AHLARGGIVLL 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-223 |
4.54e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKStlLTMTGRLLGLDAGVIEIAGH----DVARTPSKDLAKVVSVLRQ--ENHFVTRLTVR 93
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRvlldGKPVAPCALRGRKIATIMQnpRSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 Q-----LVAFGRfPHSRGRLTAADEEVvsraidfldlgGLEN------RYLDQLSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:PRK10418 100 TharetCLALGK-PADDATLTAALEAV-----------GLENaarvlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-224 |
7.55e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 73.32 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLltmtGRLL----GLDAGVIEIAGHDVARTPSKDLAKVVSVLRQEnhfvTRL---TV 92
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTL----ARLLfrfyDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD----TVLfndTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQLVAFgrfphsrGRLTAADEEVVsRAI------DFLDlgGLENRYLDQ-------LSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:COG5265 449 AYNIAY-------GRPDASEEEVE-AAAraaqihDFIE--SLPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 160 DEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLH------DinfaghyADRICAVKDGAVVEFGTPEEIM 224
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAELL 580
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-218 |
9.14e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 6 GVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDL--AKVVSVLRQE 83
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseAERRRLLRTE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 84 NHFVT-------RLTV-------RQLVAFGRFPHSRGRLTAAD--EEV---VSRaIDflDLGGlenryldQLSGGQRQRA 144
Cdd:PRK11701 91 WGFVHqhprdglRMQVsaggnigERLMAVGARHYGDIRATAGDwlERVeidAAR-ID--DLPT-------TFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 145 YVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-223 |
1.41e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 71.35 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGL-----DAGVIEIAGHDVART---PSKDLAKVVSVLRQ 82
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPdvdPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFVTrlTVRQLVAFG-RFPHSRGRLtaadEEVVSRAI----------DFLDLGGLenryldQLSGGQRQRAYVAMVLS 151
Cdd:PRK14243 100 PNPFPK--SIYDNIAYGaRINGYKGDM----DELVERSLrqaalwdevkDKLKQSGL------SLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 152 QETEYVLLDEPLNNLD---MRHSAQMMRHLRRvaeelERTVVVVLHDINFAGHYADRIC---------AVKDGAVVEFGT 219
Cdd:PRK14243 168 VQPEVILMDEPCSALDpisTLRIEELMHELKE-----QYTIIIVTHNMQQAARVSDMTAffnveltegGGRYGYLVEFDR 242
|
....
gi 2385063227 220 PEEI 223
Cdd:PRK14243 243 TEKI 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-223 |
1.54e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.92 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLltmtGRLLGL----DAGVIEIAGHDVARtPSKDLAKVvsvLRQENHFV---- 87
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTMietpTGGELYYQGQDLLK-ADPEAQKL---LRQKIQIVfqnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 88 -----TRLTVRQLVAFGRFPHSRgrLTAAdeEVVSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:PRK11308 102 ygslnPRKKVGQILEEPLLINTS--LSAA--ERREKALAMMAKVGLRpehyDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-227 |
2.97e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 32 LVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVR-QLVAFGRfpHSRGRLTA 110
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVRfNIDPFSE--HNDADLWE 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 111 ADE-----EVVSRAIDFLDLGGLENRylDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRrvaEEL 185
Cdd:PLN03232 1344 ALErahikDVIDRNPFGLDAEVSEGG--ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EEF 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2385063227 186 ER-TVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:PLN03232 1419 KScTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-223 |
4.28e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVvsvlRQENHFV-------- 87
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV----RSDIQMIfqdplasl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 88 -TRLTVRQLVA-----FgrFPHsrgrltAADEEVVSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:PRK15079 112 nPRMTIGEIIAeplrtY--HPK------LSRQEVKDRVKAMMLKVGLLpnliNRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-196 |
4.53e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 22 LRIPR-GGVTALVGPNGAGKSTLLT-MTGRL---LGldagvieiaghDVARTPSKDlakvvSVLRQ------ENHF---- 86
Cdd:PRK13409 93 LPIPKeGKVTGILGPNGIGKTTAVKiLSGELipnLG-----------DYEEEPSWD-----EVLKRfrgtelQNYFkkly 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 ------------------VTRLTVRQLvafgrfphsrgrLTAADE-----EVVSRaidfLDLGGLENRYLDQLSGGQRQR 143
Cdd:PRK13409 157 ngeikvvhkpqyvdlipkVFKGKVREL------------LKKVDErgkldEVVER----LGLENILDRDISELSGGELQR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEelERTVVVVLHDI 196
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
5.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.73 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGE------VAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTpsKDLA 74
Cdd:PRK13633 4 MIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 75 KVVS----VLRQENHFVTRLTVRQLVAFGrfPHSRGrltAADEEVVSRAIDFLDLGGLEnRYLDQ----LSGGQRQRAYV 146
Cdd:PRK13633 82 DIRNkagmVFQNPDNQIVATIVEEDVAFG--PENLG---IPPEEIRERVDESLKKVGMY-EYRRHaphlLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 147 AMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-212 |
5.59e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGrllGLDA---GVIEIAGHDVARTPSKDLAKV----VSVLRQENHFVTRLTV 92
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLG---GLDTptsGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQLVAFgrfPHSRGRLTAAdeEVVSRAIDFLDLGGLENRYL---DQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:PRK11629 105 LENVAM---PLLIGKKKPA--EINSRALEMLAAVGLEHRANhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2385063227 170 HSAQMMRHLRRVAEELERTVVVVLHDINFAGHYaDRICAVKDG 212
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-234 |
7.62e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 7.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDA-----GVIEIAGHDV--ARTPSKDLAKVVS-VLRQ 82
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLRRQVSmVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFvtRLTVRQLVAFG-RFPHSRGRLTAADeeVVSRAIDFLDL-----GGLENRYLDqLSGGQRQRAYVAMVLSQETEY 156
Cdd:PRK14258 97 PNLF--PMSVYDNVAYGvKIVGWRPKLEIDD--IVESALKDADLwdeikHKIHKSALD-LSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKD-----GAVVEFGTPEEIMTGEVLTR 231
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSR 251
|
...
gi 2385063227 232 VFE 234
Cdd:PRK14258 252 TRE 254
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-180 |
9.08e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 9.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTpskDLAKVVSVLRQENHFVTRLTVRQLVAFGRfphsrg 106
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP---DVAEACHYLGHRNAMKPALTVAENLEFWA------ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 107 RLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDmRHS----AQMMR-HLRR 180
Cdd:PRK13539 99 AFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAvalfAELIRaHLAQ 176
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-224 |
1.78e-13 |
|
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: 69.38 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 13 GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTV 92
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQLVAfgrfphsrGRLTAADEEVVSRAIDFLDLG--------GLENRYLDQ---LSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:TIGR01193 566 ENLLL--------GAKENVSQDEIWAACEIAEIKddienmplGYQTELSEEgssISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAeelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-212 |
4.49e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAKV-VSVLR 81
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMkVLTG-IYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 82 QENHFVTRLTVRQLVAFGR-FPHSRGRLtaaDEEVVSRAIDFLdLGGLENRY-----LDQLSGGQRQRAYVAMVLSQETE 155
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGReFVNRFGRI---DWKKMYAEADKL-LARLNLRFssdklVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDG 212
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-223 |
8.18e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQeNHFVTRLTVRQLVAFG 99
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTVANNIALG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RfPHSrgrlTAADEEVVSR-AIDFLDLGGLENRYLDQ-------LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHS 171
Cdd:PRK10789 413 R-PDA----TQQEIEHVARlASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 172 AQMMRHLRRVAEelERTVVVVLHDINfAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK10789 488 HQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-223 |
8.49e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAG---------------VIE-----------IAGHDVA--- 66
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsrqVIElseqsaaqmrhVRGADMAmif 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 67 RTPSKDLAKVVSVLRQENHfvtrlTVRQLVAFGRfphsrgrltaadEEVVSRAIDFLDL------GGLENRYLDQLSGGQ 140
Cdd:PRK10261 111 QEPMTSLNPVFTVGEQIAE-----SIRLHQGASR------------EEAMVEAKRMLDQvripeaQTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 141 RQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTP 220
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSV 253
|
...
gi 2385063227 221 EEI 223
Cdd:PRK10261 254 EQI 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-225 |
1.34e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 11 YSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLT----MTGRLLGLD-AGVIEIAGHDV--ARTPSKDLAKVVSVLRQE 83
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRtlnrMNDKVSGYRySGDVLLGGRSIfnYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 84 NHFVTRLTVRQLV---AFGRFPHSRGRLTAAdeevvSRAIDFLDLGGLENRYLD---QLSGGQRQRAYVAMVLSQETEYV 157
Cdd:PRK14271 111 NPFPMSIMDNVLAgvrAHKLVPRKEFRGVAQ-----ARLTEVGLWDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-223 |
1.80e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.52 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQLVafgrfphSRG 106
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNR-SIEDNI-------RVG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 107 RLTAADEEVV-----SRAIDFLD--LGGLENRYLD---QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMR 176
Cdd:PRK13657 433 RPDATDEEMRaaaerAQAHDFIErkPDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKA 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2385063227 177 HLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK13657 513 ALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDEL 556
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-216 |
2.18e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKS-TLLTMTgRLLG-----LDAGVIEIAGHDVARTPSKDLAKV----VSVLRQEN----- 84
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGKSvTALSIL-RLLPsppvvYPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPmvsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 85 --HFVTRLTVRQLVAfgrfpHSRGRLTAADEEVvsraIDFLDLGGLE------NRYLDQLSGGQRQRAYVAMVLSQETEY 156
Cdd:PRK15134 107 plHTLEKQLYEVLSL-----HRGMRREAARGEI----LNCLDRVGIRqaakrlTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVE 216
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-222 |
2.35e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.22 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLL-TMTGRLL-GLD-AGVIEIAGHDVARtpsKDLAKVVSVLRQENHFVTRLTVRQLVAFgrFPH 103
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMnALAFRSPkGVKgSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLTVREHLMF--QAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 104 SR-GRLTAADE--EVVSRAIDFLDLG-------GLENRyLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQ 173
Cdd:TIGR00955 126 LRmPRRVTKKEkrERVDEVLQALGLRkcantriGVPGR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 174 MMRHLRRVAEElERTVVVVLH----DI--NFaghyaDRICAVKDGAVVEFGTPEE 222
Cdd:TIGR00955 205 VVQVLKGLAQK-GKTIICTIHqpssELfeLF-----DKIILMAEGRVAYLGSPDQ 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-197 |
2.86e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.11 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 7 VRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDvartPSKdlakvvsvlrQE 83
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM---LTGIlvpTSGEVRVLGYV----PFK----------RR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 84 NHFVTRLTVrqlVaFGrfphSRGRL----TAAD----------------EEVVSRAIDFLDLGGLENRYLDQLSGGQRQR 143
Cdd:COG4586 91 KEFARRIGV---V-FG----QRSQLwwdlPAIDsfrllkaiyripdaeyKKRLDELVELLDLGELLDTPVRQLSLGQRMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMrHSAQMMRH-LRRVAEELERTVVVVLHDIN 197
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDV-VSKEAIREfLKEYNRERGTTILLTSHDMD 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-220 |
2.88e-12 |
|
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: 66.19 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 10 EYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVaRTPSKDLAKVVSVLRQENHFVTR 89
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 LTVRQLVAFgrFPHSRGRltaADEEVVSRAIDFLDLGGL---ENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:TIGR01257 1018 LTVAEHILF--YAQLKGR---SWEEAQLEMEAMLEDTGLhhkRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 167 DMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTP 220
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-233 |
3.43e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 4 LSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKD-LAKVVSVLRQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 ENHFVTRLTVRQLVAFGRFPhSRGRLTaaDEEVVSR---AI-DFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYP-TKGMFV--DQDKMYRdtkAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 159 LDEPLNNLdmrhSAQMMRHLRRVAEELERT---VVVVLHDINFAGHYADRICAVKDG-----AVVEFGTPEEI---MTGE 227
Cdd:PRK10982 158 MDEPTSSL----TEKEVNHLFTIIRKLKERgcgIVYISHKMEEIFQLCDEITILRDGqwiatQPLAGLTMDKIiamMVGR 233
|
....*.
gi 2385063227 228 VLTRVF 233
Cdd:PRK10982 234 SLTQRF 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-234 |
3.58e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLT-MTGRLLGLDAGVIEIAGhDVARTPSkdlakvVSvlrqenhFVTRLTVRQLVAF 98
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-SVAYVPQ------VS-------WIFNATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRFPHSRGRLTAADEEVVSRAIDFL---DLGGLENRYLDqLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMM 175
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLDLLpgrDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 176 RHLrrVAEELE-RTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM-TGEVLTRVFE 234
Cdd:PLN03232 781 DSC--MKDELKgKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAELSkSGSLFKKLME 838
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-233 |
4.43e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLL------GLDAGVIEIAGHDV-ARTPSKDL 73
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLM----KVLsgvyphGTYEGEIIFEGEELqASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 AKVVSVLRQENHFVTRLTVRQLVAFGRFPHSRGRLtaADEEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAYVAMVL 150
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIM--DYDAMYLRAQKLLAQLKLDinpATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 151 SQETEYVLLDEPLNNLdmrhSAQMMRHLRRVAEELER---TVVVVLHDINFAGHYADRICAVKDGAVV------EFGTPE 221
Cdd:PRK13549 159 NKQARLLILDEPTASL----TESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTICVIRDGRHIgtrpaaGMTEDD 234
|
250
....*....|....
gi 2385063227 222 EI--MTGEVLTRVF 233
Cdd:PRK13549 235 IItmMVGRELTALY 248
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-234 |
5.85e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLT-MTGRLLGLDAGVIEIAGhDVARTPSkdlakvVSvlrqenhFVTRLTVRQLVAF 98
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-TVAYVPQ------VS-------WIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRfPHSRGRLTAA-DEEVVSRAIDFL---DLGGLENRYLDqLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDmrhsAQM 174
Cdd:PLN03130 702 GS-PFDPERYERAiDVTALQHDLDLLpggDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD----AHV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 175 MRHL--RRVAEELE-RTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM-TGEVLTRVFE 234
Cdd:PLN03130 776 GRQVfdKCIKDELRgKTRVLVTNQLHFLSQ-VDRIILVHEGMIKEEGTYEELSnNGPLFQKLME 838
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-227 |
5.96e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 32 LVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVR-QLVAFGRfpHSRGRLTA 110
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TVRfNLDPFNE--HNDADLWE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 111 ADE-----EVVSRAIDFLD---LGGLENryldqLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRrva 182
Cdd:PLN03130 1347 SLErahlkDVIRRNSLGLDaevSEAGEN-----FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR--- 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2385063227 183 EELER-TVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:PLN03130 1419 EEFKScTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-220 |
6.43e-12 |
|
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: 62.81 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVR-QLVAF 98
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG-TIRsNLDPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRFphsrgrltaADEEVvsRAIDFLDLGGLenryldQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHL 178
Cdd:cd03369 106 DEY---------SDEEI--YGALRVSEGGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2385063227 179 RRvaEELERTVVVVLHDINFAGHYaDRICAVKDGAVVEFGTP 220
Cdd:cd03369 169 RE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
6.52e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLL--GLDAGVIEIAGHD-VARTPSKDLAKVV 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPlKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 78 SVLRQENHFVTRLTVRQLVAFG-RFPHSRGRLtaADEEVVSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQ 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGnEITLPGGRM--AYNAMYLRAKNLLRELQLDadnvTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 153 ETEYVLLDEPLNNLdmrhSAQMMRHLRRVAEELER---TVVVVLHDINFAGHYADRICAVKDG 212
Cdd:TIGR02633 159 QARLLILDEPSSSL----TEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-216 |
7.73e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLtmtGRLLGLD---AGVIEIAGHDVARTPSKDLAKV----VSVLRQENHFVTRLTV 92
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLL---AILAGLDdgsSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 R---QLVAFGRfphsrgrlTAADEEVVSRAIDFLDLGGLENRyLD----QLSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PRK10584 106 LenvELPALLR--------GESSRQSRNGAKALLEQLGLGKR-LDhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 166 LDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHyADRICAVKDGAVVE 216
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
26-236 |
1.08e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 26 RGGVTALVGPNGAGKSTLLTMTGRLLGlDAGVIEIAGHDVARTPSKDLAKV---VSVLRQE--NHFVTRLTVRQLVAFGR 100
Cdd:PRK15134 311 PGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLLPVrhrIQVVFQDpnSSLNPRLNVLQIIEEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 101 FPHSRgRLTAADEEvvSRAIDFLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMR 176
Cdd:PRK15134 390 RVHQP-TLSAAQRE--QQVIAVMEEVGLDpetrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 177 HLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEeimtgevltRVFETP 236
Cdd:PRK15134 467 LLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE---------RVFAAP 517
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
14-168 |
1.18e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 14 EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTpskDLAKVVSVLRQ----------- 82
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHlpglkadlstl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 83 EN-HFVTRLTvrqlvafGRFPhsrgrltaadEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:PRK13543 101 ENlHFLCGLH-------GRRA----------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*..
gi 2385063227 162 PLNNLDM 168
Cdd:PRK13543 164 PYANLDL 170
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-223 |
2.69e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.45 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKST-------LLTMTGRLLgldAGVIEIAGHDVARTPSKDLAKV----VSVLRQEN 84
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRVM---AEKLEFNGQDLQRISEKERRNLvgaeVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 85 hfVTRLTVRQLVAFGRFPHSRGRLTAADEEVVSRAIDFLDLGGL---ENR---YLDQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:PRK11022 99 --MTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-222 |
4.68e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLgLDAGVIEIA-----GHdVARTPSKDLAK 75
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLrTLVGELE-PDSGTVKWSenaniGY-YAQDHAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 VVSVL------RQENHfvTRLTVRQLVafgrfphsrGRLTAADEEVvsraidfldlggleNRYLDQLSGGQRQRAYVAMV 149
Cdd:PRK15064 398 DLTLFdwmsqwRQEGD--DEQAVRGTL---------GRLLFSQDDI--------------KKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 150 LSQETEYVLLDEPLNNLDMrhsaQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEF-GTPEE 222
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFsGTYEE 522
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-194 |
5.57e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTM-TGRLLGL-DAGVIEIaghdvartpskdlakvvsvlrQENHFVTRLT-VRQLV 96
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLlAGALKGTpVAGCVDV---------------------PDNQFGREASlIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRFPHSRGRLTAADeevVSRAIDFLdlgglenRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMR 176
Cdd:COG2401 108 RKGDFKDAVELLNAVG---LSDAVLWL-------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170
....*....|....*...
gi 2385063227 177 HLRRVAEELERTVVVVLH 194
Cdd:COG2401 178 NLQKLARRAGITLVVATH 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
6.79e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.74 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGLDA------------------GVIEI--- 60
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHV---LRGMDQyeptsgriiyhvalcekcGYVERpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 61 AGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLVAFGRFPHSRGRLTAAD-------------EEVVSRAIDFLDLGG 127
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDnvlealeeigyegKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 128 LENRYLD---QLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYAD 204
Cdd:TIGR03269 158 LSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*....
gi 2385063227 205 RICAVKDGAVVEFGTPEEI 223
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-198 |
7.70e-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: 61.49 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 32 LVGPNGAGKSTLLTMtgrLLGLDAgviEIAGHdvARtPSKDLAkvVSVLRQENHFVTRLTVRQLVAFG---------RFP 102
Cdd:TIGR03719 36 VLGLNGAGKSTLLRI---MAGVDK---DFNGE--AR-PQPGIK--VGYLPQEPQLDPTKTVRENVEEGvaeikdaldRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 103 HSRGRLTAADEEV---------VSRAIDFLDLGGLENRyLDQ----------------LSGGQRQRAYVAMVLSQETEYV 157
Cdd:TIGR03719 105 EISAKYAEPDADFdklaaeqaeLQEIIDAADAWDLDSQ-LEIamdalrcppwdadvtkLSGGERRRVALCRLLLSKPDML 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRrvaeELERTVVVVLHDINF 198
Cdd:TIGR03719 184 LLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHDRYF 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-225 |
7.82e-11 |
|
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: 61.50 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYS--GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLltmtGRLL-GLD---AGVIEIAGHDVARTPSKDLAK 75
Cdd:TIGR03796 478 VELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTI----AKLVaGLYqpwSGEILFDGIPREEIPREVLAN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 VVSVLRQENhFVTRLTVRQLVAF--GRFPHSRGRLTAAD----EEVVSRAidfldlGGLENRYLD---QLSGGQRQRAYV 146
Cdd:TIGR03796 554 SVAMVDQDI-FLFEGTVRDNLTLwdPTIPDADLVRACKDaaihDVITSRP------GGYDAELAEggaNLSGGQRQRLEI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 147 AMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRvaeeleR--TVVVVLHDINfAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDPETEKIIDDNLRR------RgcTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELW 699
|
.
gi 2385063227 225 T 225
Cdd:TIGR03796 700 A 700
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-194 |
9.78e-11 |
|
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: 59.18 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLL-TMTGRllgLDAGVIE----IAGhdvaRTPSKDLAKVVSVLRQENHFVTRLTVRQlvafgrf 101
Cdd:cd03232 33 GTLTALMGESGAGKTTLLdVLAGR---KTAGVITgeilING----RPLDKNFQRSTGYVEQQDVHSPNLTVRE------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 102 phsrgrltaadeevvsrAIDFldlggleNRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRV 181
Cdd:cd03232 99 -----------------ALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170
....*....|...
gi 2385063227 182 AEElERTVVVVLH 194
Cdd:cd03232 155 ADS-GQAILCTIH 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-216 |
1.01e-10 |
|
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: 61.35 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGEV-----AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTpskdl 73
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKL---LTGLyrpESGEILLDGQPVTAD----- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 akvvsvlrqenhfvTRLTVRQLVA-----FGRFPHSRGRLTAADEEVVSRAIDFLDLGG---LENRYLD--QLSGGQRQR 143
Cdd:COG4615 400 --------------NREAYRQLFSavfsdFHLFDRLLGLDGEADPARARELLERLELDHkvsVEDGRFSttDLSQGQRKR 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 ayVAMVLS--QETEYVLLDE------PlnnldmrhsaqmmrHLRRV-AEEL--E-----RTVVVVLHDinfaGHY---AD 204
Cdd:COG4615 466 --LALLVAllEDRPILVFDEwaadqdP--------------EFRRVfYTELlpElkargKTVIAISHD----DRYfdlAD 525
|
250
....*....|..
gi 2385063227 205 RICAVKDGAVVE 216
Cdd:COG4615 526 RVLKMDYGKLVE 537
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-191 |
1.01e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.36 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrllgldagvieIAGH------DVARTPSKDLAkvvsVLRQENH 85
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA-------------IAGLwpygsgRIARPAGARVL----FLPQRPY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 86 FVTrLTVRQLVAFgrfPHSRgrlTAADEEVVSRAIDFLDLGGLENRyLDQ-------LSGGQRQRAYVAMVLSQETEYVL 158
Cdd:COG4178 437 LPL-GTLREALLY---PATA---EAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|...
gi 2385063227 159 LDEPLNNLDMRHSAQMMRHLRrvaEELERTVVV 191
Cdd:COG4178 509 LDEATSALDEENEAALYQLLR---EELPGTTVI 538
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
1.26e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.51 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtGRLLG---LDAGVIEIAGHDVARTP-SKDLAKV 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLL---GTLCGdprATSGRIVFDGKDITDWQtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTVRQLVAFGRFPHSRGRLtaadEEVVSRAID-FLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETE 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQF----QERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 156 YVLLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-218 |
1.79e-10 |
|
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: 58.81 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 19 PVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGLDA--GVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTrLTVRQL 95
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLkALANRTEGNVSveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPT-LTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 96 vafgrfphsrgrltaadeevvsraIDF-LDLGGleNRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQM 174
Cdd:cd03233 104 ------------------------LDFaLRCKG--NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2385063227 175 MRHLRRVAEELERTVVVVLH---DINFagHYADRICAVKDGAVVEFG 218
Cdd:cd03233 158 LKCIRTMADVLKTTTFVSLYqasDEIY--DLFDKVLVLYEGRQIYYG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-194 |
2.41e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLLT-MTGRLLGLD-AGVIEIAGhdvaRTPSKDLAKVVSVLRQENHFVTRLTVRQLVAFG---RF 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANN----RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCsllRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 102 PHS--RGRLTAADEEVVSRaidfLDLGGLEN-----RYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQM 174
Cdd:PLN03211 170 PKSltKQEKILVAESVISE----LGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180
....*....|....*....|
gi 2385063227 175 MRHLRRVAEElERTVVVVLH 194
Cdd:PLN03211 246 VLTLGSLAQK-GKTIVTSMH 264
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
2.76e-10 |
|
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: 57.61 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSG--EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGL---DAGVIEIAGHDVARTPSKDLAKV 76
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLlrpTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQenhfvtrltvrqlvafgrfphsrgrltaaDEEVVSRAIdfldlggLENryldQLSGGQRQRAYVAMVLSQETEY 156
Cdd:cd03246 78 VGYLPQ-----------------------------DDELFSGSI-------AEN----ILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 157 VLLDEPLNNLDMRHSAQMMRHLRRvAEELERTVVVVLHDINFAGHyADRICAVKDGAV 214
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
118-225 |
6.71e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 118 RAIDFLDLGGLENR------YLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVV 191
Cdd:PRK15093 135 RAIELLHRVGIKDHkdamrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILL 214
|
90 100 110
....*....|....*....|....*....|....
gi 2385063227 192 VLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT 225
Cdd:PRK15093 215 ISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-224 |
9.02e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLT-MTGRLLGLDaGVIEIAGhDVARTPskdlakvvsvlrqENHFVTRLTVRQLVAF 98
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHMKG-SVAYVP-------------QQAWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 GRF---PHSRGRLTA----ADEEVVSRAiDFLDLG--GLenryldQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:TIGR00957 722 GKAlneKYYQQVLEAcallPDLEILPSG-DRTEIGekGV------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 170 HSAQMMRHLRRVAEELE-RTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKnKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-224 |
9.08e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLG---LDAGVIEIAGHDVARTPSKDLAKVVSVLrQENHFVTRLTVRQLV 96
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASL---LMGyypLTEGEIRLDGRPLSSLSHSVLRQGVAMV-QQDPVVLADTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRfphsrgrltAADEEVVSRAIDFLDL--------GGLENRYLDQ---LSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PRK10790 436 TLGR---------DISEEQVWQALETVQLaelarslpDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 166 LDMRHSAQMMRHLRRVAEelERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK10790 507 IDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-224 |
9.62e-10 |
|
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: 58.43 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGLD---AGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLV 96
Cdd:TIGR03797 472 VSLQIEPGEFVAIVGPSGSGKSTLLRL---LLGFEtpeSGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRFPHSRGrLTAADEEVVSRAIDFLDLG-------GLENryldqLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:TIGR03797 549 GGAPLTLDEA-WEAARMAGLAEDIRAMPMGmhtviseGGGT-----LSGGQRQRLLIARALVRKPRILLFDEATSALDNR 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 170 HSAQMMRHLRRvaeeLERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR03797 623 TQAIVSESLER----LKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELM 672
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-223 |
1.07e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.81 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRI----PRGGVTA---------------LVGPNGAGKS-TLLTMTGRLL--GLDAGVIEIAGHDVARTPSKDLAKV-- 76
Cdd:PRK09473 17 DLRVtfstPDGDVTAvndlnfslragetlgIVGESGSGKSqTAFALMGLLAanGRIGGSATFNGREILNLPEKELNKLra 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 --VSVLRQENhfVTRLTV-----RQLVAFGRFPHSRGRLTAADEEVvsRAIDFLDLGGLENR---YLDQLSGGQRQRAYV 146
Cdd:PRK09473 97 eqISMIFQDP--MTSLNPymrvgEQLMEVLMLHKGMSKAEAFEESV--RMLDAVKMPEARKRmkmYPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2385063227 147 AMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEI 223
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-216 |
1.35e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.67 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYSGE-VAIGPVDLRIPRGGVTALVGPNGAGKSTLltmtGRLL-GL---DAGVIEIAGHDVARTPSKDLAKV 76
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTL----AMLLtGLyqpQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 77 VSVLRQENHFVTRLTvrqlvafgrfphsRGRLTAADEEVVSRAIDFLDLGG----LENRYLD-QLSGGQRQRAYVAMVLS 151
Cdd:PRK10522 399 FSAVFTDFHLFDQLL-------------GPEGKPANPALVEKWLERLKMAHklelEDGRISNlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 152 QETEYVLLDEplnnldmrHSAQMMRHLRRV--------AEELERTVVVVLHDinfaGHY---ADRICAVKDGAVVE 216
Cdd:PRK10522 466 EERDILLLDE--------WAADQDPHFRREfyqvllplLQEMGKTIFAISHD----DHYfihADRLLEMRNGQLSE 529
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-206 |
1.97e-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: 55.27 E-value: 1.97e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 136 LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRI 206
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-194 |
2.38e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.55 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 26 RGGV-TALVGPNGAGKSTLL-TMTGRLLG-LDAGVIEIAGHdvartPSKD--LAKVVSVLRQENHFVTRLTVRQLV---A 97
Cdd:PLN03140 904 RPGVlTALMGVSGAGKTTLMdVLAGRKTGgYIEGDIRISGF-----PKKQetFARISGYCEQNDIHSPQVTVRESLiysA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 98 FGRFPHSRGRltaaDEEV--VSRAIDFLDLGGLENRY-----LDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRH 170
Cdd:PLN03140 979 FLRLPKEVSK----EEKMmfVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180
....*....|....*....|....
gi 2385063227 171 SAQMMRHLRRVAEElERTVVVVLH 194
Cdd:PLN03140 1055 AAIVMRTVRNTVDT-GRTVVCTIH 1077
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-250 |
2.46e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEiaghdvaRTPSKDLAKVvsvl 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIGYV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTvrqlVAFGRFPHSRGRLTAADeevVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLD 160
Cdd:PRK09544 73 PQKLYLDTTLP----LTVNRFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 161 EPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVkDGAVVEFGTPEEIMTGEVLTRVFetpvtvv 240
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPEFISMF------- 217
|
250
....*....|..
gi 2385063227 241 dGPRGP--LAVY 250
Cdd:PRK09544 218 -GPRGAeqLGIY 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-201 |
3.42e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIPRGGVTALVGPNGAGKSTLLtmtgRLL-GL---DAGVIEIAGHDVARtpskdlakvvsvLRQENHfvtrltvRQLV 96
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLL----RILaGLarpDAGEVLWQGEPIRR------------QRDEYH-------QDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 97 AFGRFPHSRGRLTA-------------ADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVA-MVLSQETEYVlLDEP 162
Cdd:PRK13538 78 YLGHQPGIKTELTAlenlrfyqrlhgpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRAPLWI-LDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2385063227 163 LNNLDMRHSAQMMRHLrrvAEELERTVVVVL---HDINFAGH 201
Cdd:PRK13538 157 FTAIDKQGVARLEALL---AQHAEQGGMVILtthQDLPVASD 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-199 |
4.95e-09 |
|
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: 53.90 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 14 EVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGrllgldagvieiaghdvartpskdlakvvsvlrqenhfvtrltvr 93
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 qLVAFGRFPHS-RGRLTAADEEVVSRAIDFLDLgglenryLDQLSGGQRQRAYVAMVLS----QETEYVLLDEPLNNLDM 168
Cdd:cd03227 43 -LALGGAQSATrRRSGVKAGCIVAAVSAELIFT-------RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....
gi 2385063227 169 RHS---AQMMRHLRrvaeELERTVVVVLHDINFA 199
Cdd:cd03227 115 RDGqalAEAILEHL----VKGAQVIVITHLPELA 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-224 |
8.85e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLVAFG 99
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFphsrgrltaADEEV------------VSRAIDFLDL----GGlENryldqLSGGQRQRAYVAMVLSQETEYVLLDEPL 163
Cdd:TIGR00957 1385 QY---------SDEEVwwalelahlktfVSALPDKLDHecaeGG-EN-----LSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 164 NNLDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYAdRICAVKDGAVVEFGTPEEIM 224
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-195 |
9.24e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 32 LVGPNGAGKSTLLtmtgRLL-GLDAgviEIAGHdvARtPSKDLAkvVSVLRQENHFVTRLTVRQLVAFG---------RF 101
Cdd:PRK11819 38 VLGLNGAGKSTLL----RIMaGVDK---EFEGE--AR-PAPGIK--VGYLPQEPQLDPEKTVRENVEEGvaevkaaldRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 102 ---------PHSRGRLTAADEEVVSRAIDFLDLGGLENRyLDQ----------------LSGGQRQRayVAM--VLSQET 154
Cdd:PRK11819 106 neiyaayaePDADFDALAAEQGELQEIIDAADAWDLDSQ-LEIamdalrcppwdakvtkLSGGERRR--VALcrLLLEKP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2385063227 155 EYVLLDEPLNNLDMRHSAQMMRHLRRvaeeLERTVVVVLHD 195
Cdd:PRK11819 183 DMLLLDEPTNHLDAESVAWLEQFLHD----YPGTVVAVTHD 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-213 |
1.15e-08 |
|
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: 53.98 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAgHDVARTpskDLAK-----VVSVLRQENHFVT------ 88
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWV---DLAQaspreILALRRRTIGYVSqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 89 -RLTVRQLVAfgrfpHSRGRLTAADEEVVSRAIDFLDLGGLENRyLDQL-----SGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:COG4778 106 pRVSALDVVA-----EPLLERGVDREEARARARELLARLNLPER-LWDLppatfSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 163 LNNLDmrhsAQMMRHLRRVAEELER---TVVVVLHDINFAGHYADRICAVKDGA 213
Cdd:COG4778 180 TASLD----AANRAVVVELIEEAKArgtAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-221 |
1.58e-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: 53.30 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLtMTgrllgldagvieIAGHdvartPSkdlAKVVS-VLRQENHFVTRLTvrqlvaf 98
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLA-KT------------IMGH-----PK---YEVTEgEILFKGEDITDLP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 grfPHSRGRL--------TAADEEVvsRAIDFLdlgglenRYLDQ-LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLD-- 167
Cdd:cd03217 71 ---PEERARLgiflafqyPPEIPGV--KNADFL-------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDid 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 168 -MRHSAQMMRHLRrvaeELERTVVVVLHDINFAGHY-ADRICAVKDGAVVEFGTPE 221
Cdd:cd03217 139 aLRLVAEVINKLR----EEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-217 |
1.61e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAghdvartpsKDLakVVSVLRQENHFVTRLTVRQLVAFG- 99
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE---------QDL--IVARLQQDPPRNVEGTVYDFVAEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 --------RFpHSRGRLTAAD--EEVVSR------AIDFLDLGGLENRY--------------LDQLSGGQRQRAYVAMV 149
Cdd:PRK11147 92 eeqaeylkRY-HDISHLVETDpsEKNLNElaklqeQLDHHNLWQLENRInevlaqlgldpdaaLSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 150 LSQETEYVLLDEPLNNLDMrhsaQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY 234
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
26-210 |
1.87e-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: 52.99 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 26 RGGVTALVGPNGAGKSTLLtmtgrllglDAGVIEIAGHdvARTPSKDLAKVVSVLR-QENHFVTRLTVRqlVAFGRFPHS 104
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTII---------EALKYALTGE--LPPNSKGGAHDPKLIReGEVRAQVKLAFE--NANGKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 105 RGRLTAADEEVVSRAIDFLDLggLEnRYLDQLSGGQRQ------RAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHL 178
Cdd:cd03240 88 TRSLAILENVIFCHQGESNWP--LL-DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEI 164
|
170 180 190
....*....|....*....|....*....|...
gi 2385063227 179 -RRVAEELERTVVVVLHDINFAGhYADRICAVK 210
Cdd:cd03240 165 iEERKSQKNFQLIVITHDEELVD-AADHIYRVE 196
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-217 |
1.97e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 32 LVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGH-DVA----RTPSKDLAKVVSVLRQENHFvtrltvRQLVAFGRFPHSR- 105
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAwvnqETPALPQPALEYVIDGDREY------RQLEAQLHDANERn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 106 ---------GRLTAADEEVV-SRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHS 171
Cdd:PRK10636 106 dghaiatihGKLDAIDAWTIrSRAASLLHGLGFSNEQLERpvsdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2385063227 172 AQMMRHLRrvaeELERTVVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:PRK10636 186 IWLEKWLK----SYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
34-206 |
2.94e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.79 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 34 GPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQLVAfgrFPHsRGRLTAADE 113
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGD-TVYDNLI---FPW-QIRNQQPDP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 114 EvvsRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTV 189
Cdd:PRK10247 115 A---IFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAV 191
|
170
....*....|....*..
gi 2385063227 190 VVVLHDINFAGHyADRI 206
Cdd:PRK10247 192 LWVTHDKDEINH-ADKV 207
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-196 |
3.64e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 52.32 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKeYSGEVAIgpvDLRiprGGVTALVGPNGAGKSTLLT-----MTGRLLGLDAGVIEIAgHDVARTPSKDL--- 73
Cdd:COG0419 5 LRLENFRS-YRDTETI---DFD---DGLNLIVGPNGAGKSTILEairyaLYGKARSRSKLRSDLI-NVGSEEASVELefe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 74 --AKVVSVLRQENHFVTRLT---------VRQLVAFGRFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYL--------- 133
Cdd:COG0419 77 hgGKRYRIERRQGEFAEFLEakpserkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILaqlsgldpi 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 134 DQLSGGQRQRAYVAMVLSqeteyVLLDepLNNLDMRHSAQMMRHLRRVAeelertvvVVLHDI 196
Cdd:COG0419 157 ETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-224 |
3.84e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.87 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHfvTRLTVRQL 95
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPS--TSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 96 VA-FGRFP-HSRGRLTAADEEvvSRAIDFLDLGGL----ENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMR 169
Cdd:PRK15112 106 ISqILDFPlRLNTDLEPEQRE--KQIIETLRQVGLlpdhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 170 HSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK15112 184 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-218 |
6.80e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 5 SGVRKEYSGEV-AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLakvvSVLRQE 83
Cdd:PRK10261 327 SGLLNRVTREVhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKL----QALRRD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 84 NHFV-----TRLTVRQLVAFGRFPHSRGRLTAADEEVVSRAIDFLDLGGLEN----RYLDQLSGGQRQRAYVAMVLSQET 154
Cdd:PRK10261 403 IQFIfqdpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2385063227 155 EYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEFG 218
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-225 |
1.09e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 54 DAGVIEIAGHDVARTPSKDLAKVVSVLRQENhFVTRLTVRQLVAFGRfphsrgrlTAADEEVVSRAIDF--LD--LGGLE 129
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYENIKFGK--------EDATREDVKRACKFaaIDefIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 130 NRYL-------DQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINfAGHY 202
Cdd:PTZ00265 1346 NKYDtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKR 1424
|
170 180
....*....|....*....|....*...
gi 2385063227 203 ADRICAV----KDGAVVEF-GTPEEIMT 225
Cdd:PTZ00265 1425 SDKIVVFnnpdRTGSFVQAhGTHEELLS 1452
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-218 |
1.78e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 19 PVDLRIPRGGVTALVGPNGAGKSTLL-TMTGRLLGLDAGV---IEIAGHDVARTPSKDLAKVVSVLRQENHFvTRLTVRQ 94
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHIGVegvITYDGITPEEIKKHYRGDVVYNAETDVHF-PHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 95 LVAFG---RFPHSRGRLTAADEEVVSRAIDFLDLGGLE--------NRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPL 163
Cdd:TIGR00956 158 TLDFAarcKTPQNRPDGVSREEYAKHIADVYMATYGLShtrntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2385063227 164 NNLDMRHSAQMMRHLRRVAEELERTVVVVLHDIN-FAGHYADRICAVKDGAVVEFG 218
Cdd:TIGR00956 238 RGLDSATALEFIRALKTSANILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIYFG 293
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-194 |
2.81e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 27 GGVTALVGPNGAGKSTLL-TMTGRllgLDAGVIEiAGHDVARTPSKD--LAKVVSVLRQENHFVTRLTVR---QLVAFGR 100
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLnVLAER---VTTGVIT-GGDRLVNGRPLDssFQRSIGYVQQQDLHLPTSTVReslRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 101 FPHSRGRltAADEEVVSRAIDFLDLggleNRYLDQLSG--------GQRQRAYVAMVLSQETEYVL-LDEPLNNLDMRHS 171
Cdd:TIGR00956 865 QPKSVSK--SEKMEYVEEVIKLLEM----ESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180
....*....|....*....|...
gi 2385063227 172 AQMMRHLRRVAEElERTVVVVLH 194
Cdd:TIGR00956 939 WSICKLMRKLADH-GQAILCTIH 960
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
85-237 |
3.24e-07 |
|
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: 50.78 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 85 HFVTRLTVRQLVAFGRFPHSRGRLTAADEEVVSRAID---FLDLGGLE----NRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:TIGR00630 431 ADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRErlgFLIDVGLDylslSRAAGTLSGGEAQRIRLATQIGSGLTGV 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 158 L--LDEPLNNLDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHyADRICAVKDGA------VVEFGTPEEIM----- 224
Cdd:TIGR00630 511 LyvLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADYVIDIGPGAgehggeVVASGTPEEILanpds 588
|
170
....*....|....
gi 2385063227 225 -TGEVLTRVFETPV 237
Cdd:TIGR00630 589 lTGQYLSGRKKIEV 602
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-169 |
3.65e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.18 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 10 EYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVartpSKDLA---KVVSVLRQENHF 86
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCtyqKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRLTVRQLVAFGrFPHSRGRLTaadeevVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:PRK13540 86 NPYLTLRENCLYD-IHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
...
gi 2385063227 167 DMR 169
Cdd:PRK13540 159 DEL 161
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-194 |
3.75e-07 |
|
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: 48.69 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHD----VARTPskdlakvvsvlrqenhFV 87
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEdllfLPQRP----------------YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 88 TRLTVRQLVAFgrfPhsrgrltaadeevvsraidfldlgglenrYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLD 167
Cdd:cd03223 76 PLGTLREQLIY---P-----------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*..
gi 2385063227 168 MRHSAQMMRHLRrvaeELERTVVVVLH 194
Cdd:cd03223 124 EESEDRLYQLLK----ELGITVISVGH 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-66 |
4.99e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 4.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 2 ITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTlltmtgrLLGLDAGV-------IEIAGHDVA 66
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS-------LLSLIAGArkiqqgrVEVLGGDMA 66
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-236 |
1.51e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.86 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEV--AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSkDLAKVVS 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 79 VLRQENHFVTRLTVRQ-LVAFGRFphsRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYV 157
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREhLYLYARL---RGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 158 LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMT----GEVLTRVF 233
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSkfgdGYIVTMKI 2171
|
...
gi 2385063227 234 ETP 236
Cdd:TIGR01257 2172 KSP 2174
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-217 |
1.85e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 31 ALVGPNGAGKSTLLTmtgrllgLDAGVIEIAGHDVARTPskdlaKV-VSVLRQENHFVTRLTVRQLVAFGR-FPhsrgrl 108
Cdd:PLN03073 539 AMVGPNGIGKSTILK-------LISGELQPSSGTVFRSA-----KVrMAVFSQHHVDGLDLSSNPLLYMMRcFP------ 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 109 TAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRvaeeLERT 188
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL----FQGG 676
|
170 180
....*....|....*....|....*....
gi 2385063227 189 VVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-217 |
2.13e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 7 VRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLLgldAGVIEIAGHDVArtpskdLAKVVSVLRQENHf 86
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLI----KLL---AGELAPVSGEIG------LAKGIKLGYFAQH- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 vtrltvrQLvAFGRFPHS----RGRLtaADEEVVSRAIDFLDLGGLENRYL----DQLSGGQRQRAYVAMVLSQETEYVL 158
Cdd:PRK10636 384 -------QL-EFLRADESplqhLARL--APQELEQKLRDYLGGFGFQGDKVteetRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 159 LDEPLNNLDMrhsaQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAVKDGAVVEF 217
Cdd:PRK10636 454 LDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPF 508
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-223 |
2.24e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRI-PRGGVtALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRlTVRQLV-A 97
Cdd:PTZ00243 1329 VSFRIaPREKV-GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVdP 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 98 FgrfphsrgrLTAADEEvVSRAIDFLDL--------GGLENRYLD---QLSGGQRQRAYVA-MVLSQETEYVLLDEPLNN 165
Cdd:PTZ00243 1407 F---------LEASSAE-VWAALELVGLrervasesEGIDSRVLEggsNYSVGQRQLMCMArALLKKGSGFILMDEATAN 1476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 166 LDMRHSAQMMRHLRRVAEELerTVVVVLHDINFAGHYaDRICAVKDGAVVEFGTPEEI 223
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-224 |
2.91e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLtmtGRLLGldagVIEIAGHDVarTPSKDLAKVvsvlrQENHFVTRLTVRQLVAFg 99
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLL---QSLLS----QFEISEGRV--WAERSIAYV-----PQQAWIMNATVRGNILF- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 rfphsrgrltaADEEVVSRAIDFL-------DL----GGLENRYLDQ---LSGGQRQRAYVAMVLSQETEYVLLDEPLNN 165
Cdd:PTZ00243 744 -----------FDEEDAARLADAVrvsqleaDLaqlgGGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 166 LDMrHSAQmmrhlrRVAEEL------ERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIM 224
Cdd:PTZ00243 813 LDA-HVGE------RVVEECflgalaGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFM 869
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-227 |
2.93e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrLLGLD---AGVIEIAGHDVA-RTPSKDLAK---VVSVLRQENHFVTRLTV 92
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNC---LFGVDkraGGEIRLNGKDISpRSPLDAVKKgmaYITESRRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQLVAF------GRFPHSRGRLTAADEEVVsrAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEP 162
Cdd:PRK09700 359 AQNMAIsrslkdGGYKGAMGLFHEVDEQRT--AENQRELLALKCHSVNQniteLSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 163 LNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
20-221 |
4.63e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 46.49 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLL-TMTGR-LLGLDAGVIEIAGHDVARTPSKDLAKV--------------VSVLRqe 83
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSkTIAGHpSYEVTSGTILFKGQDLLELEPDERARAglflafqypeeipgVSNLE-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 84 nhFV-TRLTVRqlvafgRFPHSRGRLTAAD-EEVVSRAIDFLDL-GGLENRYLDQ-LSGGQRQRAYVAMVLSQETEYVLL 159
Cdd:TIGR01978 97 --FLrSALNAR------RSARGEEPLDLLDfEKLLKEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 160 DEPLNNLDmrhsaqmMRHLRRVAEELER------TVVVVLHDINFAGHYA-DRICAVKDGAVVEFGTPE 221
Cdd:TIGR01978 169 DEIDSGLD-------IDALKIVAEGINRlrepdrSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDVE 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
130-225 |
6.28e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.44 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 130 NRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRVAEELERTVVVVLHDINFAGHYADRICAV 209
Cdd:COG4170 153 NSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
90
....*....|....*.
gi 2385063227 210 KDGAVVEFGTPEEIMT 225
Cdd:COG4170 233 YCGQTVESGPTEQILK 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-162 |
8.75e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 15 VAIGPVDLRIPRGGVTALVGPNGAGKSTllTM---TGrLLGLDAGVIEIAGHDVArtpSKDLA--KVVSVLRQENHFVTR 89
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKST--TMkmlTG-LLPASEGEAWLFGQPVD---AGDIAtrRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2385063227 90 LTVRQ-LVAFGRFPH-SRGRLTAADEEVVSRaidFlDLGGLENRYLDQLSGGQRQR---AyVAMVlsQETEYVLLDEP 162
Cdd:NF033858 354 LTVRQnLELHARLFHlPAAEIAARVAEMLER---F-DLADVADALPDSLPLGIRQRlslA-VAVI--HKPELLILDEP 424
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-206 |
8.97e-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: 45.01 E-value: 8.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMTGrllgldAGVIEIAGHDVARTPSKDLAKVVSVLRQenhfvtrltvrqLVAFG 99
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNEGL------YASGKARLISFLPKFSRNKLIFIDQLQF------------LIDVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 rfphsrgrltaadeevvsraIDFLDLGglenRYLDQLSGGQRQRAYVAMVLSQETEYVL--LDEPLNNLDMRHSAQMMRH 177
Cdd:cd03238 76 --------------------LGYLTLG----QKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQLLEV 131
|
170 180
....*....|....*....|....*....
gi 2385063227 178 LRRVAeELERTVVVVLHDINFAgHYADRI 206
Cdd:cd03238 132 IKGLI-DLGNTVILIEHNLDVL-SSADWI 158
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-224 |
9.24e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIPRGGVTALVGPNGAGKSTL-LTMTGRLLgLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHfvTRLTVRQLVAFG 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALaRALAGELP-LLSGERQSQFSHITRLSFEQLQKLVSDEWQRNN--TDMLSPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 100 RFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLR 179
Cdd:PRK10938 100 RTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2385063227 180 RVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK10938 180 SLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-216 |
1.10e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 6 GVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL----------TMTGRLLgLDAGVIEIAG-HDvartpSKDLA 74
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMkvlsgvyphgSYEGEIL-FDGEVCRFKDiRD-----SEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 75 KVvsVLRQENHFVTRLTVRQLVAFGRFPHSRGRLtaaD-EEVVSRAIDFLDLGGLE---NRYLDQLSGGQRQRAYVAMVL 150
Cdd:NF040905 80 IV--IIHQELALIPYLSIAENIFLGNERAKRGVI---DwNETNRRARELLAKVGLDespDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2385063227 151 SQETEYVLLDEP---LNNLDMRHSAQMMRHLRrvAEELerTVVVVLHDINFAGHYADRICAVKDGAVVE 216
Cdd:NF040905 155 SKDVKLLILDEPtaaLNEEDSAALLDLLLELK--AQGI--TSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-214 |
1.39e-05 |
|
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: 45.59 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLT-MTGRLLGLDAGVIEIAGHDVA-RTPSKDLAKVVSVL---RQENHFVTRLTVRQ 94
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDiRNPAQAIRAGIAMVpedRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 95 ---LVAFGRFPhSRGRLTAADEE-VVSRAID---------FLDLGGLenryldqlSGGQRQRAYVAMVLSQETEYVLLDE 161
Cdd:TIGR02633 359 nitLSVLKSFC-FKMRIDAAAELqIIGSAIQrlkvktaspFLPIGRL--------SGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 162 PLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAV 214
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-230 |
1.53e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 130 NRYLDQLSGGQRQRAYVAMVLSQETEYV--LLDEPLNNLDMRHSAQMMRHLRRVAEElERTVVVVLHD---INFaghyAD 204
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDeqmISL----AD 545
|
90 100 110
....*....|....*....|....*....|...
gi 2385063227 205 RICAVKDGA------VVEFGTPEE-IMTGEVLT 230
Cdd:PRK00635 546 RIIDIGPGAgifggeVLFNGSPREfLAKSDSLT 578
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-214 |
1.70e-05 |
|
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: 43.96 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLL-TMTGrLLGLDAGVIEIAGHDVARTPSKDLAK----VVSVLRQENHF 86
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAeALFG-LRPPASGEITLDGKPVTRRSPRDAIRagiaYVPEDRKREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRLTVRQLVAFGRFphsrgrltaadeevvsraidfldlgglenryldqLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:cd03215 90 VLDLSVAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2385063227 167 DMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAV 214
Cdd:cd03215 136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-198 |
1.81e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 24 IPRGGVTALVGPNGAGKSTLLT-MTGRLLGlDAGVI------EIAGHDVART---PSKDLAKVVSVLRQEnhfvtrLTVR 93
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKlMLGQLQA-DSGRIhcgtklEVAYFDQHRAeldPEKTVMDNLAEGKQE------VMVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 94 qlvafGRFPHSRGRLTaadeevvsraiDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMrhsaQ 173
Cdd:PRK11147 415 -----GRPRHVLGYLQ-----------DFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----E 474
|
170 180
....*....|....*....|....*
gi 2385063227 174 MMRHLRRVAEELERTVVVVLHDINF 198
Cdd:PRK11147 475 TLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-98 |
2.73e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.13 E-value: 2.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2385063227 26 RGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHFVTRLTVRQLVAF 98
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-167 |
2.77e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.61 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 28 GVTALVGpngAGKSTLLTMTGRLLGLDAGVIEIAGHDV-ARTPSKDLAK---VVSVLRQENHFVTRLTVRQ---LVAFGR 100
Cdd:PRK10762 282 GVSGLMG---AGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANgivYISEDRKRDGLVLGMSVKEnmsLTALRY 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 101 FPHSRGRLTAADE-EVVSraiDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLNNLD 167
Cdd:PRK10762 359 FSRAGGSLKHADEqQAVS---DFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-221 |
3.31e-05 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.90 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTL-LTMTGR----------------LLGLD------AGV-------IEIAGhdvartp 69
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLaKVLMGHpkyevtsgsilldgedILELSpderarAGIflafqypVEIPG------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 70 skdlakvVSV---LRQ--ENHFVTRLTVRQLVAFGRfphsrgrlTAADEevVSRAIDFLDlgglenRYLDQ-LSGGQRQR 143
Cdd:COG0396 92 -------VSVsnfLRTalNARRGEELSAREFLKLLK--------EKMKE--LGLDEDFLD------RYVNEgFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 144 AYVAMVLSQETEYVLLDEPLNNLDMrhSAqmmrhLRRVAEELERtvvvvLHDINFAG----HY--------ADRICAVKD 211
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDI--DA-----LRIVAEGVNK-----LRSPDRGIliitHYqrildyikPDFVHVLVD 216
|
250
....*....|
gi 2385063227 212 GAVVEFGTPE 221
Cdd:COG0396 217 GRIVKSGGKE 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-227 |
4.45e-05 |
|
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: 43.74 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 7 VRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHDVARTPSKDLAKVVSVLRQENHF 86
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRlTVRqlvaFGRFPHSR---GRLTAADE--------EVVSRAIDFLDLGGLENryldqLSGGQRQRAYVAMVLSQETE 155
Cdd:cd03288 107 FSG-SIR----FNLDPECKctdDRLWEALEiaqlknmvKSLPGGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2385063227 156 YVLLDEPLNNLDMRhSAQMMRHLRRVAEElERTVVVVLHDINFAGHyADRICAVKDGAVVEFGTPEEIMTGE 227
Cdd:cd03288 177 ILIMDEATASIDMA-TENILQKVVMTAFA-DRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-224 |
5.15e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 16 AIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDAGVIEIAGHdvartpskdlakvVSVLRQENHFVTRLTVRQL 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 96 VAFGRF--PHSRGRLTAADEEVvsraIDFLDLGGLENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQ 173
Cdd:PRK13546 106 IEFKMLcmGFKRKEIKAMTPKI----IEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 174 MMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVVEFGTPEEIM 224
Cdd:PRK13546 182 CLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-44 |
5.33e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 40.28 E-value: 5.33e-05
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-224 |
8.13e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 19 PVDLRIPRG---GVTALVGpngAGKSTLL-TMTGrLLGLDAGVIEIAGHDVA-RTPSKDLAKVVSVL---RQENHFVTRL 90
Cdd:COG1129 270 DVSFSVRAGeilGIAGLVG---AGRTELArALFG-ADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 91 TVRQ---LVAFGRFpHSRGRLTAADE-EVVSRAIDFLDL--GGLENRyLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLN 164
Cdd:COG1129 346 SIREnitLASLDRL-SRGGLLDRRRErALAEEYIKRLRIktPSPEQP-VGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 165 NLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVV-EFG----TPEEIM 224
Cdd:COG1129 424 GIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVgELDreeaTEEAIM 487
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-94 |
3.24e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.56 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKeYSGEVaigpVDLRiprGGVTALVGPNGAGKSTLL-----TMTGRLLGL-DAGVIEIAGHDVARTPSKDLAK 75
Cdd:pfam13476 1 LTIENFRS-FRDQT----IDFS---KGLTLITGPNGSGKTTILdaiklALYGKTSRLkRKSGGGFVKGDIRIGLEGKGKA 72
|
90
....*....|....*....
gi 2385063227 76 VVSVLRQENHFVTRLTVRQ 94
Cdd:pfam13476 73 YVEITFENNDGRYTYAIER 91
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
87-237 |
3.57e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 87 VTRLTVRQLVAFgrFPH---SRGRLTAADE---EVVSRaIDFLDLGGLE----NRYLDQLSGGQRQRAYVAmvlSQ---- 152
Cdd:COG0178 430 LTALSIDEALEF--FENlelTEREAEIAERilkEIRSR-LGFLVDVGLDyltlDRSAGTLSGGEAQRIRLA---TQigsg 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 153 --ETEYVLlDEPLNNL---DMRHSAQMMRHLRrvaeELERTVVVVLHD---InfagHYADRIC-----A-VKDGAVVEFG 218
Cdd:COG0178 504 lvGVLYVL-DEPSIGLhqrDNDRLIETLKRLR----DLGNTVIVVEHDedtI----RAADYIIdigpgAgEHGGEVVAQG 574
|
170 180
....*....|....*....|....*
gi 2385063227 219 TPEEIM------TGEVLTRVFETPV 237
Cdd:COG0178 575 TPEEILknpdslTGQYLSGRKRIPV 599
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-223 |
7.80e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEysgevAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMT-------------------GRLLGLDA--GVIE 59
Cdd:TIGR00630 613 FLTLKGAREN-----NLKNITVSIPLGLFTCITGVSGSGKSTLINDTlypalanrlngaktvpgryTSIEGLEHldKVIH 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 60 IAGHDVARTPSKDLAKVVSV-----------------------------------------LRQENHFVTRLTVRQLVAF 98
Cdd:TIGR00630 688 IDQSPIGRTPRSNPATYTGVfdeirelfaetpeakvrgytpgrfsfnvkggrceacqgdgvIKIEMHFLPDVYVPCEVCK 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 99 G-RFP------HSRGRlTAAD------EEV---------VSRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQ 152
Cdd:TIGR00630 768 GkRYNretlevKYKGK-NIADvldmtvEEAyeffeavpsISRKLQTLCDVGLGYIRLGQpattLSGGEAQRIKLAKELSK 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 153 ----ETEYVlLDEPLNNLDMRHSAQMMRHLRRVAeELERTVVVVLHDINFAgHYADRIC------AVKDGAVVEFGTPEE 222
Cdd:TIGR00630 847 rstgRTLYI-LDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVIEHNLDVI-KTADYIIdlgpegGDGGGTVVASGTPEE 923
|
.
gi 2385063227 223 I 223
Cdd:TIGR00630 924 V 924
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-185 |
9.29e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 21 DLRIP-RGGVTALVGPNGAGKSTLLTMTGRLLGLDAG-------------------VIE---------IAGHDVARTPSK 71
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeiEIEltfgsllsrLLRLLLKEEDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 72 DLAKVVSVLRQE-----NHFVTRLTvRQLVAFGRFPHSRGRLTAADEEVVSRAIDfLDLGGLENRYLDQLSGGQRQRAYV 146
Cdd:COG3593 96 ELEEALEELNEElkealKALNELLS-EYLKELLDGLDLELELSLDELEDLLKSLS-LRIEDGKELPLDRLGSGFQRLILL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2385063227 147 AMV--LSQETEY-----VLLDEPLNNLdmrhSAQMMRHLRRVAEEL 185
Cdd:COG3593 174 ALLsaLAELKRApanpiLLIEEPEAHL----HPQAQRRLLKLLKEL 215
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-44 |
1.21e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 1.21e-03
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-167 |
1.22e-03 |
|
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: 39.45 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 13 GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDaGVIEIAGHDVARTPSKDLAKVVSVLRQENhFVTRLTV 92
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKV-FIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 93 RQ-LVAFGRfpHSRGRLTAADEEVVSRAI-----DFLDLGGLENRYLdqLSGGQRQRAYVAMVLSQETEYVLLDEPLNNL 166
Cdd:cd03289 94 RKnLDPYGK--WSDEEIWKVAEEVGLKSVieqfpGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
.
gi 2385063227 167 D 167
Cdd:cd03289 170 D 170
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
12-147 |
2.14e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 39.20 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 12 SGEVAIGPVDlRIPRGGVTALVGPNGAGKSTLLTmtgrllgldagviEIAGHDVARTPSKDLAkvvsvlrqenhFVTRLT 91
Cdd:PRK12727 336 SKRLPVAPVD-PLERGGVIALVGPTGAGKTTTIA-------------KLAQRFAAQHAPRDVA-----------LVTTDT 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 92 VR-----QLVAFGRfphsrgRLTAADEEVVSrAIDFLDLGGLENRY----LDQLSGGQRQRAYVA 147
Cdd:PRK12727 391 QRvggreQLHSYGR------QLGIAVHEADS-AESLLDLLERLRDYklvlIDTAGMGQRDRALAA 448
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-168 |
2.29e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 38.23 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 1 MITLSGVRKEYSGEVAIGPVDLRIPRGGVTALVGPNGAGKSTL-LTMTGRL-LGLDAGVIEIAGHDVARTPSKDLAK--- 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSPEDRAGegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 76 ------VVSVLRQENHFVTRLTV------RQLVAFGRFPHsrgrltaadEEVVSRAIDFLDL-GGLENRYLDQ-LSGGQR 141
Cdd:PRK09580 81 fmafqyPVEIPGVSNQFFLQTALnavrsyRGQEPLDRFDF---------QDLMEEKIALLKMpEDLLTRSVNVgFSGGEK 151
|
170 180
....*....|....*....|....*..
gi 2385063227 142 QRAYVAMVLSQETEYVLLDEPLNNLDM 168
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDI 178
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
9-44 |
2.61e-03 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 38.05 E-value: 2.61e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2385063227 9 KEYSGEVAIGPVDLRIprggvTALVGPNGAGKSTLL 44
Cdd:cd03274 12 KSYAGEQVIGPFHKSF-----SAIVGPNGSGKSNVI 42
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-219 |
3.40e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.62 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTL----------------LTMTGR-LLGL--DAGVIEIAGhdvartpskdLAKVVSVL 80
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqFLGQmdKPDVDSIEG----------LSPAIAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 81 RQENHFVTRLTVRQLVAFgrfpHSRGRLTAADEEVVSRaIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEY 156
Cdd:cd03270 84 QKTTSRNPRSTVGTVTEI----YDYLRLLFARVGIRER-LGFLVDVGLGYLTLSRsaptLSGGEAQRIRLATQIGSGLTG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2385063227 157 VL--LDEPLNNLDMRHSAQMMRHLRRVaEELERTVVVVLHDINFAGHyADRICAVKDGAVVEFGT 219
Cdd:cd03270 159 VLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDIGPGAGVHGGE 221
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-44 |
3.81e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 3.81e-03
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-215 |
3.84e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 37.97 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 19 PVDLRIPRGGVTALVGPNGAGKSTLLtmtgRLL-GLD---AGVIEIAGHDVA-RTPsKDLAKVVSVL----RQENHFVTR 89
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELM----KLLyGATrrtAGQVYLDGKPIDiRSP-RDAIRAGIMLcpedRKAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 90 LTVRQLVAFG-RFPHSRGRLTAADEEVVSRAIDFLDLGGLENRYLDQ----LSGGQRQRAYVAMVLSQETEYVLLDEPLN 164
Cdd:PRK11288 346 HSVADNINISaRRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 165 NLDMRHSAQMMRHLRRVAEElERTVVVVLHDINFAGHYADRICAVKDGAVV 215
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
20-44 |
3.95e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 3.95e-03
10 20
....*....|....*....|....*
gi 2385063227 20 VDLRIPRGgVTALVGPNGAGKSTLL 44
Cdd:COG3950 19 IDFDNPPR-LTVLVGENGSGKTTLL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-198 |
5.38e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 15 VAIGPVDLrIPRGGVT-------ALVGPNGAGKSTLLtmtgRLLGLDA--GVI----------EIAGHDVARTP---SKD 72
Cdd:PLN03073 185 ISVGGRDL-IVDASVTlafgrhyGLVGRNGTGKTTFL----RYMAMHAidGIPkncqilhveqEVVGDDTTALQcvlNTD 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 73 LAKVvSVLRQENHFVTRltVRQLVAFGRFPHSRGRLTAADE--------EVVSRAIDFLD-----------LGGL----- 128
Cdd:PLN03073 260 IERT-QLLEEEAQLVAQ--QRELEFETETGKGKGANKDGVDkdavsqrlEEIYKRLELIDaytaearaasiLAGLsftpe 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2385063227 129 -ENRYLDQLSGGQRQRAYVAMVLSQETEYVLLDEPLNNLDMRHSAQMMRHLRRvaeeLERTVVVVLHDINF 198
Cdd:PLN03073 337 mQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK----WPKTFIVVSHAREF 403
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
18-41 |
7.35e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 36.67 E-value: 7.35e-03
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-167 |
7.65e-03 |
|
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: 37.58 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 2 ITLSGVRKEYS--GEVAIGPVDLRIPRGGVTALVGPNGAGKSTLLTMTGRLLGLDaGVIEIAGHDVARTPSKDLAKVVSV 79
Cdd:TIGR01271 1218 MDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2385063227 80 LRQENHFVTRLTVRQLVAFGRFphSRGRLTAADEEVVSRAI-----DFLDLGGLENRYLdqLSGGQRQRAYVAMVLSQET 154
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQW--SDEEIWKVAEEVGLKSVieqfpDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKA 1372
|
170
....*....|...
gi 2385063227 155 EYVLLDEPLNNLD 167
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-63 |
8.81e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 36.54 E-value: 8.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2385063227 20 VDLRIPRGGVTALVGPNGAGKSTLLTMtgrllgldagvieIAGH 63
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKV-------------IAGH 56
|
|
| |
