|
Name |
Accession |
Description |
Interval |
E-value |
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-255 |
4.32e-129 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 365.59 E-value: 4.32e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPGGAEQ-- 158
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGpr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLD 238
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGAD 240
|
250
....*....|....*..
gi 759600243 239 VLVQRHPERGHPLIVAR 255
Cdd:COG4559 241 LRVLAHPEGGCPQVLPR 257
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-255 |
1.24e-128 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 364.48 E-value: 1.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLW-PGGAEQV 159
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWePDGPPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAG-RGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLD 238
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGAD 241
|
250
....*....|....*..
gi 759600243 239 VLVQRHPERGHPLIVAR 255
Cdd:PRK13548 242 VLVQPHPETGAPLVLPR 258
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-253 |
4.78e-104 |
|
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: 301.96 E-value: 4.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGRQR----DLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggA 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRpsaeDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 157 EQVLLLDEPTSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVF 235
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
250
....*....|....*...
gi 759600243 236 GLDVLVQRHPERGHPLIV 253
Cdd:COG1120 236 GVEARVIEDPVTGRPLVL 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-254 |
1.86e-69 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 218.94 E-value: 1.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPH----DSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPgga 156
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 157 eqVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFG 236
Cdd:PRK09536 160 --VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
250
....*....|....*...
gi 759600243 237 LDVLVQRHPERGHPLIVA 254
Cdd:PRK09536 238 ARTAVGTDPATGAPTVTP 255
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-220 |
1.36e-68 |
|
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: 209.21 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 3 AAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLnfafsvesvvgfgrlphdsgrqrdLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLL 162
Cdd:cd03214 81 ALEL------------------------LGL----------AHLADRPFNELSGGERQRVLLARALAQ-----EPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 163 DEPTSALDPLHQHTTLHAVREFAG-RGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-253 |
2.12e-67 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 208.78 E-value: 2.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGR--QRDLQIIAEAMAAADASHLAGRsYL-SLSGGERQRVHLARVLAQlwpggAE 157
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRltAEDREIIDEAIAYLDLEDLADR-YLdELSGGQRQRAFIAMVLAQ-----DT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFG 236
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYD 234
|
250
....*....|....*..
gi 759600243 237 LDVLVQRHPerGHPLIV 253
Cdd:COG4604 235 TDIEVEEID--GKRICV 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
6.06e-66 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 204.94 E-value: 6.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwqgteRARRLAVL 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAF--SVESVVGFGRLPHDS----GRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpg 154
Cdd:COG1121 81 PQRAEVDWDFpiTVRDVVLMGRYGRRGlfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 155 GAEqVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFGTPDEVLRAEPLRQV 234
Cdd:COG1121 157 DPD-LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRA 234
|
250
....*....|
gi 759600243 235 FGLDVLVQRH 244
Cdd:COG1121 235 YGGPVALLAH 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-255 |
9.73e-66 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 204.86 E-value: 9.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDS--GR--QRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPgga 156
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSlwGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 157 eqVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFG 236
Cdd:PRK11231 159 --VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFD 236
|
250
....*....|....*....
gi 759600243 237 LDVLVQRHPERGHPLIVAR 255
Cdd:PRK11231 237 VEAEIHPEPVSGTPMCVVR 255
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-253 |
9.68e-63 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 197.34 E-value: 9.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLP 81
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFGRLPHDS----GRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAE 157
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHRSlwagDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQ-----EP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGL 237
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGV 236
|
250
....*....|....*.
gi 759600243 238 DVLVQRHPERGHPLIV 253
Cdd:TIGR03873 237 DATVLTHPDTGRPIIA 252
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-254 |
4.76e-61 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 193.50 E-value: 4.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAG--------GSVSLDGRALEQWQGTE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 73 RARRLAVLPQSSSLNFAFSVESVVGFGRLPH----DSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVL 148
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHarraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 AQLWPGGAEQV----LLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPD 223
Cdd:PRK13547 161 AQLWPPHDAAQppryLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|.
gi 759600243 224 EVLRAEPLRQVFGLDVLVQRHPERGHPLIVA 254
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGVPPVIVP 271
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-220 |
8.26e-56 |
|
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: 178.11 E-value: 8.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQgteraRRLAVLPQS 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAF--SVESVVGFGRLPHDSG----RQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAE 157
Cdd:cd03235 77 RSIDRDFpiSVRDVVLMGLYGHKGLfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ-----DP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFG 220
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-255 |
9.54e-52 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 168.87 E-value: 9.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVkRGRqvvLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPlAGGSVSLDGRALEQWQGTERARRLAVLP 81
Cdd:COG4138 1 LQLNDVAV-AGR---LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFGrLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPGG--AEQV 159
Cdd:COG4138 76 QQQSPPFAMPVFQYLALH-QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpEGQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLDv 239
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK- 233
|
250
....*....|....*.
gi 759600243 240 lVQRHPERGHPLIVAR 255
Cdd:COG4138 234 -FRRLEVEGHRWLIPT 248
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-231 |
2.59e-49 |
|
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: 161.73 E-value: 2.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVK-RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQssslN-----FAFSVESVVGFG----RLPHDSGRQR------DLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLA 145
Cdd:COG1122 81 FQ----NpddqlFAPTVEEDVAFGpenlGLPREEIRERveealeLVGL----------EHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 146 RVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:COG1122 147 GVLA-MEP----EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
....*.
gi 759600243 226 LRAEPL 231
Cdd:COG1122 222 FSDYEL 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-235 |
1.01e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.92 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLP 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGF-GRLPHDSGRQRDlQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVL 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARLYGLPRKEAR-ERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL-----HDPELL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEvLRAEPLRQVF 235
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE-LKARLLEDVF 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-251 |
1.56e-46 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 156.10 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSS 84
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSVESVVGFGRLP-HDS-GR--QRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPwHGAlGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ-----DSRCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAG-RGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLDV 239
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
250
....*....|..
gi 759600243 240 LVQRHPERGHPL 251
Cdd:PRK10575 250 GILPHPAGAAPV 261
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-253 |
6.87e-46 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 154.37 E-value: 6.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLP 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFGRLPHD----SGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAE 157
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQplftRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-----ET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFG 236
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
250
....*....|....*..
gi 759600243 237 LDVLVQRHPERGHPLIV 253
Cdd:PRK10253 243 LRCMIIDDPVAGTPLVV 259
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
2.03e-45 |
|
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: 149.86 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLP 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLnfafsvesvvgfgrlphdsgrqrdlqiiaeamaaadASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLL 161
Cdd:cd03230 80 EEPSL------------------------------------YENLTVRENLKLSGGMKQRLALAQALL-----HDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-255 |
2.18e-45 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 152.39 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPlAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLNFAFSVesvvgFG 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV-----FQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 100 RLP---HDSGRQRDLQ-IIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPGG--AEQVLLLDEPTSALDPLH 173
Cdd:PRK03695 89 YLTlhqPDKTRTEAVAsALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 174 QHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLDvlVQRHPERGHPLIV 253
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN--FRRLDVEGHPMLI 246
|
..
gi 759600243 254 AR 255
Cdd:PRK03695 247 ST 248
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-226 |
8.08e-44 |
|
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: 148.08 E-value: 8.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVG-FGRLpHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQV 159
Cdd:COG4555 80 PDERGLYDRLTVRENIRyFAEL-YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH-----DPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-215 |
1.34e-43 |
|
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: 146.46 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQ--VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQ 82
Cdd:cd03225 3 KNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLNFAF-SVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLL 161
Cdd:cd03225 83 NPDDQFFGpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM-----DPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-215 |
2.18e-43 |
|
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: 144.31 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQs 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 sslnfafsvesvvgfgrlphdsgrqrdlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAQLWPggaeqVLLLD 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPD-----LLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759600243 164 EPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-255 |
1.12e-42 |
|
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: 151.59 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVK--RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAG---GSVSLDGRALEQWQGTERAR 75
Cdd:COG1123 4 LLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 RLAVLPQS--SSLNFAfSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWP 153
Cdd:COG1123 84 RIGMVFQDpmTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA-LDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 154 ggaeQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRA-EPL 231
Cdd:COG1123 162 ----DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAApQAL 237
|
250 260
....*....|....*....|....*..
gi 759600243 232 RQVFGLD---VLVQRHPERGHPLIVAR 255
Cdd:COG1123 238 AAVPRLGaarGRAAPAAAAAEPLLEVR 264
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-228 |
1.80e-42 |
|
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: 151.21 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV-----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTER-- 73
Cdd:COG1123 260 LLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 -ARRLAVLPQ--SSSLNFAFSVESVVGFGRLPHD--SGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVL 148
Cdd:COG1123 340 lRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGllSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 AqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:COG1123 420 A-LEP----KLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
.
gi 759600243 228 A 228
Cdd:COG1123 495 N 495
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
6.18e-42 |
|
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: 143.03 E-value: 6.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGT---ER 73
Cdd:cd03257 1 LLEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 ARRLAVLPQ--SSSLNFAFSVESVVGFGRLPHdsGRQRDLQIIAEAMAAADASHLAGRSYLS-----LSGGERQRVHLAR 146
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIH--GKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 147 VLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03257 159 ALA-LNP----KLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.07e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.49 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLnFAFSVESVVGFGRLPHDSGRQRDlQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLaQLWPggaeQVLL 161
Cdd:COG4619 81 QEPAL-WGGTVRDNLPFPFQLRERKFDRE-RALELLERLGLPPDILDKPVERLSGGERQRLALIRAL-LLQP----DVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-215 |
2.69e-41 |
|
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: 141.86 E-value: 2.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR 76
Cdd:COG1124 1 MLEVRNLSVsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQS--SSLNFAFSVESVVG-----FGRLPHDSGRQRDLQIIAEamaaadashlaGRSYLS-----LSGGERQRVHL 144
Cdd:COG1124 81 VQMVFQDpyASLHPRHTVDRILAeplriHGLPDREERIAELLEQVGL-----------PPSFLDryphqLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 145 ARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG1124 150 ARALI-LEP----ELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-238 |
3.64e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVK-RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA---RR 76
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSSLNFAFSVESVVGFGRLPHDSG--------RQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVL 148
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLGRTSTwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 AQlwpgGAEqVLLLDEPTSALDPLHQHTTLHAVREFAG-RGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:COG3638 162 VQ----EPK-LILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTD 236
|
250
....*....|.
gi 759600243 228 AEpLRQVFGLD 238
Cdd:COG3638 237 AV-LREIYGGE 246
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-227 |
2.14e-38 |
|
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: 134.10 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVL 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADA----------SHLAGRSYLSLSGGERQRVHLARVLAQ 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERaeellervglADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 151 lwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:cd03219 161 -----DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-228 |
7.98e-38 |
|
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: 139.11 E-value: 7.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVK--RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAV 79
Cdd:COG4618 331 LSVENLTVVppGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLnFAFSV-ESVVGFG---------------------RLPHdsGrqRDLQIiaeamaaadashlaGRSYLSLSGG 137
Cdd:COG4618 411 LPQDVEL-FDGTIaENIARFGdadpekvvaaaklagvhemilRLPD--G--YDTRI--------------GEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 138 ERQRVHLARVLAqlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARyCDRLLLLHDGRPH 217
Cdd:COG4618 472 QRQRIGLARALY-----GDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQ 545
|
250
....*....|.
gi 759600243 218 LFGTPDEVLRA 228
Cdd:COG4618 546 AFGPRDEVLAR 556
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-244 |
1.15e-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: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGEL-PLAGGSVSLDGRALEQWQGTERARRLAV 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LpqSSSLNFAF----SVESVV--GFgrlpHDS-GRQR-----DLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARV 147
Cdd:COG1119 83 V--SPALQLRFprdeTVLDVVlsGF----FDSiGLYReptdeQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 148 LAqlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGA-AVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:COG1119 157 LV-----KDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
250
....*....|....*...
gi 759600243 227 RAEPLRQVFGLDVLVQRH 244
Cdd:COG1119 232 TSENLSEAFGLPVEVERR 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-225 |
6.11e-37 |
|
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: 130.38 E-value: 6.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQV-VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE-RA--RRL 77
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNFAFSVESVVGFGRLPHDSGRQ--------RDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLA 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRslfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 150 QlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:cd03256 161 Q-----QPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-233 |
7.96e-37 |
|
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: 129.93 E-value: 7.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTER---ARRLAVLP 81
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGF-----GRLPHDSGRQRDLQIIAEAMaaadashLAGRSYL---SLSGGERQRVHLARVLAqLWP 153
Cdd:cd03261 84 QSGALFDSLTVFENVAFplrehTRLSEEEIREIVLEKLEAVG-------LRGAEDLypaELSGGMKKRVALARALA-LDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 154 ggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEP-- 230
Cdd:cd03261 156 ----ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDpl 231
|
...
gi 759600243 231 LRQ 233
Cdd:cd03261 232 VRQ 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-214 |
1.76e-36 |
|
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: 128.14 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQV-VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqgtERARRLAVLPQ 82
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLNFAF-SVESVVGFG-RLPHDSGRQ-----RDLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLAQlwpgg 155
Cdd:cd03226 79 DVDYQLFTdSVREELLLGlKELDAGNEQaetvlKDLDL----------YALKERHPLSLSGGQKQRLAIAAALLS----- 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 156 AEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
1.43e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.41 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQvvLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwQGTERARR-LAV 79
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPPAERpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLnFA-FSVESVVGFGRlpHDSGRQRDLQI--IAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPgga 156
Cdd:COG3840 76 LFQENNL-FPhLTVAQNIGLGL--RPGLKLTAEQRaqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 157 eqVLLLDEPTSALDPLHQHTTLHAVREFAG-RGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEP 230
Cdd:COG3840 150 --ILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-215 |
3.07e-35 |
|
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: 123.65 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL-FSGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VgfgrlphdsgrqrdlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQH 175
Cdd:cd03228 96 I-------------------------------------LSGGQRQRIAIARALLR-----DPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 759600243 176 TTLHAVREFAgRGAAVLVILHDLNLaARYCDRLLLLHDGR 215
Cdd:cd03228 134 LILEALRALA-KGKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-235 |
4.42e-35 |
|
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: 125.46 E-value: 4.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVL 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSS----LNFAFSVESVVGF-GRLPHDSGRQR------DLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLA 149
Cdd:TIGR04406 82 PQEASifrkLTVEENIMAVLEIrKDLDRAEREERlealleEFQI----------SHLRDNKAMSLSGGERRRVEIARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 150 QlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:TIGR04406 152 T-----NPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
....*.
gi 759600243 230 PLRQVF 235
Cdd:TIGR04406 227 KVRRVY 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-235 |
8.68e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 124.76 E-value: 8.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLtVKR--GRQVVlQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-L 77
Cdd:COG1137 3 TLEAENL-VKSygKRTVV-KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLnfaF---SVE----SVVGFGRLPHDSGRQR------DLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHL 144
Cdd:COG1137 81 GYLPQEASI---FrklTVEdnilAVLELRKLSKKEREERleelleEFGI----------THLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 145 ARVLAqlwpggAE-QVLLLDEPTSALDPLhqhttlhAV-------REFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRP 216
Cdd:COG1137 148 ARALA------TNpKFILLDEPFAGVDPI-------AVadiqkiiRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
250
....*....|....*....
gi 759600243 217 HLFGTPDEVLRAEPLRQVF 235
Cdd:COG1137 215 LAEGTPEEILNNPLVRKVY 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-215 |
9.92e-35 |
|
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: 122.68 E-value: 9.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR--ALEQWQGTERARRLAVLPQ 82
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdlTDLEDELPPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLNFAFSVESVVGFGrlphdsgrqrdlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAQlwpggAEQVLLL 162
Cdd:cd03229 84 DFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAM-----DPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 163 DEPTSALDPLHQHTTLHAVRE-FAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
1.13e-34 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 124.32 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAV 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLnFA-FSVES--VVGFGRLPHDSGRQRDLQIIAEA--MAAADASHLAGrsylSLSGGERQRVHLARVLAqlwpg 154
Cdd:COG0410 83 VPEGRRI-FPsLTVEEnlLLGAYARRDRAEVRADLERVYELfpRLKERRRQRAG----TLSGGEQQMLAIGRALM----- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 155 GAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQ 233
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVRE 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-229 |
1.41e-34 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 123.94 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA---RRL 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLnfaFSVESV---VGF-----GRLPHDSGRQRDLQIIaeamaaadasHLAGrsyLS---------LSGGERQ 140
Cdd:COG1127 85 GMLFQGGAL---FDSLTVfenVAFplrehTDLSEAEIRELVLEKL----------ELVG---LPgaadkmpseLSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 141 RVHLARVLAqLWPggaeQVLLLDEPTSALDP----------LHQHTTLhavrefagrGAAVLVILHDLNLAARYCDRLLL 210
Cdd:COG1127 149 RVALARALA-LDP----EILLYDEPTAGLDPitsavideliRELRDEL---------GLTSVVVTHDLDSAFAIADRVAV 214
|
250
....*....|....*....
gi 759600243 211 LHDGRPHLFGTPDEVLRAE 229
Cdd:COG1127 215 LADGKIIAEGTPEELLASD 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-220 |
1.43e-34 |
|
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: 123.40 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqgTERARRLAVLPQSS 84
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSVESVVGFG----RLPHDSGRQRDLQIIaeamAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:cd03259 82 ALFPHLTVAENIAFGlklrGVPKAEIRARVRELL----ELVGLEGLLNRYPHELSGGQQQRVALARALAR-----EPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVRE-FAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-226 |
1.54e-34 |
|
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: 123.70 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLnFA-FSVES--VVGfGRLPHDSGRQRDLQIIAEA--MAAADASHLAGrsylSLSGGERQRVHLARVLAqlwpgG 155
Cdd:cd03224 81 PEGRRI-FPeLTVEEnlLLG-AYARRRAKRKARLERVYELfpRLKERRKQLAG----TLSGGEQQMLAIARALM-----S 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 156 AEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-227 |
6.94e-34 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 122.84 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR---- 76
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 ------------------LAVLPQSSSLNFAfsveSVVGFGRLPHDSGRQRD--LQIIAEAMAAADASHLAGrsylSLSG 136
Cdd:COG0411 84 tfqnprlfpeltvlenvlVAAHARLGRGLLA----ALLRLPRARREEREAREraEELLERVGLADRADEPAG----NLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 137 GERQRVHLARVLAqlwpggAE-QVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:COG0411 156 GQQRRLEIARALA------TEpKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250
....*....|...
gi 759600243 215 RPHLFGTPDEVLR 227
Cdd:COG0411 230 RVIAEGTPAEVRA 242
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-210 |
1.47e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.03 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSldgraleqwqgTERARRLAVLPQSSSLNFAF- 90
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 -SVESVVGFGRLPHDSG----RQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:NF040873 72 lTVRDLVAMGRWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ-----EADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLL 210
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
2.48e-33 |
|
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: 126.80 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKR-GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLnFAFSVESVVGFGRlpHDSGRQRDLQIIAEAMAAADASHLA-------GRSYLSLSGGERQRVHLARVLAQlwp 153
Cdd:COG4988 417 PQNPYL-FAGTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPdgldtplGEGGRGLSGGQAQRLALARALLR--- 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 154 ggAEQVLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAEP 230
Cdd:COG4988 491 --DAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
3.18e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 120.87 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQV-VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE----RAR 75
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 ------------RLAVLPQSSSLNFAFSVESVVGFGRLPhDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVH 143
Cdd:TIGR02315 81 igmifqhynlieRLTVLENVLHGRLGYKPTWRSLLGRFS-EEDKERALSALERVGL----ADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 144 LARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTP 222
Cdd:TIGR02315 156 IARALAQ-----QPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
250
....*....|....
gi 759600243 223 DEvLRAEPLRQVFG 236
Cdd:TIGR02315 231 SE-LDDEVLRHIYG 243
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-210 |
5.20e-33 |
|
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: 119.12 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSV-ESVVGFGRLphdSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPggaeqV 159
Cdd:COG4133 81 GHADGLKPELTVrENLRFWAAL---YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP-----L 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLnLAARYCDRLLL 210
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP-LELAAARVLDL 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-235 |
6.81e-33 |
|
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: 119.57 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVE----SVVGFGRLPHDSGRQR------DLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLAQ 150
Cdd:cd03218 81 PQEASIFRKLTVEenilAVLEIRGLSKKEREEKleelleEFHI----------THLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 151 lwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEP 230
Cdd:cd03218 151 -----NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
....*
gi 759600243 231 LRQVF 235
Cdd:cd03218 226 VRKVY 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
1.12e-32 |
|
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: 117.32 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRG--RQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAV 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLnFAFSVesvvgfgrlphdsgrqrdLQIIaeamaaadashlagrsylsLSGGERQRVHLARVLAqlwpgGAEQV 159
Cdd:cd03246 81 LPQDDEL-FSGSI------------------AENI-------------------LSGGQRQRLGLARALY-----GNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-167 |
5.44e-32 |
|
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: 114.67 E-value: 5.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLNFAFSVESVV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 97 GFGRLPHDSGR----QRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTS 167
Cdd:pfam00005 81 RLGLLLKGLSKrekdARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLT-----KPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.93e-31 |
|
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: 115.28 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENL--TVKRG--RQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE----R 73
Cdd:cd03255 1 IELKNLskTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 ARRLAVLPQSSSLNFAFSVESVV----GFGRLPHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLA 149
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVelplLLAGVPKKERRERAEELLERVGLGDRLNHYPS----ELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 150 qlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLaARYCDRLLLLHDGR 215
Cdd:cd03255 157 -----NDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
2.32e-31 |
|
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: 113.29 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqGTERARRL--AV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-SPRDARRAgiAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQssslnfafsvesvvgfgrlphdsgrqrdlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAqlwpGGAEqV 159
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALA----RNAR-L 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-251 |
4.36e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLNFAFS-VESV 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDNQFVGAtVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRlpHDSGRQRDLQI--IAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLH 173
Cdd:PRK13635 103 VAFGL--ENIGVPREEMVerVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL-----QPDIIILDEATSMLDPRG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 174 QHTTLHAVREF-AGRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLR-AEPLRQVfGLDV-----LVQRHPE 246
Cdd:PRK13635 176 RREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKsGHMLQEI-GLDVpfsvkLKELLKR 253
|
....*
gi 759600243 247 RGHPL 251
Cdd:PRK13635 254 NGILL 258
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-237 |
5.59e-31 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 114.56 E-value: 5.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 22 LALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQgteraRRLAVLPQSSSL--NFAFSVESVVGFG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGW-----RHIGYVPQRHEFawDFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 100 RLPHDSGRQR----DLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQH 175
Cdd:TIGR03771 76 RTGHIGWLRRpcvaDFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALAT-----RPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 176 TTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFGTPDEVLRAEPLRQVFGL 237
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-224 |
5.87e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.14 E-value: 5.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLPQSSSLNFA 89
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 FSV-ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYlSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSA 168
Cdd:cd03263 90 LTVrEHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRAR-TLSGGMKRKLSLAIALI-----GGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 169 LDPLHQH---TTLHAVRefagRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDE 224
Cdd:cd03263 164 LDPASRRaiwDLILEVR----KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
2.92e-30 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 112.46 E-value: 2.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARR 76
Cdd:cd03266 1 MITADALTkrfrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSSLNFAFSV-ESVVGFGRLpHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpgg 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTArENLEYFAGL-YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 156 AEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-225 |
3.18e-30 |
|
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: 112.27 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPL-----AGGSVSLDGRALEQWQGT--ERA 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 RRLAVLPQSSSLnFAFSVESVVGFGrlPHDSGRQRDLQIIAEAMAAADASHLAGR-----SYLSLSGGERQRVHLARVLA 149
Cdd:cd03260 81 RRVGMVFQKPNP-FPGSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 150 qLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRgAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:cd03260 158 -NEP----EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-220 |
3.50e-30 |
|
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: 111.99 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwqGTERARRLAVLP 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSV-ESVVGFGRLpHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:cd03269 77 EERGLYPKMKViDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH-----DPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-235 |
8.10e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 8.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTvKR-GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwqgtERARRLAV 79
Cdd:COG4152 1 MLELKGLT-KRfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLNFAFSV-ESVVGFGRL---PHDSGRQR------DLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHL-ARVL 148
Cdd:COG4152 76 LPEERGLYPKMKVgEQLVYLARLkglSKAEAKRRadewleRLGL----------GDRANKKVEELSKGNQQKVQLiAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 AQlwPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRA 228
Cdd:COG4152 146 HD--P----ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
....*..
gi 759600243 229 EPLRQVF 235
Cdd:COG4152 220 FGRNTLR 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
1.39e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.90 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA-- 74
Cdd:COG1136 4 LLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 --RRLAVLPQS----SSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVL 148
Cdd:COG1136 84 rrRHIGFVFQFfnllPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQ----LSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 149 AqlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAArYCDRLLLLHDGR 215
Cdd:COG1136 160 V-----NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGR 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
1.94e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 115.46 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVK-RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:TIGR02857 322 LEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLnFAFSVESVVGFGRLP----------HDSGRQRDLQIIAEAMAAADASHLAGrsylsLSGGERQRVHLARVLAQ 150
Cdd:TIGR02857 402 PQHPFL-FAGTIAENIRLARPDasdaeirealERAGLDEFVAALPQGLDTPIGEGGAG-----LSGGQAQRLALARAFLR 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 151 LwpggaEQVLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLAARyCDRLLLL 211
Cdd:TIGR02857 476 D-----APLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-237 |
2.32e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.93 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAgGSVSLDGRALEQWQGTeRARRLAVL 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPDS-GRIVLNGRDLFTNLPP-RERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQssslNFA----FSVESVVGFG--RLPHDSGRQRD-----LQIIaeamaaaDASHLAGRsYLS-LSGGERQRVHLARVL 148
Cdd:COG1118 81 FQ----HYAlfphMTVAENIAFGlrVRPPSKAEIRArveelLELV-------QLEGLADR-YPSqLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 AqlwpggAE-QVLLLDEPTSALDP---------LHQ-HTTLHavrefagrGAAVLVIlHDLNLAARYCDRLLLLHDGRPH 217
Cdd:COG1118 149 A------VEpEVLLLDEPFGALDAkvrkelrrwLRRlHDELG--------GTTVFVT-HDQEEALELADRVVVMNQGRIE 213
|
250 260
....*....|....*....|
gi 759600243 218 LFGTPDEVLRAEPLRQVFGL 237
Cdd:COG1118 214 QVGTPDEVYDRPATPFVARF 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-230 |
1.06e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 113.71 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKR--GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLnFAFSVESVVGFGRlPHDSgrqrDLQIIAEAMAAADASHLAGRSY----------LSLSGGERQRVHLARVLA 149
Cdd:COG4987 414 VPQRPHL-FDTTLRENLRLAR-PDAT----DEELWAALERVGLGDWLAALPDgldtwlgeggRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 150 QlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREfAGRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:COG4987 488 R-----DAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 759600243 230 P 230
Cdd:COG4987 561 G 561
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-251 |
4.77e-28 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 107.92 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwqGTERARRLAVLPQSSSLNFAF--- 90
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDI----TAKKKKKLKDLRKKVGLVFQFpeh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 -----SVESVVGFG----RLPHDSGRQRDLQIIaeamaaadasHLAG-------RSYLSLSGGERQRVHLARVLAqLWPg 154
Cdd:TIGR04521 94 qlfeeTVYKDIAFGpknlGLSEEEAEERVKEAL----------ELVGldeeyleRSPFELSGGQMRRVAIAGVLA-MEP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 155 gaeQVLLLDEPTSALDP------LHQHTTLHavREfagRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR- 227
Cdd:TIGR04521 162 ---EVLILDEPTAGLDPkgrkeiLDLFKRLH--KE---KGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSd 233
|
250 260
....*....|....*....|....*....
gi 759600243 228 AEPLRQVfGLDV-----LVQRHPERGHPL 251
Cdd:TIGR04521 234 VDELEKI-GLDVpeiteLARKLKEKGLPV 261
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-227 |
9.47e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 108.65 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL-----EQwqgteraR 75
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppEK-------R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 RLAVLPQSSSLnfaF---SVESVVGFG----RLPHDSGRQR-----DL-QIiaeamaaadaSHLAGRSYLSLSGGERQRV 142
Cdd:COG3842 78 NVGMVFQDYAL---FphlTVAENVAFGlrmrGVPKAEIRARvaellELvGL----------EGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 143 HLARVLAqlwpggAE-QVLLLDEPTSALDP-LHQHT-----TLHavREFagrGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG3842 145 ALARALA------PEpRVLLLDEPLSALDAkLREEMreelrRLQ--REL---GITFIYVTHDQEEALALADRIAVMNDGR 213
|
250
....*....|..
gi 759600243 216 PHLFGTPDEVLR 227
Cdd:COG3842 214 IEQVGTPEEIYE 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-230 |
1.07e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.33 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLA-- 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 -------VLPQSSSL-NFAFSVESVVGFGRlphDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAq 150
Cdd:PRK09493 81 mvfqqfyLFPHLTALeNVMFGPLRVRGASK---EEAEKQARELLAKVGLAERAHHYPSE----LSGGQQQRVAIARALA- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 151 LWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEP 230
Cdd:PRK09493 153 VKP----KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 |
1.62e-27 |
|
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: 105.43 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG---ELPLAGGSVSLDGRALE--QWQgteraRRLAVLPQSSSLNFAF 90
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKpdQFQ-----KCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 SVESVVGFG---RLP-HDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLwPGgaeqVLLLDEPT 166
Cdd:cd03234 97 TVRETLTYTailRLPrKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD-PK----VLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 167 SALDPLHQHTTLHAVREFAGRGAAVLVILH----DLnlaARYCDRLLLLHDGRP 216
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEI 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-231 |
1.89e-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: 110.31 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSL-------NF 88
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLfsgtireNI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 AFSVESV-----------VGFG----RLPHdsgrQRDLQIiaeamaaadashlaGRSYLSLSGGERQRVHLARVLAQLwP 153
Cdd:COG2274 570 TLGDPDAtdeeiieaarlAGLHdfieALPM----GYDTVV--------------GEGGSNLSGGQRQRLAIARALLRN-P 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 154 ggaeQVLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLaARYCDRLLLLHDGRPHLFGTPDEVLRAEPL 231
Cdd:COG2274 631 ----RILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-235 |
2.08e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLT-VKRGRQVVlQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAV 79
Cdd:PRK10895 4 LTAKNLAkAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLNFAFSV-ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQ 158
Cdd:PRK10895 83 LPQEASIFRRLSVyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA-----ANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVF 235
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-216 |
2.47e-27 |
|
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: 104.48 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwqgTERARRL 77
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSL--------NFAFSVEsvvgFGRLPHDSGRQRDLQIIAEAmaaadasHLAG--RSYLS-LSGGERQRVHLAR 146
Cdd:cd03293 76 GYVFQQDALlpwltvldNVALGLE----LQGVPKAEARERAEELLELV-------GLSGfeNAYPHqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 147 VLAQlwpggAEQVLLLDEPTSALDPL---HQHTTLHAVREfaGRGAAVLVILHDLNLAARYCDRLLLLHdGRP 216
Cdd:cd03293 145 ALAV-----DPDVLLLDEPFSALDALtreQLQEELLDIWR--ETGKTVLLVTHDIDEAVFLADRVVVLS-ARP 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-199 |
2.96e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPL---AGGSVSLDGRALEQWQgTERaRRL 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-AEQ-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNFAFSVESVVGFGrLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpggAE 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL------AE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759600243 158 -QVLLLDEPTSALDPLHQHTTLHAVREFAG-RGAAVLVILHDLN 199
Cdd:COG4136 152 pRALLLDEPFSKLDAALRAQFREFVFEQIRqRGIPALLVTHDEE 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
3.93e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.17 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwqgTERARR 76
Cdd:COG1116 7 ALELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSSLnfaF---SVESVVGFG----RLPHDSGRQRDLQIIAEAmaaadasHLAG--RSYLS-LSGGERQRVHLAR 146
Cdd:COG1116 82 RGVVFQEPAL---LpwlTVLDNVALGlelrGVPKAERRERARELLELV-------GLAGfeDAYPHqLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 147 VLAQlwpggAEQVLLLDEPTSALDPLhqhTTLH----AVREFAGRGAAVLVILHDLNLAARYCDRLLLLhDGRP 216
Cdd:COG1116 152 ALAN-----DPEVLLMDEPFGALDAL---TRERlqdeLLRLWQETGKTVLFVTHDVDEAVFLADRVVVL-SARP 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-227 |
1.07e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLdGRALeqwqgterarRLAVL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQS-SSLNFAFSVesvvgfgrlphdsgrqrdLQIIAEAMAAADASHLagRSYL---------------SLSGGERQRVHL 144
Cdd:COG0488 384 DQHqEELDPDKTV------------------LDELRDGAPGGTEQEV--RGYLgrflfsgddafkpvgVLSGGEKARLAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 145 ARVLAQlwpgGAeQVLLLDEPTSALDPlhqhTTLHAV----REFAGrgaAVLVILHDLNLAARYCDRLLLLHDGRPHLF- 219
Cdd:COG0488 444 AKLLLS----PP-NVLLLDEPTNHLDI----ETLEALeealDDFPG---TVLLVSHDRYFLDRVATRILEFEDGGVREYp 511
|
....*...
gi 759600243 220 GTPDEVLR 227
Cdd:COG0488 512 GGYDDYLE 519
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-222 |
1.86e-26 |
|
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: 102.66 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAGgSVSLDGRALEQWQGTE---RARRLAVLPQSSS 85
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPTSG-SVLVDGTDLTLLSGKElrkARRRIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 LnfaFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGR--SYLS-LSGGERQRVHLARVLAqlwpgGAEQVLLL 162
Cdd:cd03258 93 L---LSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKadAYPAqLSGGQKQRVGIARALA-----NNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 163 DEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGR-------PHLFGTP 222
Cdd:cd03258 165 DEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEvveegtvEEVFANP 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-231 |
2.52e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFL-FSGTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLPHDsgrqrDLQIIaeamaaadasHLAGRSYL--------------------SLSGGERQRVHLARVLAQlwpgg 155
Cdd:COG1132 434 IRYGRPDAT-----DEEVE----------EAAKAAQAhefiealpdgydtvvgergvNLSGGQRQRIAIARALLK----- 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 156 AEQVLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVLRAEPL 231
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELLARGGL 567
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-227 |
3.21e-26 |
|
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: 103.11 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE----RARRL-------A 78
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKIsmvfqsfA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSSL-NFAFSVEsVVGfgrLPHDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAQlwpggAE 157
Cdd:cd03294 113 LLPHRTVLeNVAFGLE-VQG---VPRAEREERAAEALELVGLEGWEHKYPDE----LSGGMQQRVGLARALAV-----DP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 158 QVLLLDEPTSALDPL----HQHTTLHAVREfagRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:cd03294 180 DILLMDEAFSALDPLirreMQDELLRLQAE---LQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-229 |
8.03e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.58 E-value: 8.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARrLAVLPQSS 84
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSV-ESVVGFGR---LPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:PRK13537 90 NLDPDFTVrENLLVFGRyfgLSAAAARAL----VPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN-----DPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-220 |
1.31e-25 |
|
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: 99.96 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGeVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLP 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGF-GRLPHDSGRQRDLQIIAEAMAAADASHlAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVL 160
Cdd:cd03264 79 QEFGVYPNFTVREFLDYiAWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALV-----GDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 161 LLDEPTSALDPLHQhttlHAVREFAGR-GAAVLVIL--HDLNLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03264 153 IVDEPTAGLDPEER----IRFRNLLSElGEDRIVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-224 |
1.41e-25 |
|
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: 102.08 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLPQSSSLNFAFS 91
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 -VESVVGFGRL---PHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTS 167
Cdd:TIGR01188 83 gRENLEMMGRLyglPKDEAEERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLI-----HQPDVLFLDEPTT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 168 ALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDE 224
Cdd:TIGR01188 154 GLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-224 |
1.94e-25 |
|
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: 99.75 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERaRRLAVLPQS 83
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAFS-VESVVGFGRL---PHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAQlwpggAEQV 159
Cdd:cd03265 82 LSVDDELTgWENLYIHARLygvPGAERRERIDELLDFVGLLEAADRLVK----TYSGGMRRRLEIARSLVH-----RPEV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 160 LLLDEPTSALDPlhqHTTLHA-------VREFagrGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDE 224
Cdd:cd03265 153 LFLDEPTIGLDP---QTRAHVweyieklKEEF---GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
2.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALE-QWQGTERARRLA--VLPQSSSLNFAFS 91
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVgiVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFG----RLPHDSGRQR---DLQIIAEAMAAADASHlagrsylSLSGGERQRVHLARVLAQlwpggAEQVLLLDE 164
Cdd:PRK13639 96 VEEDVAFGplnlGLSKEEVEKRvkeALKAVGMEGFENKPPH-------HLSGGQKKRVAIAGILAM-----KPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 165 PTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-234 |
2.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALE-QWQGTERARRLA--VLPQSSSLNFAFSVE 93
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRESVgmVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVVGFG----RLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSAL 169
Cdd:PRK13636 102 QDVSFGavnlKLPEDEVRKR----VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM-----EPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 170 DPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL-RAEPLRQV 234
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFaEKEMLRKV 239
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-239 |
3.06e-25 |
|
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: 100.20 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDG-RALEQWQGTERARRLAVLPQSSSLNF-AFSVE 93
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGMVFQNPDNQFvGATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVVGFG----RLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPTSAL 169
Cdd:TIGR04520 97 DDVAFGlenlGVPREEMRKR----VDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA-MRP----DIIILDEATSML 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 170 DPLHQH---TTLHAVREfaGRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVL-RAEPLRQvFGLDV 239
Cdd:TIGR04520 168 DPKGRKevlETIRKLNK--EEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFsQVELLKE-IGLDV 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-226 |
4.19e-25 |
|
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: 99.33 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTvKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTEraRRLAVLP 81
Cdd:cd03299 1 LKVENLS-KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFG-RLPHDSGRQRDLQIIaEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVL 160
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGlKKRKVDKKEIERKVL-EIAEMLGIDHLLNRKPETLSGGEQQRVAIARALV-VNP----KIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVReFAGR--GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELK-KIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-201 |
4.71e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 97.88 E-value: 4.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQG--TERARRLAVLPQSSSLN-F 88
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglLERRQRVGLVFQDPDDQlF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 AFSVESVVGFGR----LPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDE 164
Cdd:TIGR01166 83 AADVDQDVAFGPlnlgLSEAEVERR----VREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVA-MRP----DVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 759600243 165 PTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLA 201
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-226 |
5.40e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARrLAVLPQSSSLNFAFS 91
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 V-ESVVGFGRLPHDSGRQRDlQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALD 170
Cdd:PRK13536 131 VrENLLVFGRYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN-----DPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 171 PLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:PRK13536 205 PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-226 |
5.44e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 21 SLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGralEQWQGTERARR-LAVLPQSSSLNFAFSVESVVGFG 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRpVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 100 -----RLPHDSGRQRDlQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAQLWPggaeqVLLLDEPTSALDPLHQ 174
Cdd:PRK10771 96 lnpglKLNAAQREKLH-AIARQMGIEDLLARLPGQ----LSGGQRQRVALARCLVREQP-----ILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759600243 175 HTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:PRK10771 166 QEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
1.84e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAVLPQS 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAFSVESVV--GFGRL-----------------PHDSGRQRDLQIIAEAMAAADASH-----LAG---------RS 130
Cdd:COG0488 70 PPLDDDLTVLDTVldGDAELraleaeleeleaklaepDEDLERLAELQEEFEALGGWEAEAraeeiLSGlgfpeedldRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 131 YLSLSGGERQRVHLARVLAQLWpggaeQVLLLDEPTSALDplhqhttLHAVR---EF-AGRGAAVLVILHDlnlaaRY-- 204
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEP-----DLLLLDEPTNHLD-------LESIEwleEFlKNYPGTVLVVSHD-----RYfl 212
|
250
....*....|....*...
gi 759600243 205 ---CDRLLLLHDGRPHLF 219
Cdd:COG0488 213 drvATRILELDRGKLTLY 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-215 |
2.49e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAG----GSVSLDG-RALEQWQGTERA 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLlEQPEAGtirvGDITIDTaRSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 RRLAV---------LPQSSSLNFAfsVESVVGFGRLPHDSGRQRDLQIIAEAMaaadashLAGR--SY-LSLSGGERQRV 142
Cdd:PRK11264 83 LRQHVgfvfqnfnlFPHRTVLENI--IEGPVIVKGEPKEEATARARELLAKVG-------LAGKetSYpRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 143 HLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK11264 154 AIARALAM-----RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-228 |
2.66e-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: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERA---RRL 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLnFA-FSV-----ESVVGFGRLPHDSGRQRdlqiiaeamaaadashlaGRSYL--------------SLSGG 137
Cdd:COG1126 80 GMVFQQFNL-FPhLTVlenvtLAPIKVKKMSKAEAEER------------------AMELLervgladkadaypaQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 138 ERQRVHLARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPH 217
Cdd:COG1126 141 QQQRVAIARALA-MEP----KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
250
....*....|.
gi 759600243 218 LFGTPDEVLRA 228
Cdd:COG1126 216 EEGPPEEFFEN 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-207 |
2.94e-24 |
|
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: 98.59 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELP---LAGGSVSLDGRALEQWQGTE- 72
Cdd:COG0444 1 LLEVRNLKVyfptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 73 ---RARRLAVLPQS--SSLNFAFSV-----ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLagRSY-LSLSGGERQR 141
Cdd:COG0444 81 rkiRGREIQMIFQDpmTSLNPVMTVgdqiaEPLRIHGGLSKAEARERAIELLERVGLPDPERRL--DRYpHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 142 VHLARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDR 207
Cdd:COG0444 159 VMIARALA-LEP----KLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADR 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-215 |
3.43e-24 |
|
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: 96.06 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwqgTERA-----RRLA 78
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD---DKKNinelrQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSSL--------NFAFSVESVVGfgrLPHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAq 150
Cdd:cd03262 80 MVFQQFNLfphltvleNITLAPIKVKG---MSKAEAEERALELLEKVGLADKADAYPA----QLSGGQQQRVAIARALA- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 151 LWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03262 152 MNP----KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-216 |
3.73e-24 |
|
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: 96.21 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 26 PGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqWQGTE-------RARRLAVLPQSSSLNFAFSVESVVGF 98
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRkkinlppQQRKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 99 GRLPHDSGRQRDLqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTL 178
Cdd:cd03297 99 GLKRKRNREDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAA-----QPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 759600243 179 HAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRP 216
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-215 |
1.13e-23 |
|
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: 94.87 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 21 SLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERArrLAVLPQSSSLNFAFSVESVVGFGR 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 101 LPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPggaeqVLLLDEPTSALDPLHQHTTLHA 180
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP-----VLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 759600243 181 VREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-228 |
1.55e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR--ALeqwqgterarrLAVlpqSSSLN 87
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsAL-----------LEL---GAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 88 FAFS----------------------VESVVGFGRLphdsGRQRDLQIiaeamaaadashlagRSYlslSGGERQRVHLA 145
Cdd:COG1134 101 PELTgreniylngrllglsrkeidekFDEIVEFAEL----GDFIDQPV---------------KTY---SSGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 146 rVLAQLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:COG1134 159 -VATAVDP----DILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
...
gi 759600243 226 LRA 228
Cdd:COG1134 234 IAA 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
2.00e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 94.81 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVK----RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPlAGGSVSLDGRALEQWQGTERAR 75
Cdd:COG4181 8 IIELRGLTKTvgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRP-TSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 RLA-----VLpQSSSLNFAFS-VESVVgfgrLP-----HDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHL 144
Cdd:COG4181 87 LRArhvgfVF-QSFQLLPTLTaLENVM----LPlelagRRDARARARALLERVGLGHRLDHYPAQ----LSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 145 ARVLAqlwpgGAEQVLLLDEPTSALDplhqHTTLHAVRE--FA---GRGAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:COG4181 158 ARAFA-----TEPAILFADEPTGNLD----AATGEQIIDllFElnrERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-215 |
2.01e-23 |
|
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: 94.19 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVE 93
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTL-FYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVVGFGRLPHDSgrQRDLQIIAEAMAAA-DASHLAGRSYL------SLSGGERQRVHLARVLAQLWPggaeqVLLLDEPT 166
Cdd:cd03245 96 DNITLGAPLADD--ERILRAAELAGVTDfVNKHPNGLDLQigergrGLSGGQRQAVALARALLNDPP-----ILLLDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759600243 167 SALDPLHQHTTLHAVREFAGrGAAVLVILHDLNLAArYCDRLLLLHDGR 215
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-227 |
2.67e-23 |
|
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: 94.67 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLT-VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQS 83
Cdd:cd03295 4 ENVTkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAFSVESVVGFgrLPHDSG------RQRDLQIIAEAMAAADasHLAGRSYLSLSGGERQRVHLARVLAqlwpggAE 157
Cdd:cd03295 84 IGLFPHMTVEENIAL--VPKLLKwpkekiRERADELLALVGLDPA--EFADRYPHELSGGQQQRVGVARALA------AD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 158 Q-VLLLDEPTSALDPLH----QHTTLHAVREFagrGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:cd03295 154 PpLLLMDEPFGALDPITrdqlQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
3.73e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.58 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVK-RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA---RR 76
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSSL--------NFAFSVEsVVGFgrlPHDSGRQRDLQIIAEAmaaadasHLAGRSYL---SLSGGERQRVHLA 145
Cdd:COG2884 81 IGVVFQDFRLlpdrtvyeNVALPLR-VTGK---SRKEIRRRVREVLDLV-------GLSDKAKAlphELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 146 RVLAqlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG2884 150 RALV-----NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 |
5.35e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTvKR-GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeQWQGTERARRL-- 77
Cdd:COG1129 4 LLEMRGIS-KSfGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAAgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNFAFSVESVVGFGRLPHDSG-------RQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAQ 150
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGGlidwramRRRARELLARLGLDIDPDTPVG----DLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 151 lwpgGAeQVLLLDEPTSALDPlHQHTTLHA-VREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG1129 158 ----DA-RVLILDEPTASLTE-REVERLFRiIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGR 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-215 |
5.47e-23 |
|
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: 91.99 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTeRARRLAVLPQSSSLnFAFSVE 93
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVLNQRPYL-FDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVVGfgrlphdsgrqrdlqiiaeamaaadashlagrsyLSLSGGERQRVHLARVLAQLWPggaeqVLLLDEPTSALDPLH 173
Cdd:cd03247 93 NNLG----------------------------------RRFSGGERQRLALARILLQDAP-----IVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 759600243 174 QHTTLHAVREFAgRGAAVLVILHDLnLAARYCDRLLLLHDGR 215
Cdd:cd03247 134 ERQLLSLIFEVL-KDKTLIWITHHL-TGIEHMDKILFLENGK 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-225 |
6.61e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.53 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwqgTE---RARRL 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDlppKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQssslNFA----FSVESVVGFG-RLPHDSGRQRD---------LQIiaeamaaadaSHLAGRSYLSLSGGERQRVH 143
Cdd:COG3839 78 AMVFQ----SYAlyphMTVYENIAFPlKLRKVPKAEIDrrvreaaelLGL----------EDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 144 LARVLAqlwpggAE-QVLLLDEPTSALDP------------LHQ---HTTLHAVrefagrgaavlvilHD----LNLAar 203
Cdd:COG3839 144 LGRALV------REpKVFLLDEPLSNLDAklrvemraeikrLHRrlgTTTIYVT--------------HDqveaMTLA-- 201
|
250 260
....*....|....*....|..
gi 759600243 204 ycDRLLLLHDGRPHLFGTPDEV 225
Cdd:COG3839 202 --DRIAVMNDGRIQQVGTPEEL 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-215 |
6.87e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.14 E-value: 6.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAGgSVSLDGRALEQWQGTE--R 73
Cdd:COG1135 1 MIELENLSktfpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERPTSG-SVLVDGVDLTALSERElrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 ARR-LAVLPQSSSL--------NFAFSVEsVVGFGRlphdsgRQRD------LQIIaeamaaadasHLAGR--SYLS-LS 135
Cdd:COG1135 80 ARRkIGMIFQHFNLlssrtvaeNVALPLE-IAGVPK------AEIRkrvaelLELV----------GLSDKadAYPSqLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 136 GGERQRVHLARVLAqlwpgGAEQVLLLDEPTSALDPlhqHTTlHAV--------REFagrGAAVLVILHDLNLAARYCDR 207
Cdd:COG1135 143 GGQKQRVGIARALA-----NNPKVLLCDEATSALDP---ETT-RSIldllkdinREL---GLTIVLITHEMDVVRRICDR 210
|
....*...
gi 759600243 208 LLLLHDGR 215
Cdd:COG1135 211 VAVLENGR 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-215 |
9.54e-23 |
|
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: 92.92 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVL-FARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLPHDSGRQRDLQIIAE-----AMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALD 170
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAHahsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIR-----NPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759600243 171 PLHQHTTLHAVREFAGRgAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:cd03248 183 AESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-214 |
1.01e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.23 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERarrlAVL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVL 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA-----ANPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 161 LLDEPTSALDPL--HQHTTLhAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:PRK11248 151 LLDEPFGALDAFtrEQMQTL-LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-211 |
1.16e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERArr 76
Cdd:COG4525 3 MLTVRHVSVrypgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 laVLPQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGA 156
Cdd:COG4525 80 --VVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA-----AD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 157 EQVLLLDEPTSALDPL---HQHTTLhaVREFAGRGAAVLVILHDLNLAARYCDRLLLL 211
Cdd:COG4525 153 PRFLLMDEPFGALDALtreQMQELL--LDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-201 |
1.30e-22 |
|
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: 91.65 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGtERARRLAVLP 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFGRLPHDsGRQRDlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARvlaqLWPGGAeQVLL 161
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHG-GAQRT---IEDALAAVGLTGFEDLPAAQLSAGQQRRLALAR----LWLSRR-PLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILH-DLNLA 201
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHqDLGLV 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-201 |
2.05e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.47 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEqwqGTERARRLAVL 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPggaeqVL 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEFWAAFLGGEELD----IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP-----IW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILH-DLNLA 201
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLP 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-225 |
2.75e-22 |
|
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: 91.63 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRalEQWQGTERARRLAVLPQSS 84
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSVESVVGFG-RLPHDSGRQRDLQI---IAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVL 160
Cdd:cd03296 84 ALFRHMTVFDNVAFGlRVKPRSERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA-VEP----KVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-215 |
3.39e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 90.18 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRgrqvVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAV 79
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LP---QSSSLNFAFSVESVVGFGRLphdsgrqrdlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAQlwpggA 156
Cdd:cd03215 80 VPedrKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLAR-----D 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 157 EQVLLLDEPTSALDP-----LHQhttlhAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03215 123 PRVLILDEPTRGVDVgakaeIYR-----LIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
4.44e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENL--TVKRGR---QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERAR 75
Cdd:COG1101 1 MLELKNLskTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 RLAVLPQ------SSSL----NFAFSvesvvgFGRlphdsGRQRDLQIiaeAMAAADASHLagRSYLS------------ 133
Cdd:COG1101 81 YIGRVFQdpmmgtAPSMtieeNLALA------YRR-----GKRRGLRR---GLTKKRRELF--RELLAtlglglenrldt 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 134 ----LSGGERQRVHLarVLAQLWPggaEQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRL 208
Cdd:COG1101 145 kvglLSGGQRQALSL--LMATLTK---PKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRL 219
|
....*..
gi 759600243 209 LLLHDGR 215
Cdd:COG1101 220 IMMHEGR 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-215 |
9.31e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 89.45 E-value: 9.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGraleqwqgterarRLAVLPQSSSLNFAfSVESV 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRlPHDSGR----------QRDLQIiaeamaaadashLA-------GRSYLSLSGGERQRVHLARVLAQLwpggaEQ 158
Cdd:cd03250 86 ILFGK-PFDEERyekvikacalEPDLEI------------LPdgdlteiGEKGINLSGGQKQRISLARAVYSD-----AD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 159 VLLLDEPTSALDPlhqHTTLH----AVREFAGRGAAVLVILHDLNLaARYCDRLLLLHDGR 215
Cdd:cd03250 148 IYLLDDPLSAVDA---HVGRHifenCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-220 |
9.73e-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: 89.15 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVK------RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAG--GSVSLDGRALEQWQGter 73
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 ARRLAVLPQSSSLnfafsvesvvgfgrLPHDSGRQrDLQIIaeamaaadaSHLAGrsylsLSGGERQRVHLARVLAQlwp 153
Cdd:cd03213 81 RKIIGYVPQDDIL--------------HPTLTVRE-TLMFA---------AKLRG-----LSGGERKRVSIALELVS--- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 154 ggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDL-NLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03213 129 --NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-228 |
1.65e-21 |
|
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: 92.83 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTV----KRG---RQV----VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPlAGGSVSLDGRALEQWQG 70
Cdd:COG4172 276 LEARDLKVwfpiKRGlfrRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 71 TERA---RRLAVLPQS--SSLNFAFSVESVVGFGRLPHD---SGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRV 142
Cdd:COG4172 355 RALRplrRRMQVVFQDpfGSLSPRMTVGQIIAEGLRVHGpglSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 143 HLARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGT 221
Cdd:COG4172 435 AIARALI-LEP----KLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
....*..
gi 759600243 222 PDEVLRA 228
Cdd:COG4172 510 TEQVFDA 516
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-235 |
1.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL----EQWQgteRARRLAVLPQSSSLNFAFSV 92
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaenEKWV---RSKVGLVFQDPDDQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 93 ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPL 172
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM-----DPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 173 HQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR------PHLFGTPDEV----LRAEPLRQVF 235
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRvlaegdKSLLTDEDIVeqagLRLPLVAQIF 245
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-249 |
2.01e-21 |
|
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: 91.32 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqWQGTER-------ARRLAVLPQSSSLnFA-FS 91
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARgiflpphRRRIGYVFQEARL-FPhLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFG--RLPHDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSAL 169
Cdd:COG4148 94 VRGNLLYGrkRAPRAERRISFDEVVELLGI----GHLLDRRPATLSGGERQRVAIGRALL-----SSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 170 DP------------LHQHTTLhavrefagrgaAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR---AEPLRQV 234
Cdd:COG4148 165 DLarkaeilpylerLRDELDI-----------PILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSrpdLLPLAGG 233
|
250
....*....|....*....
gi 759600243 235 FG----LDVLVQRHPERGH 249
Cdd:COG4148 234 EEagsvLEATVAAHDPDYG 252
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-225 |
2.73e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.44 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAgGSVSLDGRALEQWQGTERArrLAV 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTA-GQIMLDGVDLSHVPPYQRP--INM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLNFAFSVESVVGFG----RLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpgg 155
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGlkqdKLPKAEIASR----VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK----- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 156 AEQVLLLDEPTSALD-PLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK11607 167 RPKLLLLDEPMGALDkKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
3.36e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.77 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAG----GSVSLDGRALEQWQGT-ERAR 75
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSGyrysGDVLLGGRSIFNYRDVlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 RLAVLPQSSSlNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLS-----LSGGERQRVHLARVLAQ 150
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfrLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 151 lwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRgAAVLVILHDLNLAARYCDRLLLLHDGR-------PHLFGTPD 223
Cdd:PRK14271 181 -----NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRlveegptEQLFSSPK 254
|
250
....*....|....
gi 759600243 224 EvlrAEPLRQVFGL 237
Cdd:PRK14271 255 H---AETARYVAGL 265
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-225 |
4.14e-21 |
|
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: 88.45 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTEraRRLAVLPQSS 84
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSVESVVGFG----RLPHDSGRQRDLQIIaeamAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVL 160
Cdd:cd03300 82 ALFPHLTVFENIAFGlrlkKLPKAEIKERVAEAL----DLVQLEGYANRKPSQLSGGQQQRVAIARALV-NEP----KVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 161 LLDEPTSALD-PLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:cd03300 153 LLDEPLGALDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
4.97e-21 |
|
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: 85.96 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAVLP 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QssslnfafsvesvvgfgrlphdsgrqrdlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAQlwpgGAEqVLL 161
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLE----NPN-LLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREFAGrgaAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-235 |
5.29e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.40 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQgTERARR--LA 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQ-TAKIMReaVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSSLNFAFSVESVVGFGRLPHDsgRQRDLQIIAEA-----MAAADASHLAGrsylSLSGGERQRVHLARVLAQlwp 153
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVyelfpRLHERRIQRAG----TMSGGEQQMLAIGRALMS--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 154 ggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQ 233
Cdd:PRK11614 155 --QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
..
gi 759600243 234 VF 235
Cdd:PRK11614 233 AY 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-198 |
6.58e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 91.27 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFS 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFGRlphdsGRQRDLQIIAEAMAAADASHLAGRSY----------LSLSGGERQRVHLARVLAQLWPggaeqVLL 161
Cdd:TIGR02868 425 VRENLRLAR-----PDATDEELWAALERVGLADWLRALPDgldtvlgeggARLSGGERQRLALARALLADAP-----ILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREfAGRGAAVLVILHDL 198
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-226 |
6.65e-21 |
|
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: 88.06 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVL-FNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLphDSGrqrDLQIIAEAMAAADA----------SHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:cd03253 95 IRYGRP--DAT---DEEVIEAAKAAQIHdkimrfpdgyDTIVGERGLKLSGGEKQRVAIARAILK-----NPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 166 TSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:cd03253 165 TSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-224 |
6.99e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 7 LTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELP---LAGGSVSLDGRALEQWQgterARRLAVLPQS 83
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKE----MRAISAYVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNF-AFSVESVVGFG-------RLPHDSGRQRDLQIIAEAMAAADASHLAGRSYL--SLSGGERQRVHLARVLAQLWP 153
Cdd:TIGR00955 107 DDLFIpTLTVREHLMFQahlrmprRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 154 ggaeqVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNlAARYC--DRLLLLHDGRPHLFGTPDE 224
Cdd:TIGR00955 187 -----LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-235 |
1.69e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 87.63 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVK-RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwqgTERARRLAVL 80
Cdd:PRK15056 7 IVVNDVTVTwRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSV--ESVVGFGRLPH----DSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpg 154
Cdd:PRK15056 84 PQSEEVDWSFPVlvEDVVMMGRYGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 155 gAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFGTPDEVLRAEPLRQV 234
Cdd:PRK15056 160 -QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELA 237
|
.
gi 759600243 235 F 235
Cdd:PRK15056 238 F 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-219 |
1.77e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG----------ELPLAGGSVSLDGRALEQWQGTeRARRLAVLPQSSSL 86
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLARDIRKS-RANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSVESVV--GFGRLP---------HDSGRQRDLQIIaeamAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpgg 155
Cdd:PRK09984 99 NRLSVLENVLigALGSTPfwrtcfswfTREQKQRALQAL----TRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ----- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 156 AEQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGrpHLF 219
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG--HVF 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-233 |
1.99e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 87.16 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAGgSVSLDGRALeQWQGTERARRLAV 79
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLlETPDSG-EIRVGGEEI-RLKPDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQS-----SSLNFAFSvesvvGFGRLPHDS-------------GRQRDlQIIAEAMAAADASHLAGR--SYLS-LSGGE 138
Cdd:COG4598 86 DRRQlqrirTRLGMVFQ-----SFNLWSHMTvlenvieapvhvlGRPKA-EAIERAEALLAKVGLADKrdAYPAhLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 139 RQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHL 218
Cdd:COG4598 160 QQRAAIARALAM-----EPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEE 234
|
250
....*....|....*...
gi 759600243 219 FGTPDEVL---RAEPLRQ 233
Cdd:COG4598 235 QGPPAEVFgnpKSERLRQ 252
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
10-227 |
3.79e-20 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 87.99 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE----RARRLAVLPQSSS 85
Cdd:TIGR01186 2 KTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevRRKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 LNFAFSVESVVGFG----RLPHDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVHLARVLAQLWPggaeqVLL 161
Cdd:TIGR01186 82 LFPHMTILQNTSLGpellGWPEQERKEKALELLKLVGL----EEYEHRYPDELSGGMQQRVGLARALAAEPD-----ILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:TIGR01186 153 MDEAFSALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILR 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-215 |
4.88e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.56 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSL--DGRALEQWQGTERA----RR---------LAV 79
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREilalRRrtigyvsqfLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLNFAfsVESVVGFGrLPHDSGRQR------DLQIiaeamaaadASHLAGRSYLSLSGGERQRVHLARVLAQLWP 153
Cdd:COG4778 105 IPRVSALDVV--AEPLLERG-VDREEARARarellaRLNL---------PERLWDLPPATFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 154 ggaeqVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG4778 173 -----LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-239 |
6.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwQGTERARRLAVLPQSSSLNFAF------ 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI---TAGKKNKKLKPLRKKVGIVFQFpehqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 --SVESVVGFGRL----PHDSGRQRDLQIIAEAMAAADASHlagRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDE 164
Cdd:PRK13634 100 eeTVEKDICFGPMnfgvSEEDAKQKAREMIELVGLPEELLA---RSPFELSGGQMRRVAIAGVLA-MEP----EVLVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 165 PTSALDPLHQH------TTLHavREfagRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR-AEPLRQvFGL 237
Cdd:PRK13634 172 PTAGLDPKGRKemmemfYKLH--KE---KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdPDELEA-IGL 245
|
..
gi 759600243 238 DV 239
Cdd:PRK13634 246 DL 247
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-215 |
1.04e-19 |
|
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: 84.19 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGralEQWQGTERA-RRLAVLPQS 83
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEAlRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAFSVESVVGFGRLPHDSGRQRDLQIIaeamAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLD 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVL----DVVGLKDSAKKKVKGFSLGMKQRLGIALALL-----GNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 164 EPTSALDPLhqhtTLHAVREF----AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03268 152 EPTNGLDPD----GIKELRELilslRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
1.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.43 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQV--VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLA 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSSLNF-AFSVESVVGFG----RLPhdsgRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWP 153
Cdd:PRK13632 87 IIFQNPDNQFiGATVEDDIAFGlenkKVP----PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA-LNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 154 ggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLV-ILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAEPLR 232
Cdd:PRK13632 162 ----EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
....*..
gi 759600243 233 QVFGLDV 239
Cdd:PRK13632 237 EKAKIDS 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-210 |
1.15e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 84.08 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLP 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFGRLPHDSGRqrdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVL---AQLWpggaeq 158
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLlsgRPLW------ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759600243 159 vlLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILH-DLNLAARYCDRLLL 210
Cdd:cd03231 148 --ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-226 |
1.30e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.02 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE--------- 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 73 -----RARRLAVLPQSSSLNFAFSVESV----VGFGRLPHDSGRQRDLQIIAEAMAAADAShlaGRSYLSLSGGERQRVH 143
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVmeapIQVLGLSKQEARERAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 144 LARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPD 223
Cdd:PRK10619 163 IARALAM-----EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
...
gi 759600243 224 EVL 226
Cdd:PRK10619 238 QLF 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-239 |
2.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQV---VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRL 77
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNF-AFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPgga 156
Cdd:PRK13642 84 GMVFQNPDNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA-LRP--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 157 eQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVF 235
Cdd:PRK13642 160 -EIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
....
gi 759600243 236 GLDV 239
Cdd:PRK13642 238 GLDV 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-234 |
2.66e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 11 RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLN-FA 89
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQiFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 FSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSAL 169
Cdd:PRK13652 94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM-----EPQVLVLDEPTAGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 170 DPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV-LRAEPLRQV 234
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARV 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-239 |
2.71e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.71 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwqgTERARRLAVLPQSSSLNFAF---- 90
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-----TDKKVKLSDIRKKVGLVFQYpeyq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 ----SVESVVGFGrlPHDSGRQRD---------LQIIaeamaAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggae 157
Cdd:PRK13637 96 lfeeTIEKDIAFG--PINLGLSEEeienrvkraMNIV-----GLDYEDYKDKSPFELSGGQKRRVAIAGVVA-MEP---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR-AEPLRQVf 235
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKeVETLESI- 242
|
....
gi 759600243 236 GLDV 239
Cdd:PRK13637 243 GLAV 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
2.87e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTvKR-GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqGTERARRLAV 79
Cdd:COG3845 5 ALELRGIT-KRfGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIR-SPRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 --LPQSSSLNFAFSV-ESVV------GFGRLPHDSGRQRdlqiiaeamaaadASHLAGRSYL---------SLSGGERQR 141
Cdd:COG3845 83 gmVHQHFMLVPNLTVaENIVlgleptKGGRLDRKAARAR-------------IRELSERYGLdvdpdakveDLSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 142 VHLARVLAQlwpgGAEqVLLLDEPTSALDPlhQHTT--LHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG3845 150 VEILKALYR----GAR-ILILDEPTAVLTP--QEADelFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-215 |
2.88e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALN-------GELPLAGGSVSLDGRALEQwQGTERARRLAVLPQSS 84
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlletpdsGQLNIAGHQFDFSQKPSEK-AIRLLRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSV-----ESVVGFGRLPHDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVHLARVLaQLWPggaeQV 159
Cdd:COG4161 92 NLWPHLTVmenliEAPCKVLGLSKEQAREKAMKLLARLRL----TDKADRFPLHLSGGQQQRVAIARAL-MMEP----QV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-239 |
2.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVK------RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA 74
Cdd:PRK13633 4 MIKCKNVSYKyesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 RRLA--VLPQSSSLNFAFSVESVVGFGR----LPHDSGRQR---DLQIIAEAMAAADASHLagrsylsLSGGERQRVHLA 145
Cdd:PRK13633 84 RNKAgmVFQNPDNQIVATIVEEDVAFGPenlgIPPEEIRERvdeSLKKVGMYEYRRHAPHL-------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 146 RVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDE 224
Cdd:PRK13633 157 GILA-MRP----ECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKE 230
|
250
....*....|....*
gi 759600243 225 VLRAEPLRQVFGLDV 239
Cdd:PRK13633 231 IFKEVEMMKKIGLDV 245
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-251 |
4.22e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR---L 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRqqvA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAE 157
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL-----QA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL-RAEPLRQVfG 236
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAMEQA-G 234
|
250
....*....|....*..
gi 759600243 237 LDV--LVQRHPERGHPL 251
Cdd:PRK13638 235 LTQpwLVKLHTQLGLPL 251
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-231 |
5.08e-19 |
|
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: 82.92 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSL-------- 86
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLfnrsirdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 ----NFAFSVESVVGFGRL--PHDSGRQrdlqiiaeamAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:cd03252 96 ialaDPGMSMERVIEAAKLagAHDFISE----------LPEGYDTIVGEQGAGLSGGQRQRIAIARALIH-----NPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREF-AGRgaAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVLRAEPL 231
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIcAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-227 |
6.04e-19 |
|
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: 84.78 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL-EQWQG----TERaRRLAVLPQSSSLNFAFSVES 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGiflpPEK-RRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 95 --VVGFGRLPHDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPL 172
Cdd:TIGR02142 95 nlRYGMKRARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLS-----SPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 173 HQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-235 |
1.02e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGteRARRLAVLPQSSSLNFAFS 91
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA--RDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFG--RLPHdsgRQR-DLQIIAEAMAAA----DASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDE 164
Cdd:PRK10851 91 VFDNIAFGltVLPR---RERpNAAAIKAKVTQLlemvQLAHLADRYPAQLSGGQKQRVALARALA-VEP----QILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 165 PTSALDP---------LHQhttLHAVREFAGrgaaVLVIlHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVF 235
Cdd:PRK10851 163 PFGALDAqvrkelrrwLRQ---LHEELKFTS----VFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-251 |
1.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.86 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLNF-AFSVESV 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGR----LPHDSGRQR---DLQIIaeamaaaDASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPTSA 168
Cdd:PRK13650 103 VAFGLenkgIPHEEMKERvneALELV-------GMQDFKEREPARLSGGQKQRVAIAGAVA-MRP----KIIILDEATSM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 169 LDP---LHQHTTLHAVREfaGRGAAVLVILHDLNLAArYCDRLLLLHDGRPHLFGTPDEVL-RAEPLRQVfGLDV----- 239
Cdd:PRK13650 171 LDPegrLELIKTIKGIRD--DYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFsRGNDLLQL-GLDIpftts 246
|
250
....*....|..
gi 759600243 240 LVQRHPERGHPL 251
Cdd:PRK13650 247 LVQSLRQNGYDL 258
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-215 |
1.15e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.81 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 6 NLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL-----EQWQGTERARRLAVL 80
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnrAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVG--FGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQ 158
Cdd:PRK10419 97 DSISAVNPRKTVREIIRepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAV-----EPK 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-227 |
1.20e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.85 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 8 TVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLdgRALEQW--------QGTERARR-LA 78
Cdd:TIGR03269 291 SVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--RVGDEWvdmtkpgpDGRGRAKRyIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSSL--------NF--AFSVEsvvgfgrLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLS-LSGGERQRVHLARV 147
Cdd:TIGR03269 369 ILHQEYDLyphrtvldNLteAIGLE-------LPDELARMKAVITLKMVGFDEEKAEEILDKYPDeLSEGERHRVALAQV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 148 LAQlwpggAEQVLLLDEPTSALDPLHQ----HTTLHAVREFagrGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPD 223
Cdd:TIGR03269 442 LIK-----EPRIVILDEPTGTMDPITKvdvtHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
....
gi 759600243 224 EVLR 227
Cdd:TIGR03269 514 EIVE 517
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-215 |
1.35e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALN-------GELPLAGGSVSLDGRALEQwQGTERARRLAVLPQSSSLNF 88
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLNIAGNHFDFSKTPSDK-AIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 AFSV-----ESVVGFGRLPHDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVHLARVLaQLWPggaeQVLLLD 163
Cdd:PRK11124 96 HLTVqqnliEAPCRVLGLSKDQALARAEKLLERLRL----KPYADRFPLHLSGGQQQRVAIARAL-MMEP----QVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759600243 164 EPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-215 |
1.39e-18 |
|
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: 81.61 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 9 VKRGRQVV--LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSL 86
Cdd:cd03267 27 FKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSVesVVGFG------RLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLaqLWpggAEQVL 160
Cdd:cd03267 107 WWDLPV--IDSFYllaaiyDLPPARFKKR----LDELSELLDLEELLDTPVRQLSLGQRMRAEIAAAL--LH---EPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 161 LLDEPTSALDPLHQhttlHAVREF-----AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03267 176 FLDEPTIGLDVVAQ----ENIRNFlkeynRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-245 |
1.43e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTE----RARRL 77
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNFAFSVESVVGFG-RLPHDSGRQRDLQIIAEAMAAADASHLAGRSYlSLSGGERQRVHLARVLAQlwpggA 156
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGmELAGINAEERREKALDALRQVGLENYAHSYPD-ELSGGMRQRVGLARALAI-----N 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 157 EQVLLLDEPTSALDPL-HQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL--------- 226
Cdd:PRK10070 183 PDILLMDEAFSALDPLiRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpandyvr 262
|
250 260
....*....|....*....|..
gi 759600243 227 ---RAEPLRQVFGLDVLVQRHP 245
Cdd:PRK10070 263 tffRGVDISQVFSAKDIARRTP 284
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-214 |
1.59e-18 |
|
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: 81.36 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPLAGGsVSLDGRALEQwQGTERA---RRLAVLP-QSSSLNFAFS 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGG-VILEGKQITE-PGPDRMvvfQNYSLLPwLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVvgfgrLPHDSGRQRDlQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPTSALDP 171
Cdd:TIGR01184 79 VDRV-----LPDLSKSERR-AIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALS-IRP----KVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 759600243 172 LH----QHTTLHAVREfagRGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:TIGR01184 148 LTrgnlQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-215 |
1.84e-18 |
|
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: 80.76 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTEraRRLAVLPQSS 84
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSVESVVGFG----RLPHDSGRQR------DLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLAqlwpg 154
Cdd:cd03301 82 ALYPHMTVYDNIAFGlklrKVPKDEIDERvrevaeLLQI----------EHLLDRKPKQLSGGQRQRVALGRAIV----- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 155 GAEQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-222 |
1.88e-18 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 80.92 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQV--VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQ 82
Cdd:cd03369 10 ENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLnFAFSVESVVGfgrlPHDsgRQRDLQIIAEAMAAAdashlagrSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLL 162
Cdd:cd03369 90 DPTL-FSGTIRSNLD----PFD--EYSDEEIYGALRVSE--------GGLNLSQGQRQLLCLARALL-----KRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 163 DEPTSALDPLHQHTTLHAVRE-FAgrGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTP 222
Cdd:cd03369 150 DEATASIDYATDALIQKTIREeFT--NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-214 |
2.16e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLL------GALNGELPLAGgSVSLDGRAL--EQWQGTE 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmNDLNPEVTITG-SIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 73 RARRLAVLPQSSSlNFAFSV-ESVVGFGRLPHDSGRQR-DLQIIAEAMAAADASHLAGR---SYLSLSGGERQRVHLARV 147
Cdd:PRK14239 84 LRKEIGMVFQQPN-PFPMSIyENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRlhdSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 148 LAQlwpggAEQVLLLDEPTSALDPLHQ---HTTLHAVREfagrGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:PRK14239 163 LAT-----SPKIILLDEPTSALDPISAgkiEETLLGLKD----DYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-237 |
3.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRL-AVLPQSSSLNF-AFSVES 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLvGIVFQNPETQFvGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 95 VVGFGR----LPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALD 170
Cdd:PRK13644 98 DLAFGPenlcLPPIEIRKR----VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM-----EPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 171 PLHQHTTLHAVREFAGRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVLrAEPLRQVFGL 237
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVL-SDVSLQTLGL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-226 |
4.67e-18 |
|
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: 80.35 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFL-FSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLphDSGRQRDLQIIAEAMAAADASHL-------AGRSYLSLSGGERQRVHLAR-VLAQlwpggaEQVLLLDEPTS 167
Cdd:cd03254 97 IRLGRP--NATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARaMLRD------PKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 168 ALDPLHQHTTLHAVRE-FAGRgaAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:cd03254 169 NIDTETEKLIQEALEKlMKGR--TSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-225 |
5.13e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.93 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--------------------------------ELP 52
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyverpskvgePCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 53 LAGGSVSLDGRALEQWQGTERA---RRLAVLPQSSslnFAFSVESVV-----------GFgrlPHDSGRQRDLQIIAEAM 118
Cdd:TIGR03269 84 VCGGTLEPEEVDFWNLSDKLRRrirKRIAIMLQRT---FALYGDDTVldnvlealeeiGY---EGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 119 AAADASHLAgrsyLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVIL-HD 197
Cdd:TIGR03269 158 LSHRITHIA----RDLSGGEKQRVVLARQLAK-----EPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHW 228
|
250 260
....*....|....*....|....*...
gi 759600243 198 LNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-215 |
6.74e-18 |
|
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: 79.37 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA---RRLAVLPQSSSL----- 86
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRLlpdrn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 ---NFAFSVEsVVGfgrLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLD 163
Cdd:cd03292 95 vyeNVAFALE-VTG---VPPREIRKR----VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN-----SPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759600243 164 EPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-214 |
7.60e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 7.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKST----LLGALNGElplagGSVSLDGRALEQW---QGTERARRLAVLPQ-- 82
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLnrrQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLNFAFSVESVVGFG---RLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQV 159
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGlrvHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALI-LKP----SL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-215 |
9.12e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA----RRLAVLPQSSSLNFAFS 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 -VESVVgfgrLPHDSGRQRDLQIIAEAMAAADASHLAGRSY---LSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTS 167
Cdd:PRK11629 104 aLENVA----MPLLIGKKKPAEINSRALEMLAAVGLEHRANhrpSELSGGERQRVAIARALVN-----NPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759600243 168 ALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYcDRLLLLHDGR 215
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 |
9.94e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.99 E-value: 9.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRgrqvVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwqGTER---ARRL 77
Cdd:COG1129 256 VLEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI--RSPRdaiRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 A-----------VLPQSSSLNFAFSV-ESVVGFGRLphDSGRQR--------DLQIiaeamAAADASHLAGrsylSLSGG 137
Cdd:COG1129 330 AyvpedrkgeglVLDLSIRENITLASlDRLSRGGLL--DRRRERalaeeyikRLRI-----KTPSPEQPVG----NLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 138 ERQRVHLARVLAqlwpggAE-QVLLLDEPTSALDP-----LHQhttlhAVREFAGRGAAVLVILHDLNLAARYCDRLLLL 211
Cdd:COG1129 399 NQQKVVLAKWLA------TDpKVLILDEPTRGIDVgakaeIYR-----LIRELAAEGKAVIVISSELPELLGLSDRILVM 467
|
....
gi 759600243 212 HDGR 215
Cdd:COG1129 468 REGR 471
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-222 |
1.01e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 79.07 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVK--RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqGTERAR-RLAVLP 81
Cdd:cd03244 6 KNVSLRyrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRsRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLnFAFSVESVVGfgrlPHdsGRQRDLQIIAEAMAAADASHLAGRSY----------LSLSGGERQRVHLARVLAQl 151
Cdd:cd03244 85 QDPVL-FSGTIRSNLD----PF--GEYSDEELWQALERVGLKEFVESLPGgldtvveeggENLSVGQRQLLCLARALLR- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 152 wpggAEQVLLLDEPTSALDPLHQHTTLHAVRE-FAGRgaAVLVILHDLNLAARYcDRLLLLHDGRPHLFGTP 222
Cdd:cd03244 157 ----KSKILVLDEATASVDPETDALIQKTIREaFKDC--TVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-243 |
1.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 8 TVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGEL---PLAGGSVSLDGRALEQWQGTERARRLAVLPQSS 84
Cdd:PRK13640 14 TYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNF-AFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLD 163
Cdd:PRK13640 94 DNQFvGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA-VEP----KIIILD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 164 EPTSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAArYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLDV-LV 241
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIpFV 247
|
..
gi 759600243 242 QR 243
Cdd:PRK13640 248 YK 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-197 |
1.87e-17 |
|
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: 81.13 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLdGRALeqwqgterarRLAVLPQS 83
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 -SSLNFAFSVESVVgfgrlphdSGRQRDLQIiaeamaaaDASHLAGRSYLS---------------LSGGERQRVHLARV 147
Cdd:TIGR03719 394 rDALDPNKTVWEEI--------SGGLDIIKL--------GKREIPSRAYVGrfnfkgsdqqkkvgqLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 148 LAQlwpGGaeQVLLLDEPTSALDPlhqhTTLHAVRE----FAGrgaAVLVILHD 197
Cdd:TIGR03719 458 LKS---GG--NVLLLDEPTNDLDV----ETLRALEEallnFAG---CAVVISHD 499
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-215 |
2.28e-17 |
|
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: 80.88 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKS----TLLGALNGELPLAGGSVSLDGRAL-----EQ 67
Cdd:COG4172 6 LLSVEDLSVafgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglseRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 68 WQGTeRARRLAVLPQ--SSSLNFAFSVESVVG-----FGRLPHDSGRQRDLQIIAEAMAAADASHLagRSY-LSLSGGER 139
Cdd:COG4172 86 LRRI-RGNRIAMIFQepMTSLNPLHTIGKQIAevlrlHRGLSGAAARARALELLERVGIPDPERRL--DAYpHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 140 QRVHLARVLAqlwpgGAEQVLLLDEPTSALDplhqhTTLHA---------VREfagRGAAVLVILHDLNLAARYCDRLLL 210
Cdd:COG4172 163 QRVMIAMALA-----NEPDLLIADEPTTALD-----VTVQAqildllkdlQRE---LGMALLLITHDLGVVRRFADRVAV 229
|
....*
gi 759600243 211 LHDGR 215
Cdd:COG4172 230 MRQGE 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-230 |
2.63e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 11 RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAF 90
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVL-FSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 SVESVVGFGrlphdSGRQRDLQIIAEAMAAADASHLA----------GRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:TIGR00958 570 SVRENIAYG-----LTDTPDEEIMAAAKAANAHDFIMefpngydtevGEKGSQLSGGQKQRIAIARALVR-----KPRVL 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 161 LLDEPTSALDPLHQHtTLHAVREFAGRgaAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEvLRAEP 230
Cdd:TIGR00958 640 ILDEATSALDAECEQ-LLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQ-LMEDQ 704
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-229 |
3.03e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnfaFSveSV 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL---FS--GT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLPHDSGRQRDL----------QIIAEAMAAADASHLAGRSylSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLwealerahikDVIDRNPFGLDAEVSEGGE--NFSVGQRQLLSLARALLR-----RSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 166 TSALDPLHQHTTLHAVREfAGRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-202 |
3.46e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVL 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFS-VESVVGFGRLPHDSGRQRDLQIIAEAMaaadashLAGRSYL---SLSGGERQRVHLARVL---AQLWp 153
Cdd:PRK13538 80 GHQPGIKTELTaLENLRFYQRLHGPGDDEALWEALAQVG-------LAGFEDVpvrQLSAGQQRRVALARLWltrAPLW- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 154 ggaeqvlLLDEPTSALDP-----LHQHTTLHAvrefAGRGAAVLVILHDLNLAA 202
Cdd:PRK13538 152 -------ILDEPFTAIDKqgvarLEALLAQHA----EQGGMVILTTHQDLPVAS 194
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-229 |
4.77e-17 |
|
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: 76.80 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--ELPLAGGSVSLDGRALEQWQGTERARR-LA 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQS----SSLNFAFSVESV-VGFgrlphdsgrqrdlqiiaeamaaadashlagrsylslSGGERQRVHLARVLAqLWP 153
Cdd:cd03217 81 LAFQYppeiPGVKNADFLRYVnEGF------------------------------------SGGEKKRNEILQLLL-LEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 154 ggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAArYC--DRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:cd03217 124 ----DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLD-YIkpDRVHVLYDGRIVKSGDKELALEIE 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-215 |
5.30e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQV-VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAV 79
Cdd:COG3845 258 LEVENLSVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQ---------SSSL--NFA---FSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSylsLSGGERQRVHLA 145
Cdd:COG3845 338 IPEdrlgrglvpDMSVaeNLIlgrYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPARS---LSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 146 RVLAQlwpggAEQVLLLDEPTSALDP-----LHQhttlhAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG3845 415 RELSR-----DPKLLIAAQPTRGLDVgaiefIHQ-----RLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-225 |
9.55e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 9.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAV- 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 ------------------LPQSSSLNFAFsvesVVGFGRLPHDSGRQRD-LQIIAEAMAAADASHLAGRSYLSLSGGERQ 140
Cdd:PRK11300 85 tfqhvrlfremtvienllVAQHQQLKTGL----FSGLLKTPAFRRAESEaLDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 141 RVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLF 219
Cdd:PRK11300 161 RLEIARCMVT-----QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
....*.
gi 759600243 220 GTPDEV 225
Cdd:PRK11300 236 GTPEEI 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-252 |
9.85e-17 |
|
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: 77.06 E-value: 9.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 27 GEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRaleqwqgterarRLAVLPQSSSLNFAFSVESVV-----GFGRL 101
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD------------TVSYKPQYIKADYEGTVRDLLssitkDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 102 PH-DSGRQRDLQIIAeamaaadashLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHA 180
Cdd:cd03237 93 PYfKTEIAKPLQIEQ----------ILDREVPELSGGELQRVAIAACLSK-----DADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 181 VREFA-GRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFGT--PDEVLRAEPLRQVFGLDVLVQRHPERGHPLI 252
Cdd:cd03237 158 IRRFAeNNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVanPPQSLRSGMNRFLKNLDITFRRDPETGRPRI 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
2.11e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--EL-PLA--GGSVSLDGR----------ALe 66
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLiPGArvEGEILLDGEdiydpdvdvvEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 67 qwqgteRaRRLAVLPQSSslN-FAFSVESVVGFG-RLpHDSGRQRDL-QIIAeamaaadaSHL--AG----------RSY 131
Cdd:COG1117 91 ------R-RRVGMVFQKP--NpFPKSIYDNVAYGlRL-HGIKSKSELdEIVE--------ESLrkAAlwdevkdrlkKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 132 LSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPTSALDPLhqhTTLH---AVREFAGRGAAVLVIlHDLNLAARYCDRL 208
Cdd:COG1117 153 LGLSGGQQQRLCIARALA-VEP----EVLLMDEPTSALDPI---STAKieeLILELKKDYTIVIVT-HNMQQAARVSDYT 223
|
....*..
gi 759600243 209 LLLHDGR 215
Cdd:COG1117 224 AFFYLGE 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-215 |
3.46e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.76 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPlAGGSVSLDGRALEQWQGTE--R 73
Cdd:PRK11153 1 MIELKNISkvfpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERP-TSGRVLVDGQDLTALSEKElrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 ARR-LAVLPQSSSL--------NFAFSVEsvvgFGRLPHDSGRQRDLQIIaeamAAADASHLAGRSYLSLSGGERQRVHL 144
Cdd:PRK11153 80 ARRqIGMIFQHFNLlssrtvfdNVALPLE----LAGTPKAEIKARVTELL----ELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 145 ARVLAQlwpggAEQVLLLDEPTSALDPlhqhTTLHAV--------REFagrGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK11153 152 ARALAS-----NPKVLLCDEATSALDP----ATTRSIlellkdinREL---GLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-215 |
3.74e-16 |
|
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: 77.17 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLA--GGSVSLDGRALE--QWQGTERArR 76
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKasNIRDTERA-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSSLNFAFSVESVVGFG-RLPHDSGRQRDLQIIAEAMAAADASHLA----GRSYLSLSGGERQRVHLARVLAQl 151
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQLDadnvTRPVGDYGGGQQQLVEIAKALNK- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 152 wpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:TIGR02633 159 ----QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-218 |
3.83e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLnFAFSVESVVGF-----GRLPHDSGRQRDLQiiaeamAAADASHLAGRSYLSLSGGERQRVHLARVLaQLWPgg 155
Cdd:PRK10247 87 AQTPTL-FGDTVYDNLIFpwqirNQQPDPAIFLDDLE------RFALPDTILTKNIAELSGGEKQRISLIRNL-QFMP-- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 156 aeQVLLLDEPTSALDPLHQHTT----LHAVREfagRGAAVLVILHDLNlAARYCDRLLLLhdgRPHL 218
Cdd:PRK10247 157 --KVLLLDEITSALDESNKHNVneiiHRYVRE---QNIAVLWVTHDKD-EINHADKVITL---QPHA 214
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-226 |
4.08e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAgGSVSLDGRA-------LEQWQGTERARRL 77
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVeffnqniYERRVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 A--------VLPQSSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHlagRSYLSLSGGERQRVHLARVLA 149
Cdd:PRK14258 90 VsmvhpkpnLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIH---KSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 150 QlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVIL-HDLNLAARYCDRLLLLHDGRPHL-----FGTPD 223
Cdd:PRK14258 167 V-----KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVsHNLHQVSRLSDFTAFFKGNENRIgqlveFGLTK 241
|
...
gi 759600243 224 EVL 226
Cdd:PRK14258 242 KIF 244
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-225 |
4.22e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.15 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAVL 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-----------RIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVeSVVGFGRLpHDSGRQRDlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:PRK09544 73 PQKLYLDTTLPL-TVNRFLRL-RPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN-----RPQLL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDgrpHL--FGTPDEV 225
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH---HIccSGTPEVV 207
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-215 |
5.38e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTL---LGAL----NGELPLAGGSVS-LDGRALEQWQGTERA---RRLAVLPQss 84
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLmniLGCLdkptSGTYRVAGQDVAtLDADALAQLRREHFGfifQRYHLLSH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 sLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAQlwpGGaeQVLLLDE 164
Cdd:PRK10535 101 -LTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMN---GG--QVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 165 PTSALDplhQH------TTLHAVREfagRGAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:PRK10535 171 PTGALD---SHsgeevmAILHQLRD---RGHTVIIVTHDPQVAAQ-AERVIEIRDGE 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-197 |
5.80e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.70 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLdGRALeqwqgterarRLAVLPQS 83
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 -SSLNFAFSVESVVgfgrlphdSGRQRDLQIiaeamaaaDASHLAGRSYLS---------------LSGGERQRVHLARV 147
Cdd:PRK11819 396 rDALDPNKTVWEEI--------SGGLDIIKV--------GNREIPSRAYVGrfnfkggdqqkkvgvLSGGERNRLHLAKT 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 148 LAQlwpGGaeQVLLLDEPTSALDPlhqhTTL----HAVREFAGrgaAVLVILHD 197
Cdd:PRK11819 460 LKQ---GG--NVLLLDEPTNDLDV----ETLraleEALLEFPG---CAVVISHD 501
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-225 |
6.54e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAvlpQSSSLNFAFS----- 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLR---KKVSLVFQFPeaqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 ---VESVVGFGRL----PHDSGRQRDLQIIAEAMAAadaSHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDE 164
Cdd:PRK13641 100 entVLKDVEFGPKnfgfSEDEAKEKALKWLKKVGLS---EDLISKSPFELSGGQMRRVAIAGVMAY-----EPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 165 PTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-215 |
6.79e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqgTERARR--LAVLPQ-----SSSL 86
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY--SEAALRqaISVVSQrvhlfSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 --NFAFSVESVvgfgrlphdsgrqRDLQIIAEAMAAADASHLAGRSYLS---------LSGGERQRVHLARVLAQLWPgg 155
Cdd:PRK11160 431 rdNLLLAAPNA-------------SDEALIEVLQQVGLEKLLEDDKGLNawlgeggrqLSGGEQRRLGIARALLHDAP-- 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 156 aeqVLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLAARYcDRLLLLHDGR 215
Cdd:PRK11160 496 ---LLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-215 |
7.74e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeQWQGTERARR--LAVLPQSSSLNFAFSVES 94
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALAagVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 95 VVGFGRLPHDSG--RQRDLQiiaeAMAAADASHLAGR-------SYLSLsgGERQRVHLARVLAQlwpgGAeQVLLLDEP 165
Cdd:PRK11288 99 NLYLGQLPHKGGivNRRLLN----YEAREQLEHLGVDidpdtplKYLSI--GQRQMVEIAKALAR----NA-RVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-215 |
8.78e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLA--GGSVSLDGRALeQWQG---TERA------RRLAVLPQSSS 85
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL-QASNirdTERAgiaiihQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 LNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAQlwpggaeQV--LLLD 163
Cdd:PRK13549 100 LENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN----LGLGQQQLVEIAKALNK-------QArlLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759600243 164 EPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-221 |
1.41e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 27 GEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDgraleqwqgteraRRLAVLPQSSSLNFAFSVESVVG-----FGRL 101
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDLLRsitddLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 102 PHDSGRQRDLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLAQlwpgGAEqVLLLDEPTSALDPLHQHTTLHAV 181
Cdd:PRK13409 432 YYKSEIIKPLQL----------ERLLDKNVKDLSGGELQRVAIAACLSR----DAD-LYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759600243 182 REFA-GRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFGT 221
Cdd:PRK13409 497 RRIAeEREATALVVDHDIYMIDYISDRLMVF-EGEPGKHGH 536
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-214 |
2.27e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVLPQS 83
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAFSVESVVGFGRLP-----------HDSGRQRDLQIIAEAMAAADASHLAGRsyLSLSggERQRVHLARVLAQlw 152
Cdd:PRK09700 89 LSVIDELTVLENLYIGRHLtkkvcgvniidWREMRVRAAMMLLRVGLKVDLDEKVAN--LSIS--HKQMLEIAKTLML-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 153 pggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:PRK09700 163 ---DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-170 |
2.53e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.00 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLT----VKRG-----RQVV--LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQG 70
Cdd:COG4608 8 LEVRDLKkhfpVRGGlfgrtVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 71 TE-RARRLAVlpQ------SSSLNFAFSVESVVGFGRLPHD--SGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQR 141
Cdd:COG4608 88 RElRPLRRRM--QmvfqdpYASLNPRMTVGDIIAEPLRIHGlaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180
....*....|....*....|....*....
gi 759600243 142 VHLARVLAqLWPggaeQVLLLDEPTSALD 170
Cdd:COG4608 166 IGIARALA-LNP----KLIVCDEPVSALD 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-229 |
3.36e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTeRARRLAV--LPQSSSLNFAFSV 92
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 93 ESVVGFGrLPHDSGRQRDL-QIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDP 171
Cdd:PRK15439 104 KENILFG-LPKRQASMQKMkQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMR-----DSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 172 LHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-226 |
4.41e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.65 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSL---DGRALEQWQGTERARRL 77
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 ------AVLPQSS--SLNFAFSVESVVG----------FGRLphdsgRQRDLQIIAEAMAAADASHLAGRSYlslSGGER 139
Cdd:PRK11701 86 llrtewGFVHQHPrdGLRMQVSAGGNIGerlmavgarhYGDI-----RATAGDWLERVEIDAARIDDLPTTF---SGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 140 QRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHL 218
Cdd:PRK11701 158 QRLQIARNLVT-----HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
....*...
gi 759600243 219 FGTPDEVL 226
Cdd:PRK11701 233 SGLTDQVL 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
4.86e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--EL---PLAGGSVSLDGRALEQWQGTERARR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSSLNFAFSVESVVGFG----RLPHDSG--RQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAq 150
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKelQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALA- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 151 LWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVIlHDLNLAARYCDRLLLLHDGrphlfgtpdEVLRAEP 230
Cdd:PRK14247 163 FQP----EVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKG---------QIVEWGP 228
|
....*
gi 759600243 231 LRQVF 235
Cdd:PRK14247 229 TREVF 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-215 |
5.29e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL----EQWQGTERARRLAVLPQS----SSLN 87
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 88 FAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTS 167
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVALARAFN-----GRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 168 ALDplhQHTTLHAV-------REFAgrgAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:PRK10584 176 NLD---RQTGDKIAdllfslnREHG---TTLILVTHDLQLAAR-CDRRLRLVNGQ 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-229 |
5.32e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.39 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnfaFSveSV 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL---FS--GT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLPHDSGRQRDLQiiaeamAAADASHLAG---RSYLSL-----------SGGERQRVHLARVLAQlwpggAEQVLL 161
Cdd:PLN03130 1329 VRFNLDPFNEHNDADLW------ESLERAHLKDvirRNSLGLdaevseagenfSVGQRQLLSLARALLR-----RSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 162 LDEPTSAL----DPLHQHTtlhaVR-EFagRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:PLN03130 1398 LDEATAAVdvrtDALIQKT----IReEF--KSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-214 |
5.43e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.07 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGR-QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAV 79
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLnfafsvesvvGFGRL------PHDSGRQRDLQIIaEAMAAADASHLAGRSYLS------LSGGERQRVHLARV 147
Cdd:COG4178 431 LPQRPYL----------PLGTLreallyPATAEAFSDAELR-EALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 148 LAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREfAGRGAAVLVILHDLNLAArYCDRLLLLHDG 214
Cdd:COG4178 500 LLH-----KPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAA-FHDRVLELTGD 559
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-220 |
7.07e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAG--GSVSLDGRALEQwqgtERARRLAVLPQSSSLNFAFS 91
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFG---RLPHDSGRQRDL----QIIAEAMAAADASHLAGRSYL-SLSGGERQRVHLARVLAqLWPggaeQVLLLD 163
Cdd:PLN03211 157 VRETLVFCsllRLPKSLTKQEKIlvaeSVISELGLTKCENTIIGNSFIrGISGGERKRVSIAHEML-INP----SLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 164 EPTSALDPLHQHTTLHAVREFAGRGAAVLVILHD-LNLAARYCDRLLLLHDGRPHLFG 220
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-220 |
8.60e-15 |
|
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: 71.02 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR-----AL-----EQWQGTERARRLAV 79
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllGLgggfnPELTGRENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LPQSSSLNFAFSVESVVGFGRLphdsGRQRDLQIiaeamaaadashlagRSYlslSGGerQRVHLARVLAQLWPGgaeQV 159
Cdd:cd03220 111 LLGLSRKEIDEKIDEIIEFSEL----GDFIDLPV---------------KTY---SSG--MKARLAFAIATALEP---DI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFG 220
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-227 |
1.12e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 6 NLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG-ELPlAGGSVSLDGRALeqwqgTERA---RRLAVLP 81
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKP-TEGQIFIDGEDV-----THRSiqqRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFAFSVESVVGFG----RLPHDSGRQR---DLQIIaeamaaadasHLAG---RSYLSLSGGERQRVHLARVLAqL 151
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGlkmlGVPKEERKQRvkeALELV----------DLAGfedRYVDQISGGQQQRVALARALI-L 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 152 WPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:PRK11432 154 KP----KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-235 |
1.41e-14 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 70.51 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRaleQWQGTErARRLAVLP 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH---PWTRKD-LHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLnfafsVESVVGFGRLP-HDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:TIGR03740 77 ESPPL-----YENLTARENLKvHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLN-----HPKLL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRphlFGTPDEVLRAEPLRQVF 235
Cdd:TIGR03740 147 ILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGV---LGYQGKINKSENLEKLF 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-215 |
1.47e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.82 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL-FSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRlpHDSGRQRDLQIIAEAMAAADASHL-------AGRSYLSLSGGERQRVHLARVLAQlwpgGAEqVLLLDEPTSA 168
Cdd:PRK10789 409 IALGR--PDATQQEIEHVARLASVHDDILRLpqgydteVGERGVMLSGGQKQRISIARALLL----NAE-ILILDDALSA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 759600243 169 LDPLHQHTTLHAVREFaGRGAAVLVILHDLNlAARYCDRLLLLHDGR 215
Cdd:PRK10789 482 VDGRTEHQILHNLRQW-GEGRTVIISAHRLS-ALTEASEILVMQHGH 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-252 |
1.66e-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: 72.51 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 7 LTVKRGRqvvlqgvslaLQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDgraleqwqgteraRRLAVLPQSSSL 86
Cdd:COG1245 356 LEVEGGE----------IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSVESVVgFGRLPHDSGRQ-------RDLQIiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLAQlwpgGAEqV 159
Cdd:COG1245 413 DYDGTVEEFL-RSANTDDFGSSyykteiiKPLGL----------EKLLDKNVKDLSGGELQRVAIAACLSR----DAD-L 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAARYCDRLLLLhDGRPHLFGTpdeVLRAEPLRQVF--- 235
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHDIYLIDYISDRLMVF-EGEPGVHGH---ASGPMDMREGMnrf 552
|
250
....*....|....*....
gi 759600243 236 --GLDVLVQRHPERGHPLI 252
Cdd:COG1245 553 lkELGITFRRDEETGRPRI 571
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-215 |
1.82e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 9 VKRGRQVV--LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRalEQWQgtER---ARRLA-VLPQ 82
Cdd:COG4586 28 FRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY--VPFK--RRkefARRIGvVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLNFAFSV-ESVVGFG---RLPHDSGRQR--------DLqiiaeamaaadaSHLAGRSYLSLSGGERQRVHLARVLaq 150
Cdd:COG4586 104 RSQLWWDLPAiDSFRLLKaiyRIPDAEYKKRldelvellDL------------GELLDTPVRQLSLGQRMRCELAAAL-- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 151 LW-PggaeQVLLLDEPTSALDPLHQhttlHAVREF-----AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:COG4586 170 LHrP----KILFLDEPTIGLDVVSK----EAIREFlkeynRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-206 |
2.19e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.58 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLL---GALNGELP--LAGGSVSLDGRAL--EQWQGTERA 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPgfRVEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 RRLAVLPQSSSlNFAFSVESVVGFGrlPHDSGRQRDLQIIAEAMAAADA-----SHLAGRSYLSLSGGERQRVHLARVLA 149
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYG--ARINGYKGDMDELVERSLRQAAlwdevKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 150 qLWPggaeQVLLLDEPTSALDPLhqhTTLhAVREFA---GRGAAVLVILHDLNLAARYCD 206
Cdd:PRK14243 168 -VQP----EVILMDEPCSALDPI---STL-RIEELMhelKEQYTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-239 |
3.35e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.17 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLNFAFS-VESV 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSiVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFG----RLPHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPTSALDP 171
Cdd:PRK13648 105 VAFGlenhAVPYDEMHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAGVLA-LNP----SVIILDEATSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 172 LHQHTTLHAVREF-AGRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAEPLRQVFGLDV 239
Cdd:PRK13648 176 DARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLDL 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-217 |
3.37e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.52 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVvLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA---RRLAVLPQSSSLNF 88
Cdd:PRK10908 14 GRQA-LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 AFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSA 168
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN-----KPAVLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759600243 169 LDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPH 217
Cdd:PRK10908 168 LDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-229 |
3.48e-14 |
|
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: 69.98 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGE--LPLAGGSVSLDGRALEQWQGTERARR--- 76
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKGQDLLELEPDERARAglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAV-----LPQSSSLNFAFS-VESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSY-LSLSGGERQRVHLARvLA 149
Cdd:TIGR01978 81 LAFqypeeIPGVSNLEFLRSaLNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVnEGFSGGEKKRNEILQ-MA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 150 QLWPggaeQVLLLDEPTSALDplhqhttLHAVR-------EFAGRGAAVLVILHDLNLaARYC--DRLLLLHDGRPHLFG 220
Cdd:TIGR01978 160 LLEP----KLAILDEIDSGLD-------IDALKivaeginRLREPDRSFLIITHYQRL-LNYIkpDYVHVLLDGRIVKSG 227
|
....*....
gi 759600243 221 TPDEVLRAE 229
Cdd:TIGR01978 228 DVELAKELE 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-228 |
3.75e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 71.67 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVK-RGRQV-VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQ 82
Cdd:TIGR02203 334 RNVTFRyPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLnFAFSVESVVGFGRlPHDSGRQRDLQIIAEAMAAADASHL-------AGRSYLSLSGGERQRVHLARVLAQLWPgg 155
Cdd:TIGR02203 414 DVVL-FNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLplgldtpIGENGVLLSGGQRQRLAIARALLKDAP-- 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 156 aeqVLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVLRA 228
Cdd:TIGR02203 490 ---ILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-215 |
6.17e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 6.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--ELPLAGGSVSLDGRALEQWQGTERARR--- 76
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARAgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAvlpqssslnFAFSVE----SVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAG--RSYLS------LSGGERQRVHL 144
Cdd:COG0396 81 LA---------FQYPVEipgvSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGldEDFLDryvnegFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 145 ARVLAqLWPggaeQVLLLDEPTSALDplhqhttLHAVR-------EFAGRGAAVLVILHD---LNLAAryCDRLLLLHDG 214
Cdd:COG0396 152 LQMLL-LEP----KLAILDETDSGLD-------IDALRivaegvnKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDG 217
|
.
gi 759600243 215 R 215
Cdd:COG0396 218 R 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-225 |
8.44e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.98 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 6 NLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERaRRLAVLPQSSS 85
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH-VPAEN-RHVNTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 LNFAFSVESVVGFG----RLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLL 161
Cdd:PRK09452 97 LFPHMTVFENVAFGlrmqKTPAAEITPR----VMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN-----KPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 162 LDEPTSALD----PLHQHTTLHAVREFagrGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK09452 168 LDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-226 |
9.48e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALE------QWQGTERARRLAVLPQSSSLN 87
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 88 FAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLS-----LSGGERQRVHLARVLAqLWPggaeQVLLL 162
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNspasqLSGGQQQRLTIARALA-LKP----KVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 163 DEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-225 |
1.04e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 19 GVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL-----EQWQGTERARRLAVLPQSSSLNFAFSVE 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWRAVRSDIQMIFQDPLASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVVG------FGRLPHDSGRQRdlqIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPTS 167
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQEVKDR---VKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALI-LEP----KLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 168 ALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-226 |
1.11e-13 |
|
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: 68.34 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL-FDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRLPhdsgrQRDLQIIAEAMAAADASH----------LAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:cd03249 97 IRYGKPD-----ATDEEVEEAAKKANIHDFimslpdgydtLVGERGSQLSGGQKQRIAIARALLR-----NPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 166 TSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:cd03249 167 TSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-227 |
1.42e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwQGTERARRLAVLPQSSSLNFAF--------S 91
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVV---SSTSKQKEIKPVRKKVGVVFQFpesqlfeeT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFGrlPHDSG--RQRDLQIIAEAMAAADAS-HLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSA 168
Cdd:PRK13643 102 VLKDVAFG--PQNFGipKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAM-----EPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 169 LDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.59e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQ-----VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSL---------DGRALE 66
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 67 QWQGTERARRLAVLPQSSSLNFAF--------SVESVVGFG--RLPHDSGRQRDLQIIAEAMAAADASHLAgRSYLSLSG 136
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRVSMVFQFpeyqlfkdTIEKDIMFGpvALGVKKSEAKKLAKFYLNKMGLDDSYLE-RSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 137 GERQRVHLARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRP 216
Cdd:PRK13631 180 GQKRRVAIAGILA-IQP----EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
....*....
gi 759600243 217 HLFGTPDEV 225
Cdd:PRK13631 255 LKTGTPYEI 263
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-229 |
2.57e-13 |
|
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: 67.26 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL-FNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRlpHDSGRQrdlQIIAEAMAAADASHLA----------GRSYLSLSGGERQRVHLARVLAQLWPggaeqVLLLDEP 165
Cdd:cd03251 96 IAYGR--PGATRE---EVEEAARAANAHEFIMelpegydtviGERGVKLSGGQRQRIAIARALLKDPP-----ILILDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 166 TSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:cd03251 166 TSALDTESERLVQAALERLM-KNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-215 |
2.81e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVLP---QSSSLNF----AFS 91
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPedrQSSGLYLdaplAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVgFGRLPHDSGRQRDLQIIAEAMAAA--DASHlAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSAL 169
Cdd:PRK15439 362 VCALT-HNRRGFWIKPARENAVLERYRRALniKFNH-AEQAARTLSGGNQQKVLIAKCLE-----ASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 759600243 170 DPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-227 |
2.82e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.88 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 15 VVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDG-----RALEQWQGTERARRLAVLPQSSSLNFA 89
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 FSVESVVGFG----RLPHDSGRQRDLQIIAEAMAAAdasHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:PRK13646 101 DTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSR---DVMSQSPFQMSGGQMRKIAIVSILAM-----NPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 166 TSALDPLHQHTTLHAVREFA-GRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLR 227
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-198 |
3.14e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.66 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 23 ALQPGEVLGVLGPNGAGKSTLLGALNGEL-PLAG---GSVSLDgRALEQWQGTE----------RARRLAVLPQSsslnf 88
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELkPNLGdydEEPSWD-EVLKRFRGTElqdyfkklanGEIKVAHKPQY----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 afsVEsvvgfgRLP-HDSGRQRDL-------QIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpgGAEqVL 160
Cdd:COG1245 169 ---VD------LIPkVFKGTVRELlekvderGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLR----DAD-FY 234
|
170 180 190
....*....|....*....|....*....|....*....
gi 759600243 161 LLDEPTSALDpLHQHTTL-HAVREFAGRGAAVLVILHDL 198
Cdd:COG1245 235 FFDEPSSYLD-IYQRLNVaRLIRELAEEGKYVLVVEHDL 272
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-222 |
3.38e-13 |
|
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: 68.89 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 28 EVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERaRRLAVLPQSSSLNFAFSV-ESVVGFGRLPHDSG 106
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-QSLGMCPQHNILFHHLTVaEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 107 RQRDLQiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFAG 186
Cdd:TIGR01257 1036 EEAQLE-MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV-----GDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180 190
....*....|....*....|....*....|....*.
gi 759600243 187 rGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTP 222
Cdd:TIGR01257 1110 -GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
4.28e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQG-VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGgSVSLDGRAL-----EQWQgteraRRL 77
Cdd:PRK11174 352 AEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELreldpESWR-----KHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLnFAFSVESVVGFGRlpHDSGRQRDLQIIAEAMAAADASHLA-------GRSYLSLSGGERQRVHLARVLAQ 150
Cdd:PRK11174 426 SWVGQNPQL-PHGTLRDNVLLGN--PDASDEQLQQALENAWVSEFLPLLPqgldtpiGDQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 151 lwPGgaeQVLLLDEPTSALDPLHQHTTLHAVREfAGRGAAVLVILHDLN-LAAryCDRLLLLHDGR 215
Cdd:PRK11174 503 --PC---QLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEdLAQ--WDQIWVMQDGQ 560
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-228 |
5.83e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV----KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL----------- 65
Cdd:PRK10261 12 VLAVENLNIafmqEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 66 EQWQGTERARR---LAVLPQS--SSLNFAFSV-ESVVGFGRLPHDSGRQRDL---QIIAEAMAAADASHLAGRSYLSLSG 136
Cdd:PRK10261 92 EQSAAQMRHVRgadMAMIFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMveaKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 137 GERQRVHLARVLAqlwpgGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGA-AVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK10261 172 GMRQRVMIAMALS-----CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|...
gi 759600243 216 PHLFGTPDEVLRA 228
Cdd:PRK10261 247 AVETGSVEQIFHA 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-231 |
6.59e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEqwQGTERARRLAVLPQSSSLNFAF------ 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP--ANLKKIKEVKRLRKEIGLVFQFpeyqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 91 --SVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASH-LAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTS 167
Cdd:PRK13645 105 qeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAM-----DGNTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 168 ALDPLHQHTTLHA-VREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRAEPL 231
Cdd:PRK13645 180 GLDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-215 |
1.11e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERA--------------------- 74
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 ---RRLAVLPQSSSLN-FAFSVESVVGFGRL----PHDSGRQRDLQIIAEAMAAAdaSHLAgRSYLSLSGGERQRVHLAR 146
Cdd:PRK13651 102 eirRRVGVVFQFAEYQlFEQTIEKDIIFGPVsmgvSKEEAKKRAAKYIELVGLDE--SYLQ-RSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 147 VLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK13651 179 ILA-MEP----DFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-198 |
1.61e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 23 ALQPGEVLGVLGPNGAGKSTLLGALNGEL-PLAG---GSVSLDgRALEQWQGTE----------RARRLAVLPQSSSLnf 88
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELiPNLGdyeEEPSWD-EVLKRFRGTElqnyfkklynGEIKVVHKPQYVDL-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 afsVESVVgfgrlphdSGRQRDL-------QIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpgGAEqVLL 161
Cdd:PRK13409 172 ---IPKVF--------KGKVRELlkkvderGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLR----DAD-FYF 235
|
170 180 190
....*....|....*....|....*....|....*..
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDL 198
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDL 271
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-225 |
1.79e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 24 LQPGEVLGVLGPNGAGKS----TLLGAL--NGELplaGGSVSLDGRALEQWQGTE----RARRLAVLPQS--SSLNFAFS 91
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSqtafALMGLLaaNGRI---GGSATFNGREILNLPEKElnklRAEQISMIFQDpmTSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 V---------------------ESVVGFGRLPHDSGRQRdlqiiaeamaAADASHlagrsylSLSGGERQRVHLARVLAq 150
Cdd:PRK09473 116 VgeqlmevlmlhkgmskaeafeESVRMLDAVKMPEARKR----------MKMYPH-------EFSGGMRQRVMIAMALL- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 151 lwpgGAEQVLLLDEPTSALDPLHQ---HTTLHAV-REFagrGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK09473 178 ----CRPKLLIADEPTTALDVTVQaqiMTLLNELkREF---NTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-215 |
1.84e-12 |
|
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: 66.38 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESV 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVL-FNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VGFGRlPHDSGRQ-----RDLQIiaeamaaadasH------------LAGRSYLSLSGGERQRVHLARVLAQlwpggAEQ 158
Cdd:COG5265 452 IAYGR-PDASEEEveaaaRAAQI-----------HdfieslpdgydtRVGERGLKLSGGEKQRVAIARTLLK-----NPP 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREfAGRGAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-233 |
2.20e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 11 RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELP-LAGGSVSLDGraleqwqgterarRLAVLPQSSSLnFA 89
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPpRSDASVVIRG-------------TVAYVPQVSWI-FN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 FSVESVVGFGrLPHDSGR----------QRDLQIIAEAMAAADashlaGRSYLSLSGGERQRVHLARVLAqlwpgGAEQV 159
Cdd:PLN03130 693 ATVRDNILFG-SPFDPERyeraidvtalQHDLDLLPGGDLTEI-----GERGVNISGGQKQRVSMARAVY-----SNSDV 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 160 LLLDEPTSALDP-LHQHTTLHAVREFAGRGAAVLVI--LHDLNlaarYCDRLLLLHDGRPHLFGTPDEVLRAEPLRQ 233
Cdd:PLN03130 762 YIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTnqLHFLS----QVDRIILVHEGMIKEEGTYEELSNNGPLFQ 834
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-204 |
2.42e-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: 66.11 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALngelplAGGSVSLDGRALEQwqgteRARRLAVLPQSSSLNFAFSVESV 95
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM------AGVDKDFNGEARPQ-----PGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 V--GFGRLPHDSGR---------------------QRDLQ-IIAEAMAAADASHL-----AGR------SYLSLSGGERQ 140
Cdd:TIGR03719 89 VeeGVAEIKDALDRfneisakyaepdadfdklaaeQAELQeIIDAADAWDLDSQLeiamdALRcppwdaDVTKLSGGERR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 141 RVHLARVLAQlwpggAEQVLLLDEPTSALDP-----LHQHttlhaVREFAGrgaAVLVILHDlnlaaRY 204
Cdd:TIGR03719 169 RVALCRLLLS-----KPDMLLLDEPTNHLDAesvawLERH-----LQEYPG---TVVAVTHD-----RY 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-219 |
2.45e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.35 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLdgraleqwqgtERARRLAVL 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQsSSLNFAFSVESVVG-FGRL-PHDSGRQRDLQIIAEAMAAADASHLAGRsylsLSGGERQRVHLARVLAQlwpggAEQ 158
Cdd:PRK10636 381 AQ-HQLEFLRADESPLQhLARLaPQELEQKLRDYLGGFGFQGDKVTEETRR----FSGGEKARLVLALIVWQ-----RPN 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAGrgaAVLVILHDLNLAARYCDRLLLLHDGRPHLF 219
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDFEG---ALVVVSHDRHLLRSTTDDLYLVHDGKVEPF 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-214 |
3.48e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVsldgraleQWQGTERA----------------RRLAVL 80
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI--------LYLGKEVTfngpkssqeagigiihQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQ-SSSLNFAFSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAQlwpggAEQV 159
Cdd:PRK10762 92 PQlTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVG----ELSIGEQQMVEIAKVLSF-----ESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 160 LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDG 214
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-183 |
5.42e-12 |
|
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: 65.32 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVK--RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGAL------NGELPLAGgsVSLDGRALEQWQgteraRR 76
Cdd:TIGR01271 1221 QGLTAKytEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstEGEIQIDG--VSWNSVTLQTWR-----KA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQSSslnFAFSvesvvGFGRL---PHDsgRQRDLQIIAEAMAAADAS-----------HLAGRSYLsLSGGERQRV 142
Cdd:TIGR01271 1294 FGVIPQKV---FIFS-----GTFRKnldPYE--QWSDEEIWKVAEEVGLKSvieqfpdkldfVLVDGGYV-LSNGHKQLM 1362
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 759600243 143 HLAR-VLAQlwpggaEQVLLLDEPTSALDPLhqhtTLHAVRE 183
Cdd:TIGR01271 1363 CLARsILSK------AKILLLDEPSAHLDPV----TLQIIRK 1394
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-215 |
5.74e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVvlQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR-LAVLPQ 82
Cdd:PRK09700 268 VRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLN--FA-FSVESVVGFGRLPHDSG------------------RQRDLQIIAeamaaadaSHLAGRSYLSLSGGERQR 141
Cdd:PRK09700 346 SRRDNgfFPnFSIAQNMAISRSLKDGGykgamglfhevdeqrtaeNQRELLALK--------CHSVNQNITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 142 VHLARvlaqlWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK09700 418 VLISK-----WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
12-225 |
8.23e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGK------STLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSS 85
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**rgalpAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 LNFAFSVESVVGFGRlphDSGRQRDLQIIAEAMAaadaSHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEP 165
Cdd:NF000106 104 RENLYMIGR*LDLSR---KDARARADELLERFSL----TEAAGRAAAKYSGGMRRRLDLAASMI-----GRPAVLYLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-216 |
1.74e-11 |
|
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: 61.02 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGR-QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAVL 80
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNfafsvesvvgfgrlphdSGRQRDlQIIAEamaaadashlagrSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:cd03223 70 PQRPYLP-----------------LGTLRE-QLIYP-------------WDDVLSGGEQQRLAFARLLLH-----KPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREfagRGAAVLVILHDLNLAARYCDRLLLLHDGRP 216
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE---LGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-216 |
2.08e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLT----VKRG-----RQV-VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR-ALEQWQG 70
Cdd:PRK11308 6 LQAIDLKkhypVKRGlfkpeRLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 71 TERARRLAV--LPQS--SSLNFAFSVESVVGFGRLPH--DSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHL 144
Cdd:PRK11308 86 AQKLLRQKIqiVFQNpyGSLNPRKKVGQILEEPLLINtsLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 145 ARVLaQLWPggaeQVLLLDEPTSALDPLHQHTTLHAV----REFagrGAAVLVILHDLNLAARYCDRLLLLHDGRP 216
Cdd:PRK11308 166 ARAL-MLDP----DVVVADEPVSALDVSVQAQVLNLMmdlqQEL---GLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-225 |
2.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeqwQGTERARRLAVLPQSSSLNFAFS----- 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLI---TSTSKNKDIKQIRKKVGLVFQFPesqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESV---VGFGrlPHDSG-RQRDLQIIAEAMAAAD--ASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:PRK13649 100 EETVlkdVAFG--PQNFGvSQEEAEALAREKLALVgiSESLFEKNPFELSGGQMRRVAIAGILAM-----EPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-215 |
2.93e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.11 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSL-------NFA 89
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLfndtianNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 ------FSVESVVGFGRLPHDSGRQRDLQ-----IIaeamaaadashlaGRSYLSLSGGERQRVHLARVLAQLWPggaeq 158
Cdd:PRK11176 439 yarteqYSREQIEEAARMAYAMDFINKMDngldtVI-------------GENGVLLSGGQRQRIAIARALLRDSP----- 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAgRGAAVLVILHDLNLAARyCDRLLLLHDGR 215
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEK-ADEILVVEDGE 555
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-247 |
2.97e-11 |
|
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: 62.18 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTerarrlAVLPQSSSLNFAFSV--- 92
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFS------WIMPGTIKENIIFGVsyd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 93 ----ESVVGFGRLPHDSGR--QRDLQIIaeamaaadashlaGRSYLSLSGGERQRVHLARVL---AQLWpggaeqvlLLD 163
Cdd:cd03291 126 eyryKSVVKACQLEEDITKfpEKDNTVL-------------GEGGITLSGGQRARISLARAVykdADLY--------LLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 164 EPTSALDPLHQHTTLHA-VREFAGRGAAVLVILHDLNLaaRYCDRLLLLHDGRPHLFGTPDEV--LRAEPLRQVFGLDVL 240
Cdd:cd03291 185 SPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHL--KKADKILILHEGSSYFYGTFSELqsLRPDFSSKLMGYDTF 262
|
....*..
gi 759600243 241 VQRHPER 247
Cdd:cd03291 263 DQFSAER 269
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-235 |
3.02e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPL-----AGGSVSLDGRAL--EQWQGTERA 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 RRLAVLPQSSSLNFAFSVESVVGFG-RLPH--DSGRQRDLQIIAEAMAAADASHLAGR--SYLS-LSGGERQRVHLARVL 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGvKLNGlvKSKKELDERVEWALKKAALWDEVKDRlnDYPSnLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 AqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVIlHDLNLAARYCDRLLLLHDGrphlfgtpdEVLRA 228
Cdd:PRK14267 165 A-MKP----KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLG---------KLIEV 229
|
....*..
gi 759600243 229 EPLRQVF 235
Cdd:PRK14267 230 GPTRKVF 236
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-198 |
3.05e-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: 61.61 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 25 QPGEVLGVLGPNGAGKSTLLGALNGEL-PLAG---GSVSLDGrALEQWQGTE------RAR----RLAVLPQSSSL---N 87
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLkPNLGkfdDPPDWDE-ILDEFRGSElqnyftKLLegdvKVIVKPQYVDLipkA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 88 FAFSVESVVgfgRLPHDSGRQRDLqiiaeaMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTS 167
Cdd:cd03236 103 VKGKVGELL---KKKDERGKLDEL------VDQLELRHVLDRNIDQLSGGELQRVAIAAALAR-----DADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|.
gi 759600243 168 ALDPLHQHTTLHAVREFAGRGAAVLVILHDL 198
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-224 |
3.30e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 62.67 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESVV 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGL-FNRSIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 97 GFGR-------LPHDSGRQRDLQIIAEAMAAADAshLAGRSYLSLSGGERQRVHLARVLAQLWPggaeqVLLLDEPTSAL 169
Cdd:PRK13657 430 RVGRpdatdeeMRAAAERAQAHDFIERKPDGYDT--VVGERGRQLSGGERQRLAIARALLKDPP-----ILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 170 DPLHQHTTLHAVREFAgRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDE 224
Cdd:PRK13657 503 DVETEAKVKAALDELM-KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDE 555
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-170 |
3.99e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVsldgraleQWqgTERArRLAVLP 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KW--SENA-NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 82 QSSSLNFA--FSVESVVGFGRLPHDsgrqrDLQIIaeamaaadashlagRSYL---------------SLSGGERQRVHL 144
Cdd:PRK15064 389 QDHAYDFEndLTLFDWMSQWRQEGD-----DEQAV--------------RGTLgrllfsqddikksvkVLSGGEKGRMLF 449
|
170 180
....*....|....*....|....*.
gi 759600243 145 ARVLAQlwpggAEQVLLLDEPTSALD 170
Cdd:PRK15064 450 GKLMMQ-----KPNVLVMDEPTNHMD 470
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-234 |
5.22e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 13 RQVV--LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQ--SSSLNF 88
Cdd:PRK15112 23 RQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQdpSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 AFSVESVVGFG-RLPHD-SGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPT 166
Cdd:PRK15112 103 RQRISQILDFPlRLNTDlEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALI-LRP----KVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 167 SALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLrAEPLRQV 234
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL-ASPLHEL 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-221 |
7.53e-11 |
|
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: 61.95 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 22 LALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLPQSSSLNFAFS-VESVVGFGR 100
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTgREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 101 L---PHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSALDPLHQHTT 177
Cdd:TIGR01257 2039 LrgvPAEEIEKVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALI-----GCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759600243 178 LHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGT 221
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-247 |
8.28e-11 |
|
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: 61.85 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGraleqwqgterarRLAVLPQSSSLNFAFSVESV 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 96 VgFGrLPHDSGRQRdlQIIAEAMAAADASHLA-------GRSYLSLSGGERQRVHLARVL---AQLWpggaeqvlLLDEP 165
Cdd:TIGR01271 508 I-FG-LSYDEYRYT--SVIKACQLEEDIALFPekdktvlGEGGITLSGGQRARISLARAVykdADLY--------LLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 166 TSALDPLHQHTTLHA-VREFAGRGAAVLVI--LHDLNLAarycDRLLLLHDGRPHLFGTPDEVLRAEP--LRQVFGLDVL 240
Cdd:TIGR01271 576 FTHLDVVTEKEIFEScLCKLMSNKTRILVTskLEHLKKA----DKILLLHEGVCYFYGTFSELQAKRPdfSSLLLGLEAF 651
|
....*..
gi 759600243 241 VQRHPER 247
Cdd:TIGR01271 652 DNFSAER 658
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-215 |
9.02e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.48 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVlQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELP----LAGGSVSLDGRALEqwQGTERARRL 77
Cdd:PRK10418 5 IELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVA--PCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLPQSSSLNF-------AFSVESVVGFGRLPHDsgrQRDLQIIAEAMAAADASHLagRSY-LSLSGGERQRVHLARVLA 149
Cdd:PRK10418 82 ATIMQNPRSAFnplhtmhTHARETCLALGKPADD---ATLTAALEAVGLENAARVL--KLYpFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 150 QLWPggaeqVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK10418 157 CEAP-----FIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-215 |
1.11e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRgrQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR------ALEQWQG---- 70
Cdd:PRK10982 250 ILEVRNLTSLR--QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnANEAINHgfal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 71 -TERARRLAVLpqsSSLNFAF-----SVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAgrSYLSLSGGERQRVHL 144
Cdd:PRK10982 328 vTEERRSTGIY---AYLDIGFnslisNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRT--QIGSLSGGNQQKVII 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 145 ARvlaqlWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK10982 403 GR-----WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-215 |
1.13e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVlQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLA-GGSVSLDGRALE-------QW 68
Cdd:PRK13549 259 ILEVRNLTawdpVNPHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKirnpqqaIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 69 QG----TERARRLAVLPQSS-SLNFAFSV-ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAgrsYLSLSGGERQRV 142
Cdd:PRK13549 338 QGiamvPEDRKRDGIVPVMGvGKNITLAAlDRFTGGSRIDDAAELKTILESIQRLKVKTASPELA---IARLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 143 HLARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK13549 415 VLAKCLL-LNP----KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-214 |
1.16e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.18 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLT----VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--ELPLAGGSVSLDGRALEQwqgtERARRLA 78
Cdd:cd03232 7 KNLNytvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDK----NFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSSLNFAFSVESVVGFgrlphdSGRQRDlqiiaeamaaadashlagrsylsLSGGERQRVHLARVLAQLwPggaeQ 158
Cdd:cd03232 83 YVEQQDVHSPNLTVREALRF------SALLRG-----------------------LSVEQRKRLTIGVELAAK-P----S 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAA-RYCDRLLLLHDG 214
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-221 |
1.22e-10 |
|
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: 58.74 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 27 GEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRaleqwqgterarRLAVLPQssslnfafsvesvvgfgrlphdsg 106
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQ------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 107 rqrdlqiiaeamaaadashlagrsYLSLSGGERQRVHLARVLaqlwpGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAG 186
Cdd:cd03222 69 ------------------------YIDLSGGELQRVAIAAAL-----LRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 759600243 187 RGA-AVLVILHDLNLAARYCDRLLLLHdGRPHLFGT 221
Cdd:cd03222 120 EGKkTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGI 154
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-215 |
1.40e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLT----VKRGRQVVlQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLA-GGSVSLDGRALEQ-------W 68
Cdd:TIGR02633 257 ILEARNLTcwdvINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIrnpaqaiR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 69 QGT----ERARRLAVLPQ-SSSLNFAFSV-ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAgrsYLSLSGGERQRV 142
Cdd:TIGR02633 336 AGIamvpEDRKRHGIVPIlGVGKNITLSVlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP---IGRLSGGNQQKA 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 143 HLARVLAqLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:TIGR02633 413 VLAKMLL-TNP----RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-74 |
1.49e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNG--ELPLAGGSVSLDGRALEQWQGTERA 74
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRA 76
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-200 |
1.61e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERaRRLAVL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ-KQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGrLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARvlaqLWPGGAeQVL 160
Cdd:PRK13540 80 GHRSGINPYLTLRENCLYD-IHFSPGAVG----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLR----LWMSKA-KLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759600243 161 LLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILH-DLNL 200
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-204 |
1.70e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGAL-------NGELPLAGGSvsldgraleqwqgterarRLAVLPQSS 84
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkefEGEARPAPGI------------------KVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 85 SLNFAFSVESVV--GFGRL----------------PHDS-----GRQRDLQ-IIAEAMAAADASHL-----AGR------ 129
Cdd:PRK11819 80 QLDPEKTVRENVeeGVAEVkaaldrfneiyaayaePDADfdalaAEQGELQeIIDAADAWDLDSQLeiamdALRcppwda 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 130 SYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDP-----LHQHttlhaVREFAGrgaAVLVILHDlnlaaRY 204
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLE-----KPDMLLLDEPTNHLDAesvawLEQF-----LHDYPG---TVVAVTHD-----RY 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-215 |
1.81e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.69 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGeLPLAGGSVSLDGRA-LEQWQGTERarrlaVL 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELLAGTApLAEAREDTR-----LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHdsGRQRDLQIIAEAMaaadashLAGRSY---LSLSGGERQRVHLARVLAQLwPGgae 157
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQ--WRDAALQALAAVG-------LADRANewpAALSGGQKQRVALARALIHR-PG--- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759600243 158 qVLLLDEPTSALDPLhqhTTLHA----VREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK11247 154 -LLLLDEPLGALDAL---TRIEMqdliESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-221 |
2.16e-10 |
|
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: 57.75 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 26 PGEVLGVLGPNGAGKSTLLGALngeLPLAGGSVSLDGRALEQWQGTERARrlavlpqsSSLNFAFSVesvvgfgrlphds 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI---GLALGGAQSATRRRSGVKAGCIVAA--------VSAELIFTR------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 106 grqrdlqiiaeamaaadashlagrsyLSLSGGERQRVHLARVLAqLWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFA 185
Cdd:cd03227 76 --------------------------LQLSGGEKELSALALILA-LASLKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170 180 190
....*....|....*....|....*....|....*.
gi 759600243 186 GRGAAVLVILHDLNLAARYcdrLLLLHDGRPHLFGT 221
Cdd:cd03227 129 VKGAQVIVITHLPELAELA---DKLIHIKKVITGVY 161
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-194 |
2.72e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 6 NLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDgraLEQWQGTERARRLAVLPQSSS 85
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---VPDNQFGREASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 LNFAFSVESVVGFGrlphdsgrqrDLQIIAeamaaadashlagRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEP 165
Cdd:COG2401 112 FKDAVELLNAVGLS----------DAVLWL-------------RRFKELSTGQKFRFRLALLLA-----ERPKLLVIDEF 163
|
170 180
....*....|....*....|....*....
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAAVLVI 194
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVV 192
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-228 |
4.39e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 7 LTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQ---- 82
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQdpvl 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 -SSSLNF------AFSVESVVGFGRLPHDSGRQRDLQiiaeamaaADASHLAGRSYLSLSGGERQRVHLARVLAQlwpgg 155
Cdd:TIGR00957 1372 fSGSLRMnldpfsQYSDEEVWWALELAHLKTFVSALP--------DKLDHECAEGGENLSVGQRQLVCLARALLR----- 1438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759600243 156 AEQVLLLDEPTSALDpLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCdRLLLLHDGRPHLFGTPDEVLRA 228
Cdd:TIGR00957 1439 KTKILVLDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-215 |
5.50e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.95 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTV--KRGRQV--VLQGVSLALQPGEVLGVLGPNGAGKS-TLLGAL-----------NGELPLAGGSVSldgRA 64
Cdd:PRK15134 5 LLAIENLSVafRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGDIRFHGESLL---HA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 65 LEQWQGTERARRLAVLPQS--SSLNFAFSVE----SVVGFGR-LPHDSGRQRDLQIIAEAMAAADASHLAGRSYlSLSGG 137
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEpmVSLNPLHTLEkqlyEVLSLHRgMRREAARGEILNCLDRVGIRQAAKRLTDYPH-QLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 138 ERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK15134 161 ERQRVMIAMALLT-----RPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-215 |
7.15e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVsldgraleqWQgterARRLAVLPQSsslnfAFSVE 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WA----ERSIAYVPQQ-----AWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVVGFGRLPHDSGRQRDLQ-IIAEAMAAADASHLA-------GRSYLSLSGGERQRVHLAR-VLAQlwpggaEQVLLLDE 164
Cdd:PTZ00243 735 ATVRGNILFFDEEDAARLAdAVRVSQLEADLAQLGggleteiGEKGVNLSGGQKARVSLARaVYAN------RDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 165 PTSALDplhQHTTLHAVRE-FAGRGAAVLVIL--HDLNLAARyCDRLLLLHDGR 215
Cdd:PTZ00243 809 PLSALD---AHVGERVVEEcFLGALAGKTRVLatHQVHVVPR-ADYVVALGDGR 858
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-226 |
1.04e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVL-PQ-----------SSSLN 87
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcPEdrkaegiipvhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 88 FAFSVESVVGFGRLPHDSGRQRDL---QIIAEAMAAADASHLAGrsylSLSGGERQRVHLARVLAQlwpggAEQVLLLDE 164
Cdd:PRK11288 352 INISARRHHLRAGCLINNRWEAENadrFIRSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSE-----DMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 165 PTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR-----PHLFGTPDEVL 226
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRiagelAREQATERQAL 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-215 |
1.25e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 19 GVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQ------------WQGTERARRLAVLPQSSSL 86
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangivYISEDRKRDGLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFA------FSVESvvgfGRLPHDSGRQ---------------RDlQIIAEamaaadashlagrsylsLSGGERQRVHLA 145
Cdd:PRK10762 350 NMSltalryFSRAG----GSLKHADEQQavsdfirlfniktpsME-QAIGL-----------------LSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 146 RVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK10762 408 RGLMT-----RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-215 |
1.54e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.17 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVK--RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGAL------NGELPLAGgsVSLDGRALEQWQgter 73
Cdd:cd03289 3 MTVKDLTAKytEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntEGDIQIDG--VSWNSVPLQKWR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 74 aRRLAVLPQSSslnFAFSvesvvGFGRLPHDS-GRQRDLQIIAEAMAAADAS-----------HLAGRSYLsLSGGERQR 141
Cdd:cd03289 77 -KAFGVIPQKV---FIFS-----GTFRKNLDPyGKWSDEEIWKVAEEVGLKSvieqfpgqldfVLVDGGCV-LSHGHKQL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 142 VHLAR-VLAQlwpggaEQVLLLDEPTSALDPLHQHTTLHAVREfAGRGAAVLVILHDLNlAARYCDRLLLLHDGR 215
Cdd:cd03289 147 MCLARsVLSK------AKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIE-AMLECQRFLVIEENK 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-226 |
3.89e-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: 56.88 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 7 LTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGraleqwqgterarRLAVLPQSSSL 86
Cdd:TIGR00957 644 FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSVESVVgFGRlPHDSGRQR----------DLQIIAEAMAAADashlaGRSYLSLSGGERQRVHLARVLAQlwpggA 156
Cdd:TIGR00957 711 QNDSLRENIL-FGK-ALNEKYYQqvleacallpDLEILPSGDRTEI-----GEKGVNLSGGQKQRVSLARAVYS-----N 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 157 EQVLLLDEPTSALDplhQHTTLHAVREFAG-----RGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:TIGR00957 779 ADIYLFDDPLSAVD---AHVGKHIFEHVIGpegvlKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-229 |
5.02e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 11 RGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWqgTERARRLAV-LPQSSSLNFA 89
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL--SHSVLRQGVaMVQQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 FSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASH----LAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEP 165
Cdd:PRK10790 429 DTFLANVTLGRDISEEQVWQALETVQLAELARSLPDglytPLGEQGNNLSVGQKQLLALARVLVQ-----TPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAAVlVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRAE 229
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTLV-VIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
20-225 |
6.85e-09 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 55.67 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFAFSVESVVGFG 99
Cdd:TIGR01192 354 VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGL-FNRSIRENIRLG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 100 RlphdsGRQRDLQIIAEAMAAADASHLAGRS--YLS--------LSGGERQRVHLARVLAQLWPggaeqVLLLDEPTSAL 169
Cdd:TIGR01192 433 R-----EGATDEEVYEAAKAAAAHDFILKRSngYDTlvgergnrLSGGERQRLAIARAILKNAP-----ILVLDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 170 DpLHQHTTLHAVREFAGRGAAVLVILHDLNlAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:TIGR01192 503 D-VETEARVKNAIDALRKNRTTFIIAHRLS-TVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-171 |
7.84e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwqgTERARRLAVL 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSSSLNFAFSVESVVGFGRLPHdsGRqRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVL---AQLWpggae 157
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGLH--GR-RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWlspAPLW----- 159
|
170
....*....|....
gi 759600243 158 qvlLLDEPTSALDP 171
Cdd:PRK13543 160 ---LLDEPYANLDL 170
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-234 |
8.66e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 6 NLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR---ALEQWQGTERARRLAVLPQ 82
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 83 SSSLNFAFSVESVVGF-----GRLPHDSGRQRDLQIIAEAMaaadashLAGRSYL---SLSGGERQRVHLARVLAqLWPg 154
Cdd:PRK11831 92 SGALFTDMNVFDNVAYplrehTQLPAPLLHSTVMMKLEAVG-------LRGAAKLmpsELSGGMARRAALARAIA-LEP- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 155 gaeQVLLLDEPTSALDPLHQHTTLHAVREF-AGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEvLRAEPLRQ 233
Cdd:PRK11831 163 ---DLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPR 238
|
.
gi 759600243 234 V 234
Cdd:PRK11831 239 V 239
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-196 |
2.25e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGElP---LAGGSVSLDGRALEQWQGTERArRL 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykILEGDILFKGESILDLEPEERA-HL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 78 AVLpqsssLNFAFSVE----SVVGFGRLPHDSGR----QRDLQIIAEAMAAADASHLAG--RSYLS------LSGGERQR 141
Cdd:CHL00131 85 GIF-----LAFQYPIEipgvSNADFLRLAYNSKRkfqgLPELDPLEFLEIINEKLKLVGmdPSFLSrnvnegFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 142 VHLARvLAQLWPggaeQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILH 196
Cdd:CHL00131 160 NEILQ-MALLDS----ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-170 |
2.35e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRA----LEQ-----WQGT----------ERA--- 74
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivarLQQdpprnVEGTvydfvaegieEQAeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 75 -------RRLAVLPQSSSLNFAFSVESVvgfgrLPHDSGRQRDLQIIAEAMAAadasHLAGRSYLS-LSGGERQRVHLAR 146
Cdd:PRK11147 99 kryhdisHLVETDPSEKNLNELAKLQEQ-----LDHHNLWQLENRINEVLAQL----GLDPDAALSsLSGGWLRKAALGR 169
|
170 180
....*....|....*....|....
gi 759600243 147 VLAQlwpggAEQVLLLDEPTSALD 170
Cdd:PRK11147 170 ALVS-----NPDVLLLDEPTNHLD 188
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-220 |
3.00e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 52.26 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAG---GSVSLDGraLEQWQGTERARRLAVLPQSSSLNFA-FSV 92
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG--IPYKEFAEKYPGEIIYVSEEDVHFPtLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 93 ESVVGFgrlphdSGRQRdlqiiaeamaaadashlaGRSYLS-LSGGERQRVHLARVLAqlwpGGAeQVLLLDEPTSALDP 171
Cdd:cd03233 101 RETLDF------ALRCK------------------GNEFVRgISGGERKRVSIAEALV----SRA-SVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759600243 172 LHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYC-DRLLLLHDGRPHLFG 220
Cdd:cd03233 152 STALEILKCIRTMADVlKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYYG 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-170 |
4.50e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERarrlAVL 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQET----PAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 81 PQSsslnfafSVESVVGFGRlphdSGRQ--RDLQIIAEAMAAADASHLAG-----------------------------R 129
Cdd:PRK10636 77 PQP-------ALEYVIDGDR----EYRQleAQLHDANERNDGHAIATIHGkldaidawtirsraasllhglgfsneqleR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759600243 130 SYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSALD 170
Cdd:PRK10636 146 PVSDFSGGWRMRLNLAQALI-----CRSDLLLLDEPTNHLD 181
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-228 |
4.94e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLAVLPQS 83
Cdd:NF033858 269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIATRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 84 SSLNFAFSV-ESVVGFGRL---PHDSGRQRDLQIIAEAMAAADASHLAGrsylSLSGGERQRVHLA-RVLAQlwPggaeQ 158
Cdd:NF033858 348 FSLYGELTVrQNLELHARLfhlPAAEIAARVAEMLERFDLADVADALPD----SLPLGIRQRLSLAvAVIHK--P----E 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 159 VLLLDEPTSALDPLHQ----HTTLHAVREfagRGAAVLVILHDLNLAARyCDRLLLLHDGRPHLFGTPDEVLRA 228
Cdd:NF033858 418 LLILDEPTSGVDPVARdmfwRLLIELSRE---DGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-228 |
5.17e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAG----GSVSLDGRALEQWqgTERARR------LAVLPQS--SSLN 87
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRI--SEKERRnlvgaeVAMIFQDpmTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 88 FAFSVESVVGFGRLPHDSG-----RQRDLQIIAEAMAAADASHLAGRSYlSLSGGERQRVHLARVLAqlwpgGAEQVLLL 162
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHQGGnkktrRQRAIDLLNQVGIPDPASRLDVYPH-QLSGGMSQRVMIAMAIA-----CRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 163 DEPTSALDPLHQHTTLHAVREFAGR-GAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRA 228
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-227 |
5.61e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVS-LDG----RAleqwqgtERAR---R 76
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGdmadAR-------HRRAvcpR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 77 LAVLPQ--SSSLNFAFSV-ESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHL---AGRsylsLSGGERQRVHLARVL-- 148
Cdd:NF033858 78 IAYMPQglGKNLYPTLSVfENLDFFGRLFGQDAAERRRRIDELLRATGLAPFAdrpAGK----LSGGMKQKLGLCCALih 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 149 -AQLwpggaeqvLLLDEPTSALDPLhqhttlhAVREF--------AGR-GAAVLVILHDLNLAARYcDRLLLLHDGRPHL 218
Cdd:NF033858 154 dPDL--------LILDEPTTGVDPL-------SRRQFwelidrirAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217
|
....*....
gi 759600243 219 FGTPDEVLR 227
Cdd:NF033858 218 TGTPAELLA 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-170 |
7.30e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERArrLAVLPQSSSLNFAFS 91
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFG-RLPHDSGRQRDlQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqlwpgGAEQVLLLDEPTSALD 170
Cdd:PRK11000 92 VAENMSFGlKLAGAKKEEIN-QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV-----AEPSVFLLDEPLSNLD 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-214 |
9.52e-08 |
|
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: 51.18 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARR----LAVLPQSSSLNFAfSV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 93 ESVVGFGRlPHDSGR----------QRDLQIIAEAMAAADashlaGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLL 162
Cdd:cd03290 96 EENITFGS-PFNKQRykavtdacslQPDIDLLPFGDQTEI-----GERGINLSGGQRQRICVARALYQ-----NTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 163 DEPTSALD-PLHQHTTLHAVREFAGRGAAVLVIL-HDLNLAArYCDRLLLLHDG 214
Cdd:cd03290 165 DDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVtHKLQYLP-HADWIIAMKDG 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-233 |
1.37e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSvSLDGRaleqwqGTerarrLAVLPQSSSLnFAFSVESVV 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVVIR------GS-----VAYVPQVSWI-FNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 97 GFGRlphDSGRQRDLQIIAEAMAAADASHLAGRSY-------LSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSAL 169
Cdd:PLN03232 700 LFGS---DFESERYWRAIDVTALQHDLDLLPGRDLteigergVNISGGQKQRVSMARAVYS-----NSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 170 DPLHQHTTLHAVREFAGRGAA-VLVI--LHDLNLAarycDRLLLLHDGRPHLFGTPDEVLRAEPLRQ 233
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTrVLVTnqLHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-214 |
1.43e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 9 VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELP---LAGGSVSLDGRALEqwqgTERARRLAV------ 79
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD----SSFQRSIGYvqqqdl 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 -LPQSS---SLNFAfsvesvvGFGRLP-HDSGRQRDL---QIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAql 151
Cdd:TIGR00956 847 hLPTSTvreSLRFS-------AYLRQPkSVSKSEKMEyveEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELV-- 917
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 152 wpggAEQVLL--LDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILH--DLNLAARYcDRLLLLHDG 214
Cdd:TIGR00956 918 ----AKPKLLlfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEF-DRLLLLQKG 979
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-225 |
2.32e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 10 KRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQWQGTERARRLAVLPQSSSLnFA 89
Cdd:PTZ00243 1319 REGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVL-FD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 90 FSVESVVGFGRLPHDSGRQRDLQIIAEAMAAADASH------LAGRSYLSLsgGERQRVHLARVLAQLWPGgaeqVLLLD 163
Cdd:PTZ00243 1398 GTVRQNVDPFLEASSAEVWAALELVGLRERVASESEgidsrvLEGGSNYSV--GQRQLMCMARALLKKGSG----FILMD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 164 EPTS----ALDPLHQHTTLHAVREFagrgaAVLVILHDLNLAARYcDRLLLLHDGRPHLFGTPDEV 225
Cdd:PTZ00243 1472 EATAnidpALDRQIQATVMSAFSAY-----TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
7-209 |
3.49e-07 |
|
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: 48.86 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 7 LTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLgalngelplaggsvsLDGRAleqwqgTERARRLAVLPQSSSL 86
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEGLY------ASGKARLISFLPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSVESV-----VGFGRLPhdsgrqrdlqiiaeamaaadashlAGRSYLSLSGGERQRVHLARVLAQLWPGgaeQVLL 161
Cdd:cd03238 60 NKLIFIDQLqflidVGLGYLT------------------------LGQKLSTLSGGELQRVKLASELFSEPPG---TLFI 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759600243 162 LDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLaARYCDRLL 209
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV-LSSADWII 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-215 |
5.59e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 30 LGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAVLPQSSSLNFAFSVESVVGFGRLPHDSGRQR 109
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 110 dlqIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGrga 189
Cdd:PLN03073 607 ---LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFK-----KPHILLLDEPSNHLDLDAVEALIQGLVLFQG--- 675
|
170 180
....*....|....*....|....*.
gi 759600243 190 AVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PLN03073 676 GVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-243 |
7.34e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 128 GRSYLS-------LSGGERQRVHLARVLaqlwpgGAEQV---LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHD 197
Cdd:PRK00635 464 GLPYLTperalatLSGGEQERTALAKHL------GAELIgitYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD 537
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 198 LNLAArYCDRLL------------LLHDGRPHLFGTPDEVLRAEPLRQVFGLDVLVQR 243
Cdd:PRK00635 538 EQMIS-LADRIIdigpgagifggeVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKR 594
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-225 |
7.40e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAL---EQ--WQGTERaRRLAVLPQSSSLNFAFSVES 94
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaEKgiCLPPEK-RRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 95 VVGFGRLPHDSGrQRDlQIIAEAMAAadasHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDplhq 174
Cdd:PRK11144 96 NLRYGMAKSMVA-QFD-KIVALLGIE----PLLDRYPGSLSGGEKQRVAIGRALLT-----APELLLMDEPLASLD---- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759600243 175 httLHAVRE---FAGRGAA-----VLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK11144 161 ---LPRKREllpYLERLAReinipILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-225 |
1.26e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.69 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 12 GRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGR---ALEqwqgtERARRLAVLPQssslNF 88
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELE-----PADRDIAMVFQ----NY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 89 AF----SVESVVGFG----RLPHDSGRQRdlqiIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVL 160
Cdd:PRK11650 86 ALyphmSVRENMAYGlkirGMPKAEIEER----VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR-----EPAVF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 161 LLDEPTSALDP-LHQHTTLHaVREFAGR-GAAVLVILHD----LNLAarycDRLLLLHDGRPHLFGTPDEV 225
Cdd:PRK11650 157 LFDEPLSNLDAkLRVQMRLE-IQRLHRRlKTTSLYVTHDqveaMTLA----DRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
128-202 |
2.04e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 2.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 128 GRSYLSLSGGERQRVHLARVLAQLWPGgaEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAA 202
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRSTG--KTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-226 |
3.01e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarrlAVLPQSSSLNFAFSVESVV 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------ALIAISSGLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 97 GFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLArVLAQLWPggaeQVLLLDEPTSALDPLHQHT 176
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFA-ISVHINP----DILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759600243 177 TLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVV 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-211 |
3.40e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 128 GRSYLSLSGGERQRVHLARVLaqLWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLaARYCDR 207
Cdd:PRK00635 804 GRPLSSLSGGEIQRLKLAYEL--LAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV-VKVADY 880
|
....
gi 759600243 208 LLLL 211
Cdd:PRK00635 881 VLEL 884
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-215 |
4.78e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALE-----QWQGTERARRLAVLPQSSSLNFAFS 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDPYASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 V-----ESVVGFGRLPHDSGRQRdlqIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAqLWPggaeQVLLLDEPT 166
Cdd:PRK10261 420 VgdsimEPLRVHGLLPGKAAAAR---VAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALA-LNP----KVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759600243 167 SALDPLHQ----HTTLHAVREFagrGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:PRK10261 492 SALDVSIRgqiiNLLLDLQRDF---GIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-96 |
5.28e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 1 MLAAENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDgraleqwqgteRARRLAVL 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNERLGKL 69
|
90
....*....|....*.
gi 759600243 81 PQSsslNFAFSVESVV 96
Cdd:PRK15064 70 RQD---QFAFEEFTVL 82
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-215 |
7.02e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.71 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEqWQGTERARRLavlpqssslnfaFSV------- 92
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-ADNREAYRQL------------FSAvfsdfhl 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 93 -ESVVGFGRLPHDS-GRQ--RDLQIiaeamaaadaSHL----AGR-SYLSLSGGERQRvhLARVLAQLwpggaEQ--VLL 161
Cdd:COG4615 418 fDRLLGLDGEADPArAREllERLEL----------DHKvsveDGRfSTTDLSQGQRKR--LALLVALL-----EDrpILV 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 162 LDEPTSALDPLHQ----HTTLHAVREfagRGAAVLVILHDlnlaARY---CDRLLLLHDGR 215
Cdd:COG4615 481 FDEWAADQDPEFRrvfyTELLPELKA---RGKTVIAISHD----DRYfdlADRVLKMDYGK 534
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-198 |
8.39e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 8.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 134 LSGGERQRVHLARVLAQLWPGGAeqVLLLDEPTSAldpLHQH------TTLHAVREfagRGAAVLVILHDL 198
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTGKT--LYILDEPTTG---LHFHdirkllEVLHRLVD---KGNTVVVIEHNL 889
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-198 |
1.03e-05 |
|
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: 46.16 E-value: 1.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 128 GRSYLSLSGGERQRVHLARVLAQlwPGGAEQVLLLDEPTSAldpLHQHTT---LHAVREFAGRGAAVLVILHDL 198
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSK--RSTGRTLYILDEPTTG---LHFDDIkklLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-172 |
1.04e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 6 NLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLA-GGSVSLDGRAleqwQGT-----ERARRLAV 79
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRR----RGSgetiwDIKKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 80 LpqSSSLNFAFSVESVV------GF----GRLPHDSGRQRDLqIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLA 149
Cdd:PRK10938 341 V--SSSLHLDYRVSTSVrnvilsGFfdsiGIYQAVSDRQQKL-AQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALV 417
|
170 180
....*....|....*....|...
gi 759600243 150 QLWPggaeqVLLLDEPTSALDPL 172
Cdd:PRK10938 418 KHPT-----LLILDEPLQGLDPL 435
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-251 |
1.48e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNG----ELPLAGGSVSLDGRALEQWqgTERARRLAV---------LPQSSsL 86
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRL--SPRERRKLVghnvsmifqEPQSC-L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSV-----ESVVGF---GRLPHDSGRQRDLQIIAEAMAAADASHLAGRSY-LSLSGGERQRVHLARVLAQlwpggAE 157
Cdd:PRK15093 103 DPSERVgrqlmQNIPGWtykGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFpYELTEGECQKVMIAIALAN-----QP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 158 QVLLLDEPTSALDPLHQHTTLHAV-REFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVLRA--EPLRQv 234
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTphHPYTQ- 256
|
250
....*....|....*..
gi 759600243 235 fgldVLVQRHPERGHPL 251
Cdd:PRK15093 257 ----ALIRAIPDFGSAM 269
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2-208 |
2.25e-05 |
|
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: 44.18 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 2 LAAENLTVKRGRQVV-LQGVSLAlqpgEVLGVLGPNGAGKSTLLGA----LNGELPLAGGSVSLDG-RALEQwqgterar 75
Cdd:cd03279 6 LELKNFGPFREEQVIdFTGLDNN----GLFLICGPTGAGKSTILDAityaLYGKTPRYGRQENLRSvFAPGE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 76 rlavlpQSSSLNFAFSVesvvgfGRLPHDSGRQRDL------QIIAEAMAAAdaSHLAGRSYLSLSGGERQRVHLARVLA 149
Cdd:cd03279 74 ------DTAEVSFTFQL------GGKKYRVERSRGLdydqftRIVLLPQGEF--DRFLARPVSTLSGGETFLASLSLALA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759600243 150 -----QLWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRL 208
Cdd:cd03279 140 lsevlQNRGGARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRL 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-175 |
3.57e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 26 PGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDgraleqwqgterarrlavlpqssslnfafsvesvvgfgrlphds 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 106 grqrDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQLWPggaeqVLLLDEPTSALDPLHQH 175
Cdd:smart00382 37 ----DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-----VLILDEITSLLDAEQEA 97
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-226 |
5.88e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 16 VLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELP----LAGGSVSLDGRALEQWQGTERArrlavlpqssslNFAFS 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRG------------DVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFGRLP-----HDSGRQRDLQI----IAEAMAAADASHLAGRSY-LS--------------LSGGERQRVHLARV 147
Cdd:TIGR00956 144 AETDVHFPHLTvgetlDFAARCKTPQNrpdgVSREEYAKHIADVYMATYgLShtrntkvgndfvrgVSGGERKRVSIAEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 148 LAqlwpgGAEQVLLLDEPTSALDplhQHTTLhavrEFAGRGAAVLVILHDLNLAARY-C--------DRLLLLHDGRPHL 218
Cdd:TIGR00956 224 SL-----GGAKIQCWDNATRGLD---SATAL----EFIRALKTSANILDTTPLVAIYqCsqdayelfDKVIVLYEGYQIY 291
|
....*...
gi 759600243 219 FGTPDEVL 226
Cdd:TIGR00956 292 FGPADKAK 299
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-170 |
6.17e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 4 AENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLdGRALE-----QWqgterarRLA 78
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdQH-------RAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 79 VLPQSSslnfafsVESVVGFGRlpHD---SGRQRdlqiiaeamaaadasHLAGrsYL---------------SLSGGERQ 140
Cdd:PRK11147 394 LDPEKT-------VMDNLAEGK--QEvmvNGRPR---------------HVLG--YLqdflfhpkramtpvkALSGGERN 447
|
170 180 190
....*....|....*....|....*....|
gi 759600243 141 RVHLARVLaqLWPGgaeQVLLLDEPTSALD 170
Cdd:PRK11147 448 RLLLARLF--LKPS---NLLILDEPTNDLD 472
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-253 |
6.23e-05 |
|
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: 43.85 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 128 GRSYLSLSGGERQRVHLArvlAQLWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNlAARYCDR 207
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLA---TQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADY 558
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 759600243 208 LLLL------HDGRPHLFGTPDEVLR------AEPLRQVFGLDVLVQRHPERGHPLIV 253
Cdd:TIGR00630 559 VIDIgpgageHGGEVVASGTPEEILAnpdsltGQYLSGRKKIEVPAERRPGNGKFLTL 616
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-226 |
7.49e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVsldgraleqwqgtERARRLAVLPQSSSLNFAFSVESVV 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------------DRNGEVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 97 GFGRLPHDSGRQrdlQIIAEAMAAADASHLAGRSYLSL---SGGERQRVHLArVLAQLWPggaeQVLLLDEPTSALDPLH 173
Cdd:PRK13546 107 EFKMLCMGFKRK---EIKAMTPKIIEFSELGEFIYQPVkkySSGMRAKLGFS-INITVNP----DILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759600243 174 QHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRPHLFGTPDEVL 226
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-215 |
9.79e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPlAG---GSVSLDG--RALEQWQGTERA------RRLAVLPQsss 85
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGevCRFKDIRDSEALgiviihQELALIPY--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 86 lnfaFSVESVVGFGRLPHDSGrqrdlqIIAEAMAAADASHLAGRSYLSLS--------G-GERQRVHLARVLAQlwpgga 156
Cdd:NF040905 93 ----LSIAENIFLGNERAKRG------VIDWNETNRRARELLAKVGLDESpdtlvtdiGvGKQQLVEIAKALSK------ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 157 eQV--LLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGR 215
Cdd:NF040905 157 -DVklLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-249 |
1.04e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 17 LQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALeQWQGTERARRLAVLPQSSSLNFAF--SVES 94
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQELNLVLqrSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 95 VVGFGRLPH-----DSGRQ-RDLQIIAEAMAAADASHlagRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSA 168
Cdd:PRK10982 93 NMWLGRYPTkgmfvDQDKMyRDTKAIFDELDIDIDPR---AKVATLSVSQMQMIEIAKAFSY-----NAKIVIMDEPTSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 169 LDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLHDGRphlfGTPDEVLRAEPLRQVFGLDV---LVQRHP 245
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ----WIATQPLAGLTMDKIIAMMVgrsLTQRFP 240
|
....
gi 759600243 246 ERGH 249
Cdd:PRK10982 241 DKEN 244
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
128-197 |
1.45e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.86 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 128 GRSYLSLSGGERQRVHLARvlaQLWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHD 197
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLAT---QIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
9-214 |
2.16e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 9 VKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGElpLAGGSVSLDGR--ALEQWQGTeRARRLAVLPQSSSL 86
Cdd:PLN03140 888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIEGDIRisGFPKKQET-FARISGYCEQNDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 87 NFAFSV-ESVV--GFGRLPHDSGRQRDL----QIIAEAMAAADASHLAGRSYLS-LSGGERQRVHLARVLAqlwpgGAEQ 158
Cdd:PLN03140 965 SPQVTVrESLIysAFLRLPKEVSKEEKMmfvdEVMELVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELV-----ANPS 1039
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759600243 159 VLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAA-RYCDRLLLLHDG 214
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIfEAFDELLLMKRG 1096
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-181 |
2.31e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 5 ENLTVKRGRQVVLQGVSLALQPGEVLGVLGPNGAGKSTLLG-----ALNG----------ELPLAGGSVSLDGRALEQwq 69
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGipkncqilhvEQEVVGDDTTALQCVLNT-- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 70 GTERARRLAVLPQSSSLNFAFSVESVVGFGRLPHDSGRQRDL-------------QIIAEAMAAADASHLAGRSYLS--- 133
Cdd:PLN03073 259 DIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAvsqrleeiykrleLIDAYTAEARAASILAGLSFTPemq 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759600243 134 ------LSGGERQRVHLARVLAqLWPggaeQVLLLDEPTSALDplhqhttLHAV 181
Cdd:PLN03073 339 vkatktFSGGWRMRIALARALF-IEP----DLLLLDEPTNHLD-------LHAV 380
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
126-213 |
4.11e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 126 LAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVIL-HDLNlAARY 204
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIR-----NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIaHRLS-TIRY 645
|
....*....
gi 759600243 205 CDRLLLLHD 213
Cdd:PTZ00265 646 ANTIFVLSN 654
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-229 |
6.31e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 133 SLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDPLHQ---HTTLHAVREFAGRgaAVLVILHDLNLAARyCDRLL 209
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLR-----EPKILLLDEATSSLDSNSEkliEKTIVDIKDKADK--TIITIAHRIASIKR-SDKIV 1429
|
90 100
....*....|....*....|....*
gi 759600243 210 LLHD-GRPHLF----GTPDEVLRAE 229
Cdd:PTZ00265 1430 VFNNpDRTGSFvqahGTHEELLSVQ 1454
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-171 |
1.02e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.12 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 14 QVVLQGVSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRAleqwqgterarRLAVLPQSSSLNFAFSVE 93
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLFYVPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 94 SVV-----------GFgrlphdsgRQRDL-QIIAEAMAAADASHLAGRSYLS-----LSGGERQRVHLARVLAQlwpggA 156
Cdd:TIGR00954 534 QIIypdssedmkrrGL--------SDKDLeQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYH-----K 600
|
170
....*....|....*
gi 759600243 157 EQVLLLDEPTSALDP 171
Cdd:TIGR00954 601 PQFAILDECTSAVSV 615
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-203 |
1.15e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 34 GPNGAGKSTLLGALN----GELPL----------------AGGSVSLdgrALEQWQGTERA--RRLAVLpqsssLNFAFS 91
Cdd:cd03240 29 GQNGAGKTTIIEALKyaltGELPPnskggahdpkliregeVRAQVKL---AFENANGKKYTitRSLAIL-----ENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 vesvvgfgrlphdsgRQRDLQIIAEAMAaadashlaGRsylsLSGGERQ------RVHLARVLaqlwpGGAEQVLLLDEP 165
Cdd:cd03240 101 ---------------HQGESNWPLLDMR--------GR----CSGGEKVlasliiRLALAETF-----GSNCGILALDEP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 759600243 166 TSALDPLHQHTTLHAVREFAGRGAA--VLVILHDLNLAAR 203
Cdd:cd03240 149 TTNLDEENIEESLAEIIEERKSQKNfqLIVITHDEELVDA 188
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-195 |
1.38e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 21 SLALQPGEVLGVLGPNGAGKSTLLGALNGELPLaggsvsLDGRALEQWQgteRARRLAVLPQSSSLNFAFSVESVVGFGR 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPL------LSGERQSQFS---HITRLSFEQLQKLVSDEWQRNNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 101 LPHDSGRQ---------RDLQIIAEAMAAADASHLAGRSYLSLSGGERQRVHLARVLAQlwpggAEQVLLLDEPTSALDP 171
Cdd:PRK10938 94 GEDDTGRTtaeiiqdevKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMS-----EPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|....
gi 759600243 172 LHQHTTLHAVREFAGRGAAVLVIL 195
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVLVL 192
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
32-86 |
1.70e-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: 38.29 E-value: 1.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 759600243 32 VLGPNGAGKSTLLGALNGELPLAGGSVSL-DGRAleqwQGTERARRLAVLPQSSSL 86
Cdd:pfam03193 111 LAGQSGVGKSTLLNALLPELDLRTGEISEkLGRG----RHTTTHVELFPLPGGGLL 162
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
129-229 |
2.59e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 129 RSYLSLSGGERQRVHLARvlaQLwpgGAE--QVL-LLDEPTSAldpLHQH------TTLHAVREfagRGAAVLVILHDLN 199
Cdd:COG0178 481 RSAGTLSGGEAQRIRLAT---QI---GSGlvGVLyVLDEPSIG---LHQRdndrliETLKRLRD---LGNTVIVVEHDED 548
|
90 100 110
....*....|....*....|....*....|....*...
gi 759600243 200 --LAArycDRLLLL------HDGRPHLFGTPDEVLRAE 229
Cdd:COG0178 549 tiRAA---DYIIDIgpgageHGGEVVAQGTPEEILKNP 583
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-59 |
4.41e-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: 37.38 E-value: 4.41e-03
10 20
....*....|....*....|....*...
gi 759600243 32 VLGPNGAGKSTLLGALNGELPLAGGSVS 59
Cdd:cd01854 90 LVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
92-200 |
4.62e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 92 VESVVGFGRLPHDSGRQRDLQIIAEAMAAADASHLAGRSYLSLSGGERQrvhLARVLAQLW-PGGAEQVLLLDEPTSALD 170
Cdd:pfam13304 195 ADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKR---LLALLAALLsALPKGGLLLIDEPESGLH 271
|
90 100 110
....*....|....*....|....*....|
gi 759600243 171 PLHQHTTLHAVREFAGRGAAVLVILHDLNL 200
Cdd:pfam13304 272 PKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
32-86 |
4.76e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.49 E-value: 4.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 759600243 32 VLGPNGAGKSTLLGALNGELPLAGGSVSldgRALEQWQGTERARRLAVLPQSSSL 86
Cdd:PRK00098 169 LAGQSGVGKSTLLNALAPDLELKTGEIS---EALGRGKHTTTHVELYDLPGGGLL 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
133-229 |
5.35e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 133 SLSGGERQRVHLARvlaqlWPGGAEQVLLLDEPTSALDPLHQHTTLHAVREFAGRGAAVLVILHDLNLAARYCDRLLLLH 212
Cdd:NF040905 404 NLSGGNQQKVVLSK-----WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
90
....*....|....*..
gi 759600243 213 DGRphLFGtpdEVLRAE 229
Cdd:NF040905 479 EGR--ITG---ELPREE 490
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-215 |
6.44e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 37.64 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 20 VSLALQPGEVLGVLGPNGAGKSTLLGALNGELPLAGGSVSLDGRALEQwQGTERARRLavlpqssslnFAFSVESVVGFG 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKL----------FSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759600243 100 RLPHDSGRQRDLQIIAEAMAAADASH----LAGR-SYLSLSGGERQRVHLARVLaqlwpggAEQ--VLLLDEPTSALDPl 172
Cdd:PRK10522 411 QLLGPEGKPANPALVEKWLERLKMAHklelEDGRiSNLKLSKGQKKRLALLLAL-------AEErdILLLDEWAADQDP- 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759600243 173 hqhttlHAVREF--------AGRGAAVLVILHDlNLAARYCDRLLLLHDGR 215
Cdd:PRK10522 483 ------HFRREFyqvllpllQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
134-198 |
7.11e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 7.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759600243 134 LSGGERQRVHLARVLAQLWPGgaEQVLLLDEPTSAldpLHQH------TTLHAVREfagRGAAVLVILHDL 198
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTG--KTLYILDEPTTG---LHFEdirkllEVLHRLVD---KGNTVVVIEHNL 893
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