|
Name |
Accession |
Description |
Interval |
E-value |
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-276 |
5.59e-124 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 353.65 E-value: 5.59e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLDFPFLVKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQLEYSGfhRDE 177
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRapHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPV--DGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYVY 257
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250 260
....*....|....*....|
gi 1579913621 258 DFPVEIMQHP-KGWPLVVSQ 276
Cdd:COG4559 238 GADLRVLAHPeGGCPQVLPR 257
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-276 |
1.01e-106 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 309.78 E-value: 1.01e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLDFPFLVKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQL-EYSGfhrd 176
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLwEPDG---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 177 EPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYV 256
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
250 260
....*....|....*....|.
gi 1579913621 257 YDFPVEIMQHPK-GWPLVVSQ 276
Cdd:PRK13548 238 YGADVLVQPHPEtGAPLVLPR 258
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-274 |
9.07e-94 |
|
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: 276.92 E-value: 9.07e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLDFPFLVKEVVQM-------ALRSVSKSNIETVTlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysg 172
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgryphlgLFGRPSAEDREAVE-EALERTGLEHLADRPVDELSGGERQRVLIARALAQ----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRL 252
Cdd:COG1120 155 ----EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPEL 230
|
250 260
....*....|....*....|...
gi 1579913621 253 LSYVYDFPVEIMQHP-KGWPLVV 274
Cdd:COG1120 231 LEEVYGVEARVIEDPvTGRPLVL 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-240 |
4.15e-70 |
|
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: 213.84 E-value: 4.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 22 QATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQ 101
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 siyldfpflvkevvqmalrsvsksnietvtlqALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYL 181
Cdd:cd03214 81 --------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ---------EPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-274 |
2.52e-58 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 187.34 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSG--------YDGKVMLNFKNIKDFSGLQ 91
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVRAVMPQSIYLDFPFLVKEVVQMA----LRSVSKSNIET--VTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVL 165
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGryphARRAGALTHRDgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 166 AQLEYSGFHRDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIE 245
Cdd:PRK13547 161 AQLWPPHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|....*....
gi 1579913621 246 KVYQNRLLSYVYDFPVEIMQHPKGWPLVV 274
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGVPPVI 269
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-266 |
8.34e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 184.91 E-value: 8.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfsglQLSGVRA 97
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 VMPQSIYLD--FPFLVKEVVQM-------ALRSVSKSNIETVtLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQl 168
Cdd:COG1121 79 YVPQRAEVDwdFPITVRDVVLMgrygrrgLFRRPSRADREAV-DEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 169 eysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVqALNKIEKVY 248
Cdd:COG1121 157 --------DPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVL 226
|
250
....*....|....*...
gi 1579913621 249 QNRLLSYVYDFPVEIMQH 266
Cdd:COG1121 227 TPENLSRAYGGPVALLAH 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-238 |
4.26e-54 |
|
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: 174.26 E-value: 4.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 22 QATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlsgvrAVMPQ 101
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI-----GYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 SIYLD--FPFLVKEVVQMAL-------RSVSKSNIETVtLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysg 172
Cdd:cd03235 76 RRSIDrdFPISVRDVVLMGLyghkglfRRLSKADKAKV-DEALERVGLSELADRQIGELSGGQQQRVLLARALVQ----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03235 150 ----DPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-274 |
4.74e-48 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 160.18 E-value: 4.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLDFPFLVKEVVQMAlRS--------VSKSNIETVTlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleys 171
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYG-RSpwlslwgrLSAEDNARVN-QAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 172 gfhrDEPRYLfLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNR 251
Cdd:PRK11231 156 ----DTPVVL-LDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
250 260
....*....|....*....|....
gi 1579913621 252 LLSYVYDFPVEIMQHP-KGWPLVV 274
Cdd:PRK11231 230 LLRTVFDVEAEIHPEPvSGTPMCV 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-247 |
1.51e-45 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 157.70 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLDFPFLVKEVVQMAlRSVSKSNI-------ETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysg 172
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMG-RTPHRSRFdtwtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ----- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKV 247
Cdd:PRK09536 157 ----ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-274 |
1.39e-44 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 151.00 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNC----LTGDysgyDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMisrlLPPD----SGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYLDFPFLVKEVV--------QMALRSVSKSNIEtvtlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQ 167
Cdd:COG4604 77 LAILRQENHINSRLTVRELVafgrfpysKGRLTAEDREIID----EAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 168 leysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKV 247
Cdd:COG4604 153 ---------DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
250 260
....*....|....*....|....*..
gi 1579913621 248 YQNRLLSYVYDFPVEIMQHPkGWPLVV 274
Cdd:COG4604 224 ITPEVLSDIYDTDIEVEEID-GKRICV 249
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-266 |
1.41e-43 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 148.45 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAfdnkPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGyDGKVMLNFKNIKDFSGLQLSGVRAVMP 100
Cdd:COG4138 1 LQLNDVAVA----GRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSIYLDFPFLVKEVVQMAL-RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQLeysgfHRD--- 176
Cdd:COG4138 76 QQQSPPFAMPVFQYLALHQpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQV-----WPTinp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 177 EPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYV 256
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEV 229
|
250
....*....|
gi 1579913621 257 YDFPVEIMQH 266
Cdd:COG4138 230 FGVKFRRLEV 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-237 |
8.81e-42 |
|
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: 142.61 E-value: 8.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQs 102
Cdd:cd03225 4 NLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 103 iyldFPF--LVKEVVQ------MALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfh 174
Cdd:cd03225 83 ----NPDdqFFGPTVEeevafgLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA-------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 175 rDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:cd03225 151 -MDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-251 |
2.52e-41 |
|
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: 142.09 E-value: 2.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQsiyldFPF--LVKEVVQ----MALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleys 171
Cdd:COG1122 81 FQ-----NPDdqLFAPTVEedvaFGPENlgLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 172 gfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNR 251
Cdd:COG1122 152 -----EPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-238 |
2.00e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.18 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQL-SGVRAVM 99
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSI--------YLDFPFLVKEVvqmalrsvsKSNIETVtLQALERFDV-MHLAERNFLTLSGGEKQRVHLSRVLAQley 170
Cdd:COG4619 81 QEPAlwggtvrdNLPFPFQLRER---------KFDRERA-LELLERLGLpPDILDKPVERLSGGERQRLALIRALLL--- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 171 sgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG4619 148 ------QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-252 |
7.90e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.27 E-value: 7.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVRA--- 97
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVRRrig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 VMPQSIYLDfPFL-VKEVVQM--ALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfH 174
Cdd:COG1131 77 YVPQEPALY-PDLtVRENLRFfaRLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL-------H 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 175 RdePRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRigvvAVL---HDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNR 251
Cdd:COG1131 149 D--PELLILDEPTSGLDPEARRELWELLRELAAEGK----TVLlstHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
.
gi 1579913621 252 L 252
Cdd:COG1131 223 L 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-254 |
3.75e-39 |
|
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: 136.91 E-value: 3.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVR--- 96
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREARrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 AVMPQSIYLdFPFL-VKEVVQM--ALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgf 173
Cdd:COG4555 77 GVLPDERGL-YDRLtVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 174 hrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLL 253
Cdd:COG4555 150 ---DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
.
gi 1579913621 254 S 254
Cdd:COG4555 226 E 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-238 |
2.49e-38 |
|
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: 133.77 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDN----KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVR 96
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 A----VMPQSIYLdFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQle 169
Cdd:cd03255 81 RrhigFVFQSFNL-LPDLtALENVELPLLlaGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLaAQYGDRALLLKQGKV 238
Cdd:cd03255 158 -------DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-266 |
1.78e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 132.52 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY---SGYDGKVMlnfknikdfsGLQLSG 94
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptYGNDVRLF----------GERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 --VRAVMPQ------SIYLDFP--FLVKEVVQMAL-------RSVSKSNIETVtLQALERFDVMHLAERNFLTLSGGEKQ 157
Cdd:COG1119 71 edVWELRKRiglvspALQLRFPrdETVLDVVLSGFfdsiglyREPTDEQRERA-RELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 158 RVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:COG1119 150 RVLIARALVK---------DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
250 260
....*....|....*....|....*....
gi 1579913621 238 VQALNKIEKVYQNRLLSYVYDFPVEIMQH 266
Cdd:COG1119 221 VVAAGPKEEVLTSENLSEAFGLPVEVERR 249
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-250 |
7.87e-37 |
|
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: 136.57 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG---DYSGYDGKVMLNFKNIKDFSGLQL 92
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SGVRAVMPQSIYLDF-PFLVKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqle 169
Cdd:COG1123 82 GRRIGMVFQDPMTQLnPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 170 ysgfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:COG1123 159 ------LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 1579913621 250 N 250
Cdd:COG1123 233 A 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-240 |
3.13e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.62 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLtgdySGYD----GKVMLNFKNIKDFSG 89
Cdd:COG1136 2 SPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL----GGLDrptsGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 LQLSGVRA----VMPQSIYLdFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLS 162
Cdd:COG1136 78 RELARLRRrhigFVFQFFNL-LPELtALENVALPLLlaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 163 RVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAqYGDRALLLKQGKVQA 240
Cdd:COG1136 157 RALVN---------RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-237 |
5.76e-36 |
|
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: 125.82 E-value: 5.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 22 QATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQ 101
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 siyldfpflvkevvqmalrsvsksnietvtlqalerfdvmhlaernfltLSGGEKQRVHLSRVLAQleysgfhrdEPRYL 181
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLL---------NPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-250 |
2.06e-35 |
|
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: 132.72 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 3 LVAATQSSRLVKISGEDMLQATNLSLAFDNK-----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKV 77
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 78 MLNFKNIKDFSGLQLSGVRAVMpQSIYLD-----FPFL-VKEVVQMALR---SVSKSNIETVTLQALERFDVM-HLAERN 147
Cdd:COG1123 323 LFDGKDLTKLSRRSLRELRRRV-QMVFQDpysslNPRMtVGDIIAEPLRlhgLLSRAERRERVAELLERVGLPpDLADRY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 148 FLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYG 227
Cdd:COG1123 402 PHELSGGQRQRVAIARALAL---------EPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIA 472
|
250 260
....*....|....*....|...
gi 1579913621 228 DRALLLKQGKVQALNKIEKVYQN 250
Cdd:COG1123 473 DRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-262 |
4.33e-35 |
|
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: 126.46 E-value: 4.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAF----DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYLDF-PFL-VKEVVQMALRSVSKSNIETVTLQALERFDvmhLAERnFLT-----LSGGEKQRVHLSRVLAQl 168
Cdd:COG1124 81 VQMVFQDPYASLhPRHtVDRILAEPLRIHGLPDREERIAELLEQVG---LPPS-FLDryphqLSGGQRQRVAIARALIL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 169 eysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKV- 247
Cdd:COG1124 156 --------EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLl 227
|
250 260
....*....|....*....|.
gi 1579913621 248 ------YQNRLLSYVYDFPVE 262
Cdd:COG1124 228 agpkhpYTRELLAASLAFERA 248
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
36-259 |
1.58e-34 |
|
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: 124.76 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGlQLSGVrAVMPQSIYLdFPFL-VKEV 114
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-EKRDI-SYVPQNYAL-FPHMtVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 115 VQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDL 192
Cdd:cd03299 92 IAYGLKkrKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVV---------NPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 193 SHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYVYDF 259
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEF 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-238 |
3.55e-34 |
|
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: 121.74 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVrAVMP 100
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI-GYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSIYLdFPFLvkevvqmalrsvsksnieTVtlqalerfdvmhlaeRNFLTLSGGEKQRVHLSRVLAqleysgfHRdePRY 180
Cdd:cd03230 80 EEPSL-YENL------------------TV---------------RENLKLSGGMKQRLALAQALL-------HD--PEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 181 LFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-269 |
1.14e-33 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 123.36 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIY 104
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LDFPFLVKEVVQM-------ALRSVSKSNIETVTlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:PRK10575 96 AAEGMTVRELVAIgrypwhgALGRFGAADREKVE-EAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ---------D 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYVY 257
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
250
....*....|..
gi 1579913621 258 DFPVEIMQHPKG 269
Cdd:PRK10575 246 GIPMGILPHPAG 257
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-238 |
1.18e-33 |
|
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: 122.29 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDN-KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 pQSIYLDFPfLVKEV----------------VQMALRSVSKSNIEtVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSR 163
Cdd:cd03256 81 -GMIFQQFN-LIERLsvlenvlsgrlgrrstWRSLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 164 VLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03256 158 ALMQ---------QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
25-237 |
2.39e-33 |
|
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: 119.41 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQS 102
Cdd:cd03228 5 NVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 103 IYLdFPFLVKEvvqmalrsvsksNIetvtlqalerfdvmhlaernfltLSGGEKQRVHLSRVLAQleysgfhrdEPRYLF 182
Cdd:cd03228 85 PFL-FSGTIRE------------NI-----------------------LSGGQRQRIAIARALLR---------DPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 183 LDECTSSLDLSHQHQVFAKVKEFAQYHriGVVAVLHDLNLAAQYgDRALLLKQGK 237
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-240 |
7.62e-33 |
|
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: 119.55 E-value: 7.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlsgvRAV-- 98
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----RNIgm 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLdFPFL-VKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:cd03259 77 VFQDYAL-FPHLtVAENIAFGLKLrgVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR-------- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03259 148 -EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-238 |
2.37e-32 |
|
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: 118.76 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 R---AVMPQSIY--LDFPFLVKEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLT-----LSGGEKQRVHLSRVL 165
Cdd:cd03257 81 RkeiQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 166 AQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03257 161 AL---------NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-274 |
2.48e-31 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 117.01 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMP 100
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSIYLDFPFLVKEVV-------QMALRSVSKSNIETVTlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgf 173
Cdd:PRK10253 88 QNATTPGDITVQELVargryphQPLFTRWRKEDEEAVT-KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ------ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 174 hrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLL 253
Cdd:PRK10253 161 ---ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
250 260
....*....|....*....|..
gi 1579913621 254 SYVYDFPVEIMQHP-KGWPLVV 274
Cdd:PRK10253 238 ERIYGLRCMIIDDPvAGTPLVV 259
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-238 |
1.85e-30 |
|
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: 114.07 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS-------GL--- 90
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiarlGIgrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 -QLSGVravmpqsiyldFPFL-VKEVVQMALRSVSKSNIETV------------TLQALERFDVMHLAERNFLTLSGGEK 156
Cdd:cd03219 81 fQIPRL-----------FPELtVLENVMVAAQARTGSGLLLArarreerearerAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 157 QRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQG 236
Cdd:cd03219 150 RRLEIARALAT---------DPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
..
gi 1579913621 237 KV 238
Cdd:cd03219 220 RV 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-266 |
5.60e-30 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 113.10 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 39 ISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGyDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIylDFPFLVkEVVQMA 118
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQ--TPPFAM-PVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 119 LRSVSKSNIETVTLQAL----ERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQLeysgfHRD---EPRYLFLDECTSSLD 191
Cdd:PRK03695 91 TLHQPDKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQV-----WPDinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 192 LSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYVYDFPVEIMQH 266
Cdd:PRK03695 166 VAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDV 239
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-188 |
7.63e-30 |
|
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: 109.66 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIYLdFPFL-VKEV 114
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQL-FPRLtVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 115 VQMALR--SVSKSNIETVTLQALERFDVMHLAER----NFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTS 188
Cdd:pfam00005 80 LRLGLLlkGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLT---------KPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
31-238 |
1.17e-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: 110.81 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfSGLQLSGVRAVMPQSIYLDFPFL 110
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYVMQDVDYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVQMALRSVSKSNIETVTLqaLERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSL 190
Cdd:cd03226 89 VREELLLGLKELDAGNEQAETV--LKDLDLYALKERHPLSLSGGQKQRLAIAAALLS---------GKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1579913621 191 DLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-238 |
1.34e-29 |
|
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: 116.78 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 5 AATQSSRLVKISGEDMLQATNLSLAFDN-KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKN 83
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 84 IKDFSGLQLSGVRAVMPQSIYLdFPFLVKEVVQMALRSVSKSNIEtvtlQALERFDV------------MHLAERNFlTL 151
Cdd:COG4988 401 LSDLDPASWRRQIAWVPQNPYL-FAGTIRENLRLGRPDASDEELE----AALEAAGLdefvaalpdgldTPLGEGGR-GL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 152 SGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIgVVAVLHDLNLAAQYgDRAL 231
Cdd:COG4988 475 SGGQAQRLALARALLR---------DAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRT-VILITHRLALLAQA-DRIL 542
|
....*..
gi 1579913621 232 LLKQGKV 238
Cdd:COG4988 543 VLDDGRI 549
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-239 |
1.36e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.42 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsGLQLSGVRA-- 97
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD--------GRDVTGLPPek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 ----VMPQSiYLDFPFL-VKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQley 170
Cdd:COG3842 77 rnvgMVFQD-YALFPHLtVAENVAFGLRMrgVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 171 sgfhrdEPRYLFLDECTSSLDlshqhqvfAKVK-----EFAQYHR-IGVVAVL--HDLNLAAQYGDRALLLKQGKVQ 239
Cdd:COG3842 153 ------EPRVLLLDEPLSALD--------AKLReemreELRRLQReLGITFIYvtHDQEEALALADRIAVMNDGRIE 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-237 |
1.96e-28 |
|
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: 107.56 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglqlsgVRAVM 99
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--------AREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSI-YLD-----FPFL-VKEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysg 172
Cdd:COG4133 74 RRRLaYLGhadglKPELtVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS----- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAqyGDRALLLKQGK 237
Cdd:COG4133 149 ----PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
21-240 |
2.95e-28 |
|
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: 107.56 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfsglQLSGVR 96
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 AVMPQSIYLdFPFL-VKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgf 173
Cdd:cd03293 76 GYVFQQDAL-LPWLtVLDNVALGLelQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV------ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 174 hrdEPRYLFLDECTSSLDL---SHQHQVFAKVKefaQYHRIGVVAVLHDLNLAAQYGDRALLLKQ--GKVQA 240
Cdd:cd03293 149 ---DPDVLLLDEPFSALDAltrEQLQEELLDIW---RETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-236 |
3.66e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.25 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfsglQ 91
Cdd:COG1116 3 AAAPALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVRAVMPQSIYLdFPFL-VKEVVQMAL--RSVSKSNIETVTLQALERfdvMHLAErnFL-----TLSGGEKQRVHLSR 163
Cdd:COG1116 78 PGPDRGVVFQEPAL-LPWLtVLDNVALGLelRGVPKAERRERARELLEL---VGLAG--FEdayphQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 164 VLAQleysgfhrdEPRYLFLDECTSSLD----LSHQHQVFAKVKEfaqyHRIGVVAVLHDLNLAAQYGDRALLLKQG 236
Cdd:COG1116 152 ALAN---------DPEVLLMDEPFGALDaltrERLQDELLRLWQE----TGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-238 |
7.02e-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: 106.46 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGydGKVMLNFKNIkDFSGLQLSGVRAV 98
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPDS--GTIIIDGLKL-TDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MP---QSIYLdFPFL-VKEVVQMALRSV---SKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleys 171
Cdd:cd03262 78 VGmvfQQFNL-FPHLtVLENITLAPIKVkgmSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM---- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 172 gfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHrIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03262 153 -----NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-238 |
2.42e-27 |
|
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: 105.21 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLS--GVRAV 98
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 mPQSIYLdFPFL-VKEVVQMALRSVSKSNIETVTLQALERFDVmhLAERnfL-----TLSGGEKQRVHLSRVLAQleysg 172
Cdd:cd03224 81 -PEGRRI-FPELtVEENLLLGAYARRRAKRKARLERVYELFPR--LKER--RkqlagTLSGGEQQMLAIARALMS----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03224 150 ----RPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-238 |
2.83e-27 |
|
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: 110.69 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 11 RLVKISGEdmLQATNLSLAF--DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS 88
Cdd:COG2274 466 SLPRLKGD--IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 89 glqLSGVR---AVMPQSIYLdFPFLVKEVVQMALRSVSKSNIetvtLQALERFDV------------MHLAERNfLTLSG 153
Cdd:COG2274 544 ---PASLRrqiGVVLQDVFL-FSGTIRENITLGDPDATDEEI----IEAARLAGLhdfiealpmgydTVVGEGG-SNLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 154 GEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyhRIGVVAVLHDLNLAAQYgDRALLL 233
Cdd:COG2274 615 GQRQRLAIARALLR---------NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLA-DRIIVL 682
|
....*
gi 1579913621 234 KQGKV 238
Cdd:COG2274 683 DKGRI 687
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
21-239 |
3.54e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.11 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlSGVRAVMp 100
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RHVNTVF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSiYLDFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDE 177
Cdd:PRK09452 93 QS-YALFPHMtVFENVAFGLRmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV---------NK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 178 PRYLFLDECTSSLD--LSHQHQVfakvkEFAQYHR---IGVVAVLHDLNLAAQYGDRALLLKQGKVQ 239
Cdd:PRK09452 163 PKVLLLDESLSALDykLRKQMQN-----ELKALQRklgITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-239 |
1.04e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.59 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDN-KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVR-- 96
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 -AVMPQsiylDFPFL----VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqle 169
Cdd:COG2884 81 iGVVFQ----DFRLLpdrtVYENVALPLRvtGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV--- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 170 ysgfHRdePRYLFLDECTSSLDLSHQHQVfakVKEFAQYHRIGvVAVL---HDLNLAAQYGDRALLLKQGKVQ 239
Cdd:COG2884 154 ----NR--PELLLADEPTGNLDPETSWEI---MELLEEINRRG-TTVLiatHDLELVDRMPKRVLELEDGRLV 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-240 |
2.06e-26 |
|
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: 103.58 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS-------G 89
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphriarlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 L----QLSGVravmpqsiyldFPFL-VKEVVQMALRSVSKSNIETVTL-----------------QALERFDVMHLAERN 147
Cdd:COG0411 81 IartfQNPRL-----------FPELtVLENVLVAAHARLGRGLLAALLrlprarreereareraeELLERVGLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 148 FLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYG 227
Cdd:COG0411 150 AGNLSYGQQRRLEIARALAT---------EPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
250
....*....|...
gi 1579913621 228 DRALLLKQGKVQA 240
Cdd:COG0411 221 DRIVVLDFGRVIA 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-250 |
2.15e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.61 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkdFSGL--QLSGVrAV 98
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLppRERRV-GF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSiYLDFPFL-VKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:COG1118 80 VFQH-YALFPHMtVAENIAFGLRVrpPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 176 dEPRYLFLDECTSSLDlshqhqvfAKVK-----EFAQYHR-IGVVAVL--HDLNLAAQYGDRALLLKQGKVQALNKIEKV 247
Cdd:COG1118 151 -EPEVLLLDEPFGALD--------AKVRkelrrWLRRLHDeLGGTTVFvtHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
...
gi 1579913621 248 YQN 250
Cdd:COG1118 222 YDR 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-232 |
3.27e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 29 AFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsgLQLSGVR-AVMPQSIYLD- 106
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARvAYVPQRSEVPd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 107 -FPFLVKEVVQM-------ALRSVSKSNIETVTlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEP 178
Cdd:NF040873 69 sLPLTVRDLVAMgrwarrgLWRRLTRDDRAAVD-DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ---------EA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 179 RYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALL 232
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARGA-TVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-249 |
5.09e-26 |
|
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: 102.19 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVR---AVMPQ 101
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrmGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 SIYLdFPFL-VKEVVQMALR---SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDE 177
Cdd:cd03261 85 SGAL-FDSLtVFENVAFPLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA---------LD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-247 |
5.51e-26 |
|
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: 101.87 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGY-----DGKVMLNFKNIKDFSGLQLSGV 95
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAV-MP-QSIYLdFPFLVKEVVQMALR---SVSKSNIETVTLQALERfdvMHLAER-----NFLTLSGGEKQRVHLSRVL 165
Cdd:cd03260 81 RRVgMVfQKPNP-FPGSIYDNVAYGLRlhgIKLKEELDERVEEALRK---AALWDEvkdrlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 166 AQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAqyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIE 245
Cdd:cd03260 157 AN---------EPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
..
gi 1579913621 246 KV 247
Cdd:cd03260 226 QI 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-237 |
2.68e-25 |
|
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: 98.80 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAV-- 98
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLdFPFL-VKEVVQMALrsvsksnietvtlqalerfdvmhlaernfltlSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:cd03229 81 VFQDFAL-FPHLtVLENIALGL--------------------------------SGGQQQRVALARALAM---------D 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-250 |
3.05e-25 |
|
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: 99.96 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQsIYLDFPFL----VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqle 169
Cdd:cd03258 81 RRRIGM-IFQHFNLLssrtVFENVALPLEiaGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 170 ysgfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:cd03258 157 ------NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 1579913621 250 N 250
Cdd:cd03258 231 N 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-259 |
3.61e-24 |
|
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: 97.41 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSgLQLSGVRAVMP 100
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QsiYLDFPFL-VKEVVQMALR---SVSKSNIETVTLQALERFDVMHL---AERNFLTLSGGEKQRVHLSRVLAQleysgf 173
Cdd:cd03296 82 H--YALFRHMtVFDNVAFGLRvkpRSERPPEAEIRAKVHELLKLVQLdwlADRYPAQLSGGQRQRVALARALAV------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 174 hrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFaqYHRIGV--VAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNR 251
Cdd:cd03296 154 ---EPKVLLLDEPFGALDAKVRKELRRWLRRL--HDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
....*...
gi 1579913621 252 LLSYVYDF 259
Cdd:cd03296 229 ASPFVYSF 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-239 |
4.25e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSG----YDGKVMLNFK----NIkdfsg 89
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSgeilIGGRDVTDLPpkdrNI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 lqlsgvrAVMPQSIYLdFPFL-VKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLA 166
Cdd:COG3839 78 -------AMVFQSYAL-YPHMtVYENIAFPLKLrkVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 167 QleysgfhrdEPRYLFLDECTSSLDlshqhqvfAKVK-----EFAQYHR---IGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG3839 150 R---------EPKVFLLDEPLSNLD--------AKLRvemraEIKRLHRrlgTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
.
gi 1579913621 239 Q 239
Cdd:COG3839 213 Q 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-259 |
4.52e-24 |
|
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: 97.71 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAfdnkpiLDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:cd03294 26 SKEEILKKTGQTVG------VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELREL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 R-----------AVMPQSIYLD---FPflvkevvqMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHL 161
Cdd:cd03294 100 RrkkismvfqsfALLPHRTVLEnvaFG--------LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 162 SRVLAqleysgfhrDEPRYLFLDECTSSLD----LSHQHQVFAKVKEfaqyHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:cd03294 172 ARALA---------VDPDILLMDEAFSALDplirREMQDELLRLQAE----LQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
250 260
....*....|....*....|..
gi 1579913621 238 VQALNKIEKVYQNRLLSYVYDF 259
Cdd:cd03294 239 LVQVGTPEEILTNPANDYVREF 260
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-239 |
4.81e-24 |
|
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: 96.55 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKD-----------FSG 89
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrdiamvFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 LqlsgvrAVMPQ-SIYLDFPFLVKevvqmaLRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQl 168
Cdd:cd03301 81 Y------ALYPHmTVYDNIAFGLK------LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 169 eysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQ 239
Cdd:cd03301 148 --------EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
25-259 |
4.97e-24 |
|
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: 96.92 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlSGVRAVMpQSiY 104
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK-RPVNTVF-QN-Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LDFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDEPRYL 181
Cdd:cd03300 82 ALFPHLtVFENIAFGLRlkKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV---------NEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSYVYDF 259
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-238 |
5.05e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 96.99 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG----DysgyDGKVMLNFKNIkDFSGLQLSGV 95
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleepD----SGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVM---PQSIYLdFPFL-VKEVVQMALRSV---SKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQl 168
Cdd:COG1126 76 RRKVgmvFQQFNL-FPHLtVLENVTLAPIKVkkmSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 169 eysgfhrdEPRYLFLDECTSSLD-------LshqhQVfakVKEFAQYHrIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG1126 154 --------EPKVMLFDEPTSALDpelvgevL----DV---MRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-241 |
2.06e-23 |
|
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: 94.88 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAF--DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVRAV 98
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 M---PQSIYLdFPFL-VKEVVQ-MA-LRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysG 172
Cdd:cd03263 77 LgycPQFDAL-FDELtVREHLRfYArLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI-----G 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRiGVVAVLHDLNLAAQYGDRALLLKQGKVQAL 241
Cdd:cd03263 151 ----GPSVLLLDEPTSGLDPASRRAIWDLILEVRK-GR-SIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-238 |
2.76e-23 |
|
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: 94.66 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsGLQLSGVR- 96
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD--------GEDITGLPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 --------AVMPQS--IyldFPFL-VKEVVQMAL-----RSVSKSNIETVtlqaLERFDVmhLAER-NFL--TLSGGEKQ 157
Cdd:COG0410 73 hriarlgiGYVPEGrrI---FPSLtVEENLLLGAyarrdRAEVRADLERV----YELFPR--LKERrRQRagTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 158 RVHLSRVLAQleysgfhrdEPRYLFLDECtsSLDLSHQ--HQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQ 235
Cdd:COG0410 144 MLAIGRALMS---------RPKLLLLDEP--SLGLAPLivEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLER 211
|
...
gi 1579913621 236 GKV 238
Cdd:COG0410 212 GRI 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-240 |
3.09e-23 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 95.57 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSL---LNCLTGDYSG---YDGKVMLNFKNIKD---FSGL--- 90
Cdd:TIGR04520 5 NVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLLPTSGkvtVDGLDTLDEENLWEirkKVGMvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 ----QLsgVRAVmpqsiyldfpflVKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRV 164
Cdd:TIGR04520 85 npdnQF--VGAT------------VEDDVAFGLenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 165 LAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKVQA 240
Cdd:TIGR04520 151 LAM---------RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVA 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-191 |
5.78e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 5.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDN----KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsGLQLSGV 95
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD--------GVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 ---RAVMPQSIYLdFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQle 169
Cdd:COG4525 75 gadRGVVFQKDAL-LPWLnVLDNVAFGLRlrGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA-- 151
|
170 180
....*....|....*....|..
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLD 191
Cdd:COG4525 152 -------DPRFLLMDEPFGALD 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-235 |
7.70e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.03 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 19 DMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKvmlnfknIKDFSGLQLSGVrav 98
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRNGKLRIGYV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 mPQSIYLD--FPFLVKEVvqMALR-SVSKSNIetvtLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhr 175
Cdd:PRK09544 73 -PQKLYLDttLPLTVNRF--LRLRpGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL--------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 176 DEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQ 235
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-257 |
1.96e-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: 92.61 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDF-----SGLQLSgv 95
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmhkrARLGIG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 raVMPQ--SIYLDFPflVKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleys 171
Cdd:cd03218 79 --YLPQeaSIFRKLT--VEENILAVLeiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 172 gfhrdEPRYLFLDECTSSLD---LSHQHQVFAKVKEFAqyhrIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVY 248
Cdd:cd03218 151 -----NPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRG----IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
....*....
gi 1579913621 249 QNRLLSYVY 257
Cdd:cd03218 222 ANELVRKVY 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-238 |
1.97e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 91.96 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkDFSGLQLSGV----- 95
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNRIGYlpeer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 -----RAVMPQSIYLdfpflvkevvqMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVhlsrvlaQLEY 170
Cdd:cd03269 80 glypkMKVIDQLVYL-----------AQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKV-------QFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 171 SGFHRdePRYLFLDECTSSLDLSHQhQVFAKVkeFAQYHRIGVVAVL--HDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03269 142 AVIHD--PELLILDEPFSGLDPVNV-ELLKDV--IRELARAGKTVILstHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-267 |
2.12e-22 |
|
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: 92.75 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIYLdFP-F 109
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGL-FPhM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 110 LVKEVVQM--ALRSVSKSNIETVTLQALE--RFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDE 185
Cdd:cd03295 91 TVEENIALvpKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAA---------DPPLLLMDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 186 CTSSLD----LSHQHQvFAKVKEfaqyhRIG--VVAVLHDLNLAAQYGDRALLLKQGKVQalnkiekvyqnrllsyVYDF 259
Cdd:cd03295 162 PFGALDpitrDQLQEE-FKRLQQ-----ELGktIVFVTHDIDEAFRLADRIAIMKNGEIV----------------QVGT 219
|
....*...
gi 1579913621 260 PVEIMQHP 267
Cdd:cd03295 220 PDEILRSP 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-192 |
2.21e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 1 MALVAATQSSRLVKI-------SGEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGY 73
Cdd:COG0488 289 LEREEPPRRDKTVEIrfppperLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 74 DGKVMLNfknikdfSGLQLsgvrAVMPQS-IYLDfpfLVKEVVQmALRSVSKSNIETVTLQALERF-----DVMHLAErn 147
Cdd:COG0488 369 SGTVKLG-------ETVKI----GYFDQHqEELD---PDKTVLD-ELRDGAPGGTEQEVRGYLGRFlfsgdDAFKPVG-- 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1579913621 148 flTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDL 192
Cdd:COG0488 432 --VLSGGEKARLALAKLLLS---------PPNVLLLDEPTNHLDI 465
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
20-240 |
3.29e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.74 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPIldNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVR--A 97
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA----LPPAERpvS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 VMPQSIYLdFPFL-VKEVVQMALR------SVSKSNIEtvtlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqley 170
Cdd:COG3840 75 MLFQENNL-FPHLtVAQNIGLGLRpglkltAEQRAQVE----QALERVGLAGLLDRLPGQLSGGQRQRVALARCLV---- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 171 sgfhRDEPrYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:COG3840 146 ----RKRP-ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
39-255 |
3.52e-22 |
|
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: 94.02 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 39 ISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS-GLQLSG-VRAV--MPQSIYLdFPFL-VKE 113
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkGIFLPPeKRRIgyVFQEARL-FPHLsVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 114 VVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSR-VLAQleysgfhrdePRYLFLDECTSSLDL 192
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRaLLSS----------PRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 193 SHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSY 255
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-240 |
3.87e-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: 89.80 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLN-----FKNIKDfsglqlsgv 95
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevsFASPRD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 ravmpqsiyldfpflvkevvqmALRsvskSNIETVTlQalerfdvmhlaernfltLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:cd03216 72 ----------------------ARR----AGIAMVY-Q-----------------LSVGERQMVEIARALAR-------- 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03216 100 -NARLLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-233 |
4.99e-22 |
|
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: 95.05 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNK-PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVM 99
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLdFPFLVKEVVQMALRSVSKSNIEtvtlQALERFDVMHLAE-----------RNFLTLSGGEKQRVHLSRVLAql 168
Cdd:TIGR02857 402 PQHPFL-FAGTIAENIRLARPDASDAEIR----EALERAGLDEFVAalpqgldtpigEGGAGLSGGQAQRLALARAFL-- 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 169 eysgfhRDEPrYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNLAAQYgDRALLL 233
Cdd:TIGR02857 475 ------RDAP-LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT--HRLALAALA-DRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-238 |
6.34e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 91.14 E-value: 6.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFD-NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsgLQLSGVR---AVMP 100
Cdd:cd03253 5 NVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE---VTLDSLRraiGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSIYLdFPFLVKEVVQMALRSVSKSNIETVTLQA-----LERF----DVMhLAERNfLTLSGGEKQRVHLSRVLAQleys 171
Cdd:cd03253 82 QDTVL-FNDTIGYNIRYGRPDATDEEVIEAAKAAqihdkIMRFpdgyDTI-VGERG-LKLSGGEKQRVAIARAILK---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 172 gfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVaVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:cd03253 155 -----NPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIV-IAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-238 |
6.81e-22 |
|
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: 90.30 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLNFKNIKDFSGLQLSGvraVMPQSIYLdFPFL 110
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKIIG---YVPQDDIL-HPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 -VKEVVQMA--LRSvsksnietvtlqalerfdvmhlaernfltLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECT 187
Cdd:cd03213 98 tVRETLMFAakLRG-----------------------------LSGGERKRVSIALELVS---------NPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 188 SSLDLSHQHQVFAKVKEFAQYHRiGVVAVLH-----DLNLAaqygDRALLLKQGKV 238
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGR-TIICSIHqpsseIFELF----DKLLLLSQGRV 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-238 |
1.10e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.92 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNC------------LTGDYSGYDGKVmlNFKNIKDF 87
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCinkleeitsgdlIVDGLKVNDPKV--DERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 88 SGLQLsgvravmpQSIYLdFPFLVK-EVVQMALRSVSKSNIETVTLQALERFDVMHLAER--NFLT-LSGGEKQRVHLSR 163
Cdd:PRK09493 79 AGMVF--------QQFYL-FPHLTAlENVMFGPLRVRGASKEEAEKQARELLAKVGLAERahHYPSeLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 164 VLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK09493 150 ALAV---------KPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-192 |
1.52e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 23 ATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsglqlSGVR-AVMPQ 101
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRiGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 SIYLDFPFLVKEVVQMALRSVSK--------------SNIETVTLQAL-ERFDVMH--------------------LAER 146
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRAleaeleeleaklaePDEDLERLAELqEEFEALGgweaearaeeilsglgfpeeDLDR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1579913621 147 NFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDL 192
Cdd:COG0488 149 PVSELSGGWRRRVALARALLS---------EPDLLLLDEPTNHLDL 185
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-238 |
1.62e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFD--NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGlQLSGVRAV 98
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLdfpflvkevvqmalrsvsksnIETVTLQALERfdvmhlaernflTLSGGEKQRVHLSRVLAQleysgfhrDEP 178
Cdd:cd03247 80 LNQRPYL---------------------FDTTLRNNLGR------------RFSGGERQRLALARILLQ--------DAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 179 rYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgvVAVLHDLnLAAQYGDRALLLKQGKV 238
Cdd:cd03247 119 -IVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHL-TGIEHMDKILFLENGKI 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-185 |
1.86e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.09 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlsgvRAVM 99
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK----RARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 -----PQ--SIyldFPFL-VKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQle 169
Cdd:COG1137 79 gigylPQeaSI---FRKLtVEDNILAVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT-- 153
|
170
....*....|....*.
gi 1579913621 170 ysgfhrdEPRYLFLDE 185
Cdd:COG1137 154 -------NPKFILLDE 162
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-238 |
2.17e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.53 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAF-----DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNI---KDFSglq 91
Cdd:COG1101 1 MLELKNLSKTFnpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 lsgvRAVMPQSIYLDfPFL-------VKEVVQMALR---------SVSKSNIETVTLQaLERFDvMHLAERnfLT----- 150
Cdd:COG1101 78 ----RAKYIGRVFQD-PMMgtapsmtIEENLALAYRrgkrrglrrGLTKKRRELFREL-LATLG-LGLENR--LDtkvgl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 151 LSGGekQRVHLSRVLAQLeysgfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRA 230
Cdd:COG1101 149 LSGG--QRQALSLLMATL-------TKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRL 219
|
....*...
gi 1579913621 231 LLLKQGKV 238
Cdd:COG1101 220 IMMHEGRI 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-240 |
2.72e-21 |
|
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: 88.89 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 38 NISLDVEaGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS-GLQLSGVR---AVMPQSIYLdFPFL-VK 112
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkKINLPPQQrkiGLVFQQYAL-FPHLnVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 113 EVVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDL 192
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAA---------QPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1579913621 193 SHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-191 |
3.86e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglqLSGVRAVM 99
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLdFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrd 176
Cdd:PRK11248 76 FQNEGL-LPWRnVQDNVAFGLQlaGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA--------- 145
|
170
....*....|....*
gi 1579913621 177 EPRYLFLDECTSSLD 191
Cdd:PRK11248 146 NPQLLLLDEPFGALD 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-259 |
4.36e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.44 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsGLQLSGV---- 95
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD--------GVDLSHVppyq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAV--MPQSiYLDFPFL-VKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQley 170
Cdd:PRK11607 91 RPInmMFQS-YALFPHMtVEQNIAFGLKQdkLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 171 sgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyhRIGV--VAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVY 248
Cdd:PRK11607 167 ------RPKLLLLDEPMGALDKKLRDRMQLEVVDILE--RVGVtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
250
....*....|.
gi 1579913621 249 QNRLLSYVYDF 259
Cdd:PRK11607 239 EHPTTRYSAEF 249
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-267 |
4.75e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.68 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfSGLQlsgvRAVMPQSiYLDFPFL-VKEV 114
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPD----RMVVFQN-YSLLPWLtVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 115 VQMA----LRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSL 190
Cdd:TIGR01184 75 IALAvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSI---------RPKVLLLDEPFGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 191 DLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVyqnrllsyvyDFP-----VEIMQ 265
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV----------PFPrprdrLEVVE 215
|
..
gi 1579913621 266 HP 267
Cdd:TIGR01184 216 DP 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-257 |
6.80e-21 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 88.49 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsgLQLSGvRAVM- 99
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH---LPMHE-RARLg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 ----PQ--SIyldFPFL-VKEVVQMAL---RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQle 169
Cdd:TIGR04406 78 igylPQeaSI---FRKLtVEENIMAVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLD---LSHQHQVFAKVKEFAqyhrIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEK 246
Cdd:TIGR04406 153 -------NPKFILLDEPFAGVDpiaVGDIKKIIKHLKERG----IGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAE 221
|
250
....*....|.
gi 1579913621 247 VYQNRLLSYVY 257
Cdd:TIGR04406 222 IVANEKVRRVY 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-263 |
9.07e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.14 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKvmLNFKNiKDFSGLQLSGVRAVMPQSIY 104
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH--IRFHG-TDVSRLHARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LDFPFL-VKEVVQMALRSV------SKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:PRK10851 84 ALFRHMtVFDNIAFGLTVLprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV---------E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 178 PRYLFLDECTSSLDlshqhqvfAKV-KEFAQYHR-------IGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:PRK10851 155 PQILLLDEPFGALD--------AQVrKELRRWLRqlheelkFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
250
....*....|....
gi 1579913621 250 NRLLSYVYDFPVEI 263
Cdd:PRK10851 227 EPATRFVLEFMGEV 240
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-245 |
1.10e-20 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 89.37 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 30 FDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVR---AVMPQSIYLD 106
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRrsiGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 107 FPFLVKEVVQM--ALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLaqleysgFHRdePRYLFLD 184
Cdd:TIGR01188 79 EDLTGRENLEMmgRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASL-------IHQ--PDVLFLD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 185 ECTSSLDLSHQHQVFAKVKEFAQyhrIGVVAVL--HDLNLAAQYGDRALLLKQGKVQALNKIE 245
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKE---EGVTILLttHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-238 |
1.98e-20 |
|
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: 87.14 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKP---ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQ 101
Cdd:cd03248 16 NVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 SIYLdFPFLVKEVVQMALRSVSKSNIeTVTLQALERFDVMHLAERNFLT--------LSGGEKQRVHLSRVLAQleysgf 173
Cdd:cd03248 96 EPVL-FARSLQDNIAYGLQSCSFECV-KEAAQKAHAHSFISELASGYDTevgekgsqLSGGQKQRVAIARALIR------ 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 174 hrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNLaAQYGDRALLLKQGKV 238
Cdd:cd03248 168 ---NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA--HRLST-VERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-240 |
2.12e-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: 86.87 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKPI--LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQS 102
Cdd:cd03245 7 NVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 103 IYLdFPFLVKEVVQMALRSVSKSNI-ETVTLQALERF-------DVMHLAERNFLtLSGGEKQRVHLSRVLAQleysgfh 174
Cdd:cd03245 87 VTL-FYGTLRDNITLGAPLADDERIlRAAELAGVTDFvnkhpngLDLQIGERGRG-LSGGQRQAVALARALLN------- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 175 rdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIgVVAVLHD---LNLAaqygDRALLLKQGKVQA 240
Cdd:cd03245 158 --DPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKT-LIIITHRpslLDLV----DRIIVMDSGRIVA 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-246 |
2.46e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 5 AATQSSRLVKISGEDMLQATNLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfkn 83
Cdd:COG4178 347 ALPEAASRIETSEDGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 84 ikdfsglqlSGVRA-VMPQSIY---------LDFPFLVKEVVQMALRSVsksnIETVTLQAL-ERFDVmhlaERNF-LTL 151
Cdd:COG4178 424 ---------AGARVlFLPQRPYlplgtlreaLLYPATAEAFSDAELREA----LEAVGLGHLaERLDE----EADWdQVL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 152 SGGEKQRVHLSRVLaqleysgFHRdePRYLFLDECTSSLDLSHQHQVFAKVKEfaQYHRIGVVAVLHDLNLAAQYgDRAL 231
Cdd:COG4178 487 SLGEQQRLAFARLL-------LHK--PDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFH-DRVL 554
|
250
....*....|....*
gi 1579913621 232 LLKQGKVQALNKIEK 246
Cdd:COG4178 555 ELTGDGSWQLLPAEA 569
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-240 |
2.56e-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: 86.72 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKnikDFSGL---QL 92
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALdedAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SGVRA----VMPQSiyldFPFL----VKEVVQMALRSVSKSNIETVTLQALERfdvMHLAERnfLT-----LSGGEKQRV 159
Cdd:COG4181 85 ARLRArhvgFVFQS----FQLLptltALENVMLPLELAGRRDARARARALLER---VGLGHR--LDhypaqLSGGEQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 160 HLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQV----FAKVKEFaqyhriGVVAVL--HDLNLAAQyGDRALLL 233
Cdd:COG4181 156 ALARAFAT---------EPAILFADEPTGNLDAATGEQIidllFELNRER------GTTLVLvtHDPALAAR-CDRVLRL 219
|
....*..
gi 1579913621 234 KQGKVQA 240
Cdd:COG4181 220 RAGRLVE 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-250 |
2.73e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.35 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSG- 94
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 --VRAVmpQSIYLDFPFLVKEVVQMALRSVSKSNI---------------ETVTLQA--LERFDVMHLAERNFLTLSGGE 155
Cdd:PRK11300 81 gvVRTF--QHVRLFREMTVIENLLVAQHQQLKTGLfsgllktpafrraesEALDRAAtwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 156 KQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQ 235
Cdd:PRK11300 159 QRRLEIARCMVT---------QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250
....*....|....*
gi 1579913621 236 GKVQALNKIEKVYQN 250
Cdd:PRK11300 230 GTPLANGTPEEIRNN 244
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-238 |
2.80e-20 |
|
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: 85.35 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAF--DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAV 98
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLdFPFLVKEvvqmalrsvsksNIetvtlqalerfdvmhlaernfltLSGGEKQRVHLSRVLaqleysgfHRDeP 178
Cdd:cd03246 81 LPQDDEL-FSGSIAE------------NI-----------------------LSGGQRQRLGLARAL--------YGN-P 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 179 RYLFLDECTSSLDLSHQHQVFAKVKEfAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-238 |
4.04e-20 |
|
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: 86.13 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNK-PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSI 103
Cdd:cd03254 7 NVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YLdFPFLVKEVVQMA-LRSVSKSNIETVTLQALERFdVMHLAE-------RNFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:cd03254 87 FL-FSGTIMENIRLGrPNATDEEVIEAAKEAGAHDF-IMKLPNgydtvlgENGGNLSQGERQLLAIARAMLR-------- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNlAAQYGDRALLLKQGKV 238
Cdd:cd03254 157 -DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA--HRLS-TIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-249 |
5.00e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.99 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsGLQLS-- 93
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG--------GMVLSee 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 94 ---GVRAVM------PqsiylDFPFL---VKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRV 159
Cdd:PRK13635 75 tvwDVRRQVgmvfqnP-----DNQFVgatVQDDVAFGLenIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 160 HLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKVQ 239
Cdd:PRK13635 150 AIAGVLAL---------QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
250
....*....|
gi 1579913621 240 ALNKIEKVYQ 249
Cdd:PRK13635 220 EEGTPEEIFK 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
32-238 |
5.11e-20 |
|
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: 85.54 E-value: 5.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMpQSIYLDFPFL- 110
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI-GVVFQDFRLLp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 ---VKEVVQMALRSVSKS--NIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDEPRYLFLDE 185
Cdd:cd03292 92 drnVYENVAFALEVTGVPprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV---------NSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 186 CTSSLDLSHQHQVfakVKEFAQYHRIGVVAVL--HDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03292 163 PTGNLDPDTTWEI---MNLLKKINKAGTTVVVatHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-238 |
9.07e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 9.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 13 VKISGEDMLQATNLSLAFDN---------KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKN 83
Cdd:PRK11160 324 VTFPTTSTAAADQVSLTLNNvsftypdqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 84 IKDFSGLQLSGVRAVMPQSIYLdFPFLVKEVVQMALRSVSKSNIETVtlqaLERFDVMHLAE-------------RnflT 150
Cdd:PRK11160 404 IADYSEAALRQAISVVSQRVHL-FSATLRDNLLLAAPNASDEALIEV----LQQVGLEKLLEddkglnawlgeggR---Q 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 151 LSGGEKQRVHLSRVLAqleysgfhRDEPrYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIgVVAVLHDLNLAAQYgDRA 230
Cdd:PRK11160 476 LSGGEQRRLGIARALL--------HDAP-LLLLDEPTEGLDAETERQILELLAEHAQ-NKT-VLMITHRLTGLEQF-DRI 543
|
....*...
gi 1579913621 231 LLLKQGKV 238
Cdd:PRK11160 544 CVMDNGQI 551
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-238 |
1.16e-19 |
|
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: 84.97 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIYLdFPFL 110
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL-FNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVQMALRSVSKSNIETVTLQAL---------ERFDVMhLAERNfLTLSGGEKQRVHLSRVLAqleysgfhRDePRYL 181
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARAANahefimelpEGYDTV-IGERG-VKLSGGQRQRIAIARALL--------KD-PPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVaVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMK-NRTTFV-IAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
36-250 |
1.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.87 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfSGLQLSGVRA------------VMPQSI 103
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKkvglvfqypeyqLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YLDFPFLVKEvvqmalRSVSKSNIETVTLQALE--RFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYL 181
Cdd:PRK13637 102 EKDIAFGPIN------LGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM---------EPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQN 250
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-221 |
1.73e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSG----LQLS-- 93
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrQQVSyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 94 -GVRAVMPQSIY--LDFPFLVKEvvqmalrsvsKSNIETVTLQALERFDV-MHLAERNFLTLSGGEKQRVHLSRVLAQLe 169
Cdd:PRK10247 87 aQTPTLFGDTVYdnLIFPWQIRN----------QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFM- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 170 ysgfhrdePRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLN 221
Cdd:PRK10247 156 --------PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
33-238 |
2.05e-19 |
|
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: 85.24 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlNFKNiKDFSGLQLSGVRAVMP--QSIYLDFP-- 108
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTV--SFRG-QDLYQLDRKQRRAFRRdvQLVFQDSPsa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 ----FLVKEVVQMALR---SVSKSNIETVTLQALERFDV-MHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRY 180
Cdd:TIGR02769 101 vnprMTVRQIIGEPLRhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAV---------KPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 181 LFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-238 |
2.23e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSL---LNCLTGDYSGydgkvMLNFKNIK-DFS-------G 89
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLEMPRSG-----TLNIAGNHfDFSktpsdkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 LQL-SGVRAVMPQsiYLDFPFLVkeVVQ------MALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLS 162
Cdd:PRK11124 78 RELrRNVGMVFQQ--YNLWPHLT--VQQnlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 163 RVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHrIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK11124 154 RALMM---------EPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-238 |
4.18e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSglqLSGVR---AVMPQSIYLdF 107
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRrqiGVVPQDTFL-F 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 108 PFLVKEVVQMALRSVSKSNIETVTLQA-LERFdVMHLAE-------RNFLTLSGGEKQRVHLSRVLAqleysgfhRDePR 179
Cdd:COG1132 427 SGTIRENIRYGRPDATDEEVEEAAKAAqAHEF-IEALPDgydtvvgERGVNLSGGQRQRIAIARALL--------KD-PP 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 180 YLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIgVVAVLHDLNLAAQYgDRALLLKQGKV 238
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMK-GRT-TIVIAHRLSTIRNA-DRILVLDDGRI 552
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-250 |
1.07e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.12 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML--------NFKNIKDFSG 89
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskeNLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 L-------QLSGVRavmpqsiyldfpflVKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVH 160
Cdd:PRK13632 87 IifqnpdnQFIGAT--------------VEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 161 LSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKVQA 240
Cdd:PRK13632 153 IASVLAL---------NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIA 222
|
250
....*....|
gi 1579913621 241 LNKIEKVYQN 250
Cdd:PRK13632 223 QGKPKEILNN 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-229 |
1.47e-18 |
|
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: 82.10 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAF-----DNK--PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFknikDFSGLQL 92
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH----DGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SG--------VRA-----------VMPQSIYLDfpflvkeVVQMALRS--VSKSNIETVTLQALERFdvmHLAERNF--- 148
Cdd:COG4778 80 AQaspreilaLRRrtigyvsqflrVIPRVSALD-------VVAEPLLErgVDREEARARARELLARL---NLPERLWdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 149 -LTLSGGEKQRVHLSRvlaqleysGFHRDePRYLFLDECTSSLDLSHQHQVFAKVKEfAQYHRIGVVAVLHDLNLAAQYG 227
Cdd:COG4778 150 pATFSGGEQQRVNIAR--------GFIAD-PPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVA 219
|
..
gi 1579913621 228 DR 229
Cdd:COG4778 220 DR 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-238 |
1.84e-18 |
|
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: 81.03 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLNFKNIKDFSglqlSGVRAV 98
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLP----PEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MpqSIYLDF--PFLVKEV-VQMALRSVSKSnietvtlqalerfdvmhlaernfltLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:cd03217 77 L--GIFLAFqyPPEIPGVkNADFLRYVNEG-------------------------FSGGEKKRNEILQLLLL-------- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQY-GDRALLLKQGKV 238
Cdd:cd03217 122 -EPDLAILDEPDSGLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-238 |
1.91e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSG---YDGKVMLnFKNIKDFSGLQLSG 94
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdksAGSHIEL-LGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 VRAVMPQSIYLDFPF-------LVKEVVQMALRSVS--KSNIETVT-------LQALERFDVMHLAERNFLTLSGGEKQR 158
Cdd:PRK09984 81 IRKSRANTGYIFQQFnlvnrlsVLENVLIGALGSTPfwRTCFSWFTreqkqraLQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 159 VHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK09984 161 VAIARALMQ---------QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-240 |
2.68e-18 |
|
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: 81.26 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGlqlsGVRA--- 97
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR----EVRRrig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 VMPQSIYLDFPFLVKE--VVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLaqleysgFHR 175
Cdd:cd03265 77 IVFQDLSVDDELTGWEnlYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL-------VHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 176 dePRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03265 150 --PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
35-238 |
3.05e-18 |
|
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: 81.16 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 35 ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYD---GKVMLNfknikdfsGLQLSgvRAVMPQSI-YLD---- 106
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFN--------GQPRK--PDQFQKCVaYVRqddi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 107 -FPFL-VKE----VVQMALRSVSKSNIET--VTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEP 178
Cdd:cd03234 92 lLPGLtVREtltyTAILRLPRKSSDAIRKkrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW---------DP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 179 RYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLH----DLnlaAQYGDRALLLKQGKV 238
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARRNRI-VILTIHqprsDL---FRLFDRILLLSSGEI 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
31-237 |
3.29e-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: 80.59 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsglQLSGVRAVMPQSiyldfPFL 110
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQE-----PWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVqmalrsvsKSNI------------ETVTLQALER-FDVMHLAER-----NFLTLSGGEKQRVHLSRVLaqleYSg 172
Cdd:cd03250 78 QNGTI--------RENIlfgkpfdeeryeKVIKACALEPdLEILPDGDLteigeKGINLSGGQKQRISLARAV----YS- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKV-KEFAQYHRIgVVAVLHDLNLAAQyGDRALLLKQGK 237
Cdd:cd03250 145 ----DADIYLLDDPLSAVDAHVGRHIFENCiLGLLLNNKT-RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-256 |
4.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlsGVRAV 98
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ--GIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MpqSIYLDFPflvkeVVQMALRSVSKS---NIETVTLQALE---RFDvMHLAE--------RNFLTLSGGEKQRVHLSRV 164
Cdd:PRK13644 79 V--GIVFQNP-----ETQFVGRTVEEDlafGPENLCLPPIEirkRVD-RALAEiglekyrhRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 165 LAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFaqyHRIG--VVAVLHDLNlAAQYGDRALLLKQGKVQALN 242
Cdd:PRK13644 151 LTM---------EPECLIFDEVTSMLDPDSGIAVLERIKKL---HEKGktIVYITHNLE-ELHDADRIIVMDRGKIVLEG 217
|
250
....*....|....
gi 1579913621 243 KIEKVYQNRLLSYV 256
Cdd:PRK13644 218 EPENVLSDVSLQTL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
32-238 |
5.52e-18 |
|
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: 83.64 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIYLDFPFLV 111
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMALRSVSKSNIETVTLQALERFDV--------MHLAERNFlTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFL 183
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWAACEIAEIKDDIenmplgyqTELSEEGS-SISGGQKQRIALARALLT---------DSKVLIL 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 184 DECTSSLDLSHQHQVfakVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:TIGR01193 636 DESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKI 686
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-229 |
7.14e-18 |
|
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: 81.64 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGY-DGKVMLNFKNIKDFSGLQL 92
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllPPPGItSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SGVR----AVMPQSIY--LDfPFL-VKEVVQMALRS---VSKSNIETVTLQALERfdV-MHLAERnFLT-----LSGGEK 156
Cdd:COG0444 81 RKIRgreiQMIFQDPMtsLN-PVMtVGDQIAEPLRIhggLSKAEARERAIELLER--VgLPDPER-RLDrypheLSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 157 QRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDR 229
Cdd:COG0444 157 QRVMIARALAL---------EPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-238 |
7.65e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLN-----FKNIKDfsGLQL 92
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrFRSPRD--AQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 sGVRAVmPQSIYLdFP--------FLVKEVVQMALRSVSKSNIEtvTLQALERF----DVMHLAErnflTLSGGEKQRVH 160
Cdd:COG1129 80 -GIAII-HQELNL-VPnlsvaeniFLGREPRRGGLIDWRAMRRR--ARELLARLgldiDPDTPVG----DLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 161 LSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG1129 151 IARALSR---------DARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-192 |
9.38e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 9.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLNFKNIKDFS-------GLQ 91
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSpderaraGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LS--------GVRavmpqsiyldfpflVKEVVQMALRSVSKSNIETVTLQAL--ERFDVMHLAErNFLT------LSGGE 155
Cdd:COG0396 81 LAfqypveipGVS--------------VSNFLRTALNARRGEELSAREFLKLlkEKMKELGLDE-DFLDryvnegFSGGE 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 1579913621 156 KQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDL 192
Cdd:COG0396 146 KKRNEILQMLLL---------EPKLAILDETDSGLDI 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-238 |
1.00e-17 |
|
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: 82.54 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLN------------------ 80
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 81 --------FKNIK-DFSGLQLSGVRAVMPQ-SIYLDFPFL------VKEVVQMALRSVSKSNIETVTlQALERFDVMHLA 144
Cdd:TIGR03269 81 pcpvcggtLEPEEvDFWNLSDKLRRRIRKRiAIMLQRTFAlygddtVLDNVLEALEEIGYEGKEAVG-RAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 145 ERnfLT-----LSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHD 219
Cdd:TIGR03269 160 HR--IThiardLSGGEKQRVVLARQLAK---------EPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250
....*....|....*....
gi 1579913621 220 LNLAAQYGDRALLLKQGKV 238
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEI 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-237 |
2.12e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.72 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsglqlSGVR-AVM 99
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKiGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQsiyldfpflvkevvqmalrsvsksnietvtlqalerfdvmhlaernfltLSGGEKQRVHLSRVLAQleysgfhrdEPR 179
Cdd:cd03221 69 EQ-------------------------------------------------LSGGEKMRLALAKLLLE---------NPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 180 YLFLDECTSSLDLSHQHQvfakVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:cd03221 91 LLLLDEPTNHLDLESIEA----LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
31-251 |
2.59e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkDFSGLQLSGVRA------------V 98
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLREsvgmvfqdpdnqL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLDFPFlvkEVVQMALrsvSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEP 178
Cdd:PRK13636 96 FSASVYQDVSF---GAVNLKL---PEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM---------EP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 179 RYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNR 251
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-238 |
3.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdFSGLQLSGVRA- 97
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 ---VMPQSIYLDFPFLVKEVVQ---MALrSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleys 171
Cdd:PRK13639 80 vgiVFQNPDDQLFAPTVEEDVAfgpLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 172 gfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK13639 155 -----KPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-240 |
3.97e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.01 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML--------NFKNIKDFS 88
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmgrevnaeNEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 89 GLQLSGV-RAVMPQSIYLDFPFlvkEVVQMALRsvsKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQ 167
Cdd:PRK13647 82 GLVFQDPdDQVFSSTVWDDVAF---GPVNMGLD---KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 168 leysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVlHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:PRK13647 156 ---------DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAT-HDVDLAAEWADQVIVLKEGRVLA 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-259 |
7.71e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 15 ISGEDMLQATNLSLAfdnkpiLDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSG 94
Cdd:PRK10070 29 LSKEQILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 VR-----------AVMPQSIYLDfpflvKEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSR 163
Cdd:PRK10070 103 VRrkkiamvfqsfALMPHMTVLD-----NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 164 VLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNK 243
Cdd:PRK10070 178 ALAI---------NPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
250
....*....|....*.
gi 1579913621 244 IEKVYQNRLLSYVYDF 259
Cdd:PRK10070 249 PDEILNNPANDYVRTF 264
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-249 |
8.56e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.99 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 19 DMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfSGLQLSGVRAV 98
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MpQSiYLDFPFL-VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:PRK11432 84 F-QS-YALFPHMsLGENVGYGLKmlGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL-------- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:PRK11432 154 -KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-238 |
1.02e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMpQSIYLDFP---- 108
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDI-QMVFQDSIsavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 --FLVKEVVQMALR---SVSKSNIETVTLQALERFDV-MHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLF 182
Cdd:PRK10419 104 prKTVREIIREPLRhllSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAV---------EPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 183 LDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-238 |
1.25e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLT------------GDYSgYDGKVMLN-----FK 82
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDIT-IDTARSLSqqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 83 NIKD-----FSGLQLSGVRAVMPQSIylDFPFLVKEVVQMALRSVSKSNIETVTLQALERfdvmHLAERnfltLSGGEKQ 157
Cdd:PRK11264 82 QLRQhvgfvFQNFNLFPHRTVLENII--EGPVIVKGEPKEEATARARELLAKVGLAGKET----SYPRR----LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 158 RVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVaVLHDLNLAAQYGDRALLLKQGK 237
Cdd:PRK11264 152 RVAIARALAM---------RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGR 221
|
.
gi 1579913621 238 V 238
Cdd:PRK11264 222 I 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-191 |
1.30e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSglqlsgvraVM 99
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---------VA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYL---DF--PFL-VKEVVQM--ALRSVSKSNIEtvtlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleys 171
Cdd:PRK13539 73 EACHYLghrNAmkPALtVAENLEFwaAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLV----- 143
|
170 180
....*....|....*....|
gi 1579913621 172 gFHRdePRYLfLDECTSSLD 191
Cdd:PRK13539 144 -SNR--PIWI-LDEPTAALD 159
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-248 |
1.42e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkDFSGLQLSGVRAVM 99
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 P--------QSIYLDfpflVKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQle 169
Cdd:PRK13638 80 AtvfqdpeqQIFYTD----IDSDIAFSLRNlgVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL-- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVY 248
Cdd:PRK13638 154 -------QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-260 |
1.64e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.46 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFD---NKPILDNISLDVEAGELLCILGPNGAGKSS---LLNCLTGDYSG---YDGKVML--NFKNIKD 86
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGqiiIDGDLLTeeNVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 87 FSGLQLSGvravmPqsiylDFPFL---VKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHL 161
Cdd:PRK13650 82 KIGMVFQN-----P-----DNQFVgatVEDDVAFGLenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 162 SRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAqYGDRALLLKQGKVQAL 241
Cdd:PRK13650 152 AGAVAM---------RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVEST 221
|
250 260
....*....|....*....|.
gi 1579913621 242 NKIEKVYQ--NRLLSYVYDFP 260
Cdd:PRK13650 222 STPRELFSrgNDLLQLGLDIP 242
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
2.09e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.43 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNK-PI----LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsgLQLSGV 95
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKN---KKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYLDFPFL-----VKE-------VVQMALRSVSKSNIE-----------TVTLQALER---------FDVMHL 143
Cdd:PRK13651 80 KEKVLEKLVIQKTRFkkikkIKEirrrvgvVFQFAEYQLFEQTIEkdiifgpvsmgVSKEEAKKRaakyielvgLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 144 aERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDlshQHQVFAKVKEFAQYHRIG--VVAVLHDLN 221
Cdd:PRK13651 160 -QRSPFELSGGQKRRVALAGILAM---------EPDFLVFDEPTAGLD---PQGVKEILEIFDNLNKQGktIILVTHDLD 226
|
250
....*....|....*..
gi 1579913621 222 LAAQYGDRALLLKQGKV 238
Cdd:PRK13651 227 NVLEWTKRTIFFKDGKI 243
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-218 |
2.21e-16 |
|
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: 74.50 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsglQLSGVRAVM--PQ 101
Cdd:cd03223 5 NLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------GMPEGEDLLflPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 102 SIYLdfpflvkevVQMALRSVsksnietvtlqalerfdVMHLAERnflTLSGGEKQRVHLSRVLaqleysgFHRdePRYL 181
Cdd:cd03223 72 RPYL---------PLGTLREQ-----------------LIYPWDD---VLSGGEQQRLAFARLL-------LHK--PKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEfaqyHRIGVVAVLH 218
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-238 |
2.36e-16 |
|
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: 76.04 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKP---ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsgLQLSGVR---AV 98
Cdd:cd03249 5 NVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD---LNLRWLRsqiGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLdFPFLVKEVVQMALRSVSKSNIETVTLQAL---------ERFDVMhLAERNFlTLSGGEKQRVHLSRVLAQle 169
Cdd:cd03249 82 VSQEPVL-FDGTIAENIRYGKPDATDEEVEEAAKKANihdfimslpDGYDTL-VGERGS-QLSGGQKQRIAIARALLR-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFaqyhRIG--VVAVLHDLNlAAQYGDRALLLKQGKV 238
Cdd:cd03249 157 -------NPKILLLDEATSALDAESEKLVQEALDRA----MKGrtTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-191 |
2.91e-16 |
|
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: 75.31 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGeLLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVRAV-- 98
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRRRig 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 -MPQSIYLDFPFLVKEVV--QMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:cd03264 76 yLPQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG-------- 147
|
170
....*....|....*.
gi 1579913621 176 dEPRYLFLDECTSSLD 191
Cdd:cd03264 148 -DPSILIVDEPTAGLD 162
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-257 |
3.25e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSgLQLSGVRAV-- 98
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP-LHARARRGIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQ--SIYLDFPFLVKEVVQMALR-SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:PRK10895 83 LPQeaSIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVfAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSY 255
Cdd:PRK10895 155 -NPKFILLDEPFAGVDPISVIDI-KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
..
gi 1579913621 256 VY 257
Cdd:PRK10895 233 VY 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-238 |
4.00e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 15 ISGEDMLQATNLSLAFDNKP-----ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG------------------DYS 71
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGlikskygtiqvgdiyigdKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 72 GYDGKVMLNFKNIKDFSGLQlsgvRAVmpqSIYLDFP--FLVKEVVQ-------MALrSVSKSNIETVTLQALERfdvMH 142
Cdd:PRK13631 96 NHELITNPYSKKIKNFKELR----RRV---SMVFQFPeyQLFKDTIEkdimfgpVAL-GVKKSEAKKLAKFYLNK---MG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 143 LA----ERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLH 218
Cdd:PRK13631 165 LDdsylERSPFGLSGGQKRRVAIAGILAI---------QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITH 234
|
250 260
....*....|....*....|
gi 1579913621 219 DLNLAAQYGDRALLLKQGKV 238
Cdd:PRK13631 235 TMEHVLEVADEVIVMDKGKI 254
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-191 |
4.07e-16 |
|
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: 74.95 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglqLSGVRAVMP 100
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSIylDFPFLVKE-------VVQMALRSVSKSNIEtvtlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgf 173
Cdd:cd03268 76 ALI--EAPGFYPNltarenlRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALL------- 142
|
170
....*....|....*...
gi 1579913621 174 hrDEPRYLFLDECTSSLD 191
Cdd:cd03268 143 --GNPDLLILDEPTNGLD 158
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-240 |
4.66e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDN----KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYL------DFPFLvkEVVQMALRsVSKSNIETVTLQALERFDVMHLAERNF---LTLSGGEKQRVHLSRVLA 166
Cdd:PRK11629 85 RNQKLGFIYQfhhllpDFTAL--ENVAMPLL-IGKKKPAEINSRALEMLAAVGLEHRANhrpSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 167 qleysgfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYgDRALLLKQGKVQA 240
Cdd:PRK11629 162 ---------NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-240 |
4.71e-16 |
|
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: 74.84 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 40 SLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKnikDFSGLQLSGvRAVmpQSIYLD---FPFLVKE--- 113
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPAD-RPV--SMLFQEnnlFAHLTVEqnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 114 ----VVQMALRSVSKSNIETvtlqALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPrYLFLDECTSS 189
Cdd:cd03298 92 glglSPGLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLV--------RDKP-VLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 190 LDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-191 |
5.86e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG---DYSG---YDGKVmLNFKNIKDF------ 87
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGilaPDSGevlWDGEP-LDPEDRRRIgylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 88 SGL--QLSgvraVMPQSIYLdfpflvkevvqMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHL-SRV 164
Cdd:COG4152 80 RGLypKMK----VGEQLVYL-----------ARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLiAAL 144
|
170 180
....*....|....*....|....*..
gi 1579913621 165 LaqleysgfHrdEPRYLFLDECTSSLD 191
Cdd:COG4152 145 L--------H--DPELLILDEPFSGLD 161
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-191 |
8.52e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.88 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG----DysgyDGKVMLNFKNIKDFSGLQ 91
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlerpT----SGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVR---AVMPQSiyldFPFL----VKEVVQMALR--SVSKSNIEtvtlqalERfdVMHLAERNFLT---------LSG 153
Cdd:COG1135 77 LRAARrkiGMIFQH----FNLLssrtVAENVALPLEiaGVPKAEIR-------KR--VAELLELVGLSdkadaypsqLSG 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 1579913621 154 GEKQRVHLSRVLAqleysgfhrDEPRYLFLDECTSSLD 191
Cdd:COG1135 144 GQKQRVGIARALA---------NNPKVLLCDEATSALD 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
33-240 |
8.83e-16 |
|
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: 74.68 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLN----FKNIKDFsglqLSGVRAVMPQSIYL--D 106
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvpWKRRKKF----LRRIGVVFGQKTQLwwD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 107 FP-----FLVKEVVQMALRSVsKSNIETVTlQALERFDVMHLAERNfltLSGGEKQRVHLSRVLaqleysgFHrdEPRYL 181
Cdd:cd03267 110 LPvidsfYLLAAIYDLPPARF-KKRLDELS-ELLDLEELLDTPVRQ---LSLGQRMRAEIAAAL-------LH--EPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-251 |
9.24e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlSGVRAVMpQSiY 104
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RGVGMVF-QS-Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LDFPFL-VKEVVQ--MALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYL 181
Cdd:PRK11000 85 ALYPHLsVAENMSfgLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA---------EPSVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 182 FLDECTSSLD--LSHQHQVfakvkEFAQYH-RIG--VVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVY---QNR 251
Cdd:PRK11000 156 LLDEPLSNLDaaLRVQMRI-----EISRLHkRLGrtMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYhypANR 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-250 |
1.02e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIK------------ 85
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 86 DFSGLQLSGVRAVMP-QSIYLDFPFLVKEVVQMA---LRSVSKSNIETVTLQALERFDVMHLAERNF-LTLSGGEKQRVH 160
Cdd:PRK10619 83 DKNQLRLLRTRLTMVfQHFNLWSHMTVLENVMEApiqVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 161 LSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVaVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:PRK10619 163 IARALAM---------EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEE 232
|
250
....*....|
gi 1579913621 241 LNKIEKVYQN 250
Cdd:PRK10619 233 EGAPEQLFGN 242
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-240 |
1.44e-15 |
|
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: 76.33 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAF--DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSgvRAV 98
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG--RHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 --MPQSIYLdFPFLVKEvvqmalrsvsksNI--------ETVtLQALERFDV----MHLAE-------RNFLTLSGGEKQ 157
Cdd:COG4618 409 gyLPQDVEL-FDGTIAE------------NIarfgdadpEKV-VAAAKLAGVhemiLRLPDgydtrigEGGARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 158 RVHLSRVLaqleysgFHRdePRYLFLDECTSSLD------LShqhQVFAKVKEfaqyHRIGVVAVLHDLNLAAQyGDRAL 231
Cdd:COG4618 475 RIGLARAL-------YGD--PRLVVLDEPNSNLDdegeaaLA---AAIRALKA----RGATVVVITHRPSLLAA-VDKLL 537
|
....*....
gi 1579913621 232 LLKQGKVQA 240
Cdd:COG4618 538 VLRDGRVQA 546
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-238 |
1.47e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPIldNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlsgvravM 99
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLD----FPFL-VKEVVQMALRSVSKsnietvtLQALERFDVMHLAERNFLT---------LSGGEKQRVHLSRVL 165
Cdd:PRK10771 72 PVSMLFQennlFSHLtVAQNIGLGLNPGLK-------LNAAQREKLHAIARQMGIEdllarlpgqLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 166 AqleysgfhRDEPrYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK10771 145 V--------REQP-ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-250 |
1.51e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSS---LLNCLTGDYSGYDGKVM-----LNFKNIKDFSglQLSGVRAVMPqsiy 104
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITvdgitLTAKTVWDIR--EKVGIVFQNP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 lDFPFL---VKEVVQMAL--RSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPR 179
Cdd:PRK13640 94 -DNQFVgatVGDDVAFGLenRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV---------EPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 180 YLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKVQALNKIEKVYQN 250
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-250 |
1.86e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.36 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSL---LNCLTGDYSGY--------DGKVMLNFKNIKDFSg 89
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFlrtLNRMNDKVSGYrysgdvllGGRSIFNYRDVLEFR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 lQLSGVRAVMPQSiyldFPFLV-----------KEVVQMALRSVSKSNIETVTLqalerFDVM--HLAERNFlTLSGGEK 156
Cdd:PRK14271 101 -RRVGMLFQRPNP----FPMSImdnvlagvrahKLVPRKEFRGVAQARLTEVGL-----WDAVkdRLSDSPF-RLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 157 QRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyhRIGVVAVLHDLNLAAQYGDRALLLKQG 236
Cdd:PRK14271 170 QLLCLARTLAV---------NPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDG 238
|
250
....*....|....
gi 1579913621 237 KVQALNKIEKVYQN 250
Cdd:PRK14271 239 RLVEEGPTEQLFSS 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-250 |
1.87e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLT--GDYS---GYDGKVMLNFKNI----KDFS 88
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNpevTITGSIVYNGHNIysprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 89 GLQLS-GVRAVMPQSiyldFPFLVKEVVQMALR-------SVSKSNIETVTLQAL---ERFDVMHlaeRNFLTLSGGEKQ 157
Cdd:PRK14239 83 DLRKEiGMVFQQPNP----FPMSIYENVVYGLRlkgikdkQVLDEAVEKSLKGASiwdEVKDRLH---DSALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 158 RVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD-LSHqhqvfAKVKE--FAQYHRIGVVAVLHDLNLAAQYGDRALLLK 234
Cdd:PRK14239 156 RVCIARVLAT---------SPKIILLDEPTSALDpISA-----GKIEEtlLGLKDDYTMLLVTRSMQQASRISDRTGFFL 221
|
250
....*....|....*.
gi 1579913621 235 QGKVQALNKIEKVYQN 250
Cdd:PRK14239 222 DGDLIEYNDTKQMFMN 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-238 |
1.88e-15 |
|
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: 75.88 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDN----KPILDNISLDVEAGELLCILGPNGAGKS----SLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQ 91
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVRAvmpQSIYLDF--------PFL-----VKEVvqMAL-RSVSKSNIETVTLQALERFDVMHLAERnfLT-----LS 152
Cdd:COG4172 86 LRRIRG---NRIAMIFqepmtslnPLHtigkqIAEV--LRLhRGLSGAAARARALELLERVGIPDPERR--LDayphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 153 GGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALL 232
Cdd:COG4172 159 GGQRQRVMIAMALAN---------EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
....*.
gi 1579913621 233 LKQGKV 238
Cdd:COG4172 230 MRQGEI 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
35-255 |
2.53e-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: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 35 ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY---SGY---DGKV--MLNFKnikdfSGLQ--LSGVravmpQSIY 104
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILeptSGRvevNGRVsaLLELG-----AGFHpeLTGR-----ENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LdfpflvkevvQMALRSVSKSNIEtvtlqalERFD-VMHLAE-RNFL-----TLSGGEKQRVHLSrVLAQLeysgfhrdE 177
Cdd:COG1134 111 L----------NGRLLGLSRKEID-------EKFDeIVEFAElGDFIdqpvkTYSSGMRARLAFA-VATAV--------D 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKV---YQNRLLS 254
Cdd:COG1134 165 PDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEViaaYEALLAG 243
|
.
gi 1579913621 255 Y 255
Cdd:COG1134 244 R 244
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-238 |
2.65e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLL---NCLTGDYSGydgkvMLNFKNIK-DFS-GLQLSGV 95
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLETPDSG-----QLNIAGHQfDFSqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RA-------VMPQsiYLDFPFLVkeVVQ------MALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLS 162
Cdd:COG4161 78 RLlrqkvgmVFQQ--YNLWPHLT--VMEnlieapCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 163 RVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHrIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG4161 154 RALMM---------EPQVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
36-265 |
3.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML--------NFKNIKDFSGLQLSGVRAVMPQSIyldf 107
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnnqaitddNFEKLRKHIGIVFQNPDNQFVGSI---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 108 pflVKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDE 185
Cdd:PRK13648 101 ---VKYDVAFGLEnhAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL---------NPSVIILDE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 186 CTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKVQALNKIEKVY--QNRLLSYVYD--FPV 261
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFdhAEELTRIGLDlpFPI 247
|
....
gi 1579913621 262 EIMQ 265
Cdd:PRK13648 248 KINQ 251
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-222 |
3.63e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.06 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSgY---DGKVMLNFKNIKDFS-------GL 90
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPS-YevtSGTILFKGQDLLELEpderaraGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 QLSgvrAVMPQSIyldfPFL-VKEVVQMALRSVSKSNIETvTLQALERFDVMH-----------LAERNFLT-LSGGEKQ 157
Cdd:TIGR01978 80 FLA---FQYPEEI----PGVsNLEFLRSALNARRSARGEE-PLDLLDFEKLLKeklalldmdeeFLNRSVNEgFSGGEKK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 158 RVHLSRvLAQLeysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNL 222
Cdd:TIGR01978 152 RNEILQ-MALL--------EPKLAILDEIDSGLDIDALKIVAEGINRLREPDR-SFLIITHYQRL 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-238 |
4.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAFDN------KPILDNISLDVEAGELLCILGPNGAGKSSL---LNCL------TGDYSGYDGKVMLNF 81
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALlipsegKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 82 KNIKDFSGLQLSGVRAVMPQSIyldfpflVKEVVQMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRV 159
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATI-------VEEDVAFGPENlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 160 HLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:PRK13633 154 AIAGILAM---------RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-249 |
4.48e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKS----SLLNCLtgDYSGYD---GKVMLNFKN--- 83
Cdd:PRK10261 10 RDVLAVENLNIAFMQEqqkiAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQAGGLvqcDKMLLRRRSrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 84 --IKDFSGLQLSGVRAVMPQSIY------LDFPFLVKEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNFL------ 149
Cdd:PRK10261 88 ieLSEQSAAQMRHVRGADMAMIFqepmtsLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsryph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 150 TLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDR 229
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSC---------RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
250 260
....*....|....*....|
gi 1579913621 230 ALLLKQGKVQALNKIEKVYQ 249
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFH 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
8-218 |
4.54e-15 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 74.79 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 8 QSSRLVKISGEdmLQATNLSLAFDNKPI--------LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML 79
Cdd:TIGR00954 434 RNSNLVPGRGI--VEYQDNGIKFENIPLvtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 80 NFKNiKDFSGLQ--LSGVRAVMPQSIYLDFPFlvkevvQMALRSVSKSNIEtvtlQALERFDVMHLAERN---------F 148
Cdd:TIGR00954 512 PAKG-KLFYVPQrpYMTLGTLRDQIIYPDSSE------DMKRRGLSDKDLE----QILDNVQLTHILEREggwsavqdwM 580
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 149 LTLSGGEKQRVHLSRVLaqleysgFHRdePRYLFLDECTSSLDLSHQHQVFAKVKEFaqyhRIGVVAVLH 218
Cdd:TIGR00954 581 DVLSGGEKQRIAMARLF-------YHK--PQFAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-261 |
4.83e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFD-NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML--------NFKNIKDFSGL 90
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitkeNIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 QLSGVR-AVMPQSIYLDFPFlvkEVVQMALrsvSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQle 169
Cdd:PRK13652 83 VFQNPDdQIFSPTVEQDIAF---GPINLGL---DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVY- 248
Cdd:PRK13652 155 -------EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFl 227
|
250
....*....|....
gi 1579913621 249 QNRLLSYVY-DFPV 261
Cdd:PRK13652 228 QPDLLARVHlDLPS 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-238 |
8.39e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMlnfknikdfSG-LQLSGVRA-- 97
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---------AGtAPLAEAREdt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 -VMPQSIYLdFPFlvkevvqmalrsvsKSNIETVTL--------QALERFDVMHLAERNF---LTLSGGEKQRVHLSRVL 165
Cdd:PRK11247 84 rLMFQDARL-LPW--------------KKVIDNVGLglkgqwrdAALQALAAVGLADRANewpAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 166 aqleysgFHRdePRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK11247 149 -------IHR--PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-203 |
8.97e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 24 TNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVrAVMPQSI 103
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARI-GVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YLDFPFLVKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDEPRYL 181
Cdd:PRK13536 124 NLDLEFTVRENLLVFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI---------NDPQLL 194
|
170 180
....*....|....*....|..
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVK 203
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLR 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-218 |
1.16e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfsglqlSGVRA 97
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------FGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 VMPQSIYLDFPFlvkevvqmalrsvsksnietvtLQALERFDVMHLAE-----RNFLTLSGGEKQRVHLSRVLAQleysg 172
Cdd:COG2401 101 SLIDAIGRKGDF----------------------KDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAE----- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLH 218
Cdd:COG2401 154 ----RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
32-191 |
1.58e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.13 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFsglQLSGVR---AVMPQSIYLDFP 108
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLRnqvALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 FLVKEVVQMALRSVSKSNIETVTLQA--------LER-FDVMhLAErNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPr 179
Cdd:PRK11176 432 TIANNIAYARTEQYSREQIEEAARMAyamdfinkMDNgLDTV-IGE-NGVLLSGGQRQRIAIARALL--------RDSP- 500
|
170
....*....|..
gi 1579913621 180 YLFLDECTSSLD 191
Cdd:PRK11176 501 ILILDEATSALD 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-220 |
1.72e-14 |
|
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: 72.89 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGEL-----LCILGPNGAGKSSLLNCLTG----DYSGYDGKVMLNFKnikdfsglqlsgvravmPQSIYLD 106
Cdd:COG1245 351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGvlkpDEGEVDEDLKISYK-----------------PQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 107 FPFLVKEVvqmaLRSVSKSNIETVTLQA--LERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPRYLfLD 184
Cdd:COG1245 414 YDGTVEEF----LRSANTDDFGSSYYKTeiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLS--------RDADLYL-LD 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 1579913621 185 ECTSSLDLSHQHQVfAKV-KEFAQYHRIGVVAVLHDL 220
Cdd:COG1245 481 EPSAHLDVEQRLAV-AKAiRRFAENRGKTAMVVDHDI 516
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-231 |
2.61e-14 |
|
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: 70.51 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAG-----ELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkdfsglqlsgvrAVMPQSIYLDFPFL 110
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVQMALRSV-SKSNIETVTLQALERFDVMhlaERNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPRYLfLDECTSS 189
Cdd:cd03237 78 VRDLLSSITKDFyTHPYFKTEIAKPLQIEQIL---DREVPELSGGELQRVAIAACLS--------KDADIYL-LDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1579913621 190 LDlSHQHQVFAKV-KEFAQYHRIGVVAVLHDLNLAAQYGDRAL 231
Cdd:cd03237 146 LD-VEQRLMASKViRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-238 |
3.11e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG---------DYSGYDGKVmlnfkniKDFSGL 90
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArlapdagevHYRMRDGQL-------RDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 QLSGVRAVMPQsiylDFPFlVKEVVQMALR-SVSK-SNIEtvtlqalERfdVMHLAERNF-------------------- 148
Cdd:PRK11701 79 SEAERRRLLRT----EWGF-VHQHPRDGLRmQVSAgGNIG-------ER--LMAVGARHYgdiratagdwlerveidaar 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 149 -----LTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLA 223
Cdd:PRK11701 145 iddlpTTFSGGMQQRLQIARNLVT---------HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA 215
|
250
....*....|....*
gi 1579913621 224 AQYGDRALLLKQGKV 238
Cdd:PRK11701 216 RLLAHRLLVMKQGRV 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-240 |
3.62e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfSGLQLSGVrAVMPQSIYLD--FPFLVKE 113
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKNLV-AYVPQSEEVDwsFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 114 VVQMA-------LRSVSKSNIETVTlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDEC 186
Cdd:PRK15056 100 VVMMGryghmgwLRRAKKRDRQIVT-AALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ---------QGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 187 TSSLDLSHQHQVFAKVKEFAQYHRIGVVAVlHDLNLAAQYGDRALLLKqGKVQA 240
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVST-HNLGSVTEFCDYTVMVK-GTVLA 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-191 |
3.88e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.37 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNK----PILDNISLDVEAGELLCILGPNGAGKSSLLNCL------TGdysgydGKVMLNFKNIKDFSG 89
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCInllerpTS------GRVLVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 LQLSGVRavmpQS---IYLDFPFL----VKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVH 160
Cdd:PRK11153 75 KELRKAR----RQigmIFQHFNLLssrtVFDNVALPLElaGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190
....*....|....*....|....*....|.
gi 1579913621 161 LSRVLAqleysgfhrDEPRYLFLDECTSSLD 191
Cdd:PRK11153 151 IARALA---------SNPKVLLCDEATSALD 172
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-236 |
4.35e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 70.66 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAfdNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKniKDFSglqlSGV 95
Cdd:cd03291 35 SDDNNLFFSNLCLV--GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFS----SQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYLDFPFLVkEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNfLTLSGGEKQRVHLSRVLaqleysgfHR 175
Cdd:cd03291 107 SWIMPGTIKENIIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGG-ITLSGGQRARISLARAV--------YK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 176 DEPRYLfLDECTSSLDLSHQHQVFAK--VKEFAQYHRIGVVAVLHDLNLAaqygDRALLLKQG 236
Cdd:cd03291 177 DADLYL-LDSPFGYLDVFTEKEIFEScvCKLMANKTRILVTSKMEHLKKA----DKILILHEG 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-191 |
5.38e-14 |
|
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: 71.39 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDN--------KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSglQL 92
Cdd:COG5265 351 LVVGGGEVRFENvsfgydpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT--QA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SgVRA---VMPQ-------SIYLDFPF--------LVKEVVQMAlrsvsksnietvtlqALERFdVMHL--------AER 146
Cdd:COG5265 429 S-LRAaigIVPQdtvlfndTIAYNIAYgrpdaseeEVEAAARAA---------------QIHDF-IESLpdgydtrvGER 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1579913621 147 NfLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD 191
Cdd:COG5265 492 G-LKLSGGEKQRVAIARTLLK---------NPPILIFDEATSALD 526
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-258 |
5.58e-14 |
|
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: 69.44 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSIYLdFPFL 110
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL-FNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVQMALRSVSKSNIETVT---------LQALERFDVMhLAERNfLTLSGGEKQRVHLSRVLaqleysgFHRdePRYL 181
Cdd:cd03252 92 IRDNIALADPGMSMERVIEAAklagahdfiSELPEGYDTI-VGEQG-AGLSGGQRQRIAIARAL-------IHN--PRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNlAAQYGDRALLLKQGK-VQALNKIEKVYQNRLLSYVYD 258
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIA--HRLS-TVKNADRIIVMEKGRiVEQGSHDELLAENGLYAYLYQ 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-262 |
6.10e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLT--GDYSG---YDGKVMLNFKNIKD----FSGL- 90
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmNELESevrVEGRVEFFNQNIYErrvnLNRLr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 -QLSGVRA---VMPQSIYLDFPFLVKEVVQMAlrSVSKSNIETVTLQALERFD-VMHLAERNFLTLSGGEKQRVHLSRVL 165
Cdd:PRK14258 88 rQVSMVHPkpnLFPMSVYDNVAYGVKIVGWRP--KLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 166 AQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKvqalNKIE 245
Cdd:PRK14258 166 AV---------KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE----NRIG 232
|
250
....*....|....*..
gi 1579913621 246 KVYQNRLLSYVYDFPVE 262
Cdd:PRK14258 233 QLVEFGLTKKIFNSPHD 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-238 |
1.09e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.50 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDN----KPILDNISLDVEAGELLCILGPNGAGKS----SLLNCLTGDYSGY-DGKVMLNFKNIKDFSGL 90
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 91 QLSGVR----AVMPQSIYLDFPFL------VKEVVQMAlRSVSKSNIETVTLQALERFDVMHLAERnfLT-----LSGGE 155
Cdd:PRK15134 85 TLRGVRgnkiAMIFQEPMVSLNPLhtlekqLYEVLSLH-RGMRREAARGEILNCLDRVGIRQAAKR--LTdyphqLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 156 KQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQ 235
Cdd:PRK15134 162 RQRVMIAMALLT---------RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
...
gi 1579913621 236 GKV 238
Cdd:PRK15134 233 GRC 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-251 |
1.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.09 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTG---------DYSGYDGKVMLNFKNIKD----------FSGLQLSGvR 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAllkpssgtiTIAGYHITPETGNKNLKKlrkkvslvfqFPEAQLFE-N 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 AVMPQSIY--LDFPFLVKEVVQMALRSVSKSNIETvtlqalerfdvmHLAERNFLTLSGGEKQRVHLSRVLAqleysgfh 174
Cdd:PRK13641 102 TVLKDVEFgpKNFGFSEDEAKEKALKWLKKVGLSE------------DLISKSPFELSGGQMRRVAIAGVMA-------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 175 rDEPRYLFLDECTSSLDLSHQHQVFakvKEFAQYHRIG--VVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNR 251
Cdd:PRK13641 162 -YEPEILCLDEPAAGLDPEGRKEMM---QLFKDYQKAGhtVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-250 |
1.50e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQL-SGVRAVMPQSIYldFPFL 110
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLhRQVALVGQEPVL--FSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVQMALRSVSKSNIETVTLQALERFDVMHLaERNFLT--------LSGGEKQRVHLSRVLAQleysgfhrdEPRYLF 182
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEF-PNGYDTevgekgsqLSGGQKQRIAIARALVR---------KPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 183 LDECTSSLDLSHQhQVFAKVKEFAQyhrIGVVAVLHDLNLaAQYGDRALLLKQGKVQALNKIEKVYQN 250
Cdd:TIGR00958 641 LDEATSALDAECE-QLLQESRSRAS---RTVLLIAHRLST-VERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-236 |
2.23e-13 |
|
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: 69.94 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAFdnKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsglQLSGV 95
Cdd:TIGR01271 424 NGDDGLFFSNFSLYV--TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYLdFPFLVKEVVQMAL-------RSVSKSNIETVTLQALERFDVMHLAERNfLTLSGGEKQRVHLSRVLaql 168
Cdd:TIGR01271 489 ISFSPQTSWI-MPGTIKDNIIFGLsydeyryTSVIKACQLEEDIALFPEKDKTVLGEGG-ITLSGGQRARISLARAV--- 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 169 eysgfHRDEPRYLfLDECTSSLDLSHQHQVFAK--VKEFAQYHRIGVVAVLHDLNLAaqygDRALLLKQG 236
Cdd:TIGR01271 564 -----YKDADLYL-LDSPFTHLDVVTEKEIFESclCKLMSNKTRILVTSKLEHLKKA----DKILLLHEG 623
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
51-253 |
2.30e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 51 ILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglqlsgvravMPQSIYLD---------------FP-FLVKEV 114
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD------------AEKGICLPpekrrigyvfqdarlFPhYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 115 VQMALRSVSKSNIET-VTLQALErfdvmHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLS 193
Cdd:PRK11144 97 LRYGMAKSMVAQFDKiVALLGIE-----PLLDRYPGSLSGGEKQRVAIGRALLT---------APELLLMDEPLASLDLP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 194 HQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLL 253
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-238 |
2.99e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGY------DGKVMLNFKNIKDFSG 89
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskikvDGKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 LQLSGVRAVMPQ--------SIYLDFPFLVKEVVQMALRSVSKSNIETVTLQAL--ERFDVMHLAERNfltLSGGEKQRV 159
Cdd:PRK14246 86 IKLRKEVGMVFQqpnpfphlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkEVYDRLNSPASQ---LSGGQQQRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 160 HLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyhRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK14246 163 TIARALAL---------KPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-235 |
3.76e-13 |
|
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: 66.75 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsGLQLSGVRAVMP 100
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN--------GGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSI-YLDFPFLVKEV--VQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDE 177
Cdd:cd03231 73 RGLlYLGHAPGIKTTlsVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLL---------SG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLaAQYGDRALLLKQ 235
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGL-SEAGARELDLGF 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-223 |
3.81e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.61 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGL---------Q 91
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphenilylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVRAVMPQSIYLDFpflVKEVVQMALRSVSksnietvtlQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleys 171
Cdd:TIGR01189 81 LPGLKPELSALENLHF---WAAIHGGAQRTIE---------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWL----- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 172 gfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLA 223
Cdd:TIGR01189 144 ----SRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-77 |
4.90e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 4.90e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKV 77
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-238 |
5.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKP---ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLS--- 93
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 94 GVRAVMPQSIYLDFPFLVKEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgf 173
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL------ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 174 hrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:PRK13642 158 ---RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-192 |
5.03e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 67.12 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLNFKNIKDFSGLQLSGvra 97
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 vmpQSIYLDFPFLV-------KEVVQMALRSVSKSNietvTLQALERFDVMHLAER---------NFLT------LSGGE 155
Cdd:PRK09580 78 ---EGIFMAFQYPVeipgvsnQFFLQTALNAVRSYR----GQEPLDRFDFQDLMEEkiallkmpeDLLTrsvnvgFSGGE 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1579913621 156 KQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDL 192
Cdd:PRK09580 151 KKRNDILQMAVL---------EPELCILDESDSGLDI 178
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-239 |
6.79e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 35 ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRA----VMPQSIYLDFPFL 110
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkhvgFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVVQMA--LRSVSKSNIETvtlQALERFDVMHLAER-NFL--TLSGGEKQRVHLSRVlaqleYSGfhrdEPRYLFLDE 185
Cdd:PRK10584 105 ALENVELPalLRGESSRQSRN---GAKALLEQLGLGKRlDHLpaQLSGGEQQRVALARA-----FNG----RPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 186 CTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYgDRALLLKQGKVQ 239
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARC-DRRLRLVNGQLQ 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-240 |
6.91e-13 |
|
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: 66.24 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKP----ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLN-FKNIKDFSGLQ--- 91
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgFDVVKEPAEARrrl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 --LSGVRAVMPQsiyldfpFLVKEVVQM--ALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLaq 167
Cdd:cd03266 81 gfVSDSTGLYDR-------LTARENLEYfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL-- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 168 leysgFHRdePRYLFLDECTSSLDlshqhqVFAK--VKEFAQYHRIGVVAVL---HDLNLAAQYGDRALLLKQGKVQA 240
Cdd:cd03266 152 -----VHD--PPVLLLDEPTTGLD------VMATraLREFIRQLRALGKCILfstHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-238 |
6.93e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQ-LSGVRAV 98
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 99 MPQSIYLDFPFLVKEVVQMALRSVSKSNIETVTLQALERFDvmHLAERNFL---TLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFP--RLHERRIQragTMSGGEQQMLAIGRALMS-------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK11614 155 -QPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
38-240 |
7.83e-13 |
|
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: 67.43 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 38 NISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfsG--LQLSGVRAVMP----------QSIYL 105
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG--------GevLQDSARGIFLPphrrrigyvfQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 106 dFPFL-VKEVVQMALRSVSKSNiETVTL-QALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFL 183
Cdd:COG4148 89 -FPHLsVRGNLLYGRKRAPRAE-RRISFdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLS---------SPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 184 DECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQA 240
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-250 |
9.68e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNC---LTGDYSGY--DGKVMLNFKNIKDfSGLQL 92
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFrvEGKVTFHGKNLYA-PDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SGVRAVM----------PQSIYLDFPFLVK---------EVVQMALRsvsksnietvtlQALERFDVMHLAERNFLTLSG 153
Cdd:PRK14243 87 VEVRRRIgmvfqkpnpfPKSIYDNIAYGARingykgdmdELVERSLR------------QAALWDEVKDKLKQSGLSLSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 154 GEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgvVAVLHDLNLAAQYGDRALLL 233
Cdd:PRK14243 155 GQQQRLCIARAIAV---------QPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFF 223
|
250 260
....*....|....*....|....*.
gi 1579913621 234 ---------KQGKVQALNKIEKVYQN 250
Cdd:PRK14243 224 nveltegggRYGYLVEFDRTEKIFNS 249
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
33-238 |
9.92e-13 |
|
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: 65.59 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkdfSGLQLSGVR---AVMPQSiyldfPF 109
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI---SKIGLHDLRsriSIIPQD-----PV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 110 LVKEVVQMALRSVSKSNIETVtLQALERfdvMHLAER--------------NFLTLSGGEKQRVHLSRVLAQleysgfhr 175
Cdd:cd03244 89 LFSGTIRSNLDPFGEYSDEEL-WQALER---VGLKEFveslpggldtvveeGGENLSVGQRQLLCLARALLR-------- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFAKVKE-FAQYhriGVVAVLHDLNLAAQYgDRALLLKQGKV 238
Cdd:cd03244 157 -KSKILVLDEATASVDPETDALIQKTIREaFKDC---TVLTIAHRLDTIIDS-DRILVLDKGRV 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-219 |
1.24e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfKNIKdfsglqlsgvRAVMPQSIYLDFPFLV 111
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMALRSVsksnietvtLQALERFDVMHL------AERNFL------------------------------------ 149
Cdd:TIGR03719 86 RENVEEGVAEI---------KDALDRFNEISAkyaepdADFDKLaaeqaelqeiidaadawdldsqleiamdalrcppwd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 150 ----TLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLshqhQVFAKVKEFAQYHRIGVVAVLHD 219
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLS---------KPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-238 |
2.05e-12 |
|
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: 64.86 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY---SGY---DGKV--MLNFKnikdfSGLQ--LSGVravmpQS 102
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYppdSGTvtvRGRVssLLGLG-----GGFNpeLTGR-----EN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 103 IYLDfpflvkevvqMALRSVSKSNI-----ETVTLQALERFDVMHLaernfLTLSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:cd03220 105 IYLN----------GRLLGLSRKEIdekidEIIEFSELGDFIDLPV-----KTYSSGMKARLAFAIATAL---------E 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
35-255 |
2.18e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 35 ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSiyldfPFLVKEV 114
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD-----PVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 115 VQMALRSVSKSNIETV----TLQALERFDVMHLAERNFLTLSGGE------KQRVHLSRVLAQleysgfhrdEPRYLFLD 184
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVwwalELAHLKTFVSALPDKLDHECAEGGEnlsvgqRQLVCLARALLR---------KTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 185 ECTSSLDLSHQHQVFAKVKefAQYHRIGVVAVLHDLNLAAQYgDRALLLKQGKVQALNKIEKVYQNRLLSY 255
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-238 |
2.93e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAF-----------DNKPILDNISLDVEAGELLCILGPNGAGKSS----LLNCLTGDysgydGKVMLNFKNI 84
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 85 KDFSGLQLSGVRAVMpQSIYLD-----FPFL-VKEVVQMALR----SVSKSNIETVTLQALERF----DVMHLAERNFlt 150
Cdd:PRK15134 350 HNLNRRQLLPVRHRI-QVVFQDpnsslNPRLnVLQIIEEGLRvhqpTLSAAQREQQVIAVMEEVgldpETRHRYPAEF-- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 151 lSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRA 230
Cdd:PRK15134 427 -SGGQRQRIAIARALIL---------KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQV 496
|
....*...
gi 1579913621 231 LLLKQGKV 238
Cdd:PRK15134 497 IVLRQGEV 504
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-203 |
3.18e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.60 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVrAVMP 100
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 101 QSIYLDFPFLVKEVVQMALR--SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDEP 178
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV---------NDP 157
|
170 180
....*....|....*....|....*
gi 1579913621 179 RYLFLDECTSSLDLSHQHQVFAKVK 203
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLR 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-238 |
3.35e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 34 PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSiyldfPFLVKE 113
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 114 VVQMALRSVSKSNiETVTLQALERFDVMHLAERNFLTL-----SGGEK----QRVHLSRVLAQLEYSgfhrdepRYLFLD 184
Cdd:PLN03232 1325 TVRFNIDPFSEHN-DADLWEALERAHIKDVIDRNPFGLdaevsEGGENfsvgQRQLLSLARALLRRS-------KILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 185 ECTSSLDLSHQHQVFAKVKEfaQYHRIGVVAVLHDLNLAAQYgDRALLLKQGKV 238
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDC-DKILVLSSGQV 1447
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
32-220 |
4.12e-12 |
|
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: 63.89 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNiKDFSGLQLSGVRAVMPQSIYLDFPFLV 111
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN-ESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMAL-------RSVSKSNIETVTLQA----LERFDVMHLAERNfLTLSGGEKQRVHLSRVLAQleysgfhrdEPRY 180
Cdd:cd03290 92 NATVEENItfgspfnKQRYKAVTDACSLQPdidlLPFGDQTEIGERG-INLSGGQRQRICVARALYQ---------NTNI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1579913621 181 LFLDECTSSLDLS-HQHQVFAKVKEFAQYHRIGVVAVLHDL 220
Cdd:cd03290 162 VFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKL 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-231 |
4.19e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGEL-----LCILGPNGAGKSSLLNCLTGDysgydgkvmlnfknIKDFSGLQLSGVR-AVMPQSIYLDFPf 109
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGV--------------LKPDEGEVDPELKiSYKPQYIKPDYD- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 110 lvkEVVQMALRSVsKSNIETVTLQA--LERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPRYLfLDECT 187
Cdd:PRK13409 415 ---GTVEDLLRSI-TDDLGSSYYKSeiIKPLQLERLLDKNVKDLSGGELQRVAIAACLS--------RDADLYL-LDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1579913621 188 SSLDLSHQHQVfAKV-KEFAQYHRIGVVAVLHDLNLAAQYGDRAL 231
Cdd:PRK13409 482 AHLDVEQRLAV-AKAiRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-238 |
4.38e-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: 63.59 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAF--DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkdfSGLQLSGVR---AVM 99
Cdd:cd03369 11 NLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRsslTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSiyldfPFLVKEVVqmalrsvsKSNIETVTLQA-LERFDVMHLAERNfLTLSGGEKQRVHLSRVLAQleysgfhrdEP 178
Cdd:cd03369 88 PQD-----PTLFSGTI--------RSNLDPFDEYSdEEIYGALRVSEGG-LNLSQGQRQLLCLARALLK---------RP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 179 RYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNLAAQYgDRALLLKQGKV 238
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIA--HRLRTIIDY-DKILVMDAGEV 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
43-220 |
1.14e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 43 VEAGELLCILGPNGAGKSSLLNCLTG-------DYSG----------YDGKVMLNFknikdFSGLQLSGVRAVM-PQsiY 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgDYEEepswdevlkrFRGTELQNY-----FKKLYNGEIKVVHkPQ--Y 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LDF-PFLVKEVVQMALRSVSKSNietVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPRYLFl 183
Cdd:PRK13409 169 VDLiPKVFKGKVRELLKKVDERG---KLDEVVERLGLENILDRDISELSGGELQRVAIAAALL--------RDADFYFF- 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 1579913621 184 DECTSSLDLSHQHQVFAKVKEFAQYHRigVVAVLHDL 220
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKY--VLVVEHDL 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-253 |
1.15e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGkvmlnfknikdfSGLQLSGVRAVMPQSIYLdFPFLVK 112
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET------------SSVVIRGSVAYVPQVSWI-FNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 113 EVVQMALRSVSKSNIETVTLQALER-------FDVMHLAERNfLTLSGGEKQRVHLSRvlaqleysGFHRDEPRYLFlDE 185
Cdd:PLN03232 697 ENILFGSDFESERYWRAIDVTALQHdldllpgRDLTEIGERG-VNISGGQKQRVSMAR--------AVYSNSDIYIF-DD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 186 CTSSLDLSHQHQVFAKV--KEFAQYHRIGVVAVLHDLNLAaqygDRALLLKQGKVQALNKIEKVYQNRLL 253
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCmkDELKGKTRVLVTNQLHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-238 |
1.33e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.21 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFDNK-PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSglqLSGVRavmpQSI 103
Cdd:PRK13657 339 DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR----RNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YLdfpflvkeVVQMAL---RSVSKsNI----ETVT----LQALERFDVMHLAERN---FLT--------LSGGEKQRVHL 161
Cdd:PRK13657 412 AV--------VFQDAGlfnRSIED-NIrvgrPDATdeemRAAAERAQAHDFIERKpdgYDTvvgergrqLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 162 SRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNLAAQyGDRALLLKQGKV 238
Cdd:PRK13657 483 ARALLK---------DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIA--HRLSTVRN-ADRILVFDNGRV 547
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-238 |
1.51e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.35 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMlnFKNIKdFSGLQLSGVR---AVMPQSiyldfP 108
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIR--FHDIP-LTKLQLDSWRsrlAVVSQT-----P 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 FLVKEVV--QMAL--RSVSKSNIETVTLQALERFDVMHL--------AERNFLtLSGGEKQRVHLSRVLAQleysgfhrd 176
Cdd:PRK10789 399 FLFSDTVanNIALgrPDATQQEIEHVARLASVHDDILRLpqgydtevGERGVM-LSGGQKQRISIARALLL--------- 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 177 EPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAvlHDLNlAAQYGDRALLLKQGKV 238
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISA--HRLS-ALTEASEILVMQHGHI 527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-254 |
1.72e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLT-----GDYSG---YDGKVmLNFKNIKDfsg 89
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphGTYEGeiiFEGEE-LQASNIRD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 90 LQLSGVR------AVMPQSIYLDFPFLVKEVVQMALRSVSKSNIETVTLQALERFD------VMHlaernfltLSGGEKQ 157
Cdd:PRK13549 79 TERAGIAiihqelALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDinpatpVGN--------LGLGQQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 158 RVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFaQYHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:PRK13549 151 LVEIAKALNK---------QARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
250
....*....|....*..
gi 1579913621 238 VQALNKIEKVYQNRLLS 254
Cdd:PRK13549 221 HIGTRPAAGMTEDDIIT 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-249 |
1.84e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 30 FDNKPILDnISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfkNIKDFSGLQLSGVRAVMPQ----SIYL 105
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-----TVGDIVVSSTSKQKEIKPVrkkvGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 106 DFP--FLVKEVVQMALR------SVSKSNIETVTLQALERFDV-MHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrd 176
Cdd:PRK13643 91 QFPesQLFEETVLKDVAfgpqnfGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAM--------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 177 EPRYLFLDECTSSLDLSHQHQVfakVKEFAQYHRIG--VVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEM---MQLFESIHQSGqtVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-85 |
1.97e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.97e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIK 85
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR 66
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-237 |
2.42e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.58 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAF-DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQL-SGVRAVMPQS 102
Cdd:PRK10790 345 NVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLrQGVAMVQQDP 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 103 IYLDFPFLVKevVQMAlRSVSKSNI----ETVTLQALERF--DVMH--LAERNFlTLSGGEKQRVHLSRVLAQLeysgfh 174
Cdd:PRK10790 425 VVLADTFLAN--VTLG-RDISEEQVwqalETVQLAELARSlpDGLYtpLGEQGN-NLSVGQKQLLALARVLVQT------ 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 175 rdePRYLFLDECTSSLDLSHQH---QVFAKVKEFAQY----HRIGVVA------VLHDLNLAAQYGDRALLLKQGK 237
Cdd:PRK10790 495 ---PQILILDEATANIDSGTEQaiqQALAAVREHTTLvviaHRLSTIVeadtilVLHRGQAVEQGTHQQLLAAQGR 567
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
36-238 |
2.69e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY---SG---YDGKVmLNFKNIKDfsGLQLsGVraVMpqsIYLDF-- 107
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqpdSGeilIDGKP-VRIRSPRD--AIAL-GI--GM---VHQHFml 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 108 --PFLVKEVVQMALRSVSKSNIetvTLQALERfDVMHLAERNFL---------TLSGGEKQRVHLSRVLAQleysgfhrd 176
Cdd:COG3845 92 vpNLTVAENIVLGLEPTKGGRL---DRKAARA-RIRELSERYGLdvdpdakveDLSVGEQQRVEILKALYR--------- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 177 EPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-237 |
3.95e-11 |
|
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: 62.92 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY--SGYDGKVMlnfknikdFSG--LQLSGV 95
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIY--------WSGspLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 R--------------AVMPQSIYLDFPFLVKEVVQMALRsvskSNIETVTLQALE-----RFDVMHLAeRNFLTLSGGEK 156
Cdd:TIGR02633 73 RdteragiviihqelTLVPELSVAENIFLGNEITLPGGR----MAYNAMYLRAKNllrelQLDADNVT-RPVGDYGGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 157 QRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQG 236
Cdd:TIGR02633 148 QLVEIAKALNK---------QARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDG 217
|
.
gi 1579913621 237 K 237
Cdd:TIGR02633 218 Q 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-240 |
4.21e-11 |
|
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: 62.92 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSlAFD--NKPI--LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSG-YDGKVMLNFKNIKDFSGLQ 91
Cdd:TIGR02633 254 GDVILEARNLT-CWDviNPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGkFEGNVFINGKPVDIRNPAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 L--SGVrAVMPQSIYLD--FPFLV--KEVVQMALRSVSKSNI------ETVTLQALERFDVMhlAERNFL---TLSGGEK 156
Cdd:TIGR02633 333 AirAGI-AMVPEDRKRHgiVPILGvgKNITLSVLKSFCFKMRidaaaeLQIIGSAIQRLKVK--TASPFLpigRLSGGNQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 157 QRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRALLLKQG 236
Cdd:TIGR02633 410 QKAVLAKMLLT---------NPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
....
gi 1579913621 237 KVQA 240
Cdd:TIGR02633 480 KLKG 483
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-192 |
4.58e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLNFKNIKDFSGLQLSgvra 97
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERA---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 vmPQSIYLDFPFLVK-------EVVQMALRSVSKSNiETVTLQALERFDVM-----------HLAERN----FltlSGGE 155
Cdd:CHL00131 83 --HLGIFLAFQYPIEipgvsnaDFLRLAYNSKRKFQ-GLPELDPLEFLEIIneklklvgmdpSFLSRNvnegF---SGGE 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1579913621 156 KQRVHLSRvLAQLeysgfhrdEPRYLFLDECTSSLDL 192
Cdd:CHL00131 157 KKRNEILQ-MALL--------DSELAILDETDSGLDI 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-191 |
5.08e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 24 TNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfKNIKdFSGLQLSGVRAVmPQSI 103
Cdd:PRK11147 7 HGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI-VARLQQDPPRNV-EGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YlDFpflVKEVVQ----------MALRSV----SKSNI-ETVTLQA-LERFDVMHL--------------AERNFLTLSG 153
Cdd:PRK11147 84 Y-DF---VAEGIEeqaeylkryhDISHLVetdpSEKNLnELAKLQEqLDHHNLWQLenrinevlaqlgldPDAALSSLSG 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1579913621 154 GEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD 191
Cdd:PRK11147 160 GWLRKAALGRALVS---------NPDVLLLDEPTNHLD 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
36-238 |
5.53e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQsIYLDFPFLVKEVV 115
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGM-IFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 116 ------QMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhrDEPRYLFLDECTSS 189
Cdd:PRK10908 97 ydnvaiPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV---------NKPAVLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 190 LDLSHQHQVFakvKEFAQYHRIGVVAVL--HDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK10908 168 LDDALSEGIL---RLFEEFNRVGVTVLMatHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-238 |
6.79e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLS-LAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGdYSGYDGKVMLNfkNIkDFSGLQLSGVR--- 96
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIN--GI-ELRELDPESWRkhl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 AVMPQSIYLdFPFLVKEVVQMALRSVSKSNIEtvtlQALERFDVMHLAER-----------NFLTLSGGEKQRVHLSRVL 165
Cdd:PRK11174 426 SWVGQNPQL-PHGTLRDNVLLGNPDASDEQLQ----QALENAWVSEFLPLlpqgldtpigdQAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 166 AQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRigVVAVLHDLNLAAQYgDRALLLKQGKV 238
Cdd:PRK11174 501 LQ---------PCQLLLLDEPTASLDAHSEQLVMQALNAASRRQT--TLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-220 |
7.44e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.11 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 44 EAGELLCILGPNGAGKSSLLNCLTG-------DYSG----------YDGKVMLN-FKNIKDfsglqlSGVRAVM-PQSIY 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgDYDEepswdevlkrFRGTELQDyFKKLAN------GEIKVAHkPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 105 LdFPFLVKEVVQMALRSVSKSNietVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhRDEPRYLFlD 184
Cdd:COG1245 171 L-IPKVFKGTVRELLEKVDERG---KLDELAEKLGLENILDRDISELSGGELQRVAIAAALL--------RDADFYFF-D 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 1579913621 185 ECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDL 220
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEEGKY-VLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-220 |
7.45e-11 |
|
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: 60.84 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 43 VEAGELLCILGPNGAGKSSLLNCLTGdysgydgKVMLNFKN----------IKDFSGLQLS---------GVRAVM-PQs 102
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAG-------KLKPNLGKfddppdwdeiLDEFRGSELQnyftkllegDVKVIVkPQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 103 iYLDfpfLVKEVVQMALRSVSKSNIETVTLQAL-ERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYL 181
Cdd:cd03236 95 -YVD---LIPKAVKGKVGELLKKKDERGKLDELvDQLELRHVLDRNIDQLSGGELQRVAIAAALAR---------DADFY 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDL 220
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDL 199
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-250 |
7.95e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGY-----DGKVMLNFKNIKDFSGLQLSGv 95
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMPQSIYLDFPFL-VKEVVQMALR----SVSKSNIETVTLQALERF----DVMHLAERNFLTLSGGEKQRVHLSRVLA 166
Cdd:PRK14247 83 RVQMVFQIPNPIPNLsIFENVALGLKlnrlVKSKKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 167 qleysgFhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyhRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEK 246
Cdd:PRK14247 163 ------F---QPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....
gi 1579913621 247 VYQN 250
Cdd:PRK14247 232 VFTN 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-238 |
9.14e-11 |
|
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: 61.62 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 2 ALVAA--TQSSRLVKISGEDMLQATNLSLAFdnkPI--------------LDNISLDVEAGELLCILGPNGAGKSSL--- 62
Cdd:COG4172 255 KLLAAepRGDPRPVPPDAPPLLEARDLKVWF---PIkrglfrrtvghvkaVDGVSLTLRRGETLGLVGESGSGKSTLgla 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 63 -LNCLtgdysGYDGKVMLNFKNIKDFSGLQLSGVRAVMpQSIYLDfPF-------LVKEVVQMALR----SVSKSNIETV 130
Cdd:COG4172 332 lLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRM-QVVFQD-PFgslsprmTVGQIIAEGLRvhgpGLSAAERRAR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 131 TLQALER----FDVMHlaeR---NFltlSGGEKQRVHLSRVLAqLEysgfhrdePRYLFLDECTSSLDLSHQHQVFAKVK 203
Cdd:COG4172 405 VAEALEEvgldPAARH---RyphEF---SGGQRQRIAIARALI-LE--------PKLLVLDEPTSALDVSVQAQILDLLR 469
|
250 260 270
....*....|....*....|....*....|....*
gi 1579913621 204 EFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:COG4172 470 DLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-207 |
1.23e-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: 59.58 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 30 FDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGY---DGKVMLNFKNIKDFSGLQLSgvravmpQSIYld 106
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG-------EIIY-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 107 fpflvkeVVQmalrsvSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDEC 186
Cdd:cd03233 88 -------VSE------EDVHFPTLTVRETLDFALRCKGNEFVRGISGGERKRVSIAEALVS---------RASVLCWDNS 145
|
170 180
....*....|....*....|.
gi 1579913621 187 TSSLDLSHQHQVFAKVKEFAQ 207
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMAD 166
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
37-255 |
1.51e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 37 DNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMpQSIYLDfPF------- 109
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDI-QMIFQD-PLaslnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 110 LVKEVVQMALRS----VSKSNIEtvtlqalERFDVM--------HLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:PRK15079 116 TIGEIIAEPLRTyhpkLSRQEVK-------DRVKAMmlkvgllpNLINRYPHEFSGGQCQRIGIARALIL---------E 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLSY 255
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-240 |
1.89e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSlAFD----NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSG-YDGKVMLNFKNIKdfsglq 91
Cdd:PRK13549 256 GEVILEVRNLT-AWDpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGrWEGEIFIDGKPVK------ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVRAVMPQSIYldfpfLVKE-------VVQMalrSVSKsNIetvTLQALERFDVMHL----AE----RNFLT------ 150
Cdd:PRK13549 329 IRNPQQAIAQGIA-----MVPEdrkrdgiVPVM---GVGK-NI---TLAALDRFTGGSRiddaAElktiLESIQrlkvkt 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 151 ---------LSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHrIGVVAVLHDLN 221
Cdd:PRK13549 397 aspelaiarLSGGNQQKAVLAKCLLL---------NPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELP 466
|
250
....*....|....*....
gi 1579913621 222 LAAQYGDRALLLKQGKVQA 240
Cdd:PRK13549 467 EVLGLSDRVLVMHEGKLKG 485
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-178 |
1.96e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVMP---QSIYLDFPFLVKEVVQMALR---SVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqLE 169
Cdd:PRK11831 83 RKRMSmlfQSGALFTDMNVFDNVAYPLRehtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA-LE 161
|
....*....
gi 1579913621 170 YSGFHRDEP 178
Cdd:PRK11831 162 PDLIMFDEP 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-238 |
2.18e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 58.21 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLafdnKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQL--SG 94
Cdd:cd03215 1 GEPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAirAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 VRAVmP-----QSIYLDFPflVKEvvqmalrsvsksNIetvtlqALERFdvmhlaernfltLSGGEKQRVHLSRVLAQle 169
Cdd:cd03215 77 IAYV-PedrkrEGLVLDLS--VAE------------NI------ALSSL------------LSGGNQQKVVLARWLAR-- 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 170 ysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDL----NLAaqygDRALLLKQGKV 238
Cdd:cd03215 122 -------DPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELdellGLC----DRILVMYEGRI 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-238 |
2.57e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 13 VKISGEDMLQATNLSLAFDN----KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSG---YDGKVMLNFKNIk 85
Cdd:TIGR00955 14 VAQDGSWKQLVSRLRGCFCRerprKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 86 dfsGLQLSGVRAVMPQSIYLDFPFL-VKEVVQ-MAL----RSVSKSN----IETVtLQALERFDVMHL---AERNFLTLS 152
Cdd:TIGR00955 93 ---DAKEMRAISAYVQQDDLFIPTLtVREHLMfQAHlrmpRRVTKKEkrerVDEV-LQALGLRKCANTrigVPGRVKGLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 153 GGEKQRVHL-SRVLAqleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNlAAQYG--DR 229
Cdd:TIGR00955 169 GGERKRLAFaSELLT----------DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKT-IICTIHQPS-SELFElfDK 236
|
....*....
gi 1579913621 230 ALLLKQGKV 238
Cdd:TIGR00955 237 IILMAEGRV 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
36-86 |
2.62e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 2.62e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTG-----DYSG---YDGKVMlNFKNIKD 86
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgSYEGeilFDGEVC-RFKDIRD 74
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-247 |
3.10e-10 |
|
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: 60.20 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 1 MALVAATQSSRLVKIsGEDMLQATNLS---LAFDNKPI--LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDG 75
Cdd:TIGR03269 261 MEGVSEVEKECEVEV-GEPIIKVRNVSkryISVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 76 KV---------------MLNFKNIKDFSGL-----QLSGVRAV---MPQSIYLDFPF-LVKEVVQMALRSVSKSNIETVT 131
Cdd:TIGR03269 340 EVnvrvgdewvdmtkpgPDGRGRAKRYIGIlhqeyDLYPHRTVldnLTEAIGLELPDeLARMKAVITLKMVGFDEEKAEE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 132 LqaLERFDVmhlaernflTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD----LSHQHQVFAKVKEFAQ 207
Cdd:TIGR03269 420 I--LDKYPD---------ELSEGERHRVALAQVLIK---------EPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ 479
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1579913621 208 YHRIgvvaVLHDLNLAAQYGDRALLLKQGKVQALNKIEKV 247
Cdd:TIGR03269 480 TFII----VSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
36-265 |
3.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLL------------NCLTGDYsgydgKVMLNFKNIKDFSGLQlsgvravmpQSI 103
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIqltngliisetgQTIVGDY-----AIPANLKKIKEVKRLR---------KEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YLDFPF----LVKEVVQ--MALRSVS-KSNIETVTLQALERFDVMHL----AERNFLTLSGGEKQRVHLSRVLAQleysg 172
Cdd:PRK13645 93 GLVFQFpeyqLFQETIEkdIAFGPVNlGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAM----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 173 fhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQN-R 251
Cdd:PRK13645 168 ----DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNqE 243
|
250
....*....|....
gi 1579913621 252 LLSYVYDFPVEIMQ 265
Cdd:PRK13645 244 LLTKIEIDPPKLYQ 257
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-250 |
6.65e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 19 DMLQATNLSLAFDnKPILDNISLDVEAGELLCILGPNGAGKS----SLLNCLTGDYSGYDGKVMLNFKNIkdfSGLQLSG 94
Cdd:PRK10418 3 QQIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 --VRAVM--PQSIYldfpflvKEVVQMA------LRSVSKSNIETVTLQALERF---DVMHLAERNFLTLSGGEKQRVHL 161
Cdd:PRK10418 79 rkIATIMqnPRSAF-------NPLHTMHtharetCLALGKPADDATLTAALEAVgleNAARVLKLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 162 SrvLAQLEYSGFhrdepryLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQAL 241
Cdd:PRK10418 152 A--LALLCEAPF-------IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
....*....
gi 1579913621 242 NKIEKVYQN 250
Cdd:PRK10418 223 GDVETLFNA 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-191 |
7.28e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfknikdfSGLQLSGVr 96
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-------ETVKLAYV- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 avmPQS-IYLDFPFLVKEVVQMALRSVSKSNIETVTLQALERFdvmhlaerNFL---------TLSGGEKQRVHLSRVLA 166
Cdd:TIGR03719 391 ---DQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRF--------NFKgsdqqkkvgQLSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....*
gi 1579913621 167 QleysgfhrdEPRYLFLDECTSSLD 191
Cdd:TIGR03719 460 S---------GGNVLLLDEPTNDLD 475
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
36-269 |
9.15e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTG----DysgyDGKVMLN----FKNIKDFsgLQLSGVraVMPQ--SIYL 105
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilvpT----SGEVRVLgyvpFKRRKEF--ARRIGV--VFGQrsQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 106 DFPF-----LVKEVVQMAlRSVSKSNIETVTlqalERFDVMHLAERNFLTLSGGEKQRVHLsrvLAQLeysgFHRdePRY 180
Cdd:COG4586 110 DLPAidsfrLLKAIYRIP-DAEYKKRLDELV----ELLDLGELLDTPVRQLSLGQRMRCEL---AAAL----LHR--PKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 181 LFLDECTSSLDLSHQhqvfAKVKEF-AQYHRIGVVAVL---HDLN----LAaqygDRALLLKQGKVQ---ALNKIEKVYQ 249
Cdd:COG4586 176 LFLDEPTIGLDVVSK----EAIREFlKEYNRERGTTILltsHDMDdieaLC----DRVIVIDHGRIIydgSLEELKERFG 247
|
250 260
....*....|....*....|.
gi 1579913621 250 N-RLLSYVYDFPVEIMQHPKG 269
Cdd:COG4586 248 PyKTIVLELAEPVPPLELPRG 268
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
30-251 |
1.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.72 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 30 FDNKPILDnISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML------NFKNIKDFSGLQlsgvRAVmpqSI 103
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLR----KKV---GI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 104 YLDFP--FLVKEVVQMALrSVSKSNIETVTLQALERFDVM--------HLAERNFLTLSGGEKQRVHLSRVLAQleysgf 173
Cdd:PRK13634 90 VFQFPehQLFEETVEKDI-CFGPMNFGVSEEDAKQKAREMielvglpeELLARSPFELSGGQMRRVAIAGVLAM------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 174 hrdEPRYLFLDECTSSLDLSHQHQVfakVKEFAQYHR---IGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQN 250
Cdd:PRK13634 163 ---EPEVLVLDEPTAGLDPKGRKEM---MEMFYKLHKekgLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
.
gi 1579913621 251 R 251
Cdd:PRK13634 237 P 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
36-238 |
1.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfkNIKDFSGLQLSGVRAVMpQSIYLDFPF----LV 111
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD--DITITHKTKDKYIRPVR-KRIGMVFQFpesqLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMALRSVSKS---NIETVTLQAlerFDV-MHLA-ERNFLTLS-----GGEKQRVHLSRVLAQleysgfhrdEPRYL 181
Cdd:PRK13646 100 EDTVEREIIFGPKNfkmNLDEVKNYA---HRLlMDLGfSRDVMSQSpfqmsGGQMRKIAIVSILAM---------NPDII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 182 FLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-79 |
1.88e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.88e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 30 FDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY-SGYDGKVML 79
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTL 320
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-253 |
2.19e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNfKNIK--DFSGLQLSGVRA 97
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA-KGIKlgYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 vmPQSIYLDFPFLVKEVVQMALRSVSKS---NIETVTlQALERFdvmhlaernfltlSGGEKQRVHLSRVLAQleysgfh 174
Cdd:PRK10636 391 --DESPLQHLARLAPQELEQKLRDYLGGfgfQGDKVT-EETRRF-------------SGGEKARLVLALIVWQ------- 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 175 rdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyhriGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLL 253
Cdd:PRK10636 448 --RPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLS 520
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-239 |
2.28e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGY-DGKVMLNfknikdfsglqlsGVRAVMPQSIYLdFPFLV 111
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIR-------------GTVAYVPQVSWI-FNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMALRSVSKSNIETVTLQALER-------FDVMHLAERNfLTLSGGEKQRVHLSRVLaqleYSgfhrDEPRYLFlD 184
Cdd:PLN03130 696 RDNILFGSPFDPERYERAIDVTALQHdldllpgGDLTEIGERG-VNISGGQKQRVSMARAV----YS----NSDVYIF-D 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1579913621 185 ECTSSLDLSHQHQVFAKV--KEFAQYHRIGVVAVLHDLNlaaqYGDRALLLKQGKVQ 239
Cdd:PLN03130 766 DPLSALDAHVGRQVFDKCikDELRGKTRVLVTNQLHFLS----QVDRIILVHEGMIK 818
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-254 |
2.55e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLN-----FKNIKDFSGlqlSGVrAVMPQSIYLDFPFL 110
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrFASTTAALA---AGV-AIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 111 VKEVV---QMALRS--VSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAqleysgfhRDePRYLFLDE 185
Cdd:PRK11288 96 VAENLylgQLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA--------RN-ARVIAFDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 186 CTSSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQG-KVQALNKIEKVYQNRLLS 254
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGrYVATFDDMAQVDRDQLVQ 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-249 |
3.95e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.29 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPI----LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGdYSGYDGKVM---LNFKN-----IKDF 87
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMaekLEFNGqdlqrISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 88 SGLQLSGVRAVMpqsIYLDfP-------FLVKEVVQMALRSVSKSNIETVTLQALE------------RFDVM-Hlaern 147
Cdd:PRK11022 82 ERRNLVGAEVAM---IFQD-PmtslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDllnqvgipdpasRLDVYpH----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 148 flTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYG 227
Cdd:PRK11022 153 --QLSGGMSQRVMIAMAIAC---------RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAA 221
|
250 260
....*....|....*....|..
gi 1579913621 228 DRALLLKQGKVQALNKIEKVYQ 249
Cdd:PRK11022 222 HKIIVMYAGQVVETGKAHDIFR 243
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-219 |
4.17e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG---DYSGyDGKVMLNFKnikdfsglqlsgvRAVMPQSIYLDFP 108
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkEFEG-EARPAPGIK-------------VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 FLVKEVVQMALRSVsksnietvtLQALERFDVMH------------LAER-----------------NFL---------- 149
Cdd:PRK11819 85 KTVRENVEEGVAEV---------KAALDRFNEIYaayaepdadfdaLAAEqgelqeiidaadawdldSQLeiamdalrcp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 150 -------TLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD------LsHQHqvfakvkeFAQYHriG-VVA 215
Cdd:PRK11819 156 pwdakvtKLSGGERRRVALCRLLLE---------KPDMLLLDEPTNHLDaesvawL-EQF--------LHDYP--GtVVA 215
|
....
gi 1579913621 216 VLHD 219
Cdd:PRK11819 216 VTHD 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-249 |
4.77e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.91 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 34 PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS-GLQLSGVRavmpQSIYLDFPF--- 109
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIR----KKVGLVFQFpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 110 -LVKEVVqmaLRSVS-------KSNIETVTLqALERFDVMHLAE----RNFLTLSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:PRK13649 97 qLFEETV---LKDVAfgpqnfgVSQEEAEAL-AREKLALVGISEslfeKNPFELSGGQMRRVAIAGILAM---------E 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVfakVKEFAQYHRIG--VVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQ 249
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKEL---MTLFKKLHQSGmtIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-202 |
6.27e-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: 56.49 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 29 AFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsglQLSGVRAVMPQSIYLDFP 108
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 FLVKEVV------QMALRSVSKSNIETVTLQALERFDVMHLAERNfLTLSGGEKQRVHLSRVLaqleYSgfhrDEPRYLF 182
Cdd:TIGR00957 714 SLRENILfgkalnEKYYQQVLEACALLPDLEILPSGDRTEIGEKG-VNLSGGQKQRVSLARAV----YS----NADIYLF 784
|
170 180
....*....|....*....|
gi 1579913621 183 lDECTSSLDLSHQHQVFAKV 202
Cdd:TIGR00957 785 -DDPLSAVDAHVGKHIFEHV 803
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-185 |
6.52e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 16 SGEDMLQATNLSLafdnKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKdfsglqLSGV 95
Cdd:COG1129 252 PGEVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAVM-------P-----QSIYLDFPflVKE-VVQMALRSVSKSNI------ETVTLQALERFDV-MHLAERNFLTLSGGE 155
Cdd:COG1129 322 RDAIragiayvPedrkgEGLVLDLS--IREnITLASLDRLSRGGLldrrreRALAEEYIKRLRIkTPSPEQPVGNLSGGN 399
|
170 180 190
....*....|....*....|....*....|
gi 1579913621 156 KQRVHLSRVLAQleysgfhrdEPRYLFLDE 185
Cdd:COG1129 400 QQKVVLAKWLAT---------DPKVLILDE 420
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-238 |
1.37e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 10 SRLVKISGEDMLQATNLS-LAFDNkpildnISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFS 88
Cdd:PRK15439 258 NRRQQAAGAPVLTVEDLTgEGFRN------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 89 -------GL-------QLSGvravmpqsIYLDFPF------LVKEVVQMALRSVSKSNIetvtlqaLERFdvmHLA---- 144
Cdd:PRK15439 332 taqrlarGLvylpedrQSSG--------LYLDAPLawnvcaLTHNRRGFWIKPARENAV-------LERY---RRAlnik 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 145 ----ERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHrigvVAVL--- 217
Cdd:PRK15439 394 fnhaEQAARTLSGGNQQKVLIAKCLEA---------SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN----VAVLfis 460
|
250 260
....*....|....*....|.
gi 1579913621 218 HDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK15439 461 SDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-217 |
1.54e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNI-KDFSGLQL------ 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKqlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 --SGVRA--VMPQSIYLDFPFlvkevvqmalrsvSKSNIETVTLQALerFDVMHLAERNFLTLSGGEKQRVHLSRvlaqL 168
Cdd:PRK13540 81 hrSGINPylTLRENCLYDIHF-------------SPGAVGITELCRL--FSLEHLIDYPCGLLSSGQKRQVALLR----L 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1579913621 169 EYSGfhrdePRYLFLDECTSSLDLSHQHQVFAKVKEfaqyHRIGVVAVL 217
Cdd:PRK13540 142 WMSK-----AKLWLLDEPLVALDELSLLTIITKIQE----HRAKGGAVL 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-245 |
2.14e-08 |
|
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: 55.02 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 19 DMLQATNLSLAFD--NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVR 96
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 AVM---PQSIYLDFPFLVKEVVQM--ALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRvhLSRVLAQLEYs 171
Cdd:TIGR01257 2012 QNMgycPQFDAIDDLLTGREHLYLyaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRK--LSTAIALIGC- 2088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 172 gfhrdePRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIE 245
Cdd:TIGR01257 2089 ------PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-238 |
2.75e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkdfsgLQLSGVRA-- 97
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-----ARLTPAKAhq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 ----VMPQSIYLdFPFL-VKE--VVQMALRSVSKSNIETVtLQALE-RFDVMHLAErnflTLSGGEKQRVHLSRvlaqle 169
Cdd:PRK15439 86 lgiyLVPQEPLL-FPNLsVKEniLFGLPKRQASMQKMKQL-LAALGcQLDLDSSAG----SLEVADRQIVEILR------ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 170 ysGFHRDEpRYLFLDECTSSLDLSHQHQVFAKVKEFaQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:PRK15439 154 --GLMRDS-RILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-236 |
4.57e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNI-----KDFSGLQL 92
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkldhKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 93 SGVR---AVMPQSIYLDFPF----LVKEVvqMALRSVSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVL 165
Cdd:PRK09700 83 GIIYqelSVIDELTVLENLYigrhLTKKV--CGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 166 AQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQG 236
Cdd:PRK09700 161 ML---------DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-246 |
5.18e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 40 SLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAV--------MPQSIYLDFPFLV 111
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMALRSvsksniETVTLQALERFDVMHLAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD 191
Cdd:PRK10938 103 AEIIQDEVKD------PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMS---------EPDLLILDEPFDGLD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 192 -------------LSHQHQV-------FAKVKEFAQYhrigvVAVLHDLNLAAQyGDRALLLKQGKVQALNKIEK 246
Cdd:PRK10938 168 vasrqqlaellasLHQSGITlvlvlnrFDEIPDFVQF-----AGVLADCTLAET-GEREEILQQALVAQLAHSEQ 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-237 |
7.94e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSG------YDGKVMlNFKNIKDFsglQ 91
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdagsilYLGKEV-TFNGPKSS---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 92 LSGVRAV------MPQSIYLDFPFLVKEVV-QMALRSVSKSNIETVTLqaLERFDVMHLAERNFLTLSGGEKQRVHLSRV 164
Cdd:PRK10762 78 EAGIGIIhqelnlIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKL--LARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 165 LAqleysgFhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:PRK10762 156 LS------F---ESKVIIMDEPTDALTDTETESLFRVIRELKSQGR-GIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-237 |
1.27e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 30 FDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDY--SGYDGKVMLNFKNIKDfSGLQLSGVRA---------- 97
Cdd:PLN03211 78 IQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTK-QILKRTGFVTqddilyphlt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 98 VMPQSIYLDFPFLVKEVVQMALRSVSKSNIETVTLQALERFDVMHLAERNfltLSGGEKQRVHLSRVLAQleysgfhrdE 177
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG---ISGGERKRVSIAHEMLI---------N 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGK 237
Cdd:PLN03211 225 PSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-250 |
1.35e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 34 PILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQLSGVRAVMPQSiyldfPFLVKE 113
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-----PVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 114 VVQMALRSVSKSNiETVTLQALERFDVMHLAERNFLTL-----SGGEK----QRVHLSRVLAQLEYSgfhrdepRYLFLD 184
Cdd:PLN03130 1328 TVRFNLDPFNEHN-DADLWESLERAHLKDVIRRNSLGLdaevsEAGENfsvgQRQLLSLARALLRRS-------KILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 185 ECTSSLDLSHQHQVFAKVKEfaQYHRIGVVAVLHDLNLAAQyGDRALLLKQGKVQALNKIEKVYQN 250
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-167 |
1.42e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAFDN-KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQL--S 93
Cdd:COG3845 254 GEVVLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 94 GVRAVmPQ-----SIYLDFPflVKEvvQMALRS-----------VSKSNIETVTLQALERFDVM----HLAERNfltLSG 153
Cdd:COG3845 334 GVAYI-PEdrlgrGLVPDMS--VAE--NLILGRyrrppfsrggfLDRKAIRAFAEELIEEFDVRtpgpDTPARS---LSG 405
|
170
....*....|....
gi 1579913621 154 GEKQRVHLSRVLAQ 167
Cdd:COG3845 406 GNQQKVILARELSR 419
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-86 |
1.68e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1579913621 24 TNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML-----NFKNIKD 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqgkeiDFKSSKE 69
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-275 |
2.62e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 15 ISGEDMLQATNLSLAFDNKPIL-----------DNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKN 83
Cdd:PRK10261 308 VDGEPILQVRNLVTRFPLRSGLlnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 84 IKDFSGLQLSGVRAVMpQSIYLDfPFLVKEVVQmalrSVSKSNIETVTLQAL-----ERFDVMHLAERNFL--------- 149
Cdd:PRK10261 388 IDTLSPGKLQALRRDI-QFIFQD-PYASLDPRQ----TVGDSIMEPLRVHGLlpgkaAAARVAWLLERVGLlpehawryp 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 150 -TLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGD 228
Cdd:PRK10261 462 hEFSGGQRQRICIARALAL---------NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISH 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1579913621 229 RALLLKQGKVQALNKIEKVYQN-------RLLSYVydfPVEIMQHPKGWPLVVS 275
Cdd:PRK10261 533 RVAVMYLGQIVEIGPRRAVFENpqhpytrKLMAAV---PVADPSRQRPQRVLLS 583
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-191 |
3.06e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsglqlsgvr 96
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI------------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 avmpqsiyldfpfLVKEVVQMALRSVSKSNIE---TVTLQALERFDVMHLAER-----------NFL---------TLSG 153
Cdd:PRK11819 382 -------------KIGETVKLAYVDQSRDALDpnkTVWEEISGGLDIIKVGNReipsrayvgrfNFKggdqqkkvgVLSG 448
|
170 180 190
....*....|....*....|....*....|....*...
gi 1579913621 154 GEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD 191
Cdd:PRK11819 449 GERNRLHLAKTLKQ---------GGNVLLLDEPTNDLD 477
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
35-238 |
3.57e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.88 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 35 ILDNISLDVEAGELLCILGPNGAGKSSLLN---CLTGDYSgydGKVMLNFKNIKDFSGLQLSGVRAVmpqsiylDFPFLV 111
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNilgCLDKPTS---GTYRVAGQDVATLDADALAQLRRE-------HFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 KEVVQMALRSVSKsNIETVTLQA-------LER----FDVMHLAERNFL---TLSGGEKQRVHLSRVLAqleysgfhrDE 177
Cdd:PRK10535 93 QRYHLLSHLTAAQ-NVEVPAVYAglerkqrLLRaqelLQRLGLEDRVEYqpsQLSGGQQQRVSIARALM---------NG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 178 PRYLFLDECTSSLDLSHQHQVFAKVKEF-AQYHRigVVAVLHDLNLAAQyGDRALLLKQGKV 238
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLrDRGHT--VIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-238 |
4.00e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.17 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFDNKPIL---------DNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkDFS 88
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 89 GLQLSGVRAVM-----------PQSI--YLDFPFLVKEVVQMALRSvsKSNIETVTLQALERFDVMHLAErnflTLSGGE 155
Cdd:PRK15112 81 DYSYRSQRIRMifqdpstslnpRQRIsqILDFPLRLNTDLEPEQRE--KQIIETLRQVGLLPDHASYYPH----MLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 156 KQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQ 235
Cdd:PRK15112 155 KQRLGLARALIL---------RPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
...
gi 1579913621 236 GKV 238
Cdd:PRK15112 226 GEV 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-250 |
4.01e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.84 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 21 LQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLT-----GDYSGYDGKVMLNFKNIKDFSGLQLSGV 95
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 RAV-MPQSIYLDFPFL-VKEVVQMALR----SVSKSNIETVTLQALERF----DVMHLAERNFLTLSGGEKQRVHLSRVL 165
Cdd:PRK14267 85 REVgMVFQYPNPFPHLtIYDNVAIGVKlnglVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 166 AQleysgfhrdEPRYLFLDECTSSLDLSHQhqvfAKVKE--FAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNK 243
Cdd:PRK14267 165 AM---------KPKILLMDEPTANIDPVGT----AKIEEllFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
....*..
gi 1579913621 244 IEKVYQN 250
Cdd:PRK14267 232 TRKVFEN 238
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-191 |
4.68e-07 |
|
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: 49.16 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 31 DNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG--DYSGYDGKVMLNFKNIKDfsglqlsgvravmpqsiylDFP 108
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDK-------------------NFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 FLVKEVVQMALRSVSKSNIETVTLQALERfdvmhlaernflTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTS 188
Cdd:cd03232 79 RSTGYVEQQDVHSPNLTVREALRFSALLR------------GLSVEQRKRLTIGVELAA---------KPSILFLDEPTS 137
|
...
gi 1579913621 189 SLD 191
Cdd:cd03232 138 GLD 140
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-248 |
7.48e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 18 EDMLQATNLSLAFD----NKPILDNISLDVEAGELLCILGPNGAGKSS-------LL--NCLTGDYSGYDGKVMLNFKNi 84
Cdd:PRK09473 10 DALLDVKDLRVTFStpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLaaNGRIGGSATFNGREILNLPE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 85 kdfsgLQLSGVRAVMPQSIYLD-----FPFL-VKEV---VQMALRSVSKSNI--ETVTL-------QALERfdvMHLAER 146
Cdd:PRK09473 89 -----KELNKLRAEQISMIFQDpmtslNPYMrVGEQlmeVLMLHKGMSKAEAfeESVRMldavkmpEARKR---MKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 147 NFltlSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQY 226
Cdd:PRK09473 161 EF---SGGMRQRVMIAMALLC---------RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGI 228
|
250 260
....*....|....*....|..
gi 1579913621 227 GDRALLLKQGKVQALNKIEKVY 248
Cdd:PRK09473 229 CDKVLVMYAGRTMEYGNARDVF 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-238 |
2.85e-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: 48.47 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 25 NLSLAFD--NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDfsglQLSGVRAVM--- 99
Cdd:TIGR01257 933 NLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLgmc 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 100 PQSIYLDFPFLVKEVV----QMALRSVSKSNIETVTLqaLERFDVMHLAERNFLTLSGGEKQRVHLSrvlaqLEYSGfhr 175
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHIlfyaQLKGRSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVA-----IAFVG--- 1078
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 176 dEPRYLFLDECTSSLDLSHQHQVFakvkEFAQYHRIG--VVAVLHDLNLAAQYGDRALLLKQGKV 238
Cdd:TIGR01257 1079 -DAKVVVLDEPTSGVDPYSRRSIW----DLLLKYRSGrtIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
42-191 |
3.43e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 46.88 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 42 DVEAGELLCILGPNGAGKSSLLNCLTgdYSGYdGKVmlnfknIKDFSGLQLSGVRAVMPQSIYLDFPFLVKEVVQMALRS 121
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAIT--YALY-GKT------PRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKYRVERS 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 122 VsKSNIETVTLQAL---ERFDvmHLAERNFLTLSGGEKQRVHLSRVLA---QLEYSGFHRDEprYLFLDECTSSLD 191
Cdd:cd03279 95 R-GLDYDQFTRIVLlpqGEFD--RFLARPVSTLSGGETFLASLSLALAlseVLQNRGGARLE--ALFIDEGFGTLD 165
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
36-250 |
5.21e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKN--IKDFSGL--QLSGVravmpQSIYLdfpflv 111
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAISSGLngQLTGI-----ENIEL------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 112 kEVVQMALrsvSKSNIETVTLQALERFDVMHLAERNFLTLSGGEKQRVhlsrvlaqleysGF----HRDePRYLFLDECT 187
Cdd:PRK13545 109 -KGLMMGL---TKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRL------------GFaisvHIN-PDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 188 SSLDLSHQHQVFAKVKEFAQYHRIgVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQN 250
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKT-IFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-85 |
1.04e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIK 85
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT 76
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-253 |
1.20e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAfdNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQ--LSG 94
Cdd:PRK10982 247 GEVILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEaiNHG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 VRAVMPQ----SIY--LDFPF--LVKEVVQM--ALRSVSKSNIETVTLQALERFDVMHLAERNFL-TLSGGEKQRVHLSR 163
Cdd:PRK10982 325 FALVTEErrstGIYayLDIGFnsLISNIRNYknKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVIIGR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 164 VLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRiGVVAVLHDLNLAAQYGDRALLLKQGKVQALNK 243
Cdd:PRK10982 405 WLLT---------QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVAGIVD 474
|
250
....*....|
gi 1579913621 244 IEKVYQNRLL 253
Cdd:PRK10982 475 TKTTTQNEIL 484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
32-191 |
1.43e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 32 NKPILDNISLDVEAGELLCILGPNGAGKSSLLNCL------------------TGDYSGY-----DGKVMLNFKNIKDFS 88
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehTNDMTNEqdyqgDEEQNVGMKNVNEFS 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 89 GLQLSGV---RAVMPQS--IYLD---------------FPFLVKE--VVQMALRSVSKSNIETVTLQALERFdVMHLAER 146
Cdd:PTZ00265 1260 LTKEGGSgedSTVFKNSgkILLDgvdicdynlkdlrnlFSIVSQEpmLFNMSIYENIKFGKEDATREDVKRA-CKFAAID 1338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1579913621 147 NFL----------------TLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLD 191
Cdd:PTZ00265 1339 EFIeslpnkydtnvgpygkSLSGGQKQRIAIARALLR---------EPKILLLDEATSSLD 1390
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-241 |
1.63e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 15 ISGEDMLQATNLSlAFDNKPIlDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSGLQlsg 94
Cdd:PRK09700 260 LAHETVFEVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD--- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 95 vrAVMPQSIYLD--------FP-FLVKEVVQMAlRSVSKSNI-----------ETVTLQAlERFDVM---HLAERNFLTL 151
Cdd:PRK09700 335 --AVKKGMAYITesrrdngfFPnFSIAQNMAIS-RSLKDGGYkgamglfhevdEQRTAEN-QRELLAlkcHSVNQNITEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 152 SGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGVVAVLHDLNLAAQYGDRAL 231
Cdd:PRK09700 411 SGGNQQKVLISKWLCC---------CPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIA 480
|
250
....*....|
gi 1579913621 232 LLKQGKVQAL 241
Cdd:PRK09700 481 VFCEGRLTQI 490
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-224 |
1.98e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 33 KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLtgdysGYdgKVMLNFKNIKDFSGLQLSGVRAvmpqSIYLDFPFLVK 112
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-----GL--ALGGAQSATRRRSGVKAGCIVA----AVSAELIFTRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 113 evvqmalrsvsksnietvtlqalerfdvmhlaernflTLSGGEKQRVHLSRVLAQLEysgfHRDEPRYLfLDECTSSLDL 192
Cdd:cd03227 77 -------------------------------------QLSGGEKELSALALILALAS----LKPRPLYI-LDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|..
gi 1579913621 193 SHQHQVFAKVKEFAQYHRIGVVAVlHDLNLAA 224
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVIT-HLPELAE 145
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-253 |
2.24e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 8 QSSRLVKISGEDMLQATNLSlafdnKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDF 87
Cdd:PRK10762 245 QYPRLDKAPGEVRLKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 88 S---GLQlSGVravmpqsIYldfpflVKE-------VVQMALRsvsksniETVTLQALERFD-----VMHLAER----NF 148
Cdd:PRK10762 320 SpqdGLA-NGI-------VY------ISEdrkrdglVLGMSVK-------ENMSLTALRYFSraggsLKHADEQqavsDF 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 149 LT---------------LSGGEKQRVHLSRVLAqleysgfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQyHRIGV 213
Cdd:PRK10762 379 IRlfniktpsmeqaiglLSGGNQQKVAIARGLM---------TRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSI 448
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1579913621 214 VAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLL 253
Cdd:PRK10762 449 ILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKLM 488
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-247 |
2.92e-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: 44.51 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 1 MALVAATQSSRLVKISGEdmLQATNLSLAFDN--KPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVM 78
Cdd:cd03288 2 IASISGSSNSGLVGLGGE--IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 79 LNfkNIkDFSGLQLSGVRAVMpqSIYLDFPFLVKEVVQMALRSVSKSNIETVtLQALERFDVMHLAE------------- 145
Cdd:cd03288 80 ID--GI-DISKLPLHTLRSRL--SIILQDPILFSGSIRFNLDPECKCTDDRL-WEALEIAQLKNMVKslpggldavvteg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 146 -RNFltlSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHqVFAKVKEFAQYHRIgVVAVLHDLNLAA 224
Cdd:cd03288 154 gENF---SVGQRQLFCLARAFVR---------KSSILIMDEATASIDMATEN-ILQKVVMTAFADRT-VVTIAHRVSTIL 219
|
250 260
....*....|....*....|...
gi 1579913621 225 QyGDRALLLKQGKVQALNKIEKV 247
Cdd:cd03288 220 D-ADLVLVLSRGILVECDTPENL 241
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
26-191 |
3.38e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 26 LSLAFDN-KPILDNISLDVEAGeLLCILGPNGAGKSSLLN----CLTGDYSGyDGKVMLNFKNIKDFSG-----LQLSGV 95
Cdd:COG0419 3 LRLRLENfRSYRDTETIDFDDG-LNLIVGPNGAGKSTILEairyALYGKARS-RSKLRSDLINVGSEEAsveleFEHGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 96 --RAVMPQSIYLDFPFLVKEVVQMALRSVSK-----------SNIETVTLQALERFDVMHLAERNFL----------TLS 152
Cdd:COG0419 81 ryRIERRQGEFAEFLEAKPSERKEALKRLLGleiyeelkerlKELEEALESALEELAELQKLKQEILaqlsgldpieTLS 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1579913621 153 GGEKQRVHLSRVLAqleysgfhrdepryLFLDecTSSLD 191
Cdd:COG0419 161 GGERLRLALADLLS--------------LILD--FGSLD 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-68 |
3.43e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 3.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1579913621 24 TNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTG 68
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
36-131 |
1.31e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.71 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGeLLCILGPNGAGKSSLLNC----LTGDYSGYDGKVMLNFKNikdfsglqlsgvravmpQSIYLDFPFLV 111
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAiklaLYGKTSRLKRKSGGGFVK-----------------GDIRIGLEGKG 70
|
90 100
....*....|....*....|
gi 1579913621 112 KEVVQMALRSVSKSNIETVT 131
Cdd:pfam13476 71 KAYVEITFENNDGRYTYAIE 90
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-77 |
2.17e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 16 SGEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKV 77
Cdd:PRK11147 315 SGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-246 |
2.40e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 29 AFDNKPIldniSLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIkdfSGLQLSGVRAVMpQSIYLDFp 108
Cdd:PRK10522 336 GFSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLF-SAVFTDF- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 109 FLVKEVVQMALRSVSKSNIETvTLQALERFDVMHLAERNFLT--LSGGEKQRVHLsrVLAQLEysgfHRDeprYLFLDEC 186
Cdd:PRK10522 407 HLFDQLLGPEGKPANPALVEK-WLERLKMAHKLELEDGRISNlkLSKGQKKRLAL--LLALAE----ERD---ILLLDEW 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1579913621 187 TSSLDlSHQHQVFAKV-----KEFAQyhriGVVAVLHDlNLAAQYGDRALLLKQGKVQALNKIEK 246
Cdd:PRK10522 477 AADQD-PHFRREFYQVllpllQEMGK----TIFAISHD-DHYFIHADRLLEMRNGQLSELTGEER 535
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-79 |
2.43e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 20 MLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVML 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
39-80 |
2.89e-04 |
|
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: 42.09 E-value: 2.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1579913621 39 ISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLN 80
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLD 392
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-63 |
4.15e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 4.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1579913621 20 MLQATNLSLAFDNK-PILDNISLDVEAGELLCILGPNGAGKSSLL 63
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLL 47
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
36-204 |
4.81e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLlnCLTGDYSgyDGKVMLNfKNIKDFSGLQLsgvravmpqsIYLDfpflvkevv 115
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLI-SFLPKFSRNKL----------IFID--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 116 qmALRSVSKSNIETVTLqalerfdvmhlaERNFLTLSGGEKQRVHLSRVLAQleysgfhRDEPRYLFLDECTSSLDLSHQ 195
Cdd:cd03238 67 --QLQFLIDVGLGYLTL------------GQKLSTLSGGELQRVKLASELFS-------EPPGTLFILDEPSTGLHQQDI 125
|
....*....
gi 1579913621 196 HQVFAKVKE 204
Cdd:cd03238 126 NQLLEVIKG 134
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-81 |
5.18e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 5.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1579913621 13 VKISGEDMLqatnlslafdnkpILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYS-GY--DGKVMLNF 81
Cdd:TIGR00956 769 VKIKKEKRV-------------ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtGVitGGDRLVNG 827
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
42-229 |
6.72e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 42 DVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVmlnfknikdfsglQLSGVR-AVMPQSIyldfpflvkevvqmalr 120
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWDGITpVYKPQYI----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 121 svsksnietvtlqalerfdvmhlaernflTLSGGEKQRVHLSRVLAqleysgfhRDEPRYLFlDECTSSLDLSHQHQVFA 200
Cdd:cd03222 71 -----------------------------DLSGGELQRVAIAAALL--------RNATFYLF-DEPSAYLDIEQRLNAAR 112
|
170 180
....*....|....*....|....*....
gi 1579913621 201 KVKEFAQYHRIGVVAVLHDLNLAAQYGDR 229
Cdd:cd03222 113 AIRRLSEEGKKTALVVEHDLAVLDYLSDR 141
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-77 |
1.01e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1579913621 35 ILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKV 77
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGV 118
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
151-229 |
1.42e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1579913621 151 LSGGEKQRVHLSRVLAqleysgfhrDEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDR 229
Cdd:PRK15093 159 LTEGECQKVMIAIALA---------NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
45-76 |
2.13e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.53 E-value: 2.13e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1579913621 45 AGELLCILGPNGAGKSSLLNCL-------TGDYSGYDGK 76
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALlpelvlaTGEISEKLGR 122
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
45-76 |
2.17e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1579913621 45 AGELLCILGPNGAGKSSLLNCL-------TGDYSGYDGK 76
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALlpeldlrTGEISEKLGR 143
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-198 |
3.08e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.86 E-value: 3.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1579913621 143 LAERNFLTLSGGEKQRVHLSRVLAQleysgfhrdEPRYLFLDECTSSLDLSHQHQV 198
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIR---------NPKILILDEATSSLDNKSEYLV 618
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-77 |
3.34e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.99 E-value: 3.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1579913621 5 AATQSSRLVKISGEDMLQatnlslaFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKV 77
Cdd:PTZ00243 652 TSERSAKTPKMKTDDFFE-------LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV 717
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-66 |
3.52e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 3.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1579913621 25 NLSLAFDNKPildnisldveagELLCILGPNGAGKSSLLNCL 66
Cdd:COG3950 16 DLEIDFDNPP------------RLTVLVGENGSGKTTLLEAI 45
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-255 |
3.56e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 38.41 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGYDGKVMLNFKNIKDFSglqlSGVRAVMPQSIYLDF--PF---- 109
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD----PEAQKLLRQKIQIVFqnPYgsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 110 ---LVKEVVQMALRsvsksnIETvTLQALER----FDVM--------HlAERNFLTLSGGEKQRVHLSRVLAQleysgfh 174
Cdd:PRK11308 107 prkKVGQILEEPLL------INT-SLSAAERrekaLAMMakvglrpeH-YDRYPHMFSGGQRQRIAIARALML------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 175 rdEPRYLFLDECTSSLDLSHQHQVFAKVKEFAQYHRIGVVAVLHDLNLAAQYGDRALLLKQGKVQALNKIEKVYQNRLLS 254
Cdd:PRK11308 172 --DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHP 249
|
.
gi 1579913621 255 Y 255
Cdd:PRK11308 250 Y 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-191 |
3.96e-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: 38.74 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 17 GEDMLQATNLSLAFDNKPILDNISLDVEAGELLCILGPNGAGKSSLLNCLTGDYSGyDGKVMLNFKNIKDFSGLQLSGVR 96
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1579913621 97 AVMPQSIY---------LDfPF-------LVKEVVQMALRSVsksnIEtvtlQALERFDVMhLAERNFLtLSGGEKQRVH 160
Cdd:TIGR01271 1295 GVIPQKVFifsgtfrknLD-PYeqwsdeeIWKVAEEVGLKSV----IE----QFPDKLDFV-LVDGGYV-LSNGHKQLMC 1363
|
170 180 190
....*....|....*....|....*....|..
gi 1579913621 161 LSR-VLAQleysgfhrdePRYLFLDECTSSLD 191
Cdd:TIGR01271 1364 LARsILSK----------AKILLLDEPSAHLD 1385
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
36-68 |
5.36e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 37.85 E-value: 5.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1579913621 36 LDNISLDVEAGELL------CILG-PNgAGKSSLLNCLTG 68
Cdd:pfam12631 78 LEKLLATADRGRILregikvVIVGkPN-VGKSSLLNALLG 116
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
36-64 |
5.78e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 5.78e-03
10 20
....*....|....*....|....*....
gi 1579913621 36 LDNISLDVEAGELLCILGPNGAGKSSLLN 64
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
151-196 |
5.84e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 37.28 E-value: 5.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1579913621 151 LSGGEKQRVHLSRVLAQLEYsgfhRDEPRYLfLDECTSSLDLSHQH 196
Cdd:cd03273 167 LSGGQRSLVALSLILALLLF----KPAPMYI-LDEVDAALDLSHTQ 207
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
40-66 |
8.05e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.22 E-value: 8.05e-03
10 20
....*....|....*....|....*..
gi 1579913621 40 SLDVEAGELLCILGPNGAGKSSLLNCL 66
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| |
