|
Name |
Accession |
Description |
Interval |
E-value |
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-254 |
1.84e-79 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 240.02 E-value: 1.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCP---NEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQ------DTP-V 158
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSaaqDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdGGPrW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 159 VLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGV 238
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGADL 241
|
250
....*....|....*..
gi 1093464499 239 EVLRDSAGN-PVLVPQR 254
Cdd:COG4559 242 RVLAHPEGGcPQVLPRA 258
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-252 |
1.23e-77 |
|
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: 235.32 E-value: 1.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNP----WGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLL 161
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPhlglFGRPSAEDREaveEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 162 DEPTAALDLHHAEKIMGMMRARAAAGKAVV-VVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGVEV 240
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVvMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|...
gi 1093464499 241 LRDS-AGNPVLVP 252
Cdd:COG1120 242 IEDPvTGRPLVLP 254
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-253 |
1.18e-76 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 232.74 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCPN---EELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQ------DTPVV 159
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGRAPHGLSRaedDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 160 LLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVV-LHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGV 238
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADV 242
|
250
....*....|....*.
gi 1093464499 239 EVLRD-SAGNPVLVPQ 253
Cdd:PRK13548 243 LVQPHpETGAPLVLPR 258
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-254 |
2.37e-55 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 178.35 E-value: 2.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPW--GCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYskGRLTAEdreIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 164 PTAALDLHHAEKIMGMMRARAAAGKAVVVV-LHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGVEVlR 242
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIvLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV-E 240
|
250
....*....|..
gi 1093464499 243 DSAGNPVLVPQR 254
Cdd:COG4604 241 EIDGKRICVYFR 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-251 |
1.09e-53 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 174.05 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLv 88
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qSQELSVP--FTSREVIDFGRNPW-------GCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:PRK11231 82 -PQHHLTPegITVRELVAYGRSPWlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 160 LLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGVE 239
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|...
gi 1093464499 240 VLRDS-AGNPVLV 251
Cdd:PRK11231 241 IHPEPvSGTPMCV 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-206 |
5.10e-53 |
|
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: 169.92 E-value: 5.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQ 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 sqelsvpftsrevidfgrnpwgcpneellaeVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03214 81 -------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190
....*....|....*....|....*....|....*...
gi 1093464499 170 LHHAEKIMGMMRARAAAGKAVV-VVLHDLSAAAAYADH 206
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVvMVLHDLNLAARYADR 167
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
8-251 |
1.18e-46 |
|
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: 156.13 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVL 87
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGRNP----WGC---PNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVL 160
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVVALGRIPhrslWAGdspHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 161 LDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGVEV 240
Cdd:TIGR03873 161 LDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATV 240
|
250
....*....|..
gi 1093464499 241 LRD-SAGNPVLV 251
Cdd:TIGR03873 241 LTHpDTGRPIIA 252
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-257 |
3.64e-44 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 153.46 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNP-------WGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLL 161
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRTPhrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 162 DEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGVEVL 241
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVG 243
|
250
....*....|....*..
gi 1093464499 242 RDSA-GNPVLVPQRGQD 257
Cdd:PRK09536 244 TDPAtGAPTVTPLPDPD 260
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-244 |
5.57e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 5.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElsiaelARYR-AVL 87
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARRRiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQEL--SVPFTSREVIDFGR----NPWGCPNE---ELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:COG1121 81 PQRAEVdwDFPITVRDVVLMGRygrrGLFRRPSRadrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 159 VLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVkQGPPAETLDAQTVSEVYGIGV 238
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPENLSRAYGGPV 239
|
....*.
gi 1093464499 239 EVLRDS 244
Cdd:COG1121 240 ALLAHG 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-246 |
3.25e-38 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 134.53 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 3 IHSGLGISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELAR 82
Cdd:PRK10575 6 NHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 YRAVLVQSQELSVPFTSREVIDFGRNPW-------GCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQD 155
Cdd:PRK10575 86 KVAYLPQQLPAAEGMTVRELVAIGRYPWhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 156 TPVVLLDEPTAALDLHHAEKIMGMMRARAAAG-KAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVY 234
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
250
....*....|..
gi 1093464499 235 GIGVEVLRDSAG 246
Cdd:PRK10575 246 GIPMGILPHPAG 257
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-252 |
5.75e-38 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 134.18 E-value: 5.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG--------GDVRIGEHSITELSIAEL 80
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 81 ARYRAVLVQSQELSVPFTSREVIDFGRNP-------WGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFY 153
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPharragaLTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 154 Q---------DTPVVLLDEPTAALDLHHAEKIMGMMRARAAA-GKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260 270
....*....|....*....|....*....|
gi 1093464499 224 TLDAQTVSEVYGIGVEVLRDSAG-NPVLVP 252
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGvPPVIVP 271
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
9-253 |
7.09e-35 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 125.34 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSItlgGHRiLNDISVVAEPGKVTALVGPNGAGKSTLLAALSGdhELSG-GDVRIGEHSITELSIAELARYRAVL 87
Cdd:COG4138 1 LQLNDVAV---AGR-LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGqGEILLNGRPLSDWSAAELARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGRnPWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVV----- 159
Cdd:COG4138 75 SQQQSPPFAMPVFQYLALHQ-PAGASSEAveqLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegq 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 160 --LLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIG 237
Cdd:COG4138 154 llLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK 233
|
250
....*....|....*.
gi 1093464499 238 VEVLRdSAGNPVLVPQ 253
Cdd:COG4138 234 FRRLE-VEGHRWLIPT 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-252 |
2.33e-34 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 124.71 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNP-------WGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLL 161
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPhqplftrWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 162 DEPTAALDLHHAEKIMGMMRARAAAGK-AVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGVEV 240
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGyTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
250
....*....|...
gi 1093464499 241 LRDS-AGNPVLVP 252
Cdd:PRK10253 248 IDDPvAGTPLVVP 260
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-177 |
2.37e-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: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 4 HSGLGISADNVSITL-GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELAR 82
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 YRAVLVQSQELsVPFTSREVIDFGRNpwgCPNEELLAEVIAECDVAHL-------LDREV----PTLSGGERARVHSARV 151
Cdd:COG4988 412 QIAWVPQNPYL-FAGTIRENLRLGRP---DASDEELEAALEAAGLDEFvaalpdgLDTPLgeggRGLSGGQAQRLALARA 487
|
170 180
....*....|....*....|....*.
gi 1093464499 152 FYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEIL 513
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-206 |
1.14e-32 |
|
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: 118.40 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRI-GEHSITELS-IAELARYRAVl 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKERKrIGYVPQRRSI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 vqsqELSVPFTSREVIDFGRNP-------WGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVL 160
Cdd:cd03235 80 ----DRDFPISVRDVVLMGLYGhkglfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1093464499 161 LDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADH 206
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-180 |
1.30e-32 |
|
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: 118.36 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGG----HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR 84
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 A----VLVQSQELSVPFTSREVIDF-----GRNPWGCPN--EELLAEViaecDVAHLLDREVPTLSGGERARVHSARVFY 153
Cdd:cd03255 81 RrhigFVFQSFNLLPDLTALENVELplllaGVPKKERREraEELLERV----GLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180
....*....|....*....|....*..
gi 1093464499 154 QDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELL 183
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-206 |
3.65e-31 |
|
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: 113.11 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQ 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 sqelsvpftsrevidfgrnpwgcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 1093464499 170 LHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADH 206
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADR 149
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-206 |
7.08e-31 |
|
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: 113.72 E-value: 7.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVL 87
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQE--LSVPFTSREVIdFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:cd03225 81 FQNPDdqFFGPTVEEEVA-FGLENLGLPEEEIeerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1093464499 163 EPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADH 206
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADR 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-169 |
8.15e-31 |
|
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: 113.34 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElSIAELARYRAVLV 88
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCP-NEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAA 167
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRaDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
..
gi 1093464499 168 LD 169
Cdd:COG4133 162 LD 163
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-176 |
1.40e-30 |
|
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: 113.80 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAelARyRAVLV 88
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--AR-RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVP--FTSREVIDF---GRNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:COG4555 79 LPDERGLYdrLTVRENIRYfaeLYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170
....*....|...
gi 1093464499 164 PTAALDLHHAEKI 176
Cdd:COG4555 159 PTNGLDVMARRLL 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-206 |
2.53e-30 |
|
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: 112.81 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSIT-LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARyRAVL 87
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRR-KVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 V----QSQ--ELSVpftsREVIDFG-RNpWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTP 157
Cdd:COG1122 80 VfqnpDDQlfAPTV----EEDVAFGpEN-LGLPREEIRErveEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1093464499 158 VVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADH 206
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADR 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-169 |
1.26e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.31 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARyraVLV 88
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVP--FTSREVIDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:COG1131 78 VPQEPALYpdLTVRENLRFFARLYGLPRKEArerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
....*.
gi 1093464499 164 PTAALD 169
Cdd:COG1131 158 PTSGLD 163
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-234 |
5.36e-29 |
|
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: 109.58 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLG-GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR--- 84
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AVLVQSQELSVPFTSREVIDFGR-----------NPWGcPNEELLA-EVIAECDVAHLLDREVPTLSGGERARVHSARVF 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrslfGLFP-KEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 153 YQDTPVVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVV-VVLHDLSAAAAYADHVVVVAQGHVVKQGPPAEtLDAQTVS 231
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITViVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLD 238
|
...
gi 1093464499 232 EVY 234
Cdd:cd03256 239 EIY 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-177 |
6.52e-29 |
|
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: 107.47 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGG--HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LvqSQElsvPF----TSREVIdfgrnpwgcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:cd03228 81 V--PQD---PFlfsgTIRENI----------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170
....*....|....*
gi 1093464499 163 EPTAALDLHHAEKIM 177
Cdd:cd03228 122 EATSALDPETEALIL 136
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
9-180 |
7.00e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.98 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLG----GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG-DHeLSGGDVRIGEHSITELSIAELARY 83
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGlDR-PTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLV----QSQELsVP-FTSREVIDFGRNPWGCP---NEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQD 155
Cdd:COG1136 84 RRRHIgfvfQFFNL-LPeLTALENVALPLLLAGVSrkeRRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180
....*....|....*....|....*
gi 1093464499 156 TPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELL 187
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-166 |
9.46e-29 |
|
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: 106.58 E-value: 9.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELSVPFTSREVI 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 104 DFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVP----TLSGGERARVHSARVFYQDTPVVLLDEPTA 166
Cdd:pfam00005 81 RLGLLLKGLSKREKdarAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-206 |
7.17e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 7.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsitelsiaelaRYRAVLVQSQEL--SVP 96
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpdSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 97 FTSREVIDFG----RNPWGCPNEELLAEVIAECD---VAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:NF040873 72 LTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALErvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1093464499 170 LHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAyADH 206
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRR-ADP 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-243 |
1.54e-27 |
|
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: 105.94 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGD-HELSGGDVRIGEHSITELSIAELaRYRAVL 87
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWEL-RKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VqSQELSVPFTSRE-VID---------FGRnpWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQ 154
Cdd:COG1119 83 V-SPALQLRFPRDEtVLDvvlsgffdsIGL--YREPTDEQRErarELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 155 DTPVVLLDEPTAALDLHHAEKIMGMMrarAAAGKAVVVVL----HDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTV 230
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALL---DKLAAEGAPTLvlvtHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENL 236
|
250
....*....|...
gi 1093464499 231 SEVYGIGVEVLRD 243
Cdd:COG1119 237 SEAFGLPVEVERR 249
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-169 |
1.65e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.61 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGgHRILNdISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaryRAVLVQSQ 91
Cdd:COG3840 5 DDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 E------LSVpftsREVIDFGRNPWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:COG3840 79 EnnlfphLTV----AQNIGLGLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
....*..
gi 1093464499 163 EPTAALD 169
Cdd:COG3840 155 EPFSALD 161
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-169 |
1.71e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.64 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSIT-LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELarYRAV 86
Cdd:COG1132 339 EIEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL--RRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQElsvPF----TSREVIDFGRnpwgcpNEELLAEVIAECDVAHLLD--REVP------------TLSGGERARVHS 148
Cdd:COG1132 417 GVVPQD---TFlfsgTIRENIRYGR------PDATDEEVEEAAKAAQAHEfiEALPdgydtvvgergvNLSGGQRQRIAI 487
|
170 180
....*....|....*....|.
gi 1093464499 149 ARVFYQDTPVVLLDEPTAALD 169
Cdd:COG1132 488 ARALLKDPPILILDEATSALD 508
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-177 |
3.14e-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: 109.92 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpF--TSREVIDFGrnpwgcpNEEL-LAEVIAECDVAHLLD--REVP------------TLSGGERARVHSA 149
Cdd:COG2274 554 VLQDVFL---FsgTIRENITLG-------DPDAtDEEIIEAARLAGLHDfiEALPmgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180
....*....|....*....|....*...
gi 1093464499 150 RVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIIL 651
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-176 |
6.62e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 103.36 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRYRAVLV 88
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW-RRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qSQE-----------LSVPFTSREVIdfgrnpwgcPNEELLAEVIAECDVAH-LLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:COG4619 80 -PQEpalwggtvrdnLPFPFQLRERK---------FDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180
....*....|....*....|
gi 1093464499 157 PVVLLDEPTAALDLHHAEKI 176
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRV 169
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-206 |
7.31e-27 |
|
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: 103.37 E-value: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLV 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIrarVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1093464499 166 AALDLHHAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYADH 206
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVtHDQEEALALADR 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-227 |
1.42e-26 |
|
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: 107.68 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL--GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG---GDVRIGEHSITELSIAELARY 83
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQELS-VPFTSREVIDFGRNPWGCPNEELLAEVI---AECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:COG1123 85 IGMVFQDPMTQlNPVTVGDQIAEALENLGLSRAEARARVLellEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 160 LLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYADHVVVVAQGHVVKQGPPAETLDA 227
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRERGTTVLLItHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-177 |
2.53e-26 |
|
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: 107.16 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 5 SGLGISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELAR 82
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 YRAVLVQSQELsvpF--TSREVIDFGRnpwgcPN--EELLAEVIAECDVAHLLDREvP------------TLSGGERARV 146
Cdd:COG4987 410 RIAVVPQRPHL---FdtTLRENLRLAR-----PDatDEELWAALERVGLGDWLAAL-PdgldtwlgeggrRLSGGERRRL 480
|
170 180 190
....*....|....*....|....*....|.
gi 1093464499 147 HSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALL 511
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-169 |
1.49e-25 |
|
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: 100.65 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR---A 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 86 VLVQSQELsvpFTSREVID--------FGRNPwgcpnEELLAEVIAEC-------DVAHLLDREvptLSGGERARVHSAR 150
Cdd:cd03261 81 MLFQSGAL---FDSLTVFEnvafplreHTRLS-----EEEIREIVLEKleavglrGAEDLYPAE---LSGGMKKRVALAR 149
|
170
....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALD 169
Cdd:cd03261 150 ALALDPELLLYDEPTAGLD 168
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-180 |
2.32e-25 |
|
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: 100.00 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR-ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVL 87
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSqelSVPF--TSREVIDFGRnpWGCPNEellaEVIAECDVAHLLDR--EVP------------TLSGGERARVHSARV 151
Cdd:cd03253 81 PQD---TVLFndTIGYNIRYGR--PDATDE----EVIEAAKAAQIHDKimRFPdgydtivgerglKLSGGEKQRVAIARA 151
|
170 180
....*....|....*....|....*....
gi 1093464499 152 FYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAAL 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-176 |
2.75e-24 |
|
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: 96.87 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHEL-----SGGDVRIGEHSITELSIAELARY 83
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAV-LVQSQELSVPFTSREVIDFGRNPWGCPNEELLAEVIAEC-DVAHL----LDREVPT-LSGGERARVHSARVFYQDT 156
Cdd:cd03260 81 RRVgMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEAlRKAALwdevKDRLHALgLSGGQQQRLCLARALANEP 160
|
170 180
....*....|....*....|
gi 1093464499 157 PVVLLDEPTAALDLHHAEKI 176
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKI 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-177 |
4.86e-24 |
|
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: 95.61 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 20 GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEhsitelSIAelaryravLVqSQElsvPF-- 97
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------SIA--------YV-SQE---PWiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 --TSREVIDFGRnPWgcpNEELLAEVIAEC----DVAHLLDR---EVP----TLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:cd03250 79 ngTIRENILFGK-PF---DEERYEKVIKACalepDLEILPDGdltEIGekgiNLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170
....*....|...
gi 1093464499 165 TAALDLHHAEKIM 177
Cdd:cd03250 155 LSAVDAHVGRHIF 167
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-179 |
1.25e-23 |
|
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: 95.58 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRavLV 88
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG--IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QS-------QELSV--------PFTSREVIDFGRnpWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSAR 150
Cdd:cd03219 79 RTfqiprlfPELTVlenvmvaaQARTGSGLLLAR--ARREEREAREraeELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180
....*....|....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALDLHHAEKIMGM 179
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAEL 185
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-169 |
1.25e-23 |
|
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: 94.95 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGkVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAelarYRAVL- 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRIg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVP--FTSREVIDFGRNPWGCPNEELLAEVIAECDVAHLLDRE---VPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:cd03264 76 YLPQEFGVYpnFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAkkkIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
....*..
gi 1093464499 163 EPTAALD 169
Cdd:cd03264 156 EPTAGLD 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-177 |
3.46e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 98.13 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR-ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRYRAVL 87
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGRNPwgcPNEELLAEVIAECDvAHLLDREVPT------------LSGGERARVHSARVFYQD 155
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPD---ASDAEIREALERAG-LDEFVAALPQgldtpigeggagLSGGQAQRLALARAFLRD 476
|
170 180
....*....|....*....|..
gi 1093464499 156 TPVVLLDEPTAALDLHHAEKIM 177
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVL 498
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-170 |
3.72e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsiteLSIAELAryravlv 88
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET----VKIGYFD------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qsQElsvpftsREVIDFGRNPWgcpneELLAEVIAECDVAHL-------------LDREVPTLSGGERARVHSARVFYQD 155
Cdd:COG0488 385 --QH-------QEELDPDKTVL-----DELRDGAPGGTEQEVrgylgrflfsgddAFKPVGVLSGGEKARLALAKLLLSP 450
|
170
....*....|....*
gi 1093464499 156 TPVVLLDEPTAALDL 170
Cdd:COG0488 451 PNVLLLDEPTNHLDI 465
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-236 |
5.37e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 93.84 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISV---------VAEPGKVTALVGPNGAGKSTLLAALSGdhELSG-GDVRIGEHSITELSIAELARYRAVLVQSQ-- 91
Cdd:PRK03695 3 LNDVAVstrlgplsaEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGsGSIQFAGQPLEAWSAAELARHRAYLSQQQtp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ----------ELSVPFTSREvidfgrnpwgCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVV-- 159
Cdd:PRK03695 81 pfampvfqylTLHQPDKTRT----------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 160 -----LLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVY 234
Cdd:PRK03695 151 agqllLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
..
gi 1093464499 235 GI 236
Cdd:PRK03695 231 GV 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-169 |
7.02e-23 |
|
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: 93.45 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpF--TSREVIDFGRnpwgcPNEElLAEVIAECDVAHLLD--REVP------------TLSGGERARVHSAR 150
Cdd:cd03251 81 VSQDVFL---FndTVAENIAYGR-----PGAT-REEVEEAARAANAHEfiMELPegydtvigergvKLSGGQRQRIAIAR 151
|
170
....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALD 169
Cdd:cd03251 152 ALLKDPPILILDEATSALD 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-205 |
8.99e-23 |
|
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: 92.32 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLG-GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSItelsiAELARYRAVLV 88
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTS---REVIDFGRNPWGCPNEELlAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:cd03226 76 VMQDVDYQLFTdsvREELLLGLKELDAGNEQA-ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1093464499 166 AALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYAD 205
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCD 194
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-175 |
9.62e-23 |
|
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: 93.56 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARyrAVLVQ 89
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR--LGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 S-------QELSV---------PFTSREVIDFGRNPWGCPNEELLA-----EVIAECDVAHLLDREVPTLSGGERARVHS 148
Cdd:COG0411 84 TfqnprlfPELTVlenvlvaahARLGRGLLAALLRLPRARREEREAreraeELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180
....*....|....*....|....*..
gi 1093464499 149 ARVFYQDTPVVLLDEPTAALDlhHAEK 175
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLN--PEET 188
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-169 |
1.70e-22 |
|
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: 91.93 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQ 91
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELSVPFTSREVIDFGRNPWGCPNEELLAEV--IAEC-DVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEIDERVreVAELlQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
.
gi 1093464499 169 D 169
Cdd:cd03301 162 D 162
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-169 |
3.02e-22 |
|
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: 90.15 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElSIAELARYRAVLV 88
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDfgrnpwgcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03230 80 EEPSLYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
.
gi 1093464499 169 D 169
Cdd:cd03230 127 D 127
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-180 |
3.41e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 91.34 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 1 MEIHSGLGISADNVSITLGGHR----ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELS 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 77 IAELARYRAVLV----QSQEL----------SVPFTSREVID-FGRnpwgcpNEELLAEViaecDVAHLLDREVPTLSGG 141
Cdd:COG4181 81 EDARARLRARHVgfvfQSFQLlptltalenvMLPLELAGRRDaRAR------ARALLERV----GLGHRLDHYPAQLSGG 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1093464499 142 ERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-169 |
7.11e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHEL---SGGDVRIGEHSITELSIAElaryR 84
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AVLVQSQE------LSVpftsrevidfGRN-PWGCPNE-------ELLAEVIAECDVAHLLDREVPTLSGGERARVHSAR 150
Cdd:COG4136 77 RIGILFQDdllfphLSV----------GENlAFALPPTigraqrrARVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170
....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALD 169
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLD 165
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-180 |
7.26e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYravLV 88
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGcPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:PRK13539 80 HRNAMKPALTVAENLEFWAAFLG-GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|..
gi 1093464499 169 DLHHAEKIMGMM 180
Cdd:PRK13539 159 DAAAVALFAELI 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-169 |
8.91e-22 |
|
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: 90.26 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElSIAELARYRAVLVQSQELSVPFT 98
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDELT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093464499 99 SREVIDFGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03263 92 VREHLRFYARLKGLPKSEIKEEVellLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-170 |
1.15e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 11 ADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDV------RIG----------EHSITE 74
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsipkglRIGylpqepplddDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 75 LSIAELARYRAVLVQSQELSVPFTSREvidfgrnpwgcPNEELLAEVIAECDVAH--------------------LLDRE 134
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPD-----------EDLERLAELQEEFEALGgweaearaeeilsglgfpeeDLDRP 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1093464499 135 VPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-205 |
1.20e-21 |
|
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: 90.09 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRiLNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQ 91
Cdd:cd03299 4 ENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELSVPFTSREVIDFGRNPWGCPNEELLAEV--IAE-CDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDKKEIERKVleIAEmLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1093464499 169 DLHHAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYAD 205
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVtHDFEEAWALAD 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-176 |
2.95e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 88.82 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELsVPFT 98
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFL-FSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVIDFGRNPwgcPNEEllaEVIAECDVAHLLD--REVP------------TLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:cd03254 93 IMENIRLGRPN---ATDE---EVIEAAKEAGAHDfiMKLPngydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170
....*....|..
gi 1093464499 165 TAALDLHHAEKI 176
Cdd:cd03254 167 TSNIDTETEKLI 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-169 |
4.60e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.52 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaryR--AV 86
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----RniAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQEL----SVpftsREVIDFG---RnpwGCPNEELLAEV--IAE-CDVAHLLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:COG3839 80 VFQSYALyphmTV----YENIAFPlklR---KVPKAEIDRRVreAAElLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:COG3839 153 KVFLLDEPLSNLD 165
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-206 |
5.61e-21 |
|
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: 87.95 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL----GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAELARYR 84
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AVLVQ--SQElsvPFTS-----------REVIDFGRNPWgcpNEELLAEVIAECDVAHLLDREVPT-----LSGGERARV 146
Cdd:cd03257 81 RKEIQmvFQD---PMSSlnprmtigeqiAEPLRIHGKLS---KKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093464499 147 HSARVFYQDTPVVLLDEPTAALD----------LHHAEKIMGMmraraaagkavvVVL---HDLSAAAAYADH 206
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDvsvqaqildlLKKLQEELGL------------TLLfitHDLGVVAKIADR 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-206 |
8.95e-21 |
|
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: 91.12 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSIT-----LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARY 83
Cdd:COG1123 261 LEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RavlvqsQELSV----PFTS-------REVIDFG-RNPWGCPNEEL---LAEVIAECD-VAHLLDREVPTLSGGERARVH 147
Cdd:COG1123 341 R------RRVQMvfqdPYSSlnprmtvGDIIAEPlRLHGLLSRAERrerVAELLERVGlPPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 148 SARVFYQDTPVVLLDEPTAALDLHHAEKIMGMMraraaagkavvVVL------------HDLSAAAAYADH 206
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLL-----------RDLqrelgltylfisHDLAVVRYIADR 474
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-177 |
1.11e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.03 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSIT-LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRavl 87
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 vqsQELSVPF-----------------------TSREVIdfgrnpwgcpnEELLAEVIAECDVAHLLDREVPTLSGGERA 144
Cdd:COG2884 79 ---RRIGVVFqdfrllpdrtvyenvalplrvtgKSRKEI-----------RRRVREVLDLVGLSDKAKALPHELSGGEQQ 144
|
170 180 190
....*....|....*....|....*....|...
gi 1093464499 145 RVHSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIM 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-169 |
1.14e-20 |
|
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: 87.73 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRA--- 85
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 86 VLVQSQELsvpFTSREVID--------FGRNPwgcpnEELLAEVIAEC-------DVAHLLDREvptLSGGERARVHSAR 150
Cdd:COG1127 86 MLFQGGAL---FDSLTVFEnvafplreHTDLS-----EAEIRELVLEKlelvglpGAADKMPSE---LSGGMRKRVALAR 154
|
170
....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALD 169
Cdd:COG1127 155 ALALDPEILLYDEPTAGLD 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-180 |
1.23e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QsQELS-VP--------FTSREVIDFGRNPWGCPNE---ELLAEVIAECDVahllDREVPTLSGGERARVHSARVFYQDT 156
Cdd:COG1129 85 H-QELNlVPnlsvaeniFLGREPRRGGLIDWRAMRRrarELLARLGLDIDP----DTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180
....*....|....*....|....
gi 1093464499 157 PVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRII 183
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-171 |
1.41e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.39 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaryRAV-L 87
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK----RNVgM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VqSQE------LSVpftsREVIDFGRNPWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:COG3842 82 V-FQDyalfphLTV----AENVAFGLRMRGVPKAEiraRVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170
....*....|...
gi 1093464499 159 VLLDEPTAALDLH 171
Cdd:COG3842 157 LLLDEPLSALDAK 169
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-169 |
2.76e-20 |
|
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: 84.93 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV--LVQ 89
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIgmVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 SQELSVPFTSREVIDFGrnpwgcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03229 84 DFALFPHLTVLENIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-169 |
2.90e-20 |
|
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: 86.01 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 26 DISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQELSVPFTSREVIDF 105
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093464499 106 GRNPWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03298 94 GLSPGLKLTAEdrqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-169 |
3.94e-20 |
|
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: 89.39 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRI--LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpF--TSREVIDFGRnPWGCPNEELLAEVIAE--CDVAHLLDREVPT--------LSGGERARVHSARVFYQ 154
Cdd:TIGR02203 411 VSQDVVL---FndTIANNIAYGR-TEQADRAEIERALAAAyaQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALLK 486
|
170
....*....|....*
gi 1093464499 155 DTPVVLLDEPTAALD 169
Cdd:TIGR02203 487 DAPILILDEATSALD 501
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-169 |
4.19e-20 |
|
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: 86.06 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELAR----YR 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgigYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AvlvqsQELSVpFTS----------REVIDFGRNPWgcpnEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQ 154
Cdd:cd03218 81 P-----QEASI-FRKltveenilavLEIRGLSKKER----EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170
....*....|....*
gi 1093464499 155 DTPVVLLDEPTAALD 169
Cdd:cd03218 151 NPKFLLLDEPFAGVD 165
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-180 |
5.25e-20 |
|
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: 84.02 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaryravlv 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qSQELSVpftsrevidfgrnpwgcpneellaeviaecdvahlldREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03216 72 -ARRAGI-------------------------------------AMVYQLSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170
....*....|..
gi 1093464499 169 DLHHAEKIMGMM 180
Cdd:cd03216 114 TPAEVERLFKVI 125
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-177 |
9.58e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 84.63 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG---DHELSGGDVRIGEhsiTELSIAELARYRAVLVQSQELSVPFT 98
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVIDF-----GRNPWGCPNEELLAEVIAECDVAH--LLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:cd03234 98 VRETLTYtailrLPRKSSDAIRKKRVEDVLLRDLALtrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
....*.
gi 1093464499 172 HAEKIM 177
Cdd:cd03234 178 TALNLV 183
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-168 |
1.25e-19 |
|
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: 84.41 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 -QSQELSVPFTSREVIDFG-RNPWGCPNEELLAEVIAECDV-AHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:cd03224 81 pEGRRIFPELTVEENLLLGaYARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
...
gi 1093464499 166 AAL 168
Cdd:cd03224 161 EGL 163
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-169 |
1.26e-19 |
|
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: 84.12 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSIT--ELSIAELARYRAV 86
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELSVPFTSREVIDFG-RNPWGCPNEELLAEVIAECDVAHLLDRE--VP-TLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApIKVKGMSKAEAEERALELLEKVGLADKAdaYPaQLSGGQQQRVAIARALAMNPKVMLFD 160
|
....*..
gi 1093464499 163 EPTAALD 169
Cdd:cd03262 161 EPTSALD 167
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-223 |
1.99e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.07 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSIT-ELSIAELARYR---AVLVQSQELSVpF 97
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRkkvGIVFQFPEHQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 --TSREVIDFGRNPWGCPNEELLA---EVIAECDVAH-LLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:PRK13634 100 eeTVEKDICFGPMNFGVSEEDAKQkarEMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1093464499 172 HAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVtHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-169 |
2.68e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 82.36 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAELARYRAV 86
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpFTSREVIDFGRNpwgcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTA 166
Cdd:cd03247 80 LNQRPYL---FDTTLRNNLGRR-----------------------------FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
...
gi 1093464499 167 ALD 169
Cdd:cd03247 128 GLD 130
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-171 |
3.65e-19 |
|
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: 86.41 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHR-ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRyRAVLVQS 90
Cdd:COG5265 361 ENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL-R-AAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QElSVPF--TSREVIDFGRnpWGCPNEellaEVIAECDVAHLLD--REVP----T--------LSGGERARVHSARVFYQ 154
Cdd:COG5265 439 QD-TVLFndTIAYNIAYGR--PDASEE----EVEAAARAAQIHDfiESLPdgydTrvgerglkLSGGEKQRVAIARTLLK 511
|
170
....*....|....*..
gi 1093464499 155 DTPVVLLDEPTAALDLH 171
Cdd:COG5265 512 NPPILIFDEATSALDSR 528
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-180 |
3.96e-19 |
|
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: 82.21 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 6 GLGISADNVSITL------GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG--GDVRIGEHSITELSI 77
Cdd:cd03213 1 GVTLSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 78 AELARYravlVQSQELSVP-FTSREVIDFgrnpwgcpneellaevIAECDVahlldrevptLSGGERARVHSARVFYQDT 156
Cdd:cd03213 81 RKIIGY----VPQDDILHPtLTVRETLMF----------------AAKLRG----------LSGGERKRVSIALELVSNP 130
|
170 180
....*....|....*....|....
gi 1093464499 157 PVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLL 154
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-169 |
4.12e-19 |
|
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: 83.48 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARyRAVLV 88
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERAR-LGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQE------LSVPFTSREVIDFGRNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:TIGR04406 81 LPQEasifrkLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
....*..
gi 1093464499 163 EPTAALD 169
Cdd:TIGR04406 161 EPFAGVD 167
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
9-169 |
4.63e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.60 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSIT----LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiaelaRYR 84
Cdd:COG1116 8 LELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AVLVQsQELSVPF-TSREVIDFGRNPWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVL 160
Cdd:COG1116 83 GVVFQ-EPALLPWlTVLDNVALGLELRGVPKAErreRARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
....*....
gi 1093464499 161 LDEPTAALD 169
Cdd:COG1116 162 MDEPFGALD 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-180 |
4.64e-19 |
|
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: 85.88 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELsvpF- 97
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL---Fd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 -TSREVIDFGRNpwGCPNEEL--------LAEVIAEcdVAHLLDREV----PTLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:TIGR02868 423 tTVRENLRLARP--DATDEELwaalervgLADWLRA--LPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170
....*....|....*.
gi 1093464499 165 TAALDLHHAEKIMGMM 180
Cdd:TIGR02868 499 TEHLDAETADELLEDL 514
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-177 |
7.63e-19 |
|
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: 81.70 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSI--TELSIAELARYRAVLVQS--QELS 94
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDpdDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 95 VPFTSREViDFGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:TIGR01166 83 AADVDQDV-AFGPLNLGLSEAEVERRVreaLTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
....*.
gi 1093464499 172 HAEKIM 177
Cdd:TIGR01166 162 GREQML 167
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-170 |
1.14e-18 |
|
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: 81.90 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLV 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCPNEELLAEVIAECDVAHLL---DREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEgyaNRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
....*
gi 1093464499 166 AALDL 170
Cdd:cd03300 159 GALDL 163
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-206 |
1.26e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITL-GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYrav 86
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAY--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQEL--SVPFTSREVIDFGRnpWG---------CPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQD 155
Cdd:PRK15056 83 VPQSEEVdwSFPVLVEDVVMMGR--YGhmgwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 156 TPVVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADH 206
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDY 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-169 |
1.35e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELAR----Y 83
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgigY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 -----------------RAVLvQSQELSvpftsREVIdfgrnpwgcpnEELLAEVIAECDVAHLLDREVPTLSGGERARV 146
Cdd:COG1137 83 lpqeasifrkltvedniLAVL-ELRKLS-----KKER-----------EERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180
....*....|....*....|...
gi 1093464499 147 HSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVD 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-176 |
2.13e-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: 81.22 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELSVPFTSREVI 103
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093464499 104 DFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKI 176
Cdd:cd03267 117 YLLAAIYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-169 |
2.27e-18 |
|
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: 80.98 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGG----HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAelaryR 84
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AVLVQSQELsvpFTSREVID---FGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:cd03293 76 GYVFQQDAL---LPWLTVLDnvaLGLELQGVPKAEARERAeelLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170
....*....|.
gi 1093464499 159 VLLDEPTAALD 169
Cdd:cd03293 153 LLLDEPFSALD 163
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-176 |
2.44e-18 |
|
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: 79.03 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsitelsiaelaryravlv 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qsqelsvpftsrevidfgrnpwgcpneellaeviaeCDVAHLldrevPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03221 63 ------------------------------------VKIGYF-----EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
....*...
gi 1093464499 169 DLHHAEKI 176
Cdd:cd03221 102 DLESIEAL 109
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-169 |
2.86e-18 |
|
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: 80.49 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElSIAELARYRAVLVQSQELSVPFTSREVI 103
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 104 DFGRNPWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03266 100 EYFAGLYGLKGDELTArleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-169 |
2.87e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.94 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSIT-----LGGHRI--LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIgEHSITELSIAELA 81
Cdd:COG4778 5 LEVENLSKTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV-RHDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQ-------SQELSV-PFTS-REVIdfgRNP---WGCPNEEllaeviAECDVAHLLDR-EVP---------TLS 139
Cdd:COG4778 84 PREILALRrrtigyvSQFLRViPRVSaLDVV---AEPlleRGVDREE------ARARARELLARlNLPerlwdlppaTFS 154
|
170 180 190
....*....|....*....|....*....|
gi 1093464499 140 GGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-169 |
3.71e-18 |
|
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: 79.95 E-value: 3.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELsiAELARYRAVLV 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCPNEElLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKR-IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
.
gi 1093464499 169 D 169
Cdd:cd03268 158 D 158
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-180 |
5.26e-18 |
|
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: 80.03 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 33 PGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGeHSI---TELSIAELARYRAV--LVQSQELSVPFTSREVIDFG- 106
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-GTVlfdSRKKINLPPQQRKIglVFQQYALFPHLNVRENLAFGl 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093464499 107 RNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-180 |
8.50e-18 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 79.32 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR----AVLVQSQELSVPF 97
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRnkklGFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 TSREVIDF-----GRNPwgCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHH 172
Cdd:TIGR02211 99 TALENVAMplligKKSV--KEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
....*...
gi 1093464499 173 AEKIMGMM 180
Cdd:TIGR02211 177 AKIIFDLM 184
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-169 |
1.02e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 78.03 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGG--HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQsqelsvpftsrevidfgrnpwgcpNEELLAEVIAEcdvahlldrevPTLSGGERARVHSARVFYQDTPVVLLDEPTA 166
Cdd:cd03246 81 LPQ------------------------DDELFSGSIAE-----------NILSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
...
gi 1093464499 167 ALD 169
Cdd:cd03246 126 HLD 128
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-169 |
1.25e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.79 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL--GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpF--TSREVIDFGRNPwgcPNEELLAEVIAECDVAHLLDREVP----------TLSGGERARVHSARVFYQ 154
Cdd:PRK11160 419 VSQRVHL---FsaTLRDNLLLAAPN---ASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLH 492
|
170
....*....|....*
gi 1093464499 155 DTPVVLLDEPTAALD 169
Cdd:PRK11160 493 DAPLLLLDEPTEGLD 507
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-177 |
1.79e-17 |
|
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: 78.40 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRI--LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQ 89
Cdd:cd03245 6 RNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 SQELsvpF--TSREVIDFGrNPWGCPNEELLAEVIAECDV-----AHLLDREVP----TLSGGERARVHSARVFYQDTPV 158
Cdd:cd03245 86 DVTL---FygTLRDNITLG-APLADDERILRAAELAGVTDfvnkhPNGLDLQIGergrGLSGGQRQAVALARALLNDPPI 161
|
170
....*....|....*....
gi 1093464499 159 VLLDEPTAALDLHHAEKIM 177
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLK 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-169 |
2.56e-17 |
|
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: 78.54 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 7 LGISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAV 86
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELSVPFTSREVIDFG---RNPWGCPNE-ELLAEVIAECDVAHL---LDREVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlrvKPRSERPPEaEIRAKVHELLKLVQLdwlADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170
....*....|
gi 1093464499 160 LLDEPTAALD 169
Cdd:cd03296 159 LLDEPFGALD 168
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-169 |
2.65e-17 |
|
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: 80.95 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsVPFTSREVIdfGRnpWGCPNEEllaEVIAECDVA--HLLDREVP------------TLSGGERARVHSARVF 152
Cdd:COG4618 411 LPQDVEL-FDGTIAENI--AR--FGDADPE---KVVAAAKLAgvHEMILRLPdgydtrigeggaRLSGGQRQRIGLARAL 482
|
170
....*....|....*..
gi 1093464499 153 YQDTPVVLLDEPTAALD 169
Cdd:COG4618 483 YGDPRLVVLDEPNSNLD 499
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-169 |
3.47e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARyRAVLVQSQELSVPFTSREV 102
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR-QVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 103 IDFGRNPwgCPNEELLAEVIAECdvAHLLDREVPT------------LSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:TIGR00958 575 IAYGLTD--TPDEEIMAAAKAAN--AHDFIMEFPNgydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
13-177 |
3.60e-17 |
|
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: 79.76 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRIlnDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSI--TELSIAELARYRAVLVQS 90
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QE------LSVpftsREVIDFGRnpWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLL 161
Cdd:COG4148 84 QEarlfphLSV----RGNLLYGR--KRAPRAErriSFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170
....*....|....*.
gi 1093464499 162 DEPTAALDLHHAEKIM 177
Cdd:COG4148 158 DEPLAALDLARKAEIL 173
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-169 |
4.73e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.39 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHR-ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQS 90
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELsvpF--TSREVIDFGRnPWGCPNEELLAEVIAEcdvAH--LLDREV----------PTLSGGERARVHSARVFYQDT 156
Cdd:PRK13657 418 AGL---FnrSIEDNIRVGR-PDATDEEMRAAAERAQ---AHdfIERKPDgydtvvgergRQLSGGERQRLAIARALLKDP 490
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:PRK13657 491 PILILDEATSALD 503
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
5.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 78.24 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 20 GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRYRAVLV-QSQELSVpFT 98
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-RSKVGLVfQDPDDQV-FS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SR--EVIDFGRNPWGCPNEELLAEVIAECDVAHLLD-REVPT--LSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHA 173
Cdd:PRK13647 95 STvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDfRDKPPyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 174 EKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSE 232
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-176 |
5.74e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 77.13 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELarYRAVLVQSQELSVPFTS- 99
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL--HSKVSLVGQEPVLFARSl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 100 REVIDFGRNpwGCPNEELLA--------EVIAEcdVAHLLDREV----PTLSGGERARVHSARVFYQDTPVVLLDEPTAA 167
Cdd:cd03248 105 QDNIAYGLQ--SCSFECVKEaaqkahahSFISE--LASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
....*....
gi 1093464499 168 LDLHHAEKI 176
Cdd:cd03248 181 LDAESEQQV 189
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-180 |
6.13e-17 |
|
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: 77.06 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITEL---SIAELARYRAVLVQSQELSVPFTSR 100
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 101 EVIDFGRNPWGCPNEELLAEVIAECDVAHLLD--REVPT-LSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSHkhRALPAeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
...
gi 1093464499 178 GMM 180
Cdd:cd03292 177 NLL 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-170 |
7.86e-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: 76.41 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAELARyRAVLVQS 90
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERAR-LGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QElSVPFTSREVIDFGRNpwgcPNEellaeviaecdvahlldrevpTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:cd03217 84 QY-PPEIPGVKNADFLRY----VNE---------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-177 |
8.14e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.82 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVrigehsITELSIAelaryravLVQSQELSVPFTSREV 102
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAERSIA--------YVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFgrnpWGCPNEELLAEVIA----ECDVAHL---LDREVP----TLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:PTZ00243 741 ILF----FDEEDAARLADAVRvsqlEADLAQLgggLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
....*.
gi 1093464499 172 HAEKIM 177
Cdd:PTZ00243 817 VGERVV 822
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-180 |
1.18e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAELARYRAVLV 88
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSV--PFTSREVIDFGRNP----WGCP------NEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:PRK09700 85 IYQELSVidELTVLENLYIGRHLtkkvCGVNiidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180
....*....|....*....|....
gi 1093464499 157 PVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIM 188
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-171 |
1.36e-16 |
|
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: 76.25 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIaELARYRAVLV 88
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSRE-VIDFGRnPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHAR-LYGVPGAERrerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
....*..
gi 1093464499 165 TAALDLH 171
Cdd:cd03265 159 TIGLDPQ 165
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-176 |
1.48e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 76.42 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 20 GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRYRAVLVqSQELSVPFTS 99
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL-RSQIGLV-SQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 100 -REVIDFGRNPwgcpneELLAEVIAECDVAHLLD--REVP------------TLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:cd03249 93 iAENIRYGKPD------ATDEEVEEAAKKANIHDfiMSLPdgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170
....*....|..
gi 1093464499 165 TAALDLhHAEKI 176
Cdd:cd03249 167 TSALDA-ESEKL 177
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-169 |
1.54e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.82 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR----ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAElaryR 84
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-AD----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 AVLVQSQELSVPFTSREVIDFGRNPWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLL 161
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRAraeELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
....*...
gi 1093464499 162 DEPTAALD 169
Cdd:COG4525 159 DEPFGALD 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-179 |
1.61e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITL-GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGdheL----SGgdvrigehsitELSIAELAR 82
Cdd:COG4178 362 ALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---LwpygSG-----------RIARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 yraVLVQSQELSVPFTS-REVIDFGRNPWGCPNEELlAEVIAECDVAHL---LDREVP---TLSGGERARVHSARVFYQD 155
Cdd:COG4178 428 ---VLFLPQRPYLPLGTlREALLYPATAEAFSDAEL-REALEAVGLGHLaerLDEEADwdqVLSLGEQQRLAFARLLLHK 503
|
170 180
....*....|....*....|....
gi 1093464499 156 TPVVLLDEPTAALDLHHAEKIMGM 179
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQL 527
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-169 |
1.85e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiaelARYRAV-- 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH----ARDRKVgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELSVPFTSREVIDFG-------RNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170
....*....|
gi 1093464499 160 LLDEPTAALD 169
Cdd:PRK10851 159 LLDEPFGALD 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-168 |
1.87e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElARYRAVLVQSQ 91
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA-ALAAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELS-VP-FTSREVIDFGRNP--WGCPNEELLAEVIAECdVAHL---LDREVP--TLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:PRK11288 87 ELHlVPeMTVAENLYLGQLPhkGGIVNRRLLNYEAREQ-LEHLgvdIDPDTPlkYLSIGQRQMVEIAKALARNARVIAFD 165
|
....*.
gi 1093464499 163 EPTAAL 168
Cdd:PRK11288 166 EPTSSL 171
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-168 |
1.92e-16 |
|
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: 75.79 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV- 88
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQE----LSVpftsREVIDFGRnpWGCPNEELLAEVIAEC-----DVAHLLDREVPTLSGGE-------RARVHSARvf 152
Cdd:COG0410 85 EGRRifpsLTV----EENLLLGA--YARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEqqmlaigRALMSRPK-- 156
|
170
....*....|....*.
gi 1093464499 153 yqdtpVVLLDEPTAAL 168
Cdd:COG0410 157 -----LLLLDEPSLGL 167
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-171 |
2.33e-16 |
|
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: 78.05 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEhsitelsiaelaryravlv 88
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qSQELSVPFTSREVIDFGRNPWgcpneellaEVIAE-CDVAHLLDREVPT--------------------LSGGERARVH 147
Cdd:TIGR03719 384 -TVKLAYVDQSRDALDPNKTVW---------EEISGgLDIIKLGKREIPSrayvgrfnfkgsdqqkkvgqLSGGERNRVH 453
|
170 180
....*....|....*....|....
gi 1093464499 148 SARVFYQDTPVVLLDEPTAALDLH 171
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-169 |
2.52e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARyRAVLV 88
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-RGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQE------LSVPFTSREVIDFGRNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:PRK10895 83 LPQEasifrrLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
....*..
gi 1093464499 163 EPTAALD 169
Cdd:PRK10895 163 EPFAGVD 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-169 |
2.64e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQE 92
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 93 LSVPFTSREVIDFGRNPWGCPNEELLAEV--IAEC-DVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVnqVAEVlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-169 |
3.38e-16 |
|
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: 75.41 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR-ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVL 87
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGRNPWGCPNE-------ELLAEViaECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVL 160
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEkireradELLALV--GLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
....*....
gi 1093464499 161 LDEPTAALD 169
Cdd:cd03295 159 MDEPFGALD 167
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-180 |
4.22e-16 |
|
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: 74.32 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAELARYRAVLV 88
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFgRNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:TIGR01189 80 HLPGLKPELSALENLHF-WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170
....*....|..
gi 1093464499 169 DLHHAEKIMGMM 180
Cdd:TIGR01189 159 DKAGVALLAGLL 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-223 |
6.29e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 20 GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSI--TELSIAELARYRAVLVQSQELSVPF 97
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 TS-REVIDFGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHA 173
Cdd:PRK13636 98 ASvYQDVSFGAVNLKLPEDEVRKRVdnaLKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 174 EKIMGMMRARAAAGKAVVV-VLHDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIiATHDIDIVPLYCDNVFVMKEGRVILQGNPKE 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-169 |
7.64e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHE---LSGGDVRIGEHSITelsiAELARYRAVLVQSQELSVP-F 97
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPtL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 TSREVIDF------GRNPWGCPNEELLAEVIAEC---DVAHLL---DREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:TIGR00955 115 TVREHLMFqahlrmPRRVTKKEKRERVDEVLQALglrKCANTRigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
....
gi 1093464499 166 AALD 169
Cdd:TIGR00955 195 SGLD 198
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-176 |
1.17e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELS-----GGDVRIGEHSI--TELSIAELa 81
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQELSVPFTSREVIDFGRNPWGCPNEELLAEVIAEC--------DVAHLLDREVPTLSGGERARVHSARVFY 153
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180
....*....|....*....|...
gi 1093464499 154 QDTPVVLLDEPTAALDLHHAEKI 176
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKI 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-244 |
1.83e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELsiAELARYR-AVL 87
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--ARHARQRvGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSRE-VIDFGRNpWGCPNEELLAEVIAECDVAHL---LDREVPTLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:PRK13537 86 PQFDNLDPDFTVREnLLVFGRY-FGLSAAAARALVPPLLEFAKLenkADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 164 PTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQT---VSEVYGIGVEV 240
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIYGPDPVA 244
|
....
gi 1093464499 241 LRDS 244
Cdd:PRK13537 245 LRDE 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-177 |
1.97e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGdheLSGGDVRIGEH----SITELSIAELAR-- 82
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAGSHiellGRTVQREGRLARdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 -----YRAVLVQSQELSVPFTSREVI---DFGRNP-------WGCPNEELLA-EVIAECDVAHLLDREVPTLSGGERARV 146
Cdd:PRK09984 82 rksraNTGYIFQQFNLVNRLSVLENVligALGSTPfwrtcfsWFTREQKQRAlQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190
....*....|....*....|....*....|.
gi 1093464499 147 HSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVM 192
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-177 |
2.58e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.20 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSIT------------------------ELS 76
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykrakyigrvfqdpmmgtapSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 77 IAE---LARYRAvlvQSQELSvPFTSREVIDFGRnpwgcpneELLAEViaecdvaHL-----LDREVPTLSGGERarvhs 148
Cdd:COG1101 99 IEEnlaLAYRRG---KRRGLR-RGLTKKRRELFR--------ELLATL-------GLglenrLDTKVGLLSGGQR----- 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1093464499 149 arvfyQ---------DTP-VVLLDEPTAALDLHHAEKIM 177
Cdd:COG1101 155 -----QalsllmatlTKPkLLLLDEHTAALDPKTAALVL 188
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-179 |
3.08e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.82 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAE-LARYRAVLVQSQ 91
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELSVP-FTSREVIDFG----RNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTA 166
Cdd:PRK09493 86 FYLFPhLTALENVMFGplrvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180
....*....|....*....|....
gi 1093464499 167 ALD--LHH---------AEKIMGM 179
Cdd:PRK09493 166 ALDpeLRHevlkvmqdlAEEGMTM 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-223 |
3.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.19 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 20 GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSIT--ELSIAELARYRAVLVQS--QELSV 95
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQNpdDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 96 PfTSREVIDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHH 172
Cdd:PRK13639 94 P-TVEEDVAFGPLNLGLSKEEVekrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 173 AEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-170 |
3.26e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAELARY------- 83
Cdd:COG0396 5 NLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARAgiflafq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 --------------RAVL--VQSQELSVPFTSREVidfgrnpwgcpnEELLAEV-IAEcdvaHLLDREV-PTLSGGERAR 145
Cdd:COG0396 85 ypveipgvsvsnflRTALnaRRGEELSAREFLKLL------------KEKMKELgLDE----DFLDRYVnEGFSGGEKKR 148
|
170 180
....*....|....*....|....*
gi 1093464499 146 VHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDI 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-169 |
3.54e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.77 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEhsitelsiaelaryravlv 88
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE------------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 qSQELSVPFTSREVIDFGRNPWgcpneellaEVIAE-CDVAHLLDREVP--------------------TLSGGERARVH 147
Cdd:PRK11819 386 -TVKLAYVDQSRDALDPNKTVW---------EEISGgLDIIKVGNREIPsrayvgrfnfkggdqqkkvgVLSGGERNRLH 455
|
170 180
....*....|....*....|..
gi 1093464499 148 SARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD 477
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-177 |
3.61e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.78 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLG-GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVL 87
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSqelsvPF----TSREVIDFGRNPwGCPNEELLAEV-IAEC--DVAHL-------LDREVPTLSGGERARVHSARVFY 153
Cdd:TIGR01193 554 PQE-----PYifsgSILENLLLGAKE-NVSQDEIWAACeIAEIkdDIENMplgyqteLSEEGSSISGGQKQRIALARALL 627
|
170 180
....*....|....*....|....
gi 1093464499 154 QDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIV 651
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-228 |
4.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELS-VPFTSREV 102
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQfVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGM 179
Cdd:PRK13648 105 VAFGLENHAVPYDEMhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1093464499 180 MRARAAAGKAVVVVL-HDLSAAAAyADHVVVVAQGHVVKQGPPAETLDAQ 228
Cdd:PRK13648 185 VRKVKSEHNITIISItHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-169 |
4.37e-15 |
|
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: 72.23 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR----ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAEL--AR 82
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 YRAVLVqSQELSVpFTSREVIDFGRNP---WGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:cd03258 82 RRIGMI-FQHFNL-LSSRTVFENVALPleiAGVPKAEIEErvlELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:cd03258 160 KVLLCDEATSALD 172
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-169 |
4.47e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.64 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsitELSIAELARYRAV- 86
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNLPPRERRVg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVqSQE------LSVpftsREVIDFG---RNPwgcPN-------EELLAEViaecDVAHLLDREVPTLSGGERARVHSAR 150
Cdd:COG1118 79 FV-FQHyalfphMTV----AENIAFGlrvRPP---SKaeirarvEELLELV----QLEGLADRYPSQLSGGQRQRVALAR 146
|
170
....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALD 169
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALD 165
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-169 |
4.88e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELSVPFT 98
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093464499 99 SREV-IDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13652 95 TVEQdIAFGPINLGLDEETVahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-169 |
6.08e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 72.06 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPG-----KVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITelsiaelarYRAVLVQS-QELSV-P 96
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKAdYEGTVrD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093464499 97 FTSREVIDFGRNPWgcpneeLLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03237 81 LLSSITKDFYTHPY------FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-177 |
6.13e-15 |
|
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: 71.59 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDV---RIGEHSITELSIAELARYRAVLVQSQELSVPFTSR 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 101 EVIDFGrNPWgcpNEELLAEVIAEC------------DVAHLLDREVpTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:cd03290 97 ENITFG-SPF---NKQRYKAVTDACslqpdidllpfgDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
....*....
gi 1093464499 169 DLHHAEKIM 177
Cdd:cd03290 172 DIHLSDHLM 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-171 |
6.59e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 5 SGLGISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIgeHSITELSIAELARYR 84
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--LGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 -AVLVQSQELSVPFTSRE-VIDFGRNpWGCPNEELLAEVIAECDVAHL---LDREVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:PRK13536 116 iGVVPQFDNLDLEFTVREnLLVFGRY-FGMSTREIEAVIPSLLEFARLeskADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170
....*....|..
gi 1093464499 160 LLDEPTAALDLH 171
Cdd:PRK13536 195 ILDEPTTGLDPH 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-180 |
7.09e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR----AVLVQSQELSVPFT 98
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnqklGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVIDF----GRNPWGCPNEELLaEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAE 174
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRAL-EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
....*.
gi 1093464499 175 KIMGMM 180
Cdd:PRK11629 183 SIFQLL 188
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-236 |
7.48e-15 |
|
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: 71.42 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 31 AEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSItelsiAELARYRAVLVQSQELS--VPFTSREVIDFGR- 107
Cdd:TIGR03771 3 ADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASP-----GKGWRHIGYVPQRHEFAwdFPISVAHTVMSGRt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 108 ---NPWGCPNEELLAEVIAECD---VAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMMR 181
Cdd:TIGR03771 78 ghiGWLRRPCVADFAAVRDALRrvgLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1093464499 182 ARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVkQGPPAETLDAQTVSEVYGI 236
Cdd:TIGR03771 158 ELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIA-DGTPQQLQDPAPWMTTFGV 211
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
9-180 |
8.36e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV 88
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVP-FTSREVIDFGRnPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAA 167
Cdd:PRK15439 92 PQEPLLFPnLSVKENILFGL-PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170
....*....|...
gi 1093464499 168 LDLHHAEKIMGMM 180
Cdd:PRK15439 171 LTPAETERLFSRI 183
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-177 |
9.22e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.06 E-value: 9.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 18 LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAE---LARYRAVLVQSQELs 94
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 95 vpFTSREVIDFGRNPW---GCPNEELLAEVIAECDVAHLLD--REVPT-LSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:PRK10908 91 --LMDRTVYDNVAIPLiiaGASGDDIRRRVSAALDKVGLLDkaKNFPIqLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
....*....
gi 1093464499 169 DLHHAEKIM 177
Cdd:PRK10908 169 DDALSEGIL 177
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-169 |
9.91e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.45 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 11 ADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGehsiTELSIAELARYRAVL--- 87
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHRAELdpe 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 --VQ------SQELSVPFTSREVI----DF------GRNPwgcpneellaeviaecdvahlldreVPTLSGGERARVHSA 149
Cdd:PRK11147 398 ktVMdnlaegKQEVMVNGRPRHVLgylqDFlfhpkrAMTP-------------------------VKALSGGERNRLLLA 452
|
170 180
....*....|....*....|
gi 1093464499 150 RVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLD 472
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-169 |
1.53e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAAL-------SGDHELSGGDVRIGEHsITELSIAELA 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKT-PSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQELSVPFTSRE-VIDFGRNPWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTP 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQnLIEAPCRVLGLSKDQALAraeKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170
....*....|..
gi 1093464499 158 VVLLDEPTAALD 169
Cdd:PRK11124 162 VLLFDEPTAALD 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-169 |
1.60e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.88 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAElaryRAVLV 88
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AE----RGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELsVPFtsREVID---FGRNPWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:PRK11248 77 QNEGL-LPW--RNVQDnvaFGLQLAGVEKMQRLEiahQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
....*..
gi 1093464499 163 EPTAALD 169
Cdd:PRK11248 154 EPFGALD 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-170 |
2.02e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAalsgdhelsggdVRIGEHSITELSIAELARYRAVLV 88
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVR------------VVLGLVAPDEGVIKRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQ---ELSVPFTsreVIDFGRNPWGCPNEELLAeVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:PRK09544 73 PQKlylDTTLPLT---VNRFLRLRPGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
....*
gi 1093464499 166 AALDL 170
Cdd:PRK09544 149 QGVDV 153
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-238 |
2.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELS----IAELARYRAVLVQSQELSV-P 96
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPESQLfE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 97 FTSREVIDFGRNPWGCPNEE---LLAEVIAECDVAHLLDREVP-TLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHH 172
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKaekIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093464499 173 AEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGIGV 238
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGV 245
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-169 |
2.87e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 70.45 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG-----GDVRIGEHSI--TELSIAELa 81
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveGEILLDGEDIydPDVDVVEL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQelSVPF-TS-REVIDFGRNPWGCPNEELLAEVIAEC--------DVAHLLDREVPTLSGGERARVHSARV 151
Cdd:COG1117 91 RRRVGMVFQK--PNPFpKSiYDNVAYGLRLHGIKSKSELDEIVEESlrkaalwdEVKDRLKKSALGLSGGQQQRLCIARA 168
|
170
....*....|....*...
gi 1093464499 152 FYQDTPVVLLDEPTAALD 169
Cdd:COG1117 169 LAVEPEVLLMDEPTSALD 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-169 |
2.88e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.52 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAElARYRAVLV 88
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AE-NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQELSVPFTSREVIDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEItprVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
....
gi 1093464499 166 AALD 169
Cdd:PRK09452 173 SALD 176
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-177 |
3.36e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 1 MEIHSGLGISADNVSI-TLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHElsgGDVRIGEHSITELSI 77
Cdd:PRK11174 342 LASNDPVTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflPYQ---GSLKINGIELRELDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 78 AELARYRAVLVQSQELsVPFTSREVIDFGRnpwgcPN--EELLAEVIAECDV-------AHLLDREV----PTLSGGERA 144
Cdd:PRK11174 419 ESWRKHLSWVGQNPQL-PHGTLRDNVLLGN-----PDasDEQLQQALENAWVseflpllPQGLDTPIgdqaAGLSVGQAQ 492
|
170 180 190
....*....|....*....|....*....|...
gi 1093464499 145 RVHSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-169 |
4.62e-14 |
|
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: 68.83 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLG----GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG---GDVRIGEHSITElsIAELA 81
Cdd:cd03233 4 LSWRNISFTTGkgrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKE--FAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQELSVP-FTSREVIDFGRNPWGcpneellaeviaecdvahllDREVPTLSGGERARVHSARVFYQDTPVVL 160
Cdd:cd03233 82 PGEIIYVSEEDVHFPtLTVRETLDFALRCKG--------------------NEFVRGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 1093464499 161 LDEPTAALD 169
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-176 |
4.70e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV----QSQELSVPFT 98
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVgfvfQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVIDFG---RNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEK 175
Cdd:PRK10584 105 ALENVELPallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
.
gi 1093464499 176 I 176
Cdd:PRK10584 185 I 185
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-169 |
6.10e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 7 LGISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHS------ITELSIAEL 80
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 81 ARYRAVLVQSQELSVPFTSRE-VIDFGRNPWGCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMEnLIEAPCKVLGLSKEQAREkamKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:COG4161 161 QVLLFDEPTAALD 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-169 |
6.12e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 31 AEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQELSVPFTSREVIDFGRNPW 110
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIGLGLNPG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093464499 111 GCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK10771 100 LKLNAAqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-177 |
7.72e-14 |
|
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: 68.67 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSqelsvPF----TSREVID-FGRnpwgCPNEEL--------LAEVIAEcdVAHLLDREVPT----LSGGERARVHSA 149
Cdd:cd03244 83 IPQD-----PVlfsgTIRSNLDpFGE----YSDEELwqalervgLKEFVES--LPGGLDTVVEEggenLSVGQRQLLCLA 151
|
170 180
....*....|....*....|....*...
gi 1093464499 150 RVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQ 179
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
9-180 |
1.05e-13 |
|
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: 67.18 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLG-GHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSitelsiaelaryrAVL 87
Cdd:cd03223 1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-------------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTS-REVIDFgrnPWGcpneellaeviaecDVahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTA 166
Cdd:cd03223 68 FLPQRPYLPLGTlREQLIY---PWD--------------DV----------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170
....*....|....
gi 1093464499 167 ALDLHHAEKIMGMM 180
Cdd:cd03223 121 ALDEESEDRLYQLL 134
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
13-169 |
1.08e-13 |
|
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: 68.44 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDH--ELSGGDVRIGEHSITELSIAELARyRAVLVQS 90
Cdd:TIGR01978 5 DLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPsyEVTSGTILFKGQDLLELEPDERAR-AGLFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 Q-ELSVPFTS-----REVIDFGRNPWGCPN------EELLAEVIAECD-VAHLLDREVPT-LSGGERARVHSARVFYQDT 156
Cdd:TIGR01978 84 QyPEEIPGVSnleflRSALNARRSARGEEPldlldfEKLLKEKLALLDmDEEFLNRSVNEgFSGGEKKRNEILQMALLEP 163
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:TIGR01978 164 KLAILDEIDSGLD 176
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-169 |
1.36e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSI--------TELSIAEL 80
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 81 ARYRAVLVQSQELsvpFTSREVID-FGRNPW---GCPNEELLA---EVIAECDVAHLLDREVPTLSGGERARVHSARVFY 153
Cdd:PRK11264 84 RQHVGFVFQNFNL---FPHRTVLEnIIEGPVivkGEPKEEATArarELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170
....*....|....*.
gi 1093464499 154 QDTPVVLLDEPTAALD 169
Cdd:PRK11264 161 MRPEVILFDEPTSALD 176
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-169 |
1.44e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELS-VPFTSREV 102
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDNQfVGATVQDD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13635 103 VAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-223 |
1.66e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 7 LGISADNVSITLGG-----HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELS----I 77
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 78 AELARYRAVLVQSQElSVPF--TSREVIDFGRNPWGCPNEEllAEVIAECDVA------HLLDREVPTLSGGERARVHSA 149
Cdd:PRK13649 81 KQIRKKVGLVFQFPE-SQLFeeTVLKDVAFGPQNFGVSQEE--AEALAREKLAlvgiseSLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093464499 150 RVFYQDTPVVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-169 |
1.81e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQE 92
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 93 LSVPFTSREVIDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEERkqrVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-169 |
1.85e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.66 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGG--HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpF--TSREVIDFGRNpwgcpNEELLAEVIAECDVAHL------LDREVPT--------LSGGERARVHSAR 150
Cdd:PRK11176 422 VSQNVHL---FndTIANNIAYART-----EQYSREQIEEAARMAYAmdfinkMDNGLDTvigengvlLSGGQRQRIAIAR 493
|
170
....*....|....*....
gi 1093464499 151 VFYQDTPVVLLDEPTAALD 169
Cdd:PRK11176 494 ALLRDSPILILDEATSALD 512
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-176 |
2.18e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIaelARYRAVLVQSQ 91
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELSVPF--TSREVIDFgrnPWGC----PNEELLAEVIAECDVA-HLLDREVPTLSGGERARVHSARVFyQDTP-VVLLDE 163
Cdd:PRK10247 88 QTPTLFgdTVYDNLIF---PWQIrnqqPDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNL-QFMPkVLLLDE 163
|
170
....*....|...
gi 1093464499 164 PTAALDLHHAEKI 176
Cdd:PRK10247 164 ITSALDESNKHNV 176
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-180 |
4.14e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 11 ADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSiAELARYRAVLVQS 90
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSVPFTSREVIDFGRNPWGcpnEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:cd03231 82 PGIKTTLSVLENLRFWHADHS---DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 1093464499 171 HHAEKIMGMM 180
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-240 |
4.33e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELS-VPFTSREV 102
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFGRNPWGCPNEELLAEVIAECDVAHLLD---REVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGM 179
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDfktREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093464499 180 MRARAAAGKAVVVVL-HDLSAAAAyADHVVVVAQGHVVKQGPPAETLdaQTVSEVYGIGVEV 240
Cdd:PRK13642 183 IHEIKEKYQLTVLSItHDLDEAAS-SDRILVMKAGEIIKEAAPSELF--ATSEDMVEIGLDV 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-169 |
5.08e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGK-----VTALVGPNGAGKSTLLAALSGDHELSGGDVrigehsITELSIAELARYravLVQSQELSV-PF 97
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKISYKPQY---IKPDYDGTVeDL 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093464499 98 TSREVIDFGRNPWgcpneelLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13409 421 LRSITDDLGSSYY-------KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-180 |
5.98e-13 |
|
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: 66.36 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELsVPFTSREV 102
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL-FNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFGRNpwGCPNEELLAevIAECDVAHLLDREVP------------TLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:cd03252 96 IALADP--GMSMERVIE--AAKLAGAHDFISELPegydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170
....*....|
gi 1093464499 171 HHAEKIMGMM 180
Cdd:cd03252 172 ESEHAIMRNM 181
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-169 |
9.38e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElsIAELARYRAVLVQSQE 92
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 93 LSVPFTSREVIDFGRNPWGCPNEELLAEVIAECDVAHLLD---REVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-169 |
2.72e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.96 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGK-----VTALVGPNGAGKSTLLAALSGDHELSGGDVrigehsITELSIAELARYravLVQSQELSVPFT 98
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKISYKPQY---ISPDYDGTVEEF 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093464499 99 SREVI--DFGRNPWgcpneelLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG1245 422 LRSANtdDFGSSYY-------KTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-180 |
3.28e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELS-----GGDVRIGEHSITELSIAELaRY 83
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIEL-RR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQELSVPFTS-REVIDFGR--NPWGCPNEELLAEVIAECDVAHL-------LDREVPTLSGGERARVHSARVFY 153
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSiFENVALGLklNRLVKSKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALA 162
|
170 180
....*....|....*....|....*..
gi 1093464499 154 QDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLF 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-169 |
3.88e-12 |
|
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: 63.45 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIA-------ELA 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpeERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQelsvpftsreVIDFGRnPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:cd03269 81 LYPKMKVIDQ----------LVYLAQ-LKGLKKEEARRRIdewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170
....*....|.
gi 1093464499 159 VLLDEPTAALD 169
Cdd:cd03269 150 LILDEPFSGLD 160
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-169 |
4.46e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 6 GLGISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG--GDVRIGEHSITElsiaELARY 83
Cdd:PLN03211 66 GHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQELSVPFTSREVIDFG---RNPWGCPNEE--LLAE-VIAE-----CDVAHLLDREVPTLSGGERARVHSARVF 152
Cdd:PLN03211 142 TGFVTQDDILYPHLTVRETLVFCsllRLPKSLTKQEkiLVAEsVISElgltkCENTIIGNSFIRGISGGERKRVSIAHEM 221
|
170
....*....|....*..
gi 1093464499 153 YQDTPVVLLDEPTAALD 169
Cdd:PLN03211 222 LINPSLLILDEPTSGLD 238
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-223 |
5.04e-12 |
|
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: 64.75 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRIlnDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELS--IAELARYRAVLVQS 90
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSV--PFTSREVIDFGRnpWGCPNEELL---AEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:TIGR02142 82 QEARLfpHLSVRGNLRYGM--KRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 166 AALDLHHAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVsHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-168 |
5.59e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 33 PGKVTALVGPNGAGKSTLLAALSGDHELSGGDVR-IGE------------------HS----ITELSIAE---LARyrav 86
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKevtfngpkssqeagigiiHQelnlIPQLTIAEnifLGR---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 lvqsqelsvPFTSRevidFGRNPWGCPNEE---LLAEViaecDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:PRK10762 105 ---------EFVNR----FGRIDWKKMYAEadkLLARL----NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
....*
gi 1093464499 164 PTAAL 168
Cdd:PRK10762 168 PTDAL 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-169 |
6.26e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.42 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElSIAELARYRAVLVQSQELSVPFTSREVI 103
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 104 DFGRNPWGCPNEELlaEVIAECDVAHL-----LDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:TIGR01257 2034 YLYARLRGVPAEEI--EKVANWSIQSLglslyADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-168 |
6.31e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAELARYRAVLVQs 90
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELQASNIRDTERAGIAIIH- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELS-VP--------FTSREVIDFGRNPW-----GCpnEELLAEVIAECDVAhlldREVPTLSGGERARVHSARVFYQDT 156
Cdd:PRK13549 89 QELAlVKelsvleniFLGNEITPGGIMDYdamylRA--QKLLAQLKLDINPA----TPVGNLGLGQQQLVEIAKALNKQA 162
|
170
....*....|..
gi 1093464499 157 PVVLLDEPTAAL 168
Cdd:PRK13549 163 RLLILDEPTASL 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-170 |
7.13e-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: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRigeHSitelsiaelarYRAVLVQSQELSVPFTSREV 102
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK---HS-----------GRISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093464499 103 IDFGRN---------PWGCPNEELLAeVIAECDVAHLLDREVpTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:TIGR01271 507 IIFGLSydeyrytsvIKACQLEEDIA-LFPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-176 |
7.81e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.57 E-value: 7.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG-DHELSG-----GDVRIG----------EHSITELSIAELAR 82
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKDFNGearpqPGIKVGylpqepqldpTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 YRAVLVQSQELSVPFtSREVIDFgrnpwgcpnEELLAE------VIAECDvAHLLDRE----------------VPTLSG 140
Cdd:TIGR03719 96 IKDALDRFNEISAKY-AEPDADF---------DKLAAEqaelqeIIDAAD-AWDLDSQleiamdalrcppwdadVTKLSG 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1093464499 141 GERARVHSARVFYQDTPVVLLDEPTAALDlhhAEKI 176
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD---AESV 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-177 |
8.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHR--ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG---DHELSGGDVRIGEHSITELSIAELARY 83
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQELS-VPFTSREVIDFGRNPWGCPNEELL---AEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:PRK13640 86 VGIVFQNPDNQfVGATVGDDVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170
....*....|....*...
gi 1093464499 160 LLDEPTAALDLHHAEKIM 177
Cdd:PRK13640 166 ILDESTSMLDPAGKEQIL 183
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-169 |
1.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.53 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITE--LSIAELARYRAVLVQSQELSVpF--TS 99
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPEYQL-FeeTI 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093464499 100 REVIDFGRNPWGCPNEELLAEV-----IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVkramnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-180 |
1.58e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.97 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR----AVLVQSQELSVPFT 98
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRrehfGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVIDFGRNPWGCPNEELLAEVIAECDVAHLLDR---EVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEK 175
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
....*
gi 1093464499 176 IMGMM 180
Cdd:PRK10535 183 VMAIL 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
32-170 |
1.85e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 32 EPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElsiAELARYRAVLVQSQELSVPFTSREVIDFGRNPWG 111
Cdd:PRK13543 35 DAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 112 CPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:PRK13543 112 RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-176 |
2.12e-11 |
|
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: 63.81 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIgehsitELSIAELARyrAVLVQSQELsvpftsREVI 103
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------KGSVAYVPQ--QAWIQNDSL------RENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 104 DFGrnpwgCP-NEELLAEVIAECdvAHLLDREV-PT------------LSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:TIGR00957 720 LFG-----KAlNEKYYQQVLEAC--ALLPDLEIlPSgdrteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
....*..
gi 1093464499 170 LHHAEKI 176
Cdd:TIGR00957 793 AHVGKHI 799
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-180 |
2.39e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRI-GEhsitELSIAELARYRA-- 85
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGK----PVRIRSPRDAIAlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 86 --------VLVQsqelsvPFTSREVIDFGRNPWGCPN------EELLAEVIAECDVAHLLDREVPTLSGGERARVHSARV 151
Cdd:COG3845 82 igmvhqhfMLVP------NLTVAENIVLGLEPTKGGRldrkaaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180
....*....|....*....|....*....
gi 1093464499 152 FYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEIL 184
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-176 |
3.57e-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: 61.80 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 16 ITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRigeHSitelsiaelarYRAVLVQSQELSV 95
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK---HS-----------GRISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 96 PFTSREVIDFGRNPwgcpNEELLAEVIAEC----DVAHLLDREVP-------TLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:cd03291 111 PGTIKENIIFGVSY----DEYRYKSVVKACqleeDITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170
....*....|..
gi 1093464499 165 TAALDLHHAEKI 176
Cdd:cd03291 187 FGYLDVFTEKEI 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-180 |
3.84e-11 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 60.07 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 15 SITLGGHRIL---NDISVVaePGKVTALVGPNGAGKSTLLAALS------GDHELSGGDVRIGEHSitelsiaelARYRA 85
Cdd:cd03227 1 KIVLGRFPSYfvpNDVTFG--EGSLTIITGPNGSGKSTILDAIGlalggaQSATRRRSGVKAGCIV---------AAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 86 VLVQSqelsvpftsrevidfgrnpwgcpneellaeviaecdvahlldreVPTLSGGERARVHSARVF----YQDTPVVLL 161
Cdd:cd03227 70 ELIFT--------------------------------------------RLQLSGGEKELSALALILalasLKPRPLYIL 105
|
170
....*....|....*....
gi 1093464499 162 DEPTAALDLHHAEKIMGMM 180
Cdd:cd03227 106 DEIDRGLDPRDGQALAEAI 124
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-170 |
4.72e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQ-SQ---ELSVpfts 99
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVFGQrSQlwwDLPA---- 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093464499 100 REVIDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:COG4586 114 IDSFRLLKAIYRIPDAEYkkrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-247 |
4.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG-DHELSG----GDVRIGEHSITEL-SIAELA 81
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSGyrysGDVLLGGRSIFNYrDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQElSVPFTSREVIDFG-RNPWGCPNEEL-------LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFY 153
Cdd:PRK14271 101 RRVGMLFQRPN-PFPMSIMDNVLAGvRAHKLVPRKEFrgvaqarLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 154 QDTPVVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVlHDLSAAAAYADHVVVVAQGHVVKQGPPAETLD----AQT 229
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVT-HNLAQAARISDRAALFFDGRLVEEGPTEQLFSspkhAET 258
|
250
....*....|....*...
gi 1093464499 230 VSEVYGIGVEVLRDSAGN 247
Cdd:PRK14271 259 ARYVAGLSGDVKDAKRGN 276
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-169 |
5.41e-11 |
|
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: 61.12 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRavlvqSQELSVPFTS---- 99
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELR-----RKKISMVFQSfall 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093464499 100 --REVID---FGRNPWGCPNEELL---AEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:cd03294 115 phRTVLEnvaFGLEVQGVPRAEREeraAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-225 |
5.52e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALS-------GDHELSGGDVRIGEHSITELSIAE-----LARYRAV 86
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpseGSIVVNGQTINLVRDKDGQLKVADknqlrLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LV-QSQELSVPFTSRE-VIDFGRNPWGCPNEELLAEVIAECDVAHLLDR---EVPT-LSGGERARVHSARVFYQDTPVVL 160
Cdd:PRK10619 96 MVfQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaqgKYPVhLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093464499 161 LDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETL 225
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-169 |
7.52e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 6 GLGISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElsIAELARyra 85
Cdd:PRK11247 10 GTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 86 VLVQSQELsVPFTSreVID---FG-RNPWGCPNEELLAEViaecdvaHLLDR--EVP-TLSGGERARVHSARVFYQDTPV 158
Cdd:PRK11247 85 LMFQDARL-LPWKK--VIDnvgLGlKGQWRDAALQALAAV-------GLADRanEWPaALSGGQKQRVALARALIHRPGL 154
|
170
....*....|.
gi 1093464499 159 VLLDEPTAALD 169
Cdd:PRK11247 155 LLLDEPLGALD 165
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-170 |
7.91e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.46 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 29 VVAEPGKVTALVGPNGAGKSTLLAALSG---------DHELSGGDVrigehsITELSIAELARYRAVLVQsQELSVPFTS 99
Cdd:cd03236 21 PVPREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfDDPPDWDEI------LDEFRGSELQNYFTKLLE-GDVKVIVKP 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 100 REVIDFGRNPWGCPNEEL--------LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:cd03236 94 QYVDLIPKAVKGKVGELLkkkdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-169 |
8.48e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELS-VPFTSRE 101
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNQfIGATVED 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 102 VIDFG-RNPWGCPNE--ELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13632 104 DIAFGlENKKVPPKKmkDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-169 |
1.17e-10 |
|
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: 61.34 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 30 VAEPGKVTALVGPNGAGKSTLLAALSG---------DHELSGGDVrIGEHSITEL-----SIAElARYRAVL-VQSQEL- 93
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGelkpnlgdyDEEPSWDEV-LKRFRGTELqdyfkKLAN-GEIKVAHkPQYVDLi 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093464499 94 --SVPFTSREVIDfgrnpwGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG1245 173 pkVFKGTVRELLE------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-169 |
1.27e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSIT-LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRYRAVL 87
Cdd:PRK10790 341 IDIDNVSFAyRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL-RQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGRNpwgcPNEELLAEVIAECDVAHLLdREVP------------TLSGGERARVHSARVFYQD 155
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELA-RSLPdglytplgeqgnNLSVGQKQLLALARVLVQT 494
|
170
....*....|....
gi 1093464499 156 TPVVLLDEPTAALD 169
Cdd:PRK10790 495 PQILILDEATANID 508
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-169 |
1.29e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 30 VAEPGKVTALVGPNGAGKSTLLAALSG---------DHELSGGDVrIGEHSITELS--IAELA--RYRAVL-VQSQEL-- 93
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGelipnlgdyEEEPSWDEV-LKRFRGTELQnyFKKLYngEIKVVHkPQYVDLip 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1093464499 94 -SVPFTSREVIDfgRNpwgcpNEE-LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13409 174 kVFKGKVRELLK--KV-----DERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-176 |
1.65e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.67 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG-----GDVRIGEHSITE--LSIAEL 80
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 81 ARyRAVLVQSQELSVPFTSREVIDFGRNPWGC-PNEEL---LAEVIAECD----VAHLLDREVPTLSGGERARVHSARVF 152
Cdd:PRK14258 87 RR-QVSMVHPKPNLFPMSVYDNVAYGVKIVGWrPKLEIddiVESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180
....*....|....*....|....
gi 1093464499 153 YQDTPVVLLDEPTAALDLHHAEKI 176
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKV 189
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-177 |
1.70e-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: 58.79 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 14 VSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELS--GGDVRIGEHSITElsiaELARYRAvLVQSQ 91
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQRSTG-YVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELSVPF-TSREVIDFGRNPWGcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:cd03232 88 DVHSPNlTVREALRFSALLRG--------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
....*..
gi 1093464499 171 HHAEKIM 177
Cdd:cd03232 142 QAAYNIV 148
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-169 |
2.24e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQELSVPFT 98
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNYALYPHMS 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093464499 99 SREVIDFGRNPWGCPNEElLAEVIAEC----DVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11650 93 VRENMAYGLKIRGMPKAE-IEERVAEAarilELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-169 |
3.08e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.32 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL----GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR 84
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 85 ---AVLVQSQELsvpFTSREVIDfgrN---P---WGCPNEEllaevIAEcDVAHLLDReV---------PT-LSGGERAR 145
Cdd:COG1135 82 rkiGMIFQHFNL---LSSRTVAE---NvalPleiAGVPKAE-----IRK-RVAELLEL-VglsdkadayPSqLSGGQKQR 148
|
170 180
....*....|....*....|....
gi 1093464499 146 VHSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALD 172
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-177 |
3.97e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.73 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSqelsvPFTSR 100
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-----PFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 101 EVIdfGRN-PWGCPN---EEL-----LAEViaECDVAHL---LDREVP----TLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:PRK10789 403 DTV--ANNiALGRPDatqQEIehvarLASV--HDDILRLpqgYDTEVGergvMLSGGQKQRISIARALLLNAEILILDDA 478
|
170
....*....|...
gi 1093464499 165 TAALDLHHAEKIM 177
Cdd:PRK10789 479 LSAVDGRTEHQIL 491
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-51 |
4.02e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.97 E-value: 4.02e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLL 51
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI 44
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-179 |
5.83e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGH-----RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITelsiAELARY 83
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP----ANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQELSVPF----------TSREVIDFGRNPWGCPNEELLAEVIAECDVAHL----LDREVPTLSGGERARVHSA 149
Cdd:PRK13645 83 KEVKRLRKEIGLVFqfpeyqlfqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALA 162
|
170 180 190
....*....|....*....|....*....|
gi 1093464499 150 RVFYQDTPVVLLDEPTAALDLHHAEKIMGM 179
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-169 |
6.07e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAElaRYRAVLVQSQELSVPF-- 97
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntDGFHIGVEGVITYDGITPEEIKK--HYRGDVVYNAETDVHFph 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 -TSREVIDFG---RNPWGCPN---EELLAEVIAECDVA-----HLLDREVPT-----LSGGERARVHSARVFYQDTPVVL 160
Cdd:TIGR00956 153 lTVGETLDFAarcKTPQNRPDgvsREEYAKHIADVYMAtyglsHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQC 232
|
....*....
gi 1093464499 161 LDEPTAALD 169
Cdd:TIGR00956 233 WDNATRGLD 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-170 |
7.14e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELSVPFTSREV-----IDFGRNPWGCPN------EELLAEVIAECDV-AHLLDREVPT-LSGGERARVHSARVFY 153
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFflqtaLNAVRSYRGQEPldrfdfQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAV 161
|
170
....*....|....*..
gi 1093464499 154 QDTPVVLLDEPTAALDL 170
Cdd:PRK09580 162 LEPELCILDESDSGLDI 178
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-177 |
8.26e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 38 ALVGPNGAGKSTLLAALSGDHELSGGDVrigehsitelsiAELARYR-AVLVQSQELSVPFTSREVIDFGRNPWGCPNEE 116
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTV------------FRSAKVRmAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQK 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 117 LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:PLN03073 607 LRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALI 667
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-145 |
8.90e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.40 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRI------------GEHSitELSIAELARYRAVLv 88
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVngrvsallelgaGFHP--ELTGRENIYLNGRL- 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1093464499 89 qsqeLSVpftSREVIDfgrnpwgcpneELLAEVIAECDVAHLLDREVPTLSGGERAR 145
Cdd:COG1134 116 ----LGL---SRKEID-----------EKFDEIVEFAELGDFIDQPVKTYSSGMRAR 154
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-223 |
8.91e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGE---HSITELSIAELARYRAVLV----QSQ-- 91
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIRPVRKRIGMVfqfpESQlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 92 ELSVpftSREVIdFGRNPWGCPNEE-------LLAEVIAECDVahlLDREVPTLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:PRK13646 100 EDTV---EREII-FGPKNFKMNLDEvknyahrLLMDLGFSRDV---MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 165 TAALDLHHAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYADHVVVVAQGHVVKQGPPAE 223
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVsHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-169 |
1.09e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.28 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 14 VSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGD--VRIGEHSI--TELSIAELAR---YRAV 86
Cdd:TIGR03269 290 ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVdmTKPGPDGRGRakrYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsvpFTSREVIDFGRNPWGC--PNE--------ELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:TIGR03269 370 LHQEYDL---YPHRTVLDNLTEAIGLelPDElarmkaviTLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEP 446
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:TIGR03269 447 RIVILDEPTGTMD 459
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-171 |
1.38e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLA-----ALSG----------DHELSGGDVRIGEHSI- 72
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGipkncqilhvEQEVVGDDTTALQCVLn 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 73 TELSIAELARYRAVLVQSQElSVPFTSREVIDFGRNPWGC---PNEELLAEVI----------AECDVAHLL-------- 131
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQR-ELEFETETGKGKGANKDGVdkdAVSQRLEEIYkrlelidaytAEARAASILaglsftpe 336
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1093464499 132 --DREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:PLN03073 337 mqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-174 |
1.86e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHR-ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG-DHELSG-----GDVRIG----------EHSITEL 75
Cdd:PRK11819 11 RVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKEFEGearpaPGIKVGylpqepqldpEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 76 SIAELARYRAVLVQSQELSVPFtSREVIDFgrnpwgcpnEELLAE------VIAECDvAHLLDRE--------------- 134
Cdd:PRK11819 91 VEEGVAEVKAALDRFNEIYAAY-AEPDADF---------DALAAEqgelqeIIDAAD-AWDLDSQleiamdalrcppwda 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1093464499 135 -VPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDlhhAE 174
Cdd:PRK11819 160 kVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AE 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-170 |
2.09e-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: 57.65 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELaRYRAVLVQSQELSVPFTSREV 102
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDfgrnPWGCPNEEllaEVIAECDVAHL----------LDREVP----TLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:TIGR00957 1380 LD----PFSQYSDE---EVWWALELAHLktfvsalpdkLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
..
gi 1093464499 169 DL 170
Cdd:TIGR00957 1453 DL 1454
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-180 |
2.79e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 14 VSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHE---LSGGDVRIGEHSITElSIAELARYravlVQS 90
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS-SFQRSIGY----VQQ 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSVP-FTSREVIDFG---RNPWGCPNEE---LLAEVIAECDVAHLLDREVPT----LSGGERARVhSARVFYQDTP-- 157
Cdd:TIGR00956 844 QDLHLPtSTVRESLRFSaylRQPKSVSKSEkmeYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRL-TIGVELVAKPkl 922
|
170 180
....*....|....*....|...
gi 1093464499 158 VVLLDEPTAALDLHHAEKIMGMM 180
Cdd:TIGR00956 923 LLFLDEPTSGLDSQTAWSICKLM 945
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-236 |
2.97e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.17 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSI--TELSIAELARYRAVLVQSQELSVPFTSR 100
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 101 EV-IDFGRNPWGCPNEEL---LAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKI 176
Cdd:PRK13638 96 DSdIAFSLRNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 177 MGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLDAQTVSEVYGI 236
Cdd:PRK13638 176 IAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-169 |
3.18e-09 |
|
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: 55.55 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAelaryRAVLVQSQELSVPFTSREVI 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-----RMVVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 104 DFG-----RNPWGCPNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:TIGR01184 76 ALAvdrvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-169 |
3.78e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGdhELSGGDVRiGEHSITELSIaelaryravlvqSQELSvpftsr 100
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVA-GCVDVPDNQF------------GREAS------ 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093464499 101 eVID-FGRNpwGCPNE--ELLAEV-IAEcdvAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG2401 102 -LIDaIGRK--GDFKDavELLNAVgLSD---AVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-180 |
4.19e-09 |
|
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: 56.95 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 35 KVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSItELSIAELARYRAVLVQSQELSVPFTSREVIDFGRNPWGCPN 114
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 115 EELLAEVIA---ECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:TIGR01257 1036 EEAQLEMEAmleDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-169 |
5.64e-09 |
|
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: 55.44 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL----GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHE---LSGGDVRIGEHSITELSIAELA 81
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQ--SQElsvPFTS-----------REVIDFGRnpwGCPNEELLAEVIAecdvahLLDR-EVPT---------- 137
Cdd:COG0444 82 KIRGREIQmiFQD---PMTSlnpvmtvgdqiAEPLRIHG---GLSKAEARERAIE------LLERvGLPDperrldryph 149
|
170 180 190
....*....|....*....|....*....|...
gi 1093464499 138 -LSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:COG0444 150 eLSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-164 |
6.28e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.16 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAEL--ARYR-AVLVQ 89
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRmSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 SQELsvpFTSREVIDFGRNPW----GCPNEELLAEVIAECD------VAHLLDREvptLSGGERARVHSARVFYQDTPVV 159
Cdd:PRK11831 92 SGAL---FTDMNVFDNVAYPLrehtQLPAPLLHSTVMMKLEavglrgAAKLMPSE---LSGGMARRAALARAIALEPDLI 165
|
....*
gi 1093464499 160 LLDEP 164
Cdd:PRK11831 166 MFDEP 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-169 |
6.40e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSQELS-VPFTS 99
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQfVGATV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093464499 100 REVIDFGRNPWGCPNEELLAEVIAECDVAHLLD---REVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDfkeREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-169 |
6.62e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.00 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV-- 86
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 ----------------LV-QSQELSVPFTS------------REVIDFGRNpWgcpneellAEVIAECDVAhllDREVPT 137
Cdd:PRK11300 86 fqhvrlfremtvienlLVaQHQQLKTGLFSgllktpafrraeSEALDRAAT-W--------LERVGLLEHA---NRQAGN 153
|
170 180 190
....*....|....*....|....*....|..
gi 1093464499 138 LSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-168 |
6.82e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAElARYRAVLVQSQE 92
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE-ALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 93 LSVpFTSREVID---FGRNP---WGCPNEELLAEVIA---ECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:PRK10982 82 LNL-VLQRSVMDnmwLGRYPtkgMFVDQDKMYRDTKAifdELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
....*
gi 1093464499 164 PTAAL 168
Cdd:PRK10982 161 PTSSL 165
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-170 |
6.90e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSqelsvPFTSREV 102
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFGRNPWGCPNEELLAEVIAEcdvAHL----------LDREV----PTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEALER---AHIkdvidrnpfgLDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
..
gi 1093464499 169 DL 170
Cdd:PLN03232 1403 DV 1404
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-175 |
8.44e-09 |
|
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: 54.46 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIgehsitelsiaeLARYRAVLvqsqELSVPF- 97
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV------------RGRVSSLL----GLGGGFn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 ---TSREVIDFGRNPWGCPNEE---LLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:cd03220 97 pelTGRENIYLNGRLLGLSRKEideKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
....
gi 1093464499 172 HAEK 175
Cdd:cd03220 177 FQEK 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-168 |
8.64e-09 |
|
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: 55.60 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAELARYRAVLVQS 90
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSVP-FTSREVIDFGRN---PWGCPN--------EELLAEV-IAECDVAhlldREVPTLSGGERARVHSARVFYQDTP 157
Cdd:TIGR02633 86 ELTLVPeLSVAENIFLGNEitlPGGRMAynamylraKNLLRELqLDADNVT----RPVGDYGGGQQQLVEIAKALNKQAR 161
|
170
....*....|.
gi 1093464499 158 VVLLDEPTAAL 168
Cdd:TIGR02633 162 LLILDEPSSSL 172
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-169 |
1.24e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.74 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRavlvqsqelsvpftsREV- 102
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR---------------RRMq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFgRNPWGCPN-----EELLAEVI--------AECD--VAHLLDR-------------EvptLSGGERARVHSARVFYQ 154
Cdd:COG4608 99 MVF-QDPYASLNprmtvGDIIAEPLrihglaskAERRerVAELLELvglrpehadryphE---FSGGQRQRIGIARALAL 174
|
170
....*....|....*
gi 1093464499 155 DTPVVLLDEPTAALD 169
Cdd:COG4608 175 NPKLIVCDEPVSALD 189
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-176 |
1.72e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGdhelsggdvrigehsitELSIAELARY--RAVLVQSQELSVPF--TS 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVviRGSVAYVPQVSWIFnaTV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 100 REVIDFGRN-----PWGCPNEELLA---EVIAECDVAHLLDREVpTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLH 171
Cdd:PLN03232 696 RENILFGSDfeserYWRAIDVTALQhdlDLLPGRDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
....*
gi 1093464499 172 HAEKI 176
Cdd:PLN03232 775 VAHQV 779
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-168 |
1.77e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR-AVL 87
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAvAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGrnPWGCPNEELLAEVIAECDV-AHLLDREVP---TLSGGERARVHSARVFYQDTPVVLLDE 163
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMG--GFFAERDQFQERIKWVYELfPRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
....*
gi 1093464499 164 PTAAL 168
Cdd:PRK11614 164 PSLGL 168
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-205 |
2.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSIT-ELSIAELARYRavlvqsQELSVPF----- 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLR------KKVSLVFqfpea 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 -----TSREVIDFGRNPWGCPNEEL-------LAEVIAECDVAhllDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:PRK13641 97 qlfenTVLKDVEFGPKNFGFSEDEAkekalkwLKKVGLSEDLI---SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1093464499 166 AALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYAD 205
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYAD 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-169 |
2.40e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.63 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHEL-----SGGDVRIGEHSITELSIAELA-R 82
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDPVEvR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 YRAVLVQSQELSVPFTSREVIDFGR--NPWGCPNEELLAEVIAEC----DVAHLLDREVPTLSGGERARVHSARVFYQDT 156
Cdd:PRK14243 91 RRIGMVFQKPNPFPKSIYDNIAYGAriNGYKGDMDELVERSLRQAalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:PRK14243 171 EVILMDEPCSALD 183
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-169 |
2.73e-08 |
|
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: 53.32 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 14 VSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAA----LSGDhelsgGDVRIGEHSITELSIAELARYRAVLVQ 89
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrlLNTE-----GDIQIDGVSWNSVPLQKWRKAFGVIPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 SQEL-SVPFtsREVIDfgrnPWGCPNEELLAEVIAECDVAHLLDrEVP------------TLSGGERARVHSARVFYQDT 156
Cdd:cd03289 85 KVFIfSGTF--RKNLD----PYGKWSDEEIWKVAEEVGLKSVIE-QFPgqldfvlvdggcVLSHGHKQLMCLARSVLSKA 157
|
170
....*....|...
gi 1093464499 157 PVVLLDEPTAALD 169
Cdd:cd03289 158 KILLLDEPSAHLD 170
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
23-205 |
2.92e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 53.27 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARY-RAVLVQSQELSVPFTSRE 101
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrRDVQLVFQDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 102 VIdfgRNPWGCPNEEL--LAEVIAECDVAHLL----------DREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:TIGR02769 106 TV---RQIIGEPLRHLtsLDESEQKARIAELLdmvglrsedaDKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1093464499 170 LHHAEKIMGMMRARAAAGKAVVVVL-HDLSAAAAYAD 205
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFItHDLRLVQSFCQ 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-58 |
5.02e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 5.02e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDH 58
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH 310
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-175 |
5.10e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.84 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 36 VTALVGPNGAGKSTLL----AALSGDHELSGGDVRIGEHSITELSIaelaRYRAVLVQSQELSVPFTSREVIDFGRNPWG 111
Cdd:cd03240 24 LTLIVGQNGAGKTTIIealkYALTGELPPNSKGGAHDPKLIREGEV----RAQVKLAFENANGKKYTITRSLAILENVIF 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 112 CPNEELLAeviaecdvahLLDREVPTLSGGERA------RVHSARVFYQDTPVVLLDEPTAALDLHHAEK 175
Cdd:cd03240 100 CHQGESNW----------PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
9-169 |
6.68e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRI-GEhsitelsiaELARYRAVL 87
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGE---------PIRRQRDEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQS-----------QELsvpfTSREVIDFGRNPWGCPNEELLAEVIAEcdvAHLLDRE-VP--TLSGGERARVHSARVFY 153
Cdd:PRK13538 73 HQDllylghqpgikTEL----TALENLRFYQRLHGPGDDEALWEALAQ---VGLAGFEdVPvrQLSAGQQRRVALARLWL 145
|
170
....*....|....*.
gi 1093464499 154 QDTPVVLLDEPTAALD 169
Cdd:PRK13538 146 TRAPLWILDEPFTAID 161
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-226 |
1.08e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.96 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGghriLNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR----AVL 87
Cdd:PRK10070 36 EKTGLSLG----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrkkiAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 VQSQELSVPFTSREVIDFGRNPWGCPNEE-------LLAEVIAEcDVAHLLDREvptLSGGERARVHSARVFYQDTPVVL 160
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEErrekaldALRQVGLE-NYAHSYPDE---LSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1093464499 161 LDEPTAALD-LHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYADHVVVVAQGHVVKQGPPAETLD 226
Cdd:PRK10070 188 MDEAFSALDpLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-177 |
1.32e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITElsiaELARYravlvQSQELSVPFTSrev 102
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTY-----QKQLCFVGHRS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 idfGRNPWGCPNEELL------------AEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:PRK13540 84 ---GINPYLTLRENCLydihfspgavgiTELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
....*..
gi 1093464499 171 HHAEKIM 177
Cdd:PRK13540 161 LSLLTII 167
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
13-170 |
1.37e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDVRIGEHSITELSIAELARYRAVLVQS 90
Cdd:CHL00131 12 NLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSVPFTSREviDFGRNPW-------GCPNEELLA--EVIAE-CDV----AHLLDREV-PTLSGGERARVHSARVFYQD 155
Cdd:CHL00131 92 YPIEIPGVSNA--DFLRLAYnskrkfqGLPELDPLEflEIINEkLKLvgmdPSFLSRNVnEGFSGGEKKRNEILQMALLD 169
|
170
....*....|....*
gi 1093464499 156 TPVVLLDEPTAALDL 170
Cdd:CHL00131 170 SELAILDETDSGLDI 184
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-169 |
2.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLVQSqelSVPFTSreV 102
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA---PVLFSG--T 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 103 IDFGRNPWgcpNEELLAEVIAECDVAHL----------LDREVP----TLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:PLN03130 1329 VRFNLDPF---NEHNDADLWESLERAHLkdvirrnslgLDAEVSeageNFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
.
gi 1093464499 169 D 169
Cdd:PLN03130 1406 D 1406
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-176 |
2.25e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGD-HELSGGDVRIgehsitelsiaelaryRAVLVQSQELSVPF--TSR 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVI----------------RGTVAYVPQVSWIFnaTVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 101 EVIDFGrNPWGCPNEELLAEVIAecdVAHLLD------------REVpTLSGGERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:PLN03130 697 DNILFG-SPFDPERYERAIDVTA---LQHDLDllpggdlteigeRGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
....*...
gi 1093464499 169 DLHHAEKI 176
Cdd:PLN03130 772 DAHVGRQV 779
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-176 |
2.32e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.43 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEH------SITELSIAELARYRAVLVQSQElsvP 96
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN---P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 97 FTSREVIDFGRNPW---GCPNEELLAEVIAEC--------DVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:PRK14246 102 FPHLSIYDNIAYPLkshGIKEKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170
....*....|.
gi 1093464499 166 AALDLHHAEKI 176
Cdd:PRK14246 182 SMIDIVNSQAI 192
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-169 |
2.50e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 10 SADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAEL--ARYRAVL 87
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 88 vqsqelsvpftsrevidfgRNPWGC----PNEELLAEVIAECDV-------------------AHLLDR-EVP------- 136
Cdd:PRK11701 88 -------------------RTEWGFvhqhPRDGLRMQVSAGGNIgerlmavgarhygdirataGDWLERvEIDaariddl 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1093464499 137 --TLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11701 149 ptTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
8-168 |
2.64e-07 |
|
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: 51.29 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 8 GISADNVS-ITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGdvrigehsitELSIAELAR---- 82
Cdd:TIGR00954 451 GIKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG----------RLTKPAKGKlfyv 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 83 ----YRAVLVQSQELSVPFTSREVIDFGRNpwgcpnEELLAEVIAECDVAHLLDREV---------PTLSGGERARVHSA 149
Cdd:TIGR00954 521 pqrpYMTLGTLRDQIIYPDSSEDMKRRGLS------DKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMA 594
|
170
....*....|....*....
gi 1093464499 150 RVFYQDTPVVLLDEPTAAL 168
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAV 613
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-169 |
2.75e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 50.57 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRavlvqsQELSVPF------ 97
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR------RQIGMIFqhfnll 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 TSREVIDfgrnpwgcpN-------------------EELLAEViaecDVAHLLDREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:PRK11153 95 SSRTVFD---------NvalplelagtpkaeikarvTELLELV----GLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170
....*....|.
gi 1093464499 159 VLLDEPTAALD 169
Cdd:PRK11153 162 LLCDEATSALD 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-169 |
2.78e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRI-GEHSITELS----------- 76
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQqdpprnvegtv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 77 -------IAELA----RYRAVLVQ-SQELSVPFTSR-----EVIDFgRNPWGCPNEelLAEVIAECDvahlLDREVP--T 137
Cdd:PRK11147 84 ydfvaegIEEQAeylkRYHDISHLvETDPSEKNLNElaklqEQLDH-HNLWQLENR--INEVLAQLG----LDPDAAlsS 156
|
170 180 190
....*....|....*....|....*....|..
gi 1093464499 138 LSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-180 |
3.29e-07 |
|
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: 50.96 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG--DHELSGGDV-----------------RIGE 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 70 H------SITELSI-----AELARY---RAVLVQSQELSVPFTSREVIDF---GRNPWGCPNEELL---AEVIAECDVAH 129
Cdd:TIGR03269 81 PcpvcggTLEPEEVdfwnlSDKLRRrirKRIAIMLQRTFALYGDDTVLDNvleALEEIGYEGKEAVgraVDLIEMVQLSH 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 130 LLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNAL 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-170 |
3.39e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 13 NVSITLGGHRILNDISVvaePGK-VTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsitelsiaelaryraVLVQS- 90
Cdd:PRK11144 5 NFKQQLGDLCLTVNLTL---PAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---------------VLFDAe 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSVPFTSREV-IDF------------GRNPWGCPNE--ELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQD 155
Cdd:PRK11144 67 KGICLPPEKRRIgYVFqdarlfphykvrGNLRYGMAKSmvAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTA 146
|
170
....*....|....*
gi 1093464499 156 TPVVLLDEPTAALDL 170
Cdd:PRK11144 147 PELLLMDEPLASLDL 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-170 |
3.45e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 11 ADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsitelsiAELARYravlvqS 90
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-------ANIGYY------A 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 QELSVPF-TSREVIDFGRNpWGCPNEELLAeviaecdVAHLLDR----------EVPTLSGGERARVHSARVFYQDTPVV 159
Cdd:PRK15064 389 QDHAYDFeNDLTLFDWMSQ-WRQEGDDEQA-------VRGTLGRllfsqddikkSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|.
gi 1093464499 160 LLDEPTAALDL 170
Cdd:PRK15064 461 VMDEPTNHMDM 471
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-180 |
3.78e-07 |
|
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: 48.97 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 18 LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV----QSQEL 93
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVpedrKREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 94 SVPFTSREVIDFGRnpwgcpneellaeviaecdvahlldrevpTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHA 173
Cdd:cd03215 90 VLDLSVAENIALSS-----------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
....*..
gi 1093464499 174 EKIMGMM 180
Cdd:cd03215 141 AEIYRLI 147
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-171 |
4.30e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.69 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 19 GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYR----AVLVQSQELS 94
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRrdiqMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 95 VP-FTSREVI--------DFGRNPWGCPNEELLAEViaECDVAHLlDREVPTLSGGERARVHSARVFYQDTPVVLLDEPT 165
Cdd:PRK10419 103 NPrKTVREIIreplrhllSLDKAERLARASEMLRAV--DLDDSVL-DKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
....*.
gi 1093464499 166 AALDLH 171
Cdd:PRK10419 180 SNLDLV 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-170 |
4.57e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.96 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRavlvqsQELSVPFtsrevi 103
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR------QKIQIVF------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 104 dfgRNPWGCPN-----EELLAEVIA----------ECDVAHLL----------DREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:PRK11308 99 ---QNPYGSLNprkkvGQILEEPLLintslsaaerREKALAMMakvglrpehyDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170
....*....|..
gi 1093464499 159 VLLDEPTAALDL 170
Cdd:PRK11308 176 VVADEPVSALDV 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-169 |
5.01e-07 |
|
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: 50.07 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 17 TLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHElSGGDVRIGEHSITELSIAELARYRavlvqsQELSV- 95
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPLR------RRMQVv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 96 ---PFTS-------REVIDFG------------RnpwgcpnEELLAEVIAEcdVAhlLDREV----PT-LSGGERARVHS 148
Cdd:COG4172 368 fqdPFGSlsprmtvGQIIAEGlrvhgpglsaaeR-------RARVAEALEE--VG--LDPAArhryPHeFSGGQRQRIAI 436
|
170 180
....*....|....*....|.
gi 1093464499 149 ARVFYQDTPVVLLDEPTAALD 169
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALD 457
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-170 |
5.73e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 12 DNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTL-------LAALSGDHELSGGdVRIG---EHSITELSIAELA 81
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLikllageLAPVSGEIGLAKG-IKLGyfaQHQLEFLRADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 82 RYRAVLVQSQElsvpfTSREVID----FGRNpwgcpneellAEVIAEcdvahlldrEVPTLSGGERARVHSARVFYQDTP 157
Cdd:PRK10636 395 LQHLARLAPQE-----LEQKLRDylggFGFQ----------GDKVTE---------ETRRFSGGEKARLVLALIVWQRPN 450
|
170
....*....|...
gi 1093464499 158 VVLLDEPTAALDL 170
Cdd:PRK10636 451 LLLLDEPTNHLDL 463
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
14-179 |
8.00e-07 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 48.07 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 14 VSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSgdhelsggdVRIGEHSITELSIAELA-RYRAVLVQSQE 92
Cdd:cd03239 2 KQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAIC---------FVLGGKAAKLRRGSLLFlAGGGVKAGINS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 93 LSVPFTSREVIDFgrnpwgcpneeLLAEVIAEcdvahlldrevpTLSGGERARVHSARVF----YQDTPVVLLDEPTAAL 168
Cdd:cd03239 73 ASVEITFDKSYFL-----------VLQGKVEQ------------ILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAAL 129
|
170
....*....|.
gi 1093464499 169 DLHHAEKIMGM 179
Cdd:cd03239 130 DPTNRRRVSDM 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-195 |
1.00e-06 |
|
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: 47.37 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 33 PGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGehsitelsiaelaryravlvqsqelsvpftsrevidfgrnpwgc 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 113 pNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVV 192
Cdd:smart00382 37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK 115
|
...
gi 1093464499 193 VLH 195
Cdd:smart00382 116 NLT 118
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-176 |
1.04e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSG-----GDVRIGEHSITELSIAELARY 83
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQeLSVPFTSREVID-----FGRNPWGCPNEELLAEVIAECDVAHLLD------REVPT-LSGGERARVHSARV 151
Cdd:PRK14267 85 REVGMVFQ-YPNPFPHLTIYDnvaigVKLNGLVKSKKELDERVEWALKKAALWDevkdrlNDYPSnLSGGQRQRLVIARA 163
|
170 180
....*....|....*....|....*
gi 1093464499 152 FYQDTPVVLLDEPTAALDLHHAEKI 176
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKI 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-66 |
1.29e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVR 66
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE 59
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-169 |
1.46e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 18 LGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSI--------AELARYRAVLVQ 89
Cdd:PRK10938 13 LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFeqlqklvsDEWQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 90 SQELSVPFTSREVIDFGRNpwgcpNEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK10938 93 PGEDDTGRTTAEIIQDEVK-----DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-177 |
2.81e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 22 RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGdHELSG---GDVRIGEHSITELSIAELARYravLVQSQELSVPFT 98
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGFPKKQETFARISGY---CEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVI---DFGRNPWGCPNEELLAEVIaecDVAHLLDRE-----------VPTLSGGERARVHSARVFYQDTPVVLLDEP 164
Cdd:PLN03140 970 VRESLiysAFLRLPKEVSKEEKMMFVD---EVMELVELDnlkdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
170
....*....|...
gi 1093464499 165 TAALDLHHAEKIM 177
Cdd:PLN03140 1047 TSGLDARAAAIVM 1059
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
34-66 |
2.82e-06 |
|
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: 47.01 E-value: 2.82e-06
10 20 30
....*....|....*....|....*....|...
gi 1093464499 34 GKVTALVGPNGAGKSTLLAALSGDHELSGGDVR 66
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-169 |
5.03e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.77 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSG-----DHELSGGDVRIGEHSITELSIA-----------ELARYRAV 86
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGlikskYGTIQVGDIYIGDKKNNHELITnpyskkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELSVpF--TSREVIDFGRNPWGCPNEEllAEVIAECDVAHL------LDREVPTLSGGERARVHSARVFYQDTPV 158
Cdd:PRK13631 121 VFQFPEYQL-FkdTIEKDIMFGPVALGVKKSE--AKKLAKFYLNKMglddsyLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170
....*....|.
gi 1093464499 159 VLLDEPTAALD 169
Cdd:PRK13631 198 LIFDEPTAGLD 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-168 |
6.34e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 17 TLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDH--------------ELSGGDVRIGEHS----------- 71
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphgsyegeilfdgeVCRFKDIRDSEALgiviihqelal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 72 ITELSIAE---LARYRAvlvqsqelsvpftSREVIDfgrnpWGCPN---EELLAEViaecdvaHLldREVP-TLSG---- 140
Cdd:NF040905 90 IPYLSIAEnifLGNERA-------------KRGVID-----WNETNrraRELLAKV-------GL--DESPdTLVTdigv 142
|
170 180
....*....|....*....|....*...
gi 1093464499 141 GERARVHSARVFYQDTPVVLLDEPTAAL 168
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-169 |
7.13e-06 |
|
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: 46.83 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 14 VSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAAL------SGDHELSGgdvrIGEHSITelsiaeLARYR-AV 86
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstEGEIQIDG----VSWNSVT------LQTWRkAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELSV-PFTSREVIDfgrnPWGCPNEELLAEVIAECDVAHLLDrEVP------------TLSGGERARVHSARVFY 153
Cdd:TIGR01271 1295 GVIPQKVFIfSGTFRKNLD----PYEQWSDEEIWKVAEEVGLKSVIE-QFPdkldfvlvdggyVLSNGHKQLMCLARSIL 1369
|
170
....*....|....*.
gi 1093464499 154 QDTPVVLLDEPTAALD 169
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLD 1385
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-204 |
7.94e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTL---LAAL--------------------SGDHELSGGDVRIGEHSITELS-IAE 79
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRFKKIKkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 80 LARYRAVLVQSQELSVpF--TSREVIDFGRNPWGCPNEE---LLAEVIAECDV-AHLLDREVPTLSGGERARVHSARVFY 153
Cdd:PRK13651 103 IRRRVGVVFQFAEYQL-FeqTIEKDIIFGPVSMGVSKEEakkRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 154 QDTPVVLLDEPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDLSAAAAYA 204
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWT 232
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
33-66 |
8.11e-06 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 46.08 E-value: 8.11e-06
10 20 30
....*....|....*....|....*....|....
gi 1093464499 33 PGKVTALVGPNGAGKSTLLAALSGDHELSGGDVR 66
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-180 |
2.93e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.70 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL--GGH--RILNDISVVAEPGKVTALVGPNGAGKS-TLLAAL----SGDHELSGGDVRIGEHSITELSIAE 79
Cdd:PRK15134 6 LAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 80 LARYR----AVLVQSQELSV-PFTS-----REVIDFGRnpwGCPNEELLAEVIAeCdvahlLDR-----------EVP-T 137
Cdd:PRK15134 86 LRGVRgnkiAMIFQEPMVSLnPLHTlekqlYEVLSLHR---GMRREAARGEILN-C-----LDRvgirqaakrltDYPhQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1093464499 138 LSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLL 199
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-197 |
3.33e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.21 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITL-GGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELS-IAELARYRAV 86
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELS-VPFTSREVIDFGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:PRK13644 82 VFQNPETQfVGRTVEEDLAFGPENLCLPPIEIRKRVdraLAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1093464499 163 EPTAALDLHHAEKIMGMMRARAAAGKAVVVVLHDL 197
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNL 196
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
15-77 |
3.36e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.22 E-value: 3.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093464499 15 SITLGGHRILNDISV-VAEPGKVTALVGPNGAGKSTLLAALSgdHELSGGDVRIGEHSITELSI 77
Cdd:COG3950 5 SLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIA--LALSGLLSRLDDVKFRKLLI 66
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-175 |
4.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDV-RIGEHSITELSIAELARYRAVL-VQSQELSVPFTSRE 101
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAISAGLSGQLTGIEnIEFKMLCMGFKRKE 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093464499 102 VidfgrnpwgcpnEELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEK 175
Cdd:PRK13546 120 I------------KAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
15-55 |
4.83e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.84 E-value: 4.83e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1093464499 15 SITLGGHRILNDISVVAEPGkVTALVGPNGAGKSTLLAALS 55
Cdd:COG3593 5 KIKIKNFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALR 44
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-176 |
5.19e-05 |
|
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: 43.17 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGGH--RILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAV 86
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 87 LVQSQELsVPFTSREVIDfgrnPWgcpNEELLAEVIAECDVAHLLDrevpTLSGGERARVHSARVFYQDTPVVLLDEPTA 166
Cdd:cd03369 87 IPQDPTL-FSGTIRSNLD----PF---DEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170
....*....|
gi 1093464499 167 ALDLHHAEKI 176
Cdd:cd03369 155 SIDYATDALI 164
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
34-66 |
5.25e-05 |
|
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: 42.53 E-value: 5.25e-05
10 20 30
....*....|....*....|....*....|...
gi 1093464499 34 GKVTALVGPNGAGKSTLLAALSGDHELSGGDVR 66
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-180 |
6.22e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 26 DISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHsitELSIAELaRYRAVLVQS--QELSVPFTSREVI 103
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDY-SYRSQRIRMifQDPSTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 104 ----DFgrnpwgcP---NEELLAE-----VIAECDVAHLLDREVP----TLSGGERARVHSARVFYQDTPVVLLDEPTAA 167
Cdd:PRK15112 107 sqilDF-------PlrlNTDLEPEqrekqIIETLRQVGLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170
....*....|...
gi 1093464499 168 LDLHHAEKIMGMM 180
Cdd:PRK15112 180 LDMSMRSQLINLM 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-170 |
1.07e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 26 DISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEH----------SITELSIAELARYR----AVLVQS- 90
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRgadmAMIFQEp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 91 -QELSVPFTSREVI-DFGRNPWGCPNEELLAEVIAECDVAH------LLDREVPTLSGGERARVHSARVFYQDTPVVLLD 162
Cdd:PRK10261 114 mTSLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRipeaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
....*...
gi 1093464499 163 EPTAALDL 170
Cdd:PRK10261 194 EPTTALDV 201
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-105 |
1.17e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 23 ILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELS---GGDVRIGEHSITELsiaeLARYRAVLVQSQELSV-PFT 98
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEF----VPRKTSAYISQNDVHVgVMT 255
|
....*..
gi 1093464499 99 SREVIDF 105
Cdd:PLN03140 256 VKETLDF 262
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
34-65 |
1.24e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.50 E-value: 1.24e-04
10 20 30
....*....|....*....|....*....|..
gi 1093464499 34 GKVTALVGPNGAGKSTLLAALSGDHELSGGDV 65
Cdd:PRK00098 164 GKVTVLAGQSGVGKSTLLNALAPDLELKTGEI 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-67 |
1.65e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 1.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 9 ISADNVSITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRI 67
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-170 |
1.78e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 20 GHRILND-ISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGdvrigehSITELSIAELAryrAVLVQSQELSVPfT 98
Cdd:PRK10636 12 GVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGG-------SYTFPGNWQLA---WVNQETPALPQP-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 99 SREVIDFGRNpwgcpNEELLAEVIAECD------VAHL-----------------------------LDREVPTLSGGER 143
Cdd:PRK10636 81 LEYVIDGDRE-----YRQLEAQLHDANErndghaIATIhgkldaidawtirsraasllhglgfsneqLERPVSDFSGGWR 155
|
170 180
....*....|....*....|....*..
gi 1093464499 144 ARVHSARVFYQDTPVVLLDEPTAALDL 170
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
16-54 |
1.96e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 41.33 E-value: 1.96e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1093464499 16 ITLGGHRILNDISVVAEPGkVTALVGPNGAGKSTLLAAL 54
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
15-54 |
2.43e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.84 E-value: 2.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1093464499 15 SITLGGHRILNDISVvaEPGKVTALVGPNGAGKSTLLAAL 54
Cdd:COG4637 4 RIRIKNFKSLRDLEL--PLGPLTVLIGANGSGKSNLLDAL 41
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
36-55 |
2.95e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 2.95e-04
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
24-169 |
3.12e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 41.23 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 24 LNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAELARYRAVLV-QSQELSVPFT-SRE 101
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVfQNPDNQIVATiVEE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1093464499 102 VIDFGRNPWGCPNEELLAEV---IAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK13633 106 DVAFGPENLGIPPEEIRERVdesLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-169 |
3.98e-04 |
|
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: 41.21 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 9 ISADNVSITLGG----HRILNDISVVAEPGKVTALVGPNGAGKS-TLLAAL----SGDHELSgGDVRIGEHSITELSIAE 79
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHPS-GSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 80 LARYR----AVLVqsQElsvPFTS-----------REVIDFGRnpwGCPNEELLAEVIAecdvahLLDR-EVPT------ 137
Cdd:COG4172 86 LRRIRgnriAMIF--QE---PMTSlnplhtigkqiAEVLRLHR---GLSGAAARARALE------LLERvGIPDperrld 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1093464499 138 -----LSGGERARVHSARVFYQDtPVVLL-DEPTAALD 169
Cdd:COG4172 152 ayphqLSGGQRQRVMIAMALANE-PDLLIaDEPTTALD 188
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
131-178 |
4.37e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1093464499 131 LDREVPTLSGGERARVHSARVFYQDTP--VVLLDEPTAALDLHHAEKIMG 178
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-180 |
4.99e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 21 HRILNDISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIgEHSITELSIaelaryravlvqSQELSVPFTSR 100
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-KGSAALIAI------------SSGLNGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 101 EVIDFGRNPWGCPNE---ELLAEVIAECDVAHLLDREVPTLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIM 177
Cdd:PRK13545 104 ENIELKGLMMGLTKEkikEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
...
gi 1093464499 178 GMM 180
Cdd:PRK13545 184 DKM 186
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
15-177 |
6.30e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 15 SITLGGHRILNDISVVAEPGKVTALVGPNGAGKSTLL----AALSGDHELSGGD----VRIGEHSIT---ELSIAElARY 83
Cdd:COG0419 4 RLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILeairYALYGKARSRSKLrsdlINVGSEEASvelEFEHGG-KRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 84 RAVLVQSQELSVPFTS----REVID--FGRNPWGCPNEEL------LAEVIAECDVAHLLDRE----------VPTLSGG 141
Cdd:COG0419 83 RIERRQGEFAEFLEAKpserKEALKrlLGLEIYEELKERLkeleeaLESALEELAELQKLKQEilaqlsgldpIETLSGG 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1093464499 142 ERARVHSARVFyqdtpVVLLDepTAALDLHHAEKIM 177
Cdd:COG0419 163 ERLRLALADLL-----SLILD--FGSLDEERLERLL 191
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
14-55 |
7.13e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 7.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1093464499 14 VSITLGGHRILND---ISVVAE---PGKVTALVGPNGAGKSTLLAALS 55
Cdd:COG1106 3 ISFSIENFRSFKDeltLSMVASglrLLRVNLIYGANASGKSNLLEALY 50
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-169 |
1.14e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.07 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 17 TLGGHRILNDISVVAEPGKVTALVGPNGAGKST----LLAALSgdhelSGGDVRIGEHSITELSIAELaryravlvqsqe 92
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQL------------ 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 93 lsVPFTSREVIDFgRNPWGCPNEEL-LAEVIAECDVAHL--------------------LDREV----PT-LSGGERARV 146
Cdd:PRK15134 358 --LPVRHRIQVVF-QDPNSSLNPRLnVLQIIEEGLRVHQptlsaaqreqqviavmeevgLDPETrhryPAeFSGGQRQRI 434
|
170 180
....*....|....*....|...
gi 1093464499 147 HSARVFYQDTPVVLLDEPTAALD 169
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLD 457
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
17-55 |
1.45e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1093464499 17 TLGGHRIlnDISvvaePGKVTALVGPNGAGKSTLLAALS 55
Cdd:pfam13555 11 TFDGHTI--PID----PRGNTLLTGPSGSGKSTLLDAIQ 43
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-180 |
1.81e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 38.94 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 25 NDISVVAEPGKVTALVGPNGAGKSTLLAALSG---DHELSGGDVRIGEHSITELSIAELARYRAvlvqsQELSV----PF 97
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREILNLPEKELNKLRA-----EQISMifqdPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 98 TSRevidfgrNPWGCPNEELL-----------AEVIAECdvAHLLD-----------REVP-TLSGGERARVHSARVFYQ 154
Cdd:PRK09473 108 TSL-------NPYMRVGEQLMevlmlhkgmskAEAFEES--VRMLDavkmpearkrmKMYPhEFSGGMRQRVMIAMALLC 178
|
170 180
....*....|....*....|....*.
gi 1093464499 155 DTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLL 204
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
33-180 |
2.35e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.21 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 33 PGKVTALVGPNGAGKSTLLAALsgdhelsggdvR--IGEHSITELSIAEL-------ARYRAVLVQSqELSVPFTsrevi 103
Cdd:cd03278 21 PPGLTAIVGPNGSGKSNIIDAI-----------RwvLGEQSAKSLRGEKMsdvifagSETRKPANFA-EVTLTFD----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 104 dfgrnpwgcpNEELLAEVIAECDVAHLLD------REVPTLSGGERARVHSARVF----YQDTPVVLLDEPTAALDLHHA 173
Cdd:cd03278 84 ----------NSDGRYSIISQGDVSEIIEapgkkvQRLSLLSGGEKALTALALLFaifrVRPSPFCVLDEVDAALDDANV 153
|
....*..
gi 1093464499 174 EKIMGMM 180
Cdd:cd03278 154 ERFARLL 160
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
138-179 |
2.78e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.80 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1093464499 138 LSGGERARVHSARVF----YQDTPVVLLDEPTAALDLHHAEKIMGM 179
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANL 1123
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
17-176 |
4.39e-03 |
|
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: 37.17 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 17 TLGGHRILNDISVVAEpGKVTALVGPNGAGKSTLLAALSGDHELSGGDVrigehsitelsiaELARYRaVLVQSQELSvp 96
Cdd:cd03222 9 RYGVFFLLVELGVVKE-GEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-------------EWDGIT-PVYKPQYID-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 97 ftsrevidfgrnpwgcpneellaeviaecdvahlldrevptLSGGERARVHSARVFYQDTPVVLLDEPTAALD----LHH 172
Cdd:cd03222 72 -----------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNA 110
|
....
gi 1093464499 173 AEKI 176
Cdd:cd03222 111 ARAI 114
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
36-54 |
5.08e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 37.44 E-value: 5.08e-03
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
36-55 |
5.71e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.03 E-value: 5.71e-03
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-180 |
6.80e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 37.53 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 33 PGKVTALVGPNGAGKSTLLAALSGDHELSGGDVRIGEHSITELSIAEL-ARYRAVLVQSQELSVPFTSREVIDFG-RNPW 110
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqALRRDIQFIFQDPYASLDPRQTVGDSiMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 111 GCPNeeLLAEVIAECDVAHLLDR---------EVP-TLSGGERARVHSARVFYQDTPVVLLDEPTAALDLHHAEKIMGMM 180
Cdd:PRK10261 429 RVHG--LLPGKAAAARVAWLLERvgllpehawRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
|
| TraA_Ti |
TIGR02768 |
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ... |
6-66 |
7.04e-03 |
|
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.
Pssm-ID: 274289 [Multi-domain] Cd Length: 744 Bit Score: 37.48 E-value: 7.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1093464499 6 GLGISADNVSITLGGHRILND-----ISVVAEPGKVTALVGPNGAGKSTLLAALSGDHELSGGDVR 66
Cdd:TIGR02768 335 GHGVSPPIVDAAIDQHYRLSEeqyeaVRHVTGSGDIAVVVGRAGTGKSTMLKAAREAWEAAGYRVI 400
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-177 |
7.65e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 37.70 E-value: 7.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1093464499 137 TLSGGERARVHSARVFYQDTPVVLLDEPTAALDlHHAEKIM 177
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLI 1397
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
16-180 |
7.90e-03 |
|
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: 36.82 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 16 ITLGGHRI--LNDISVVAEPGKVTALVGPNGAGKSTLL-----AALSgdHELSGGDVRIGEHSitelSIAELARYRAVLV 88
Cdd:cd03271 1 LTLKGAREnnLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALA--RRLHLKKEQPGNHD----RIEGLEHIDKVIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093464499 89 QSQEL------SVPFTSREVIDFGRNpWGCP-------NEELLaEV------IAE-----CDVAHL-------------- 130
Cdd:cd03271 75 IDQSPigrtprSNPATYTGVFDEIRE-LFCEvckgkryNRETL-EVrykgksIADvldmtVEEALEffenipkiarklqt 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093464499 131 ----------LDREVPTLSGGERARVHSA---------RVFYqdtpvvLLDEPTAALDLHHAEKIMGMM 180
Cdd:cd03271 153 lcdvglgyikLGQPATTLSGGEAQRIKLAkelskrstgKTLY------ILDEPTTGLHFHDVKKLLEVL 215
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
15-54 |
9.22e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 36.81 E-value: 9.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1093464499 15 SITLGGHRILNDISVVAEPgKVTALVGPNGAGKSTLLAAL 54
Cdd:pfam13175 5 SIIIKNFRCLKDTEIDLDE-DLTVLIGKNNSGKSSILEAL 43
|
|
| |
