|
Name |
Accession |
Description |
Interval |
E-value |
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-387 |
0e+00 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 685.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSKVKIEHLTKIFGKKVKPALKMVQENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT 80
Cdd:COG4175 1 MPKIEVRNLYKIFGKRPERALKLLDQGKSKDEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQY 160
Cdd:COG4175 81 AGEVLIDGEDITKLSKKELRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:COG4175 161 PDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 241 KVVQVGTGEDILTNPANDYVRAFTEDIDRSKVLTAENIMIQPLTTNISVDGPNVALKKMATEEVSGLVAVDRNRQFKGFL 320
Cdd:COG4175 241 RIVQIGTPEEILTNPANDYVADFVEDVDRSKVLTAGSVMRPPEAVVSEKDGPRVALRRMREEGISSLYVVDRDRRLLGVV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 321 TSDAAIKARRDQIPLTDVLV-DMQTVSQDMLVADLMPLISDSPSPLAVVDG-GRLKGVVIRGRVLEALT 387
Cdd:COG4175 321 TADDALEAVKGEKDLEEILLtDVPTVSPDTPLRDLLPLVAESPYPLAVVDEdGRLLGVISRGSLLAALA 389
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-272 |
7.65e-177 |
|
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: 492.93 E-value: 7.65e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPALKMVQENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQ 163
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....*....
gi 682099688 244 QVGTGEDILTNPANDYVRAFTEDIDRSKV 272
Cdd:cd03294 241 QVGTPEEILTNPANDYVREFFRGVDRAKV 269
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
35-391 |
4.35e-143 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 411.17 E-value: 4.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 35 EKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNF 114
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 GLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 195 DPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFTEDIDRSKVLT 274
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 275 AENIMIQPLTTNISVD---GPNVALKKMATEEVSGLVAVDRNRQFKGFLTSDAAIKARRDQIPLTDVLV-DMQTVSQDML 350
Cdd:TIGR01186 241 AERIAQRMNTGPITKTadkGPRSALQLMRDERVDSLYVVDRQNKLVGVVDVESIKQARKKAQGLQDVLIdDIYTVDAGTL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 682099688 351 VADLMPLISDSPSPLAVVD-GGRLKGVVIRGRVLEALTDNLE 391
Cdd:TIGR01186 321 LRETVRKVLKAGIKVPVVDeDQRLVGIVTRGSLVDALYDSRE 362
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-330 |
1.82e-116 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 341.30 E-value: 1.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQ 105
Cdd:COG1125 5 ENVTKR----YPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLA--FKDQYPSQLSGGMQQRVGLARALANNPE 183
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 184 ILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 264 --TEDIDRS-KVLTAENIMIQPLTTNISVDGPNVALKKMATEEVSGLVAVDRNRQFKGFLTSDAAIKARR 330
Cdd:COG1125 237 vgADRGLRRlSLLRVEDLMLPEPPTVSPDASLREALSLMLERGVDWLLVVDEDGRPLGWLTLEDLLRALA 306
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-386 |
1.84e-114 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 339.70 E-value: 1.84e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 3 KVKIEHLTKIFGKKVKPALKMVQENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSG 82
Cdd:PRK10070 4 KLEIKNLYKIFGEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 83 SIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPS 162
Cdd:PRK10070 84 QVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 163 QLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 243 VQVGTGEDILTNPANDYVRAFTEDIDRSKVLTAENIMIQPLTTNISVD---GPNVALKKMATEEVSGLVAVDRNRQFKGF 319
Cdd:PRK10070 244 VQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARRTPNGLIRKTpgfGPRSALKLLQDEDREYGYVIERGNKFVGA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 320 LTSDAAIKARRDQIPLTDVLVDMQ-TVSQDMLVADLMPLISDSPSPLAVVD-GGRLKGVVIRGRVLEAL 386
Cdd:PRK10070 324 VSIDSLKTALTQQQGLDAALIDAPlAVDAQTPLSELLSHVGQAPCAVPVVDeDQQYVGIISKGMLLRAL 392
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-310 |
7.78e-96 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 290.46 E-value: 7.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSKVKIEHLTKIFGKKvkPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT 80
Cdd:COG3842 3 MPALELENVSKRYGDV--TALD----------------------DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDISTmdkeelLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQY 160
Cdd:COG3842 59 SGRILLDGRDVTG------LPPEKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:COG3842 133 PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 241 KVVQVGTGEDILTNPANDYVRAFtedIDRSKVLTAEniMIQPLTTNISVDGPNVALKKMATEEVSGLVAV 310
Cdd:COG3842 213 RIEQVGTPEEIYERPATRFVADF---IGEANLLPGT--VLGDEGGGVRTGGRTLEVPADAGLAAGGPVTV 277
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-263 |
7.34e-95 |
|
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: 283.81 E-value: 7.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQ 105
Cdd:cd03295 4 ENVTKR----YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANL--LAFKDQYPSQLSGGMQQRVGLARALANNPE 183
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 184 ILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
26-245 |
5.08e-91 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 274.66 E-value: 5.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEILEKTGATVgVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdkeellevRRQ 105
Cdd:COG1116 11 RGVSKRFPTGGGGVTA-LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKD--GKVVQV 245
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
26-246 |
2.99e-88 |
|
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: 265.92 E-value: 2.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeilekTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdkeelLEVRRQ 105
Cdd:cd03259 4 KGLSKT-----YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
26-245 |
2.98e-87 |
|
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: 263.56 E-value: 2.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkeellEVRRQ 105
Cdd:cd03293 4 RNVSKT-YGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT--------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 kMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:cd03293 75 -RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIM--KDGKVVQV 245
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-263 |
4.27e-87 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 267.33 E-value: 4.27e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQ-ENVSKTeILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLE 101
Cdd:COG1135 1 MIElENLSKT-FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 102 VRRqKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANN 181
Cdd:COG1135 80 ARR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 182 PEILLMDEAFSALDPlirrDMQDELLEL-QESQQK---TIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAN 257
Cdd:COG1135 159 PKVLLCDEATSALDP----ETTRSILDLlKDINRElglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
....*.
gi 682099688 258 DYVRAF 263
Cdd:COG1135 235 ELTRRF 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-263 |
6.39e-84 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 259.62 E-value: 6.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSKVKIEHLTKIFGKkvkpalkmvqenvskteilektgaTVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT 80
Cdd:COG3839 1 MASLELENVSKSYGG------------------------VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDISTmdkeelLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQY 160
Cdd:COG3839 57 SGEILIGGRDVTD------LPPKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:COG3839 131 PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG 210
|
250 260
....*....|....*....|...
gi 682099688 241 KVVQVGTGEDILTNPANDYVRAF 263
Cdd:COG3839 211 RIQQVGTPEELYDRPANLFVAGF 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-263 |
2.67e-82 |
|
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: 251.82 E-value: 2.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpalkmVQENVskteilektgatvgvydaNIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:COG1127 6 IEVRNLTKSFGDRV------VLDGV------------------SLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEELLEVRRqKMSMVFQNFGLFPQRTVLENTEYGL-EVQGVDKAERQARAEKALDNANLLAFKDQYPS 162
Cdd:COG1127 62 ILVDGQDITGLSEKELYELRR-RIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 163 QLSGGMQQRVGLARALANNPEILLMDEAFSALDPlIRRDMQDEL-LELQESQQKTIIFISHDLNEALRIGDRIAIMKDGK 241
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDP-ITSAVIDELiRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
250 260
....*....|....*....|..
gi 682099688 242 VVQVGTGEDILTNPaNDYVRAF 263
Cdd:COG1127 220 IIAEGTPEELLASD-DPWVRQF 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
26-262 |
6.17e-81 |
|
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: 257.14 E-value: 6.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRq 105
Cdd:COG1123 264 RNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRR- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQN-FG-LFPQRTVLENTEYGLEVQGV-DKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQRVGLARALANN 181
Cdd:COG1123 343 RVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:COG1123 423 PKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTR 502
|
.
gi 682099688 262 A 262
Cdd:COG1123 503 A 503
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
34-264 |
7.24e-80 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 249.29 E-value: 7.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 34 LEKT-GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMdkeelLEVRRQKMSMVFQ 112
Cdd:COG1118 8 ISKRfGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----LPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 113 NFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 193 ALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFT 264
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-263 |
3.26e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 243.75 E-value: 3.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:COG1126 2 IEIENLHKSFGDLE--VLK----------------------GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDIsTMDKEELLEVRRqKMSMVFQNFGLFPQRTVLENTEYGL-EVQGVDKAERQARAEKALDNANLLAFKDQYPS 162
Cdd:COG1126 58 ITVDGEDL-TDSKKDINKLRR-KVGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 163 QLSGGMQQRVGLARALANNPEILLMDEAFSALDPlirrDMQDELL----ELQESQQkTIIFISHDLNEALRIGDRIAIMK 238
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEVLdvmrDLAKEGM-TMVVVTHEMGFAREVADRVVFMD 210
|
250 260
....*....|....*....|....*
gi 682099688 239 DGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:COG1126 211 GGRIVEEGPPEEFFENPQHERTRAF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
26-255 |
1.43e-77 |
|
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: 239.41 E-value: 1.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEvRRQ 105
Cdd:cd03258 5 KNVSKV-FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK-ARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
26-263 |
2.35e-77 |
|
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: 238.68 E-value: 2.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKteileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdkeelLEVRRQ 105
Cdd:cd03300 4 ENVSK-----FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN------LPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADF 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-242 |
1.28e-74 |
|
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: 231.22 E-value: 1.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGkkvkpalkmvqENVSKTEILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03255 1 IELKNLSKTYG-----------GGGEKVQALK---------GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQ 163
Cdd:cd03255 61 VRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDlNEALRIGDRIAIMKDGKV 242
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
45-263 |
1.48e-72 |
|
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: 226.61 E-value: 1.48e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRqKMSMVFQNFGLFPQRTVLE 124
Cdd:cd03261 18 GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-RMGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGL-EVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:cd03261 97 NVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 204 DELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPaNDYVRAF 263
Cdd:cd03261 177 DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-243 |
4.17e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 224.92 E-value: 4.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSKV-KIEHLTKIF--GKKVKPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLI 77
Cdd:COG1136 1 MSPLlELRNLTKSYgtGEGEVTALR----------------------GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLD 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 78 EPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFK 157
Cdd:COG1136 59 RPTSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 158 DQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLnEALRIGDRIAIM 237
Cdd:COG1136 139 DHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRL 217
|
....*.
gi 682099688 238 KDGKVV 243
Cdd:COG1136 218 RDGRIV 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-252 |
1.13e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 221.86 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALD----------------------GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTmdkeELLEVRRqKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQ 163
Cdd:COG1131 57 VRVLGEDVAR----DPAEVRR-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
....*....
gi 682099688 244 QVGTGEDIL 252
Cdd:COG1131 211 ADGTPDELK 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
38-255 |
1.68e-70 |
|
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: 221.05 E-value: 1.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQN---- 113
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL----RRKVGLVFQNpddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 114 -FGlfpqRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:COG1122 88 lFA----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 193 ALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:COG1122 164 GLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-263 |
5.48e-70 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 223.52 E-value: 5.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQ-ENVSKTeILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLE 101
Cdd:PRK11153 1 MIElKNISKV-FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 102 VRRQkMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANN 181
Cdd:PRK11153 80 ARRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
..
gi 682099688 262 AF 263
Cdd:PRK11153 239 EF 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
43-262 |
2.28e-69 |
|
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: 221.08 E-value: 2.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP---TSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQN-FG-LF 117
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRGREIQMIFQDpMTsLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGLEV-QGVDKAERQARAEKALDNANL---LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:COG0444 101 PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 194 LDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:COG0444 181 LDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENPRHPYTRA 249
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
26-246 |
2.36e-69 |
|
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: 218.14 E-value: 2.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkEELLEVRRQ 105
Cdd:cd03257 5 KNLSVS-FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQN-FG-LFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLL---AFKDQYPSQLSGGMQQRVGLARALAN 180
Cdd:cd03257 83 EIQMVFQDpMSsLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 181 NPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-241 |
6.26e-69 |
|
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: 215.13 E-value: 6.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03229 1 LELKNVSKRYGQKT--VLN----------------------DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDIstMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLevqgvdkaerqaraekaldnanllafkdqypsq 163
Cdd:cd03229 57 ILIDGEDL--TDLEDELPPLRRRIGMVFQDFALFPHLTVLENIALGL--------------------------------- 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 164 lSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGK 241
Cdd:cd03229 102 -SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
58-276 |
1.48e-68 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 219.29 E-value: 1.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEellevrRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDK 137
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 138 AERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTI 217
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 218 IFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFTEDIDRSKVLTAE 276
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIE 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-242 |
1.65e-67 |
|
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: 212.77 E-value: 1.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLK----------------------GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGT 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDIsTMDKEELLEVRrQKMSMVFQNFGLFPQRTVLENTEYGL-EVQGVDKAERQARAEKALDNANLLAFKDQYPS 162
Cdd:cd03262 57 IIIDGLKL-TDDKKNINELR-QKVGMVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 163 QLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQkTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGM-TMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-246 |
2.50e-66 |
|
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: 209.80 E-value: 2.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03301 1 VELENVTKRFGNVT--ALD----------------------DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEEllevrrQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKA---LDNANLLafkDQY 160
Cdd:cd03301 57 IYIGGRDVTDLPPKD------RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVaelLQIEHLL---DRK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:cd03301 128 PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
....*.
gi 682099688 241 KVVQVG 246
Cdd:cd03301 208 QIQQIG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-263 |
2.84e-65 |
|
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: 207.96 E-value: 2.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 30 KTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEellevrRQKMSM 109
Cdd:cd03299 2 KVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 110 VFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAE---KALDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILL 186
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeiaEMLGIDHLL---NRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 187 MDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEF 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-263 |
7.13e-65 |
|
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: 206.81 E-value: 7.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKteileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeelleVRRQ 105
Cdd:cd03296 6 RNVSK-----RFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGV----DKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANN 181
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
..
gi 682099688 262 AF 263
Cdd:cd03296 235 SF 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-267 |
2.76e-64 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 209.80 E-value: 2.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 22 KMVQENVSKTEILEKTGATVGvYDA-------NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTM 94
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKS-FDGkevisnlDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 95 DKEellevRRQkMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGL 174
Cdd:PRK09452 82 PAE-----NRH-VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 175 ARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
250
....*....|...
gi 682099688 255 PANDYVRAFTEDI 267
Cdd:PRK09452 236 PKNLFVARFIGEI 248
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
45-251 |
2.75e-63 |
|
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: 202.41 E-value: 2.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIE-----PTSGSIYLDGEDISTMDkEELLEVRRQkMSMVFQNFGLFPQ 119
Cdd:cd03260 18 DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLD-VDVLELRRR-VGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 120 rTVLENTEYGLEVQGV-DKAERQARAEKALDNANLLA-FKDQ-YPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:cd03260 96 -SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDeVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 197 LIRRDMQDELLELQesQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:cd03260 175 ISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
33-262 |
4.99e-63 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 204.97 E-value: 4.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 33 ILEKTGATV-GVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRqKMSMVF 111
Cdd:COG4608 23 LFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRR-RMQMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 112 QN-FG-LFPQRTVLENTEYGLEVQGV-DKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQRVGLARALANNPEILLM 187
Cdd:COG4608 102 QDpYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 188 DEAFSALDPLIR-------RDMQDEL-LelqesqqkTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDY 259
Cdd:COG4608 182 DEPVSALDVSIQaqvlnllEDLQDELgL--------TYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPY 253
|
...
gi 682099688 260 VRA 262
Cdd:COG4608 254 TQA 256
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
26-243 |
6.47e-63 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 202.21 E-value: 6.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQ 105
Cdd:COG3638 6 RNLSKR----YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 kMSMVFQNFGLFPQRTVLENteygleV---------------QGVDKAERQaRAEKALDNANLLAFKDQYPSQLSGGMQQ 170
Cdd:COG3638 82 -IGMIFQQFNLVPRLSVLTN------VlagrlgrtstwrsllGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 171 RVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-237 |
1.06e-62 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 202.01 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSKVKIEHLTKIFGKKV--KPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIE 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpQPALQ----------------------DVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 79 PTSGSIYLDGEDISTMDKEEllevrrqkmSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKD 158
Cdd:COG4525 59 PSSGEITLDGVPVTGPGADR---------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFAR 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 159 QYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIM 237
Cdd:COG4525 130 RRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-248 |
2.43e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 199.89 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQ-ENVSKT-----EILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDK 96
Cdd:COG2884 1 MIRfENVSKRypggrEALS---------DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 97 EELLEVRRqKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLAR 176
Cdd:COG2884 72 REIPYLRR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 177 ALANNPEILLMDEAFSALDPlirrDMQDELLELQES---QQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTG 248
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDP----ETSWEIMELLEEinrRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
36-241 |
7.67e-62 |
|
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: 198.07 E-value: 7.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 36 KTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQN-- 113
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----RRKVGLVFQNpd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 114 ---FGLfpqrTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:cd03225 86 dqfFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 682099688 191 FSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGK 241
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-265 |
1.52e-61 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 198.49 E-value: 1.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKV--KPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTS 81
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLK----------------------DVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 82 GSIYLDGEDISTMDKEEllevRRQKMSMVFQN-FG-LFPQRTVLENTEYGLEVQGVDkaERQARAEKALDNANL-LAFKD 158
Cdd:COG1124 60 GEVTFDGRPVTRRRRKA----FRRRVQMVFQDpYAsLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 159 QYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMK 238
Cdd:COG1124 134 RYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQ 213
|
250 260
....*....|....*....|....*..
gi 682099688 239 DGKVVQVGTGEDILTNPANDYVRAFTE 265
Cdd:COG1124 214 NGRIVEELTVADLLAGPKHPYTRELLA 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
26-251 |
1.55e-60 |
|
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: 195.86 E-value: 1.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQ 105
Cdd:cd03256 4 ENLSKT----YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 kMSMVFQNFGLFPQRTVLENTEYGL---------EVQGVDKAERQaRAEKALDNANLLAFKDQYPSQLSGGMQQRVGLAR 176
Cdd:cd03256 80 -IGMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 177 ALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
38-256 |
3.16e-60 |
|
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: 203.21 E-value: 3.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT---SGSIYLDGEDISTMDkeelLEVRRQKMSMVFQNF 114
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS----EALRGRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 G--LFPQrTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:COG1123 93 MtqLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 193 ALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:COG1123 172 ALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-254 |
1.71e-58 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 191.49 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALK----------------------NVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGedISTMDKEELLEVRrQKMSMVFQNfglfP--Q---RTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKD 158
Cdd:TIGR04520 59 VTVDG--LDTLDEENLWEIR-KKVGMVFQN----PdnQfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 159 QYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRiGDRIAIMK 238
Cdd:TIGR04520 132 REPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMN 210
|
250
....*....|....*.
gi 682099688 239 DGKVVQVGTGEDILTN 254
Cdd:TIGR04520 211 KGKIVAEGTPREIFSQ 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
46-263 |
2.32e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.97 E-value: 2.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 46 ANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdkeelLEVRRQKMSMVFQNFGLFPQRTVLEN 125
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA------LPPAERPVSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 126 TEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDE 205
Cdd:COG3840 92 IGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 206 LLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-266 |
3.35e-58 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 193.40 E-value: 3.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQENVSKteileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMdkeellEV 102
Cdd:PRK11432 7 VVLKNITK-----RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR------SI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 103 RRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNP 182
Cdd:PRK11432 76 QQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 183 EILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMAS 235
|
....
gi 682099688 263 FTED 266
Cdd:PRK11432 236 FMGD 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
45-253 |
8.54e-58 |
|
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: 189.10 E-value: 8.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEllevRRQKMSMVFQ----NFGLfpqr 120
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARRIAYVPQeppaPFGL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TVLENTEYG----LEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:COG1120 91 TVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 197 LIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
38-260 |
1.01e-57 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 189.09 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIE--P---TSGSIYLDGEDI--STMDKEELlevrRQKMSMV 110
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVEL----RRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 111 FQNFGLFPqRTVLENTEYGLEVQGV-DKAERQARAEKALDNANL-------LafkDQYPSQLSGGMQQRVGLARALANNP 182
Cdd:COG1117 98 FQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkdrL---KKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 183 EILLMDEAFSALDPLIRRDMQDELLELqeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAN----D 258
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDkrteD 251
|
..
gi 682099688 259 YV 260
Cdd:COG1117 252 YI 253
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-263 |
1.86e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 187.99 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQ-ENVSKteileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGedISTMDKEELLE 101
Cdd:PRK09493 1 MIEfKNVSK-----HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 102 VRRQKMSMVFQNFGLFPQRTVLENTEYG-LEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALAN 180
Cdd:PRK09493 74 LIRQEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 181 NPEILLMDEAFSALDPLIRRD----MQDelleLQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEvlkvMQD----LAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
....*..
gi 682099688 257 NDYVRAF 263
Cdd:PRK09493 229 SQRLQEF 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-252 |
2.84e-57 |
|
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: 187.37 E-value: 2.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 5 KIEHLTKIFGKKvkPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSI 84
Cdd:COG4555 3 EVENLSKKYGKV--PALK----------------------DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 85 YLDGEDISTMDKEellevRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQL 164
Cdd:COG4555 59 LIDGEDVRKEPRE-----ARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 165 SGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQ 244
Cdd:COG4555 134 STGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
....*...
gi 682099688 245 VGTGEDIL 252
Cdd:COG4555 213 QGSLDELR 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-269 |
5.17e-57 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 190.29 E-value: 5.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSkVKIEHLTKIFGKkvkpalkmvqenvskTEILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT 80
Cdd:PRK10851 1 MS-IEIANIKKSFGR---------------TQVLN---------DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDISTMdkeellEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEV----QGVDKAERQARAEKALDNANLLAF 156
Cdd:PRK10851 56 SGHIRFHGTDVSRL------HARDRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 157 KDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAI 236
Cdd:PRK10851 130 ADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVV 209
|
250 260 270
....*....|....*....|....*....|...
gi 682099688 237 MKDGKVVQVGTGEDILTNPANDYVRAFTEDIDR 269
Cdd:PRK10851 210 MSQGNIEQAGTPDQVWREPATRFVLEFMGEVNR 242
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
26-243 |
7.64e-57 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 186.35 E-value: 7.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRq 105
Cdd:TIGR02315 5 ENLSKV----YPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYG-LEVQ-------GVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARA 177
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHGrLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 178 LANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-247 |
6.81e-56 |
|
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: 183.09 E-value: 6.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVD----------------------DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEellevRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQ 163
Cdd:cd03263 59 AYINGYSIRTDRKA-----ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRART 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQesQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03263 134 LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
....
gi 682099688 244 QVGT 247
Cdd:cd03263 212 CIGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-242 |
2.46e-55 |
|
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: 179.90 E-value: 2.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKvkPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03230 1 IEVRNLSKRYGKK--TALD----------------------DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDIstmdKEELLEVRRqKMSMVFQNFGLFPQRTVLENTEYglevqgvdkaerqaraekaldnanllafkdqypsq 163
Cdd:cd03230 57 IKVLGKDI----KKEPEEVKR-RIGYLPEEPSLYENLTVRENLKL----------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 164 lSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:cd03230 97 -SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
36-262 |
2.05e-54 |
|
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: 187.97 E-value: 2.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 36 KTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIePTSGSIYLDGEDISTMDKEELLEVRRQkMSMVFQN-F 114
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 G-LFPQRTVLENTEYGLEVQ--GVDKAERQARAEKALDNANLL-AFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:COG4172 373 GsLSPRMTVGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 191 FSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
43-263 |
7.81e-54 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 182.73 E-value: 7.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKeellevRRQKMSMVFQNFGLFPQRTV 122
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------YQRPINMMFQSYALFPHMTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDM 202
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 203 QDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:PRK11607 189 QLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
52-246 |
4.83e-53 |
|
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: 175.56 E-value: 4.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 52 EGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLE 131
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 132 VQgvDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQE 211
Cdd:cd03297 102 RK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 682099688 212 SQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
36-242 |
3.20e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.08 E-value: 3.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 36 KTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFG 115
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQrTVLENTEYGLEVQgvDKAERQARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:COG4619 85 LWGG-TVRDNLPFPFQLR--ERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 195 DPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:COG4619 162 DPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
45-249 |
1.20e-51 |
|
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: 172.62 E-value: 1.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARHVGFVFQSFQLLPTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVDKAerQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:COG4181 110 NVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIID 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 205 ELLELQESQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGE 249
Cdd:COG4181 188 LLFELNRERGTTLVLVTHDPALAARC-DRVLRLRAGRLVEDTAAT 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
48-263 |
3.71e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 171.91 E-value: 3.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 48 IEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIST-MDKEELLEVR--------RQKMSMVFQNFGLFP 118
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkPDRDGELVPAdrrqlqriRTRLGMVFQSFNLWS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 QRTVLEN-TEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP- 196
Cdd:COG4598 109 HMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPe 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 197 LIR---RDMQDelleLQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:COG4598 189 LVGevlKVMRD----LAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQF 253
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
38-255 |
4.95e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 171.35 E-value: 4.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGE--DISTMDKEELLEVRRQKMSMVFQNFG 115
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQRTVLEN-TEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:PRK11124 93 LWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 195 DPLIRRDMQDELLELQESQQKTIIfISHDLNEALRIGDRIAIMKDGKVVQVGTgEDILTNP 255
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQP 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
45-252 |
2.02e-50 |
|
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: 180.03 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVVLQDVFLF-SGTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NteygleVQGVDKAERQARAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:COG2274 568 N------ITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 194 LDPLIRRDMQDELLELqeSQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:COG2274 642 LDAETEAIILENLRRL--LKGRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
45-228 |
2.74e-50 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 169.88 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEllevrrqkmSMVFQNFGLFPQRTVLE 124
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180
....*....|....*....|....
gi 682099688 205 ELLELQESQQKTIIFISHDLNEAL 228
Cdd:PRK11248 170 LLLKLWQETGKQVLLITHDIEEAV 193
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
45-246 |
3.12e-49 |
|
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: 164.53 E-value: 3.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEllevRRQKMSMVFQnfglfpqrtvle 124
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 nteyglevqgvdkaerqaraekALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPlirrDMQD 204
Cdd:cd03214 81 ----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI----AHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 682099688 205 ELLE----LQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03214 135 ELLEllrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
38-255 |
5.76e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.96 E-value: 5.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGE--DISTMDKEELLEVRRQKMSMVFQNFG 115
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQRTVLEN-TEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 195 DPLIRRDMQDELLELQESQQKTIIfISHDLNEALRIGDRIAIMKDGKVVQVGTGEdILTNP 255
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQP 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
43-251 |
6.14e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 167.11 E-value: 6.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGediSTMDKEELLEVRRqKMSMVFQN-FGLFPQRT 121
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRR-QVGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 682099688 202 MQDELLELQESQQKTIIFISHDLNEALRiGDRIAIMKDGKVVQVGTGEDI 251
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
45-255 |
7.58e-49 |
|
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: 165.33 E-value: 7.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLevrrqkmsmVFQNFGLFPQRTVLE 124
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTeyGLEVQGV----DKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRR 200
Cdd:TIGR01184 74 NI--ALAVDRVlpdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 201 DMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGtgeDILTNP 255
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG---QILEVP 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
45-276 |
5.69e-48 |
|
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: 166.81 E-value: 5.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLevQGVDKAERQARAEKA---LDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:COG4148 97 NLLYGR--KRAPRAERRISFDEVvelLGIGHLL---DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 202 MQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAndyVRAFTEDIDRSKVLTAE 276
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD---LLPLAGGEEAGSVLEAT 243
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-247 |
7.47e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.12 E-value: 7.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLF-SGTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEvqGVDKAErqarAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:COG1132 433 NIRYGRP--DATDEE----VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 194 LDPLIRRDMQDELLELqeSQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGT 247
Cdd:COG1132 507 LDTETEALIQEALERL--MKGRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGT 557
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
45-192 |
1.04e-47 |
|
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: 159.35 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQRTVLE 124
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 125 NTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQ----YPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
27-263 |
1.20e-47 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 165.79 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 27 NVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdkeelLEVRRQK 106
Cdd:PRK11650 8 AVRKS----YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE------LEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 107 MSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILL 186
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 187 MDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASF 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
45-241 |
1.89e-47 |
|
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: 158.95 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQnfglfpqrtvle 124
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RRRIGYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 nteyglevqgvdkaerqaraekaldnanllafkdqypsqLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:cd00267 81 ---------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 682099688 205 ELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGK 241
Cdd:cd00267 122 LLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
45-266 |
3.35e-47 |
|
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: 164.51 E-value: 3.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLevQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:TIGR02142 95 NLRYGM--KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 205 ELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYvrAFTED 266
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW--LARED 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
45-241 |
3.73e-47 |
|
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: 158.70 E-value: 3.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:cd03228 20 DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTeyglevqgvdkaerqaraekaldnanllafkdqypsqLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:cd03228 95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 682099688 205 ELLELqeSQQKTIIFISHDLnEALRIGDRIAIMKDGK 241
Cdd:cd03228 138 ALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-263 |
5.05e-47 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 164.43 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 27 NVSKTeilekTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGE---DISTMDKEellevr 103
Cdd:PRK11000 8 NVTKA-----YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 104 rqkMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPE 183
Cdd:PRK11000 77 ---VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 184 ILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGF 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
47-265 |
6.00e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.07 E-value: 6.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSI-----YLDGeDISTMDKEELLEVRRQKMSMVFQNFGLFPQRT 121
Cdd:PRK11264 23 DLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDT-ARSLSQQKGLIRQLRQHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYG-LEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRR 200
Cdd:PRK11264 102 VLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 201 DMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFTE 265
Cdd:PRK11264 182 EVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
37-262 |
8.77e-47 |
|
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: 167.55 E-value: 8.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 37 TGATVGVYDANIEIEEGEIFVIMGLSGSGKS----TLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQ 112
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 113 ------NfglfPQRTVLENTEYGLEV-QGVDKAERQARAEKALDNANL--LAFK-DQYPSQLSGGMQQRVGLARALANNP 182
Cdd:COG4172 100 epmtslN----PLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdPERRlDAYPHQLSGGQRQRVMIAMALANEP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 183 EILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:COG4172 176 DLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRK 255
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
26-261 |
3.09e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 159.62 E-value: 3.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEI----LEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeelLE 101
Cdd:COG4167 8 RNLSKTFKyrtgLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD----YK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 102 VRRQKMSMVFQ--NFGLFPQRTV---LE-----NTEYglevqgvDKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQ 170
Cdd:COG4167 84 YRCKHIRMIFQdpNTSLNPRLNIgqiLEeplrlNTDL-------TAEEREERIFATLRLVGLLPeHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 171 RVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGED 250
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|.
gi 682099688 251 ILTNPANDYVR 261
Cdd:COG4167 237 VFANPQHEVTK 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-258 |
6.33e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 158.15 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIE-----PTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQRT 121
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYGLEVQGV--DKAERQARAEKALDNANLL-AFKDQYPS---QLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PRK14247 99 IFENVALGLKLNRLvkSKKELQERVRWALEKAQLWdEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 196 PLIRRDMQDELLELQesQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAND 258
Cdd:PRK14247 179 PENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-251 |
1.69e-45 |
|
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: 155.99 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 32 EILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkEELLEVRRqKMSMVF 111
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRR-RIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 112 QNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 192 SALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
46-267 |
4.96e-45 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 156.14 E-value: 4.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 46 ANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDK---------EELLEVRRQKMSMVFQNFGL 116
Cdd:TIGR03005 19 LNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGrngplvpadEKHLRQMRNKIGMVFQSFNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 117 FPQRTVLEN-TEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:TIGR03005 99 FPHKTVLDNvTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTSALD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 196 PLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFTEDI 267
Cdd:TIGR03005 179 PELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSKV 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
48-246 |
5.11e-45 |
|
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: 154.57 E-value: 5.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 48 IEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeelleVRRQKMSMVFQNFGLFPQRTVLENTE 127
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP------PADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 128 YGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELL 207
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 682099688 208 ELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
45-256 |
5.39e-45 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 155.97 E-value: 5.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEElleVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR---IARLGIARTFQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQ-------------GVDKAERQAR--AEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDE 189
Cdd:COG0411 99 NVLVAAHARlgrgllaallrlpRARREEREARerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 190 AFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
38-256 |
1.67e-44 |
|
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: 154.13 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEellEVRRQKMSMVFQNFGLF 117
Cdd:cd03219 11 GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIARLGIGRTFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLEN--------TEYGLEVQGVDKAERQAR--AEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLM 187
Cdd:cd03219 88 PELTVLENvmvaaqarTGSGLLLARARREEREARerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 188 DEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
45-254 |
4.13e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 153.99 E-value: 4.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdKEELLEVRRqKMSMVFQN-FGLFPQRTVL 123
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENLKEIRK-KIGIIFQNpDNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 ENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:PRK13632 103 DDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 682099688 204 DELLELQESQQKTIIFISHDLNEALrIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK13632 183 KIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
5-259 |
6.91e-44 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 153.04 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 5 KIEHLTKIFGKKvkpalkmvqenvskteilekTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSI 84
Cdd:COG4107 10 SVRGLSKRYGPG--------------------CGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 85 YLDG-----EDISTMDKEELLEVRRQKMSMVFQN--FGLFPQRTVLENTEYGLEVQGVDKAER-QARAEKALDNANLLAF 156
Cdd:COG4107 70 YYRDrdggpRDLFALSEAERRRLRRTDWGMVYQNprDGLRMDVSAGGNIAERLMAAGERHYGDiRARALEWLERVEIPLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 157 K-DQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIA 235
Cdd:COG4107 150 RiDDLPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTM 229
|
250 260
....*....|....*....|....
gi 682099688 236 IMKDGKVVQVGTGEDILTNPANDY 259
Cdd:COG4107 230 VMKNGRVVESGLTDQVLEDPQHPY 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-251 |
8.39e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 154.11 E-value: 8.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqeNVSkteilektgatvgvydanIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:COG4152 2 LELKGLTKRFGDKT--AVD----DVS------------------FTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEE---LLEVRrqkmsmvfqnfGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQY 160
Cdd:COG4152 58 VLWDGEPLDPEDRRRigyLPEER-----------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKG 205
|
250
....*....|.
gi 682099688 241 KVVQVGTGEDI 251
Cdd:COG4152 206 RKVLSGSVDEI 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
49-262 |
1.68e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 153.97 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNrLIE-PTSGSIYLDGEDISTMDKEELlEVRRQKMSMVFQN-FG-LFPQRTV--- 122
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDLLKADPEAQ-KLLRQKIQIVFQNpYGsLNPRKKVgqi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LE-----NTEyglevqgVDKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:PRK11308 115 LEeplliNTS-------LSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 197 LIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQA 253
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-246 |
2.87e-43 |
|
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: 150.12 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03269 1 LEVENVTKRFGRVT--ALD----------------------DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMDKEE---LLEVRrqkmsmvfqnfGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQY 160
Cdd:cd03269 57 VLFDGKPLDIAARNRigyLPEER-----------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKG 204
|
....*.
gi 682099688 241 KVVQVG 246
Cdd:cd03269 205 RAVLYG 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
45-251 |
3.64e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 151.81 E-value: 3.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkEELLEVRRQKMSMVFQN-FGLFPQRTVL 123
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT----EENVWDIRHKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 ENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 204 DELLELQESQQKTIIFISHDLNEaLRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
38-254 |
4.80e-43 |
|
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: 149.51 E-value: 4.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLevrRQKMSMVFQNFGLF 117
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGLEVQGvdKAERQARAEKALDN-ANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:cd03224 88 PELTVEENLLLGAYARR--RAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 197 LIRRDMQDELLELQESQQkTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:cd03224 166 KIVEEIFEAIRELRDEGV-TILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
45-256 |
1.32e-42 |
|
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: 156.85 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrTVLE 124
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL----RRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 N--------TEyglevqgvdkaerqARAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEIL 185
Cdd:COG4987 428 NlrlarpdaTD--------------EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELqeSQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:COG4987 494 LLDEPTEGLDAATEQALLADLLEA--LAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
45-252 |
1.70e-42 |
|
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: 156.46 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrTVLE 124
Cdd:COG4988 355 GLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQNPYLFAG-TIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NteyglevqgVDKAERQA---RAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:COG4988 430 N---------LRLGRPDAsdeELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 191 FSALDPLIRRDMQDELLELqeSQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:COG4988 501 TAHLDAETEAEILQALRRL--AKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
45-253 |
1.73e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.08 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIstmdkeellEVRRQKMSMVfqnfglfPQR---- 120
Cdd:COG1121 24 DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---------RRARRRIGYV-------PQRaevd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 -----TVLENTEYGLEVQ-----GVDKAERQaRAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:COG1121 88 wdfpiTVRDVVLMGRYGRrglfrRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 191 FSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMkDGKVVQVGTGEDILT 253
Cdd:COG1121 167 FAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-246 |
2.47e-42 |
|
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: 147.34 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpALKMVqenvskteilektgatvgvydaNIEIEEGeIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGV----------------------SLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTMdKEELlevrRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQ 163
Cdd:cd03264 56 IRIDGQDVLKQ-PQKL----RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELqeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
...
gi 682099688 244 QVG 246
Cdd:cd03264 209 FEG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-254 |
3.80e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 149.43 E-value: 3.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSkVKIEHLTKIFGKKV---KPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLI 77
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTpfeKKALD----------------------NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 78 EPTSGSIYLDGEDIStmDKEELLEVRRQKMSMVFQ--NFGLFpQRTVLENTEYGLEVQGVDKAERQARAEKALDNANL-- 153
Cdd:PRK13637 58 KPTSGKIIIDGVDIT--DKKVKLSDIRKKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdy 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 154 LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDR 233
Cdd:PRK13637 135 EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADR 214
|
250 260
....*....|....*....|.
gi 682099688 234 IAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK13637 215 IIVMNKGKCELQGTPREVFKE 235
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
38-279 |
4.07e-42 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 149.85 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIsTMDKEELlevrRQKMSMVFQNFGLF 117
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-VREPRKV----RRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 198 IRRDMQDELLELQESqQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFTEDIDRSKVLTAEN 277
Cdd:TIGR01188 159 TRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSML 237
|
..
gi 682099688 278 IM 279
Cdd:TIGR01188 238 IA 239
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
45-255 |
7.37e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 147.57 E-value: 7.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVR---RQKMSMVFqNFglfpqrT 121
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlPQHSSLAF-PF------T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALA-------NNPEILLMDEAFSAL 194
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 195 DPLirrdMQDELLEL--QESQQK-TIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:COG4559 172 DLA----HQHAVLRLarQLARRGgGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-263 |
1.32e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 147.04 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTM-------- 94
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 95 --DKEELlEVRRQKMSMVFQNFGLFPQRTVLENT-EYGLEVQGVDKAERQARAEKALDNANLL-AFKDQYPSQLSGGMQQ 170
Cdd:PRK10619 81 vaDKNQL-RLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 171 RVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGED 250
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
250
....*....|...
gi 682099688 251 ILTNPANDYVRAF 263
Cdd:PRK10619 239 LFGNPQSPRLQQF 251
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-256 |
2.31e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.47 E-value: 2.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 39 ATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQnfglFP 118
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 Q-----RTVLENTEYGLEVQGVDKAERQARAEKALD----NANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDE 189
Cdd:PRK13634 95 EhqlfeETVEKDICFGPMNFGVSEEDAKQKAREMIElvglPEELL---ARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 190 AFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-242 |
2.60e-41 |
|
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: 144.86 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTeileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRq 105
Cdd:cd03292 4 INVTKT----YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 186 LMDEAFSALDPlirrDMQDELLELQESQQK---TIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:cd03292 159 IADEPTGNLDP----DTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-254 |
4.68e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 146.39 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 22 KMVQ-ENVS-KTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDisTMDKEEL 99
Cdd:PRK13633 3 EMIKcKNVSyKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 100 LEVRrQKMSMVFQNfglfPQRT-----VLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGL 174
Cdd:PRK13633 81 WDIR-NKAGMVFQN----PDNQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 175 ARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRiGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
45-260 |
9.14e-41 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 144.92 E-value: 9.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRL--IEP---TSGSIYLDGEDI--STMDKEELlevrRQKMSMVFQNFGLF 117
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDL----RKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQrTVLENTEYGLEVQGV-DKAERQARAEKALDNANLL-AFKDQYPSQ---LSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:PRK14239 99 PM-SIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIWdEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 193 ALDPLIRRDMQDELLELQesQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAN----DYV 260
Cdd:PRK14239 178 ALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHketeDYI 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
47-228 |
1.04e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 143.39 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP---TSGSIYLDGEDISTmdkeelLEVRRQKMSMVFQNFGLFPQRTVL 123
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA------LPAEQRRIGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 ENTEYGLeVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:COG4136 95 ENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFR 173
|
170 180
....*....|....*....|....*
gi 682099688 204 DELLELQESQQKTIIFISHDLNEAL 228
Cdd:COG4136 174 EFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
45-252 |
1.34e-40 |
|
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: 143.91 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEvqGVDKAERQARAEKALDNANLLAFKDQYPSQ-------LSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:cd03253 94 NIRYGRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 198 IRRDMQDELLELqeSQQKTIIFISHDLNEALRiGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:cd03253 172 TEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
43-246 |
2.83e-40 |
|
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: 142.29 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEellevrrqkmsmvfqnFGLFPQR-- 120
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----------------IGYVPQRrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 -------TVLENTEYGLE-----VQGVDKAERqARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMD 188
Cdd:cd03235 79 idrdfpiSVRDVVLMGLYghkglFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 189 EAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMkDGKVVQVG 246
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-255 |
3.60e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 142.86 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSKVKIEHLTKIFGKKvkpalkmvqenvskteilektgaTVgVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT 80
Cdd:COG1137 1 MMTLEAENLVKSYGKR-----------------------TV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDIST--MDkeellevRRQKMSMvfqnfGLFPQ-----R--TVLENTEYGLEVQGVDKAERQARAEKALDNA 151
Cdd:COG1137 57 SGRIFLDGEDITHlpMH-------KRARLGI-----GYLPQeasifRklTVEDNILAVLELRKLSKKEREERLEELLEEF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 152 NLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsqqKTI-IFIS-HDLNEALR 229
Cdd:COG1137 125 GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE---RGIgVLITdHNVRETLG 201
|
250 260
....*....|....*....|....*.
gi 682099688 230 IGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:COG1137 202 ICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-258 |
8.21e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 142.29 E-value: 8.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIE-----PTSGSIYLDGEDISTMDKEELlEVRRqKMSMVFQNFGLFPQ 119
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI-EVRR-EVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 120 RTVLENTEYGLEVQGV--DKAERQARAEKALDNANLL-AFKDQ---YPSQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWdEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 194 LDPLIRRDMQDELLELQEsqQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAND 258
Cdd:PRK14267 180 IDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-252 |
1.14e-39 |
|
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: 148.03 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 18 KPALKMvqENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLD-GEDISTMDK 96
Cdd:TIGR03269 277 EPIIKV--RNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 97 EELLEVRRQK--MSMVFQNFGLFPQRTVLENTEyglEVQGVDKAERQARaEKALDNANLLAFK--------DQYPSQLSG 166
Cdd:TIGR03269 355 PGPDGRGRAKryIGILHQEYDLYPHRTVLDNLT---EAIGLELPDELAR-MKAVITLKMVGFDeekaeeilDKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 167 GMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*.
gi 682099688 247 TGEDIL 252
Cdd:TIGR03269 511 DPEEIV 516
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-246 |
4.31e-39 |
|
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: 139.43 E-value: 4.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPalkmvqenvskteilektgaTVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03266 2 ITADALTKRFRDVKKT--------------------VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTmdkeELLEVRRqKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQ 163
Cdd:cd03266 62 ATVDGFDVVK----EPAEARR-RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
...
gi 682099688 244 QVG 246
Cdd:cd03266 216 YEG 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
45-267 |
4.42e-39 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 140.67 E-value: 4.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRqKMSMVFQNFGLFPQRTVLE 124
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGL-EVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:PRK11831 104 NVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 204 DELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPaNDYVRAFTEDI 267
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFLDGI 246
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
47-247 |
4.89e-39 |
|
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: 139.60 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPqRTVLENT 126
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFD-GTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGLEVQGVDKAERQARAekaldnANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:cd03249 98 RYGKPDATDEEVEEAAKK------ANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 682099688 196 PLIRRDMQDELLELQESqqKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGT 247
Cdd:cd03249 172 AESEKLVQEALDRAMKG--RTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGT 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
45-253 |
7.24e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 139.91 E-value: 7.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEL---LEVRRQKMSMVFQnFglfpqrT 121
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAVLPQHSSLSFP-F------T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALA------NNPEILLMDEAFSALD 195
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 196 PLirrdMQDELL----ELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:PRK13548 173 LA----HQHHVLrlarQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
47-253 |
8.33e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 138.95 E-value: 8.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEellevrRQKMSMVFQNFGLFPQRTVLENT 126
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYG----LEVQGVDKAERQARAEKAldnaNLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDM 202
Cdd:PRK10771 93 GLGlnpgLKLNAAQREKLHAIARQM----GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 682099688 203 QDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
45-252 |
1.03e-38 |
|
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: 138.90 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEvqgvdkAERQARAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:cd03251 95 NIAYGRP------GATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 194 LDPLIRRDMQDELLELQESqqKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:cd03251 169 LDTESERLVQAALERLMKN--RTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
43-256 |
1.21e-38 |
|
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: 138.58 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELleVRRqKMSMVFQNFGLFPQRTV 122
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARL-GIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEVQGvDKAERQARAEKALDN-ANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:COG0410 96 EENLLLGAYARR-DRAEVRADLERVYELfPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 202 MQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:COG0410 175 IFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-244 |
1.53e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.44 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 33 ILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQkMSMVFQ 112
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRD-IQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 113 N-FGLF-PQRTVLENTEYGLE-VQGVDKAERQARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMD 188
Cdd:PRK10419 97 DsISAVnPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 189 EAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQ 244
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-251 |
1.67e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.39 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 18 KPALKMvqENVSKTeilekTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKe 97
Cdd:COG1129 2 EPLLEM--RGISKS-----FGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 98 elLEVRRQKMSMVFQNFGLFPQRTVLEN-------TEYGLevqgVDKAERQARAEKALD------NANLLAfkdqypSQL 164
Cdd:COG1129 74 --RDAQAAGIAIIHQELNLVPNLSVAENiflgrepRRGGL----IDWRAMRRRARELLArlgldiDPDTPV------GDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 165 SGGMQQRVGLARALANNPEILLMDEAFSALDP--------LIRRdmqdelleLQEsQQKTIIFISHDLNEALRIGDRIAI 236
Cdd:COG1129 142 SVAQQQLVEIARALSRDARVLILDEPTASLTEreverlfrIIRR--------LKA-QGVAIIYISHRLDEVFEIADRVTV 212
|
250
....*....|....*
gi 682099688 237 MKDGKVVQVGTGEDI 251
Cdd:COG1129 213 LRDGRLVGTGPVAEL 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-256 |
4.94e-38 |
|
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: 136.90 E-value: 4.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 30 KTEILEKT-GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMdkeELLEVRRQKMS 108
Cdd:cd03218 2 RAENLSKRyGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 109 MVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMD 188
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 189 EAFSALDPLIRRDMQDELLELQESQqktI-IFIS-HDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRG---IgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-252 |
7.06e-38 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 136.75 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 1 MSK-VKIEHLTKIFGKKVKPALKMvqenvsKTEILEKTGATVGVY----DANIEIEEGEIFVIMGLSGSGKSTLIRLLNR 75
Cdd:COG1134 1 MSSmIEVENVSKSYRLYHEPSRSL------KELLLRRRRTRREEFwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 76 LIEPTSGSIYLDGEdISTmdkeeLLEVrrqkmsmvfqNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLA 155
Cdd:COG1134 75 ILEPTSGRVEVNGR-VSA-----LLEL----------GAGFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 156 FKDQ----YPSqlsgGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIG 231
Cdd:COG1134 139 FIDQpvktYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLC 213
|
250 260
....*....|....*....|.
gi 682099688 232 DRIAIMKDGKVVQVGTGEDIL 252
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEEVI 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
45-252 |
1.51e-37 |
|
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: 135.43 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPqRTVLE 124
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLFS-GTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVDKAERQARAEKALDNANLLafKDQYPSQ-------LSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:cd03254 96 NIRLGRPNATDEEVIEAAKEAGAHDFIMKL--PNGYDTVlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 198 IRRDMQDELLELQEsqQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:cd03254 174 TEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
45-252 |
2.88e-37 |
|
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: 142.16 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIstmdKEELLEVRRQKMSMVFQNFGLFpQRTVLE 124
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL----ADYTLASLRRQVALVSQDVVLF-NDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGlEVQGVDKAerqaRAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:TIGR02203 425 NIAYG-RTEQADRA----EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 194 LDPLIRRDMQDELLELQesQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:TIGR02203 500 LDNESERLVQAALERLM--QGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
41-251 |
3.29e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 136.45 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 41 VGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQnfglFPQR 120
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TVLENT-----EYGLEVQGVDKAERQARAEKALDNanlLAFK----DQYPSQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:PRK13646 97 QLFEDTvereiIFGPKNFKMNLDEVKNYAHRLLMD---LGFSrdvmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 192 SALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
45-243 |
3.51e-37 |
|
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: 133.92 E-value: 3.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeellevRRQKMSMVFQN--FGLFpQRTV 122
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RRKSIGYVMQDvdYQLF-TDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEvqgvDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDM 202
Cdd:cd03226 90 REELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 682099688 203 QDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03226 166 GELIRELAA-QGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-243 |
1.21e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 141.01 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:PRK10535 106 NVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 682099688 205 ELLELQEsQQKTIIFISHDLNEALRiGDRIAIMKDGKVV 243
Cdd:PRK10535 186 ILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
40-255 |
1.28e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.43 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 40 TVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStMDKEELLEVRrQKMSMVFQNFG--LF 117
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVR-KTVGIVFQNPDdqLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQrTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:PRK13639 93 AP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 198 IRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK13639 172 GASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
45-251 |
2.17e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 133.72 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQN-FGLFPQRTVL 123
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 ENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 204 DELLELQESQQKTIIFISHDLNEALRiGDRIAIMKDGKVVQVGTGEDI 251
Cdd:PRK13648 183 DLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
47-233 |
2.47e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 131.45 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIstmdkEELLEVRRQKMSMVFQNFGLFPQRTVLENT 126
Cdd:COG4133 22 SFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-----RDAREDYRRRLAYLGHADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGLEVQGVDKAERQARAekALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDplirRDMQDEL 206
Cdd:COG4133 97 RFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD----AAGVALL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 682099688 207 LEL--QESQQ-KTIIFISHDLNEA-----LRIGDR 233
Cdd:COG4133 171 AELiaAHLARgGAVLLTTHQPLELaaarvLDLGDF 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-243 |
2.94e-36 |
|
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: 129.86 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKteileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeeLLEVRRQ 105
Cdd:cd03216 4 RGITK-----RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQnfglfpqrtvlenteyglevqgvdkaerqaraekaldnanllafkdqypsqLSGGMQQRVGLARALANNPEIL 185
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-263 |
5.46e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 132.09 E-value: 5.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGE------DISTMDKEELlevrRQKMSMVFQNFGLFP 118
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL----RKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 QRTVLENTEYGLEVQGV-DKAERQARAEKALDNANLlaFKDQY------PSQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGL--WKEVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 192 SALDPLIRRDMQDELLELQesQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAF 263
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-243 |
2.16e-35 |
|
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: 129.26 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKvkPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLD----------------------DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDIStmdkeELLEVRRQKMSMVfQNFGLFPQRTVLENTEYGLEVQGVDKAerqaRAEKALDNANLLAFKDQYPSQ 163
Cdd:cd03268 57 ITFDGKSYQ-----KNIEALRRIGALI-EAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03268 127 FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-252 |
3.04e-35 |
|
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: 129.53 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevRRQkMSMVFQNFGLFpQRTVLE 124
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQ-VGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 N---TEYGLEVQGVDKAERQARAEkaldnanllAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:cd03252 95 NialADPGMSMERVIEAAKLAGAH---------DFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 191 FSALD----PLIRRDMQDELlelqesQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:cd03252 166 TSALDyeseHAIMRNMHDIC------AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-253 |
4.64e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.43 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQ-ENVSKteileKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEL-- 99
Cdd:COG4604 1 MIEiKNVSK-----RYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELak 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 100 -LEVRRQKMSMVFQ-------NFGLFPqrtvlenteYGlevQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQR 171
Cdd:COG4604 76 rLAILRQENHINSRltvrelvAFGRFP---------YS---KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 172 VGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
..
gi 682099688 252 LT 253
Cdd:COG4604 224 IT 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-244 |
5.26e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.78 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 22 KMVQENVSKTEILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLE 101
Cdd:PRK11629 13 KRYQEGSVQTDVLH---------NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 102 VRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANN 181
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAiMKDGKVVQ 244
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-243 |
1.51e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 133.61 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 18 KPALKMvqENVSKTeilekTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDI---STM 94
Cdd:COG3845 3 PPALEL--RGITKR-----FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 95 DkeelleVRRQKMSMVFQNFGLFPQRTVLENTEYGLE-VQGVDKAERQARAEkaldnanLLAFKDQYP---------SQL 164
Cdd:COG3845 76 D------AIALGIGMVHQHFMLVPNLTVAENIVLGLEpTKGGRLDRKAARAR-------IRELSERYGldvdpdakvEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 165 SGGMQQRVGLARALANNPEILLMDEAFSALDPlirrdmQ--DELLE-LQE--SQQKTIIFISHDLNEALRIGDRIAIMKD 239
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVLTP------QeaDELFEiLRRlaAEGKSIIFITHKLREVMAIADRVTVLRR 216
|
....
gi 682099688 240 GKVV 243
Cdd:COG3845 217 GKVV 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
43-273 |
1.73e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 130.21 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQkMSMVFQN--FGLFPQR 120
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TVLENTEYGLEV--QGVDKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 198 IRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRAFTE-------DIDRS 270
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSavpipdpDLERN 275
|
...
gi 682099688 271 KVL 273
Cdd:PRK15079 276 KTI 278
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
45-242 |
2.84e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.49 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIyLDGEdistmdkeELLEVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--------APLAEAREDTRLMFQDARLLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLevqgvdKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:PRK11247 101 NVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 682099688 205 ELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:PRK11247 175 LIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-297 |
5.10e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 127.64 E-value: 5.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQ 105
Cdd:PRK13641 6 ENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQnfglFP-----QRTVLENTEYGLEVQGVDKAERQARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALA 179
Cdd:PRK13641 86 KVSLVFQ----FPeaqlfENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 180 NNPEILLMDEAFSALDPLIRRDMQDELLELQESQQkTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPanDY 259
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK--EW 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 682099688 260 VRAFTEDIDRSKVLTAE------NIMIQPLTTNISVDGPNVALK 297
Cdd:PRK13641 239 LKKHYLDEPATSRFASKlekggfKFSEMPLTIDELVDGIKNNLK 282
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-275 |
7.27e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 128.84 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRTVLE 124
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLevqgvdKAERQARAEKALDnanLLAFK---DQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:PRK11144 96 NLRYGM------AKSMVAQFDKIVA---LLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 202 MQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAndyVRAFTEDIDRSKVLTA 275
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA---MRPWLPKEEQSSILKV 237
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-246 |
9.74e-34 |
|
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: 125.34 E-value: 9.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPALKMvqenvsKTEILEKTGATVGVY----DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP 79
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSL------KKLGILGRKGEVGEFwalkDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 80 TSGSIYLDGEDIStmdkeeLLEVrrqkmsmvfqNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQ 159
Cdd:cd03220 75 DSGTVTVRGRVSS------LLGL----------GGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 160 YPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKD 239
Cdd:cd03220 139 PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEK 217
|
....*..
gi 682099688 240 GKVVQVG 246
Cdd:cd03220 218 GKIRFDG 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
38-253 |
3.16e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 124.74 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLevrrqkmsmvfQNFGLF 117
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----------RRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQR-------TVLENTEYG----LEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILL 186
Cdd:PRK11231 82 PQHhltpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 187 MDEAFSALDplIRRdmQDELLEL-QESQQ--KTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:PRK11231 162 LDEPTTYLD--INH--QVELMRLmRELNTqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-255 |
4.88e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 131.00 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLF-SGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLevQGVDKAERQARAEKALDNANLLAFKDQYP-------SQLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:TIGR00958 574 NIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 198 IRRDMQdellELQESQQKTIIFISHDLNEALRiGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:TIGR00958 652 CEQLLQ----ESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
49-252 |
7.11e-33 |
|
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: 129.94 E-value: 7.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVfqnfglfPQRTVL----- 123
Cdd:COG5265 380 EVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIV-------PQDTVLfndti 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 -ENTEYGLEvqGVDKAErqarAEKALDNANLLAF----KDQYPSQ-------LSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:COG5265 449 aYNIAYGRP--DASEEE----VEAAARAAQIHDFieslPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 192 SALDPLIRRDMQDELLELqeSQQKTIIFISHDLN---EAlrigDRIAIMKDGKVVQVGTGEDIL 252
Cdd:COG5265 523 SALDSRTERAIQAALREV--ARGRTTLVIAHRLStivDA----DEILVLEAGRIVERGTHAELL 580
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-254 |
8.13e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 124.81 E-value: 8.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 3 KVKIEHLTKIFGKKVKPALKMVqENVSkteilektgatvgvydanIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSG 82
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELKAL-DNVS------------------VEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 83 SIYLDGEDISTMDKEELLEVR--------------------RQKMSMVFQ--NFGLFPQrTVLENTEYGLEVQGVDKAER 140
Cdd:PRK13651 63 TIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 141 QARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIF 219
Cdd:PRK13651 142 KKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIIL 220
|
250 260 270
....*....|....*....|....*....|....*
gi 682099688 220 ISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK13651 221 VTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
53-261 |
8.43e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 129.05 E-value: 8.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIePTSGSIYLDGEDISTMDKEELLEVRRQkMSMVFQ--NFGLFPQRTVLENTEYGL 130
Cdd:PRK15134 312 GETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNSSLNPRLNVLQIIEEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 131 EVQ--GVDKAERQARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELL 207
Cdd:PRK15134 390 RVHqpTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 208 ELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:PRK15134 470 SLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
40-256 |
1.13e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 123.94 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 40 TVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGedISTMDKEELLEVRRQkMSMVFQNFGL-FP 118
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKL-VGIVFQNPETqFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 QRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLI 198
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 199 RRDMQDELLELQEsQQKTIIFISHDLNEaLRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:PRK13644 172 GIAVLERIKKLHE-KGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
42-247 |
1.41e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.93 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 42 GVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRT 121
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYGLEvqGVDKAERQARAEKALDNANLLAFKDQYP-------SQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:PRK13657 425 IEDNIRVGRP--DATDEEMRAAAERAQAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 682099688 195 DPLIRRDMQDELLELqeSQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGT 247
Cdd:PRK13657 503 DVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGS 552
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-265 |
2.21e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 122.58 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEILEKT-------GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNR---LIEP--TSGSIYLDGEDIST 93
Cdd:PRK14243 2 STLNGTETVLRTenlnvyyGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 94 MDKEELlEVRRqKMSMVFQNFGLFPqRTVLENTEYGLEVQGVdKAERQARAEKALDNANLL-AFKD---QYPSQLSGGMQ 169
Cdd:PRK14243 82 PDVDPV-EVRR-RIGMVFQKPNPFP-KSIYDNIAYGARINGY-KGDMDELVERSLRQAALWdEVKDklkQSGLSLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 170 QRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsqQKTIIFISHDLNEALRIGDRIAIM---------KDG 240
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTAFFnveltegggRYG 235
|
250 260
....*....|....*....|....*
gi 682099688 241 KVVQVGTGEDILTNPANDYVRAFTE 265
Cdd:PRK14243 236 YLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
47-253 |
2.29e-32 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 122.12 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSG-SIYLDGEdisTMDKEELLEVRRqkmsmvfqNFGLF-P--QRTV 122
Cdd:COG1119 23 SWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE---RRGGEDVWELRK--------RIGLVsPalQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEyGLEV------------QGVDKAERQaRAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:COG1119 92 PRDET-VLDVvlsgffdsiglyREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 191 FSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
47-244 |
3.28e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.89 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdkEELLEVRRqKMSMVFQN-FGLFPQRTVLEN 125
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRR-KIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 126 TEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDE 205
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 682099688 206 LLELQESQQKTIIFISHDLNEALRiGDRIAIMKDGKVVQ 244
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
53-261 |
5.99e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 127.28 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQkMSMVFQN--FGLFPQRTVLENTEYGL 130
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPRQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 131 EVQGV-DKAERQARAEKALDNANLLAFKD-QYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLE 208
Cdd:PRK10261 429 RVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 682099688 209 LQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:PRK10261 509 LQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
38-263 |
7.42e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 121.25 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEElleVRRQKMSMVFQNFGLF 117
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ---IARMGVVRTFQHVRLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLEN--------TEYGL-----EVQGVDKAERQA--RAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNP 182
Cdd:PRK11300 93 REMTVIENllvaqhqqLKTGLfsgllKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 183 EILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPanDYVRA 262
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIKA 250
|
.
gi 682099688 263 F 263
Cdd:PRK11300 251 Y 251
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
43-255 |
7.75e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 7.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS---IYLDGediSTMDKEELLEVRrQKMSMVFQN-FGLFP 118
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG---ITLTAKTVWDIR-EKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 QRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLI 198
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 199 RRDMQDELLELQESQQKTIIFISHDLNEAlRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-249 |
1.49e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.21 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEIlektGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQ 105
Cdd:PRK10908 5 EHVSKAYL----GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 kMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:PRK10908 81 -IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 186 LMDEAFSALDplirRDMQDELLELQESQQK---TIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGE 249
Cdd:PRK10908 160 LADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
43-261 |
1.78e-31 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 120.28 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeelLEVRRQKMSMVFQN--FGLFPQR 120
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TVLENTEYGLEVQ-GVDKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLI 198
Cdd:PRK15112 105 RISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 199 RRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTK 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-256 |
5.25e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 120.34 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 21 LKMVQENVSKTEILEKTGATVgVYDANIE------------IEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLdg 88
Cdd:PRK13631 9 KLKVPNPLSDDIILRVKNLYC-VFDEKQEnelvalnnisytFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 89 EDISTMDKEELLEVR--------------RQKMSMVFQ--NFGLFpQRTVLENTEYGLEVQGVDKAERQARAEKALDNAN 152
Cdd:PRK13631 86 GDIYIGDKKNNHELItnpyskkiknfkelRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 153 L-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLElQESQQKTIIFISHDLNEALRIG 231
Cdd:PRK13631 165 LdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVA 243
|
250 260
....*....|....*....|....*
gi 682099688 232 DRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
45-242 |
5.52e-31 |
|
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: 116.16 E-value: 5.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrTVLE 124
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTeyglevqgvdkaerqaraekaldnanllafkdqypsqLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:cd03246 95 NI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 682099688 205 ELLELQeSQQKTIIFISHDLnEALRIGDRIAIMKDGKV 242
Cdd:cd03246 138 AIAALK-AAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
39-280 |
8.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 119.07 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 39 ATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQnfglFP 118
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 -----QRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLA-FKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:PRK13643 94 esqlfEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 193 ALDPLIRRDMQdELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPanDYVRA---------- 262
Cdd:PRK13643 174 GLDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV--DFLKAhelgvpkath 250
|
250
....*....|....*...
gi 682099688 263 FTEDIDRSKVLTAENIMI 280
Cdd:PRK13643 251 FADQLQKTGAVTFEKLPI 268
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-242 |
8.20e-31 |
|
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: 115.99 E-value: 8.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 32 EILEKTGATVG--VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevRRQKMSM 109
Cdd:cd03215 3 PVLEVRGLSVKgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 110 V---FQNFGLFPQRTVLENTeyglevqgvdkaerqaraekALdnanllafkdqyPSQLSGGMQQRVGLARALANNPEILL 186
Cdd:cd03215 80 VpedRKREGLVLDLSVAENI--------------------AL------------SSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 187 MDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-242 |
1.15e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.19 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQENVSKTEILEKTgatVGVYDANIEI--------EEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTM 94
Cdd:PRK10584 1 MPAENIVEVHHLKKS---VGQGEHELSIltgvelvvKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 95 DKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGL 174
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 175 ARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAiMKDGKV 242
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLR-LVNGQL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
47-243 |
1.19e-30 |
|
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: 116.92 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLENT 126
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLF-YGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGlevqgvDKAERQARAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:cd03245 99 TLG------APLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 196 PLIRRDMQDELLELQEsqQKTIIFISHDLNeALRIGDRIAIMKDGKVV 243
Cdd:cd03245 173 MNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
43-251 |
1.20e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.69 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQnfglFPQ--- 119
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----FPEsql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 120 --RTVLENTEYGLEVQGVDKAERQARAEKALDNANLL-AFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:PRK13649 99 feETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 197 LIRRDMQDELLELQESQQkTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGM-TIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
58-271 |
1.48e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 118.27 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLLNRLIEPTSGSIY-----LDGEDIstMDKEELLEVRRqKMSMVFQNFGLFPQrTVLENTEYGLEV 132
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSI--FNYRDVLEFRR-RVGMLFQRPNPFPM-SIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 133 QG-VDKAERQARAEKALDNANLL-AFKDQY---PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELL 207
Cdd:PRK14271 128 HKlVPRKEFRGVAQARLTEVGLWdAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 208 ELqeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAN----DYVRAFTEDIDRSK 271
Cdd:PRK14271 208 SL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaetaRYVAGLSGDVKDAK 273
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
49-262 |
2.20e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 119.08 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIE-P---TSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQN--FGLFPQRTV 122
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpmTSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEV-QGVDKAERQARAEKAL------DNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PRK11022 109 GFQIMEAIKVhQGGNKKTRRQRAIDLLnqvgipDPASRL---DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 196 PLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQA 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-263 |
2.24e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.45 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTS-----GSIYLDGEDISTMdKEELLEVRRQkMSMVFQNFGLFPQrT 121
Cdd:PRK14258 27 SMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYER-RVNLNRLRRQ-VSMVHPKPNLFPM-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENTEYGLEVQGVD-KAERQARAEKALDNANLL-AFKDQYPS---QLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:PRK14258 104 VYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWdEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 197 LIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKD-----GKVVQVGTGEDILTNPANDYVRAF 263
Cdd:PRK14258 184 IASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-240 |
3.31e-30 |
|
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: 115.99 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEILEKTGAT--VGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGE----DISTMDKEEL 99
Cdd:COG4778 8 ENLSKTFTLHLQGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 100 LEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANL---LAfkDQYPSQLSGGMQQRVGLAR 176
Cdd:COG4778 88 LALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLperLW--DLPPATFSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 177 ALANNPEILLMDEAFSALDPLIRRDMQDELLELQeSQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
38-255 |
4.70e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 119.56 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELleVRR-----QKMSMVFQ 112
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA--SRRvasvpQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 113 nfglFPQRTVLE--NTEYGLEVQGVDKAERQArAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:PRK09536 92 ----FDVRQVVEmgRTPHRSRFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 191 FSALDplIRRDMQD-ELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK09536 167 TASLD--INHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
47-252 |
4.80e-30 |
|
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: 121.39 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrrqkmsmvFQNFGLFPQR------ 120
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-----------GRHIGYLPQDvelfdg 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TVLENTeyglevqgvdkaerqAR-----AEKALDNANL-------LAFKDQY-------PSQLSGGMQQRVGLARALANN 181
Cdd:COG4618 421 TIAENI---------------ARfgdadPEKVVAAAKLagvhemiLRLPDGYdtrigegGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
45-242 |
7.97e-30 |
|
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: 114.88 E-value: 7.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLF-ARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLevQGVDKAERQARAEKALDNANLLAFKDQYP-------SQLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:cd03248 107 NIAYGL--QSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 198 IRRDMQDELLELQESQqkTIIFISHDLNEALRiGDRIAIMKDGKV 242
Cdd:cd03248 185 SEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
47-247 |
1.08e-29 |
|
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: 121.66 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMdkeelLEVRRQKMSMVFQNFGLFPQRTVLENT 126
Cdd:TIGR01257 950 NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETN-----LDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDEL 206
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 682099688 207 LELQESqqKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGT 247
Cdd:TIGR01257 1105 LKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
50-256 |
1.11e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.60 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 50 IEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFG--LFPQrTVLENTE 127
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV----RSKVGLVFQDPDdqVFSS-TVWDDVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 128 YGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQdELL 207
Cdd:PRK13647 103 FGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM-EIL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 682099688 208 ELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGtGEDILTNPA 256
Cdd:PRK13647 182 DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
45-252 |
4.81e-29 |
|
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: 119.07 E-value: 4.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYLPQEPYIF-SGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 N----TEYGLEVQGVDKAERQARAEKALDNANLLAFKD--QYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLI 198
Cdd:TIGR01193 567 NlllgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTElsEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 199 RRDMQDELLELQEsqqKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDIL 252
Cdd:TIGR01193 647 EKKIVNNLLNLQD---KTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-262 |
6.46e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.42 E-value: 6.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 35 EKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGE----------DISTMDKEELLEVRR 104
Cdd:PRK10261 24 QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 105 QKMSMVFQN--FGLFPQRTVLENTEYGLEV-QGVDKAERQARAEKALDNANL---LAFKDQYPSQLSGGMQQRVGLARAL 178
Cdd:PRK10261 104 ADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 179 ANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAND 258
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....
gi 682099688 259 YVRA 262
Cdd:PRK10261 264 YTRA 267
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
44-255 |
1.43e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.97 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 44 YDANIEIEEGEIFV--------IMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdKEELLEVRRqKMSMVFQNFG 115
Cdd:PRK13652 13 YSGSKEALNNINFIaprnsriaVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRK-FVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 --LFpQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:PRK13652 89 dqIF-SPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 194 LDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
38-259 |
2.23e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 113.67 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKS----TLIRLL--NRLIeptSGSIYLDGEDISTMDKEELLEVRRQKMSMVF 111
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaaNGRI---GGSATFNGREILNLPEKELNKLRAEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 112 QN--FGLFPQRTVLENTeygLEV----QGVDKAERQARAEKALDNANLLAFKDQ---YPSQLSGGMQQRVGLARALANNP 182
Cdd:PRK09473 104 QDpmTSLNPYMRVGEQL---MEVlmlhKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 183 EILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDY 259
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-251 |
6.58e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.99 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeelLEVRRQ--KMSmvfQNFG 115
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD----IATRRRvgYMS---QAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQRTVLENTE-----YGLEvqgvdKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:NF033858 350 LYGELTVRQNLElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 191 FSALDPlIRRDMQDELL-ELQESQQKTiIFIS-HDLNEALRIgDRIAIMKDGKVVQVGTGEDI 251
Cdd:NF033858 425 TSGVDP-VARDMFWRLLiELSREDGVT-IFIStHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
45-247 |
1.22e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.32 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEeLLEVRrQKMSMVFQ--NFGLFpQRTV 122
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMKLR-ESVGMVFQdpDNQLF-SASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDM 202
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 203 QDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGT 247
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
45-247 |
1.67e-27 |
|
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: 108.35 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLE 124
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLF-SGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NteyglevqgVDKAERQARAE--KALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:cd03244 97 N---------LDPFGEYSDEElwQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 192 SALDPLIRRDMQDELLElqESQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGT 247
Cdd:cd03244 168 ASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDS 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-261 |
1.78e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 113.65 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKS-TLIRLLNRLIEP----TSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQN--FG 115
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQRTvLENTEYglEVQGVDKAERQ--ARAE--KALDN------ANLLAfkdQYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:PRK15134 105 LNPLHT-LEKQLY--EVLSLHRGMRReaARGEilNCLDRvgirqaAKRLT---DYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 186 LMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
38-253 |
3.85e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.51 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEllevrRQKMSMVFQNFGLF 117
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-----RQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:PRK13537 93 PDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 198 IRRDMQDELLELQeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:PRK13537 173 ARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-254 |
6.98e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.56 E-value: 6.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRL-IEPTSGSIYLDGEDISTMDKEELLE 101
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 102 VRRQKMSMVFQ--NFGLFpQRTVLENTEYGLEVQGVDKAERQARAEKALDnanLLAFKDQY----PSQLSGGMQQRVGLA 175
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLF-QETIEKDIAFGPVNLGENKQEAYKKVPELLK---LVQLPEDYvkrsPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 176 RALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
36-226 |
8.57e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 36 KTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFG 115
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQrTVLENTEYGLEVQGvDKAERQARAeKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:PRK10247 92 LFGD-TVYDNLIFPWQIRN-QQPDPAIFL-DDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190
....*....|....*....|....*....|..
gi 682099688 195 DPLIRRDMQDELLELQESQQKTIIFISHDLNE 226
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-249 |
1.42e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.02 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 26 ENVSKTEILEKT-GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLI--EPTSGS-IYLDGediSTMDKEELL- 100
Cdd:PRK09984 2 QTIIRVEKLAKTfNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLG---RTVQREGRLa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 101 -EVR--RQKMSMVFQNFGLFPQRTVLENTEYGLE---------VQGVDKAERQaRAEKALDNANLLAFKDQYPSQLSGGM 168
Cdd:PRK09984 79 rDIRksRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 169 QQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTG 248
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
.
gi 682099688 249 E 249
Cdd:PRK09984 238 Q 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
47-254 |
2.33e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.68 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrTVLENT 126
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQAISVVSQRVHLFSA-TLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGLEVQGVDK---AERQARAEKALDNANLLafkDQY----PSQLSGGMQQRVGLARALANNPEILLMDEAFSALDplir 199
Cdd:PRK11160 435 LLAAPNASDEAlieVLQQVGLEKLLEDDKGL---NAWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD---- 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 200 RDMQDELLEL--QESQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK11160 508 AETERQILELlaEHAQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-251 |
2.43e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 110.26 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 23 MVQENVSKTEILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEV 102
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 103 rrqKMSMVFQNFGLFPQRTVLENTEYG-------LEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLA 175
Cdd:PRK09700 81 ---GIGIIYQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 176 RALANNPEILLMDEAFSALDP-------LIRRDMQDEllelqesqQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTG 248
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNkevdylfLIMNQLRKE--------GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
...
gi 682099688 249 EDI 251
Cdd:PRK09700 230 SDV 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
44-252 |
3.11e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.49 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 44 YDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIstmdKEELLEVRRQKMSMVFQNFGLFpQRTVL 123
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL----RDYTLASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 ENTEYGLEvqgvDKAERqARAEKALDNANLLAFKDQYPS-----------QLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:PRK11176 435 NNIAYART----EQYSR-EQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 193 ALDPLIRRDMQDELLELQesQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK11176 510 ALDTESERAIQAALDELQ--KNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
38-237 |
4.09e-26 |
|
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: 109.68 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeelLEVRRQKMSMVFQNFGLF 117
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQrTVLENTEYGLEVQGVDKAERQARAEKALDNANLL----AFK-DQYPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:TIGR02857 409 AG-TIAENIRLARPDASDAEIREALERAGLDEFVAALpqglDTPiGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 193 ALDPLIRRDMQDELLELqeSQQKTIIFISHDLNEALRIgDRIAIM 237
Cdd:TIGR02857 488 HLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
47-246 |
1.44e-25 |
|
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: 102.01 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEellevRRQKMSMVFQNFGLFpQRTVLENT 126
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPYLF-DTTLRNNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 eyGLevqgvdkaerqaraekaldnanllafkdqypsQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRdmqdEL 206
Cdd:cd03247 96 --GR--------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER----QL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 682099688 207 LEL--QESQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03247 138 LSLifEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
43-254 |
2.50e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.05 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMdkeELLEVRRQKMSMVFQNFGLFPQRTV 122
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEV-QGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:PRK10895 96 YDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 682099688 202 MQDELLELQESQQKTIIfISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLI-TDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-251 |
2.97e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 32 EILEKTGATVG--VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLevrRQKMSM 109
Cdd:COG1129 255 VVLEVEGLSVGgvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI---RAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 110 VFQN---FGLFPQRTVLENTeyGLEVQG-------VDKAERQARAEKALDnanLLAFK----DQYPSQLSGGMQQRVGLA 175
Cdd:COG1129 332 VPEDrkgEGLVLDLSIRENI--TLASLDrlsrgglLDRRRERALAEEYIK---RLRIKtpspEQPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 176 RALANNPEILLMDEafsaldP--------------LIRrdmqdELLElqesQQKTIIFISHDLNEALRIGDRIAIMKDGK 241
Cdd:COG1129 407 KWLATDPKVLILDE------PtrgidvgakaeiyrLIR-----ELAA----EGKAVIVISSELPELLGLSDRILVMREGR 471
|
250
....*....|
gi 682099688 242 VVQVGTGEDI 251
Cdd:COG1129 472 IVGELDREEA 481
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-253 |
4.25e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.14 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELleVRRqkMSMVFQNFGLFPQRTVLE 124
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--ARR--IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYG------LEVQGvdKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLI 198
Cdd:PRK10253 101 LVARGryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 199 RRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-243 |
5.31e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKV---KPALKmvqenvskteilektgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT 80
Cdd:COG1101 2 LELKNLSKTFNPGTvneKRALD----------------------GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDISTMDkeellEVRRQKM-SMVFQN--FGLFPQRTVLEN--------TEYGLeVQGVDKAERQARAE--KA 147
Cdd:COG1101 60 SGSILIDGKDVTKLP-----EYKRAKYiGRVFQDpmMGTAPSMTIEENlalayrrgKRRGL-RRGLTKKRRELFREllAT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 148 LDN--ANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPlirrDMQDELLELQE----SQQKTIIFIS 221
Cdd:COG1101 134 LGLglENRL---DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEkiveENNLTTLMVT 206
|
250 260
....*....|....*....|..
gi 682099688 222 HDLNEALRIGDRIAIMKDGKVV 243
Cdd:COG1101 207 HNMEQALDYGNRLIMMHEGRII 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
38-259 |
7.41e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 102.22 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFglf 117
Cdd:TIGR02323 14 GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLMRTEWGF--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 pqrtVLENTEYGLEVQ---GVDKAER------------QARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANN 181
Cdd:TIGR02323 91 ----VHQNPRDGLRMRvsaGANIGERlmaigarhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDY 259
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPY 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
38-256 |
1.56e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 100.72 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLevrRQKMSMVFQNFGLF 117
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM---REAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGlevqG--VDKAERQARAEKALD-NANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL 194
Cdd:PRK11614 93 SRMTVEENLAMG----GffAERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 195 DPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPA 256
Cdd:PRK11614 169 APIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
47-249 |
1.99e-24 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 105.05 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrtVLent 126
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY----RKLFSAVFTDFHLFDQ--LL--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 eyGLEVQGVDKAERQARAEKaLDNANLLAFKDQYPS--QLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:PRK10522 414 --GPEGKPANPALVEKWLER-LKMAHKLELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 205 ELLELQESQQKTIIFISHDlNEALRIGDRIAIMKDGKVVQVgTGE 249
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL-TGE 533
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
38-259 |
9.21e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.23 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMsmvfqnfglf 117
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRL---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 pQRT----VLENTEYGLEVQ---GVDKAER------------QARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARA 177
Cdd:PRK11701 87 -LRTewgfVHQHPRDGLRMQvsaGGNIGERlmavgarhygdiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 178 LANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPAN 257
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
..
gi 682099688 258 DY 259
Cdd:PRK11701 246 PY 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-252 |
1.23e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.29 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 27 NVSKTeilekTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKeelleVRRQK 106
Cdd:PRK13536 46 GVSKS-----YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-----LARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 107 MSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILL 186
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 187 MDEAFSALDPLIRRDMQDELLELQeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| CBS_pair_ABC_Gly_Pro_assoc |
cd09831 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
277-386 |
1.50e-23 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. 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. They 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. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341402 [Multi-domain] Cd Length: 116 Bit Score: 94.55 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 277 NIMIQPLTTNI--SVDGPNVALKKMATEEVSGLVAVDRNRQFKGFLTSDAAIKARRDQI-PLTDVLV-DMQTVSQDMLVA 352
Cdd:cd09831 1 DIARKTQVTVIekTGDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENAqSLEDAFLtDVETVPADTSLS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 682099688 353 DLMPLISDSPSPLAVVDG-GRLKGVVIRGRVLEAL 386
Cdd:cd09831 81 DILGLVASAPCPLPVVDEdGRYLGVISKASLLETL 115
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
45-243 |
7.20e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVR-------RQKMsmvfqnfGLF 117
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGvayipedRLGR-------GLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLEN---TEYGLEVQG----VDKAERQARAEKALDnanllAFKDQYPS------QLSGGMQQRVGLARALANNPEI 184
Cdd:COG3845 349 PDMSVAENlilGRYRRPPFSrggfLDRKAIRAFAEELIE-----EFDVRTPGpdtparSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 185 LLMDEAFSALDP----LIRRdmqdELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:COG3845 424 LIAAQPTRGLDVgaieFIHQ----RLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-246 |
8.76e-23 |
|
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: 94.54 E-value: 8.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 27 NVSKTEILEKTGATVgVYDANIEIEEGEIFVIMGLSGSGKSTLIRLL-NRLIEP-TSGSIYLDGEDIStmdkeelLEVRR 104
Cdd:cd03213 10 TVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLINGRPLD-------KRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 105 QKMSMVFQNFGLFPQRTVLENTEYGLEVQGvdkaerqaraekaldnanllafkdqypsqLSGGMQQRVGLARALANNPEI 184
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 185 LLMDEAFSALDPLIRRDMQDELLELQeSQQKTIIFISHDL-NEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
47-262 |
9.05e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 97.67 E-value: 9.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP----TSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQN--FGLFPQR 120
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEpsSCLDPSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TVLENTEYGL---EVQGVDKAERQARAEKALdnaNLL---AFKDQ------YPSQLSGGMQQRVGLARALANNPEILLMD 188
Cdd:COG4170 107 KIGDQLIEAIpswTFKGKWWQRFKWRKKRAI---ELLhrvGIKDHkdimnsYPHELTEGECQKVMIAMAIANQPRLLIAD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 189 EAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:COG4170 184 EPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKA 257
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-243 |
2.11e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 94.71 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPA-LKMVQENVSKTEILEKtgatVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSG 82
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPgLIGSLKSLFKRKYREV----EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 83 SIYLDGEDISTmDKEELLevrrQKMSMVFQnfglfpQRT-------VLENTEYGLEVQGVDKAERQARAEKALDNANLLA 155
Cdd:cd03267 77 EVRVAGLVPWK-RRKKFL----RRIGVVFG------QKTqlwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 156 FKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIA 235
Cdd:cd03267 146 LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
....*...
gi 682099688 236 IMKDGKVV 243
Cdd:cd03267 226 VIDKGRLL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
47-255 |
4.53e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIePTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrTVLENT 126
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESW----RKHLSWVGQNPQLPHG-TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGlevqgvDKAERQARAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSALd 195
Cdd:PRK11174 444 LLG------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASL- 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 196 plirrDMQDELLELQ----ESQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK11174 517 -----DAHSEQLVMQalnaASRRQTTLMVTHQL-EDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-251 |
5.26e-22 |
|
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: 97.57 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRL--IEPTSGSI-----------YLD-----GE--------------DIS 92
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvGEpcpvcggtlepeevDFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 93 TMDKEELLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRV 172
Cdd:TIGR03269 98 NLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 173 GLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDI 251
Cdd:TIGR03269 178 VLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
47-245 |
2.36e-21 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 95.64 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkEELLEVRRQKMSMVFQNFGLFPqrtvlent 126
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT----ADNREAYRQLFSAVFSDFHLFD-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 eyglEVQGVDKAERQARAE---KALDNANLLAFKDQYPS--QLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:COG4615 420 ----RLLGLDGEADPARARellERLELDHKVSVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 202 MQDELL-ELQEsQQKTIIFISHD---LNEAlrigDRIAIMKDGKVVQV 245
Cdd:COG4615 496 FYTELLpELKA-RGKTVIAISHDdryFDLA----DRVLKMDYGKLVEL 538
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
45-252 |
3.45e-21 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 92.19 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEdistmdkeellevrrqkMSMVFQNFGLFPQRTVLE 124
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQD 204
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 205 ELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK13546 185 KIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
43-262 |
4.71e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKS-TLIRLLNRL---IEPTSGSIYLDGEDISTMDkeelleVRRQKMSMVFQN----F 114
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCA------LRGRKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 GlfPQRTVLEN---TEYGLEVQGVDKAERQARAEKALDNANLLAfkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:PRK10418 93 N--PLHTMHTHareTCLALGKPADDATLTAALEAVGLENAARVL--KLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 192 SALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNPANDYVRA 262
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRS 239
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
49-257 |
7.26e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLirlLNRL--IEPTSGSIYLDGEDISTMDKEELLEVR----RQKMS---M-VFQNFGLFP 118
Cdd:COG4138 18 QVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAELARHRaylsQQQSPpfaMpVFQYLALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 QRTVlenteyglevqgvdkaeRQARAEKALDN-ANLLAFKDQYP---SQLSGGMQQRVGLARAL-----ANNPE--ILLM 187
Cdd:COG4138 95 PAGA-----------------SSEAVEQLLAQlAEALGLEDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 188 DEAFSALDpLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTnPAN 257
Cdd:COG4138 158 DEPMNSLD-VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PEN 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
38-224 |
1.14e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.58 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLF 117
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 pQRTVLENTEYGLEvqGVDKAErqarAEKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILL 186
Cdd:TIGR02868 422 -DTTVRENLRLARP--DATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 682099688 187 MDEAFSALDPLIRRDMQDELleLQESQQKTIIFISHDL 224
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
43-237 |
1.31e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGED-------ISTMDKEELLEVrRQKMSMvfqnfG 115
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayvpqRSEVPDSLPLTV-RDLVAM-----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQRTVLenteyglevqGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:NF040873 82 RWARRGLW----------RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 682099688 196 PLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIgDRIAIM 237
Cdd:NF040873 152 AESRERIIALLAEEHA-RGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
45-246 |
3.04e-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: 88.48 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP---TSGSIYLDGEdistmdkeellEVRRQKM----SMVFQNFGLF 117
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ-----------PRKPDQFqkcvAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGLEVQG---VDKAERQARAE-KALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:cd03234 94 PGLTVRETLTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 682099688 194 LDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVG 246
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
49-255 |
3.54e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIePTSGSIYLDGEDISTMDKEELLEVR-------RQKMSM-VFQNFGLF-PQ 119
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAMpVFQYLTLHqPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 120 RTVLENTEYGLE-----VQGVDKAERQAraekaldnanllafkdqypSQLSGGMQQRVGLARAL-----ANNPE--ILLM 187
Cdd:PRK03695 97 KTRTEAVASALNevaeaLGLDDKLGRSV-------------------NQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 188 DEAFSALDpLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK03695 158 DEPMNSLD-VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
49-247 |
7.27e-20 |
|
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: 87.08 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLENtey 128
Cdd:cd03369 30 KVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL----RSSLTIIPQDPTLF-SGTIRSN--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 129 glevqgVDKAERQARAE--KALDNAnllafkdQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL----DPLIRRDM 202
Cdd:cd03369 102 ------LDPFDEYSDEEiyGALRVS-------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQKTI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 203 QDELlelqesQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGT 247
Cdd:cd03369 169 REEF------TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-241 |
1.20e-19 |
|
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: 86.37 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIR-LLNRLiEPTSGSIYLDGedistmdkeellevrrqkmsmvfqNFGLFPQ---- 119
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPG------------------------SIAYVSQepwi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 120 --RTVLENTEYGLEVqgvdkaeRQARAEKALDNANL------LAFKDQYP-----SQLSGGMQQRVGLARALANNPEILL 186
Cdd:cd03250 78 qnGTIRENILFGKPF-------DEERYEKVIKACALepdleiLPDGDLTEigekgINLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 187 MDEAFSALDPLIRRDMQDELL--ELQESqqKTIIFISHDLnEALRIGDRIAIMKDGK 241
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENCIlgLLLNN--KTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
45-222 |
1.32e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYL-DGEDIstmdkeellevrrqkmsmvfqnfgLF-PQR-- 120
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV------------------------LFlPQRpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 ----TVLENTEYGLEVQGVDKAErqarAEKALDNANLLAFKDQY------PSQLSGGMQQRVGLARALANNPEILLMDEA 190
Cdd:COG4178 437 lplgTLREALLYPATAEAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|....
gi 682099688 191 FSALDPlirrDMQDELLEL--QESQQKTIIFISH 222
Cdd:COG4178 513 TSALDE----ENEAALYQLlrEELPGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-242 |
1.44e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 6 IEHLTKIFGKKVkpalkmvqenvskteILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIY 85
Cdd:COG0488 1 LENLSKSFGGRP---------------LLD---------DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 86 LDgedistmdkeellevRRQKMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAER------------------------- 140
Cdd:COG0488 57 IP---------------KGLRIGYLPQEPPLDDDLTVLDTVLDGDAELRALEAELeeleaklaepdedlerlaelqeefe 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 141 -------QARAEKALDNanlLAFKDQYP----SQLSGGMQQRVGLARALANNPEILLMDEafsaldP---LirrDMQD-E 205
Cdd:COG0488 122 alggweaEARAEEILSG---LGFPEEDLdrpvSELSGGWRRRVALARALLSEPDLLLLDE------PtnhL---DLESiE 189
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 682099688 206 LLE--LQESqQKTIIFISHD---LNealRIGDRIAIMKDGKV 242
Cdd:COG0488 190 WLEefLKNY-PGTVLVVSHDryfLD---RVATRILELDRGKL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
42-254 |
1.85e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 42 GVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFPQRT 121
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 122 VLENT------EYGLEVQGVDKAERQARAEKALDNAnlLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PRK15439 358 LAWNVcalthnRRGFWIKPARENAVLERYRRALNIK--FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 196 PLIRRDMQDeLLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK15439 436 VSARNDIYQ-LIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVD 493
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-254 |
5.73e-19 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 88.79 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 3 KVKIEHLTKIFGKKVKPALKMvqenvskTEILEKTGATVGVYDAN---IEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP 79
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPFDKL-------KDLFFRSKDGEYHYALNnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 80 TSGSIYLDGEdistmdkeellevrrqkMSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQ 159
Cdd:PRK13545 77 NKGTVDIKGS-----------------AALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 160 YPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKD 239
Cdd:PRK13545 140 PVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLSQVKSFCTKALWLHY 218
|
250
....*....|....*
gi 682099688 240 GKVVQVGTGEDILTN 254
Cdd:PRK13545 219 GQVKEYGDIKEVVDH 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
32-267 |
6.29e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 86.78 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 32 EILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLL----NRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKM 107
Cdd:PRK15093 12 EFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRKLVGHNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 108 SMVFQNfglfPQRTVLENTEYGLE-VQGVD----KAE-------RQARAEKALDNANLLAFKD---QYPSQLSGGMQQRV 172
Cdd:PRK15093 92 SMIFQE----PQSCLDPSERVGRQlMQNIPgwtyKGRwwqrfgwRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 173 GLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
250
....*....|....*
gi 682099688 253 TNPANDYVRAFTEDI 267
Cdd:PRK15093 248 TTPHHPYTQALIRAI 262
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
53-196 |
7.04e-19 |
|
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: 83.95 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkeELLEVRRQKMSMVFQNFGLFPQRTVLENteygLEV 132
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELSALEN----LHF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 133 QGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:TIGR01189 97 WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
47-195 |
1.79e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.93 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKE---ELLEVRRQKmsmvfqnfGLFPQRTVL 123
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLLYLGHQP--------GIKTELTAL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 124 ENTEYGLEVQGVdkAERQARAEkALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PRK13538 93 ENLRFYQRLHGP--GDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-312 |
2.44e-18 |
|
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: 86.42 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 33 ILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRlIEPT---SGSIYLDGEDISTmdkEELLEVRRQKMSM 109
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKA---SNIRDTERAGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 110 VFQNFGLFPQRTVLENTEYGLEV----QGVDKAERQARAEKALDNANLLAFKDQYP-SQLSGGMQQRVGLARALANNPEI 184
Cdd:TIGR02633 83 IHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 185 LLMDEAFSAldpLIRRDMQDELLELQESQQKTI--IFISHDLNEALRIGDRIAIMKDGKvvQVGTG-------EDILTNP 255
Cdd:TIGR02633 163 LILDEPSSS---LTEKETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVIRDGQ--HVATKdmstmseDDIITMM 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 256 ANDYVRAF--TEDID-RSKVLTAENIMI-QPLTTNIS-VDGPNVALKKMATEEVSGLVAVDR 312
Cdd:TIGR02633 238 VGREITSLypHEPHEiGDVILEARNLTCwDVINPHRKrVDDVSFSLRRGEILGVAGLVGAGR 299
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
45-255 |
2.96e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQrTVLE 124
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVDKAERQARAEKALDNanLLAFKDQYPSQ-------LSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:PRK10789 408 NIALGRPDATQQEIEHVARLASVHDD--ILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 198 IRRDMQDELleLQESQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PRK10789 486 TEHQILHNL--RQWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-266 |
4.01e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.75 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 32 EILEKTGATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRlIEPT---SGSIYLDGEDI---STMDKEellevrRQ 105
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELqasNIRDTE------RA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMSMVFQNFGLFPQRTVLENTEYGLEVQ--GV-DKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNP 182
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITpgGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 183 EILLMDEAFSALDPLIRRDMQDELLELQeSQQKTIIFISHDLNEALRIGDRIAIMKDGKvvqvgtgeDILTNPAndyvRA 262
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGR--------HIGTRPA----AG 229
|
....
gi 682099688 263 FTED 266
Cdd:PRK13549 230 MTED 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
53-254 |
6.63e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkeELLEVRRQKMS--MVFQNFGLFPQRTVLENTEYGL 130
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RLTPAKAHQLGiyLVPQEPLLFPNLSVKENILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 131 evqgvdkAERQARAEKAldnANLLAfkdQYPSQLSGGM---------QQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:PRK15439 112 -------PKRQASMQKM---KQLLA---ALGCQLDLDSsagslevadRQIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 682099688 202 MQDELLELQeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PRK15439 179 LFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
47-222 |
1.35e-17 |
|
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: 79.51 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYL-DGEDIstmdkeellevrrqkmsmvfqnfgLF-PQRTVLe 124
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDL------------------------LFlPQRPYL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 nteygleVQGvdkaerqaraekaldnaNLlafKDQ--YPSQ--LSGGMQQRVGLARALANNPEILLMDEAFSALDPlirr 200
Cdd:cd03223 76 -------PLG-----------------TL---REQliYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---- 124
|
170 180
....*....|....*....|..
gi 682099688 201 DMQDELLELQESQQKTIIFISH 222
Cdd:cd03223 125 ESEDRLYQLLKELGITVISVGH 146
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
53-252 |
2.20e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFPQRTVLENTEYGLE- 131
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQLPAAEGMTVRELVAIGRYp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 132 ---VQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDplIRRdmQDELLE 208
Cdd:PRK10575 113 whgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IAH--QVDVLA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 682099688 209 L--QESQQK--TIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK10575 189 LvhRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
45-244 |
2.27e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRlIEPT---SGSIYLDGE-----DIStmDKEELLEVrrqkmsMVFQNFGL 116
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEvcrfkDIR--DSEALGIV------IIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 117 FPQRTVLENTEYGLEVQ--GV-DKAERQARAEKALDNANLlafkDQYPSQLSG----GMQQRVGLARALANNPEILLMDE 189
Cdd:NF040905 90 IPYLSIAENIFLGNERAkrGViDWNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 190 AFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQ 244
Cdd:NF040905 166 PTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-309 |
3.61e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVK-PALKMVQENVSKTEILEKTGatvgVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSG 82
Cdd:COG4586 2 IEVENLSKTYRVYEKePGLKGALKGLFRREYREVEA----VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 83 SIYLDGEDISTmDKEELLevrrQKMSMVfqnFGlfpQRT-------VLENTEYGLEVQGVDKAERQARAEKALDNANLLA 155
Cdd:COG4586 78 EVRVLGYVPFK-RRKEFA----RRIGVV---FG---QRSqlwwdlpAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 156 FKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIA 235
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVI 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 236 IMKDGKVVQVGTGEDILTNPAND-YVRAFTEDidrskvlTAENIMIQPLTTNISVDGPNVALKKMATEEVSGLVA 309
Cdd:COG4586 227 VIDHGRIIYDGSLEELKERFGPYkTIVLELAE-------PVPPLELPRGGEVIEREGNRVRLEVDPRESLAEVLA 294
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
58-270 |
3.79e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStMDKEELLEVRrQKMSMVFQNfglfPQRTVL-----ENTEYGLEV 132
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQD----PEQQIFytdidSDIAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 133 QGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQdELLELQES 212
Cdd:PRK13638 106 LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI-AIIRRIVA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 213 QQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGT-GEdiltnpandyVRAFTEDIDRS 270
Cdd:PRK13638 185 QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGApGE----------VFACTEAMEQA 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-246 |
5.47e-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: 78.72 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 28 VSKTEILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLL--NRLIEPTSGSIYLDGEDISTMDKEEllevrRQ 105
Cdd:cd03217 10 VGGKEILK---------GVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 106 KMS--MVFQnfglfpqrtvlenteYGLEVQGVDkaerqaraekaldNANLLAFKDQypsQLSGGMQQRVGLARALANNPE 183
Cdd:cd03217 76 RLGifLAFQ---------------YPPEIPGVK-------------NADFLRYVNE---GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 184 ILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRI-GDRIAIMKDGKVVQVG 246
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
45-244 |
6.25e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEvrrQKMSMVFQNFGLFPQRTVLE 124
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA---AGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 N-------TEYGLevqgVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL--- 194
Cdd:PRK11288 99 NlylgqlpHKGGI----VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLsar 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 195 --DPLIR--RDMQDEllelqesqQKTIIFISHDLNEALRIGDRIAIMKDGKVVQ 244
Cdd:PRK11288 175 eiEQLFRviRELRAE--------GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
45-240 |
6.68e-17 |
|
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: 78.91 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGLFpQRTVLE 124
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGlevQGVDKAERQARAEKA--LDNANLLAFKDQYPS-----QLSGGMQQRVGLARALANNPEILLMDEAFSALD-P 196
Cdd:cd03290 98 NITFG---SPFNKQRYKAVTDACslQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDiH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 682099688 197 LIRRDMQDELLELQESQQKTIIFISHDLnEALRIGDRIAIMKDG 240
Cdd:cd03290 175 LSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
27-249 |
1.04e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.96 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 27 NVSKTEILEktgatvGVydaNIEIEEGEIFVIMGLSGSGKSTLIRLL--NRLIEPTSGSIYLDGEDISTMDKEEllevRR 104
Cdd:COG0396 9 SVEGKEILK------GV---NLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDE----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 105 QK-MSMVFQnfglfpqrtvlenteYGLEVQGVD-----KAERQARAEKALDNANLLAFKDQYPSQL-------------- 164
Cdd:COG0396 76 RAgIFLAFQ---------------YPVEIPGVSvsnflRTALNARRGEELSAREFLKLLKEKMKELgldedfldryvneg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 165 -SGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQeSQQKTIIFISH-----DLNEAlrigDRIAIMK 238
Cdd:COG0396 141 fSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLR-SPDRGILIITHyqrilDYIKP----DFVHVLV 215
|
250
....*....|.
gi 682099688 239 DGKVVQVGTGE 249
Cdd:COG0396 216 DGRIVKSGGKE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-258 |
1.37e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.00 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 14 GKKVKPALKMVQENVsktEILEKTGATVGVY-DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYL-DGEDI 91
Cdd:PTZ00265 374 GKKLKDIKKIQFKNV---RFHYDTRKDVEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 92 STMDkeelLEVRRQKMSMVFQNFGLFpQRTVLENTEYGL----------------------------------------- 130
Cdd:PTZ00265 451 KDIN----LKWWRSKIGVVSQDPLLF-SNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndm 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 131 --------------EVQGVDKAERQARAEKALDNANLLAFKDQY-------PSQLSGGMQQRVGLARALANNPEILLMDE 189
Cdd:PTZ00265 526 snttdsneliemrkNYQTIKDSEVVDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDE 605
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 190 AFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDILTNPAND 258
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-253 |
3.17e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 19 PALKMVQENVSKTEILEKTGATV----GVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTM 94
Cdd:PRK09700 251 NAMKENVSNLAHETVFEVRNVTSrdrkKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 95 DKeelLEVRRQKMSMVFQN---FGLFPQRTV---------LENTEYGLEVQGVDKAERQARAEKALDnanLLAFK----D 158
Cdd:PRK09700 331 SP---LDAVKKGMAYITESrrdNGFFPNFSIaqnmaisrsLKDGGYKGAMGLFHEVDEQRTAENQRE---LLALKchsvN 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 159 QYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMK 238
Cdd:PRK09700 405 QNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFC 483
|
250
....*....|....*
gi 682099688 239 DGKVVQVGTGEDILT 253
Cdd:PRK09700 484 EGRLTQILTNRDDMS 498
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
49-195 |
3.55e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIstmdkeELLEVRRQKMSMVFQNfGLFPQRTVLENTEY 128
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACHYLGHRN-AMKPALTVAENLEF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 129 GLEVQGvdkaERQARAEKALDNANL-----LAFKDqypsqLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PRK13539 97 WAAFLG----GEELDIAAALEAVGLaplahLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-241 |
3.99e-16 |
|
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: 74.79 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpalkmvqenvskteILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:cd03221 1 IELENLSKTYGGKL---------------LLK---------DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IyldgedistmdkeellevrrqkmsmvfqnfglfpqrTVLENTEYGlevqgvdkaerqaraekaldnanllafkdqYPSQ 163
Cdd:cd03221 57 V------------------------------------TWGSTVKIG------------------------------YFEQ 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 164 LSGGMQQRVGLARALANNPEILLMDEAFSALDPlirrDMQDELLELQESQQKTIIFISHD---LNealRIGDRIAIMKDG 240
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL----ESIEALEEALKEYPGTVILVSHDryfLD---QVATKIIELEDG 143
|
.
gi 682099688 241 K 241
Cdd:cd03221 144 K 144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-260 |
8.52e-16 |
|
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: 79.67 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVKPALKMVqenvskteilektgaTVGVydanieiEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRL---------------CVGV-------RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD 1995
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLDGEDISTmdkeellevrrqKMSMVFQNFGLFPQRTVLENTEYGLE-------VQGVDKAERQARAEKALDNANLLAF 156
Cdd:TIGR01257 1996 ATVAGKSILT------------NISDVHQNMGYCPQFDAIDDLLTGREhlylyarLRGVPAEEIEKVANWSIQSLGLSLY 2063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 157 KDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAI 236
Cdd:TIGR01257 2064 ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAI 2142
|
250 260
....*....|....*....|....
gi 682099688 237 MKDGKVVQVGTGEDILTNPANDYV 260
Cdd:TIGR01257 2143 MVKGAFQCLGTIQHLKSKFGDGYI 2166
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
53-195 |
9.19e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.22 E-value: 9.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGedisTMDKEELLEVRRQKMSMVFQNfGLFPQRTVLENTEYGLEV 132
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLGHAP-GIKTTLSVLENLRFWHAD 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 682099688 133 QGVDKAErqaraeKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:cd03231 101 HSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
45-256 |
1.11e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLL-NRLIEPT-------SGSIYLDGEDISTMDKEELLEVRRQKMSMVFQNFGL 116
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 117 FPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALAN---------NPEILLM 187
Cdd:PRK13547 99 SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 188 DEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILTnPA 256
Cdd:PRK13547 179 DEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PA 246
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
81-253 |
1.40e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.92 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 81 SGSIYLDGEDISTMDKEELlevrRQKMSMVFQNFGLFpQRTVLENTEYGLEVQGVDKAERQARAeKALDNanllaFKDQY 160
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKF-AAIDE-----FIESL 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 161 PSQ-----------LSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLnEALR 229
Cdd:PTZ00265 1345 PNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIK 1423
|
170 180
....*....|....*....|....*....
gi 682099688 230 IGDRIAIM----KDGKVVQV-GTGEDILT 253
Cdd:PTZ00265 1424 RSDKIVVFnnpdRTGSFVQAhGTHEELLS 1452
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
45-243 |
1.67e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.85 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEvrrQKMSMVFQNFGLFPQRTVLE 124
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NT---EYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRD 201
Cdd:PRK10982 93 NMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 682099688 202 MQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:PRK10982 173 LFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
45-245 |
2.20e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIE--PTSGSIYLDGEDIStmdkeellevrrqkmsmvfqnfglfPQRTV 122
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG-------------------------REASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENteYGLEVQGVDKAERQARAeKALDNANLLAfkdqYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDM 202
Cdd:COG2401 103 IDA--IGRKGDFKDAVELLNAV-GLSDAVLWLR----RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 203 QDELLELQESQQKTIIFISH--DLNEALrIGDRIAIMKDGKVVQV 245
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGVPEE 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
46-243 |
2.78e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 46 ANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELL--------EVRRQKmsmvfqnfGLF 117
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragimlcpEDRKAE--------GII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTE---------YGLEVQG---VDKAERQARAekaldnanlLAFKDQYPSQ----LSGGMQQRVGLARALANN 181
Cdd:PRK11288 344 PVHSVADNINisarrhhlrAGCLINNrweAENADRFIRS---------LNIKTPSREQlimnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
49-249 |
3.65e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEP---TSGSIYLDGEdisTMDKEELlevrrQKMSMVFQNFGLF-PQRTVLE 124
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEM-----RAISAYVQQDDLFiPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQ---GVDKAERQARAEKALDNANLLAFKD---QYPSQ---LSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:TIGR00955 119 HLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 196 PLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGE 249
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-264 |
3.78e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 28 VSKTEILEKTGATvGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEVRRQKM 107
Cdd:PRK15056 9 VNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 108 SmVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLM 187
Cdd:PRK15056 88 E-VDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 188 DEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDrIAIMKDGKVVQVGTGEDILTnpANDYVRAFT 264
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT--AENLELAFS 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-243 |
4.21e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpalkmvqenvskteILEktgatvgvyDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS 83
Cdd:COG0488 316 LELEGLSKSYGDKT---------------LLD---------DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLdGEDIstmdkeellevrrqkmsmvfqNFGLFPQ--------RTVLENTEYGLEvqgvDKAERQARaekaldnaNLLA 155
Cdd:COG0488 372 VKL-GETV---------------------KIGYFDQhqeeldpdKTVLDELRDGAP----GGTEQEVR--------GYLG 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 156 ---FK----DQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPlirrDMQDELLELQESQQKTIIFISHD---LN 225
Cdd:COG0488 418 rflFSgddaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDryfLD 493
|
250
....*....|....*...
gi 682099688 226 ealRIGDRIAIMKDGKVV 243
Cdd:COG0488 494 ---RVATRILEFEDGGVR 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-241 |
5.62e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 5.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYdanieieEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELLEvrrQKMSMVFQNFGLF 117
Cdd:PRK10762 22 GAALNVY-------PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE---AGIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 118 PQRTVLENTEYGLEVQ----GVDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSA 193
Cdd:PRK10762 92 PQLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 682099688 194 LDplirrDMQDELL-----ELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGK 241
Cdd:PRK10762 172 LT-----DTETESLfrvirELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
48-270 |
1.46e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.93 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 48 IEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeeLLEVRRqkmsmvfqNFGLFPQRTVLE--- 124
Cdd:PLN03130 1260 FEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRK--------VLGIIPQAPVLFsgt 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 ---NTEYGLEVQGVDKAERQARAE-KALDNANLLAFKDQYPS---QLSGGMQQRVGLARALANNPEILLMDEAFSALDpl 197
Cdd:PLN03130 1329 vrfNLDPFNEHNDADLWESLERAHlKDVIRRNSLGLDAEVSEageNFSVGQRQLLSLARALLRRSKILVLDEATAAVD-- 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 198 IRRD--MQDELLElqESQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDILTN-------------PAN-DYVR 261
Cdd:PLN03130 1407 VRTDalIQKTIRE--EFKSCTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSNegsafskmvqstgAANaQYLR 1483
|
250
....*....|.
gi 682099688 262 --AFTEDIDRS 270
Cdd:PLN03130 1484 slVFGGDEDRL 1494
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
58-261 |
1.68e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdKEELLEVRRqKMSMVFQNFGLFpQRTVLENTEYGLEVQGVD- 136
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---KFGLTDLRR-VLSIIPQSPVLF-SGTVRFNIDPFSEHNDADl 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 137 -KAERQARAEKALDNA--NLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSAL----DPLIRRDMQDELlel 209
Cdd:PLN03232 1342 wEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVdvrtDSLIQRTIREEF--- 1418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 682099688 210 qesQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDILTNPANDYVR 261
Cdd:PLN03232 1419 ---KSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
56-252 |
1.86e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 56 FV-IMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVFQNfglfPqrTVLENTEYGLEVQG 134
Cdd:PRK10790 369 FVaLVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQD----P--VVLADTFLANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 135 VDKAERQARaeKALDNANLLAFKDQYP-----------SQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQ 203
Cdd:PRK10790 439 RDISEEQVW--QALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 682099688 204 DELLELQEsqQKTIIFISHDLN---EAlrigDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK10790 517 QALAAVRE--HTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-253 |
6.62e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 38 GATVGVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLN--RLIEptSGSIYLDGEDIStmDKEELLEVRRQKMSMVfQNFG 115
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMA--DARHRRAVCPRIAYMP-QGLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 --LFPQRTVLENTE-----YGLevqgvDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMD 188
Cdd:NF033858 87 knLYPTLSVFENLDffgrlFGQ-----DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 189 EAFSALDPLIRR---DMQDELleLQESQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDILT 253
Cdd:NF033858 162 EPTTGVDPLSRRqfwELIDRI--RAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
49-241 |
1.78e-13 |
|
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: 69.74 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTmdKEELLEVR-----RQKMSMVFQNFGLFPQRtvl 123
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQYIKADyegtvRDLLSSITKDFYTHPYF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 eNTEYGLEVQGVDKAERQARaekaldnanllafkdqypsQLSGGMQQRVGLARALANNPEILLMDEAFSALD-------- 195
Cdd:cd03237 96 -KTEIAKPLQIEQILDREVP-------------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmas 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 682099688 196 PLIRRdmqdelleLQESQQKTIIFISHDLNEALRIGDRIaIMKDGK 241
Cdd:cd03237 156 KVIRR--------FAENNEKTAFVVEHDIIMIDYLADRL-IVFEGE 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
47-246 |
3.01e-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: 68.83 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLL--NRLIEPTSGSIYLDGEDISTMDKEEllevR-RQKMSMVFQnfglfpqrtvl 123
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPDE----RaRAGLFLAFQ----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 enteYGLEVQGVD---------KAERQARAEKALD----------NANLLAFKDQYPSQ-----LSGGMQQRVGLARALA 179
Cdd:TIGR01978 85 ----YPEEIPGVSnleflrsalNARRSARGEEPLDlldfekllkeKLALLDMDEEFLNRsvnegFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 180 NNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDlneaLRIGDRIA-----IMKDGKVVQVG 246
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLRE-PDRSFLIITHY----QRLLNYIKpdyvhVLLDGRIVKSG 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
34-224 |
9.70e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 34 LEKTGATVG----VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIyldgedistmdkeelleVRRQKMSM 109
Cdd:PRK09544 7 LENVSVSFGqrrvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 110 vfqnfGLFPQRTVLENTeYGLEVQ-------GVDKAERQArAEKALDNANLLafkdQYPSQ-LSGGMQQRVGLARALANN 181
Cdd:PRK09544 70 -----GYVPQKLYLDTT-LPLTVNrflrlrpGTKKEDILP-ALKRVQAGHLI----DAPMQkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDL 224
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
50-255 |
1.09e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.81 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 50 IEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeeLLEVRRQkMSMVFQNFGLFpQRTVLENTEYG 129
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQ-FSMIPQDPVLF-DGTVRQNVDPF 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 130 LE---------VQGVDKAERQARAEKALDNANLlafkdQYPSQLSGGMQQRVGLARA-LANNPEILLMDEAFSALDPLIR 199
Cdd:PTZ00243 1408 LEassaevwaaLELVGLRERVASESEGIDSRVL-----EGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATANIDPALD 1482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 200 RDMQDELLELQESQqkTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PTZ00243 1483 RQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
42-242 |
1.14e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 42 GVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELL--------EVRRQK-----MS 108
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangivyisEDRKRDglvlgMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 109 mVFQNFGLfpqrTVLENTEYGLeVQGVDKAERQARAekalDNANLLAFK----DQYPSQLSGGMQQRVGLARALANNPEI 184
Cdd:PRK10762 347 -VKENMSL----TALRYFSRAG-GSLKHADEQQAVS----DFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 185 LLMDEAFSALD--------PLIRRDMQDELlelqesqqkTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:PRK10762 417 LILDEPTRGVDvgakkeiyQLINQFKAEGL---------SIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
45-243 |
3.61e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLnrlieptSGSIYLD-GEDISTMDkeeLLEVR------RQKMSMVFqNF--- 114
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQD---LIVARlqqdppRNVEGTVY-DFvae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 GLFPQRTVLENTEYGLEVQGVDKAERQ----ARAEKALDNANLLAFK--------------DQYPSQLSGGMQQRVGLAR 176
Cdd:PRK11147 90 GIEEQAEYLKRYHDISHLVETDPSEKNlnelAKLQEQLDHHNLWQLEnrinevlaqlgldpDAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 682099688 177 ALANNPEILLMDEAFSALDPlirrDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
43-242 |
3.78e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT-SGSIYLDGEDISTMDKEELLevrRQKMSMVFQN---FGLFP 118
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAI---RAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 QRTVLENTEYGL-----EVQGVDKAERQARAEKALDNANLLAFKDQYP-SQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:TIGR02633 353 ILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 682099688 193 ALDPLIRRDMQdELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:TIGR02633 433 GVDVGAKYEIY-KLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
50-196 |
6.50e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 50 IEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDkeellevRRQKMSMVFQNFGLFPQRTVLENTEYG 129
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 130 LEVQGvdkaeRQAR--AEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:PRK13543 107 CGLHG-----RRAKqmPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-254 |
9.34e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYldgedistmdkeelleVRRQKMSMVFQNFGLFpQRTVLENT 126
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV----------------VIRGTVAYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGLEVQgvdkaerQARAEKALDNANLLAFKDQYPS-----------QLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PLN03130 700 LFGSPFD-------PERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 682099688 196 PLIRRDMQDELLElQESQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDILTN 254
Cdd:PLN03130 773 AHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-242 |
1.62e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 27 NVSKTEILEKTGATV----GVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELL-- 100
Cdd:PRK10982 244 NKPGEVILEVRNLTSlrqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 101 ------EVRRQkmSMVFQNFGLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNANLlafkdQYPSQ------LSGGM 168
Cdd:PRK10982 324 gfalvtEERRS--TGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRV-----KTPGHrtqigsLSGGN 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 682099688 169 QQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
43-222 |
3.98e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrrqkmSMVFQNFGLFPQRTV 122
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC--------TYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 123 LENTEYGLEVqgVDKAErqaRAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLiRRDM 202
Cdd:PRK13541 88 FENLKFWSEI--YNSAE---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE-NRDL 161
|
170 180
....*....|....*....|
gi 682099688 203 QDELLELQESQQKTIIFISH 222
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSH 181
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-254 |
4.40e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 19 PALKMVQENVSKTEILEKTGATvgvyDANIEIEEGEIFVIMGLSGSGKSTLIR-LLNRLIEPTSGSIyldgedistmdke 97
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSKPTLS----DINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSV------------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 98 elleVRRQKMSMVFQNFGLFpQRTVLENTEYGLEVQgvdkaerQARAEKALDNANLLAFKDQYPSQ-----------LSG 166
Cdd:PLN03232 676 ----VIRGSVAYVPQVSWIF-NATVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 167 GMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLElQESQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVG 246
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEG 821
|
....*...
gi 682099688 247 TGEDILTN 254
Cdd:PLN03232 822 TFAELSKS 829
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
43-242 |
4.90e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLL-----NRliepTSGSIYLDGEDISTMDKEELLevrRQKMSMVFQN---F 114
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKPVKIRNPQQAI---AQGIAMVPEDrkrD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 GLFPQRTVLEN---------TEYGLevqgVDKAERQARAEKALDNanlLAFKDQYP----SQLSGGMQQRVGLARALANN 181
Cdd:PRK13549 351 GIVPVMGVGKNitlaaldrfTGGSR----IDDAAELKTILESIQR---LKVKTASPelaiARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 182 PEILLMDEAFSALDPLIRRDMQDELLELQEsQQKTIIFISHDLNEALRIGDRIAIMKDGKV 242
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
45-252 |
5.06e-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: 64.58 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrRQKMSMVfqnfglfPQRTVLE 124
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITII-------PQDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NteyGLEVQGVDKAERQARAE--KALDNANLLAFKDQYPSQL-----------SGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:TIGR00957 1373 S---GSLRMNLDPFSQYSDEEvwWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 192 SAL----DPLIRRDMQDELlelqesQQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDIL 252
Cdd:TIGR00957 1450 AAVdletDNLIQSTIRTQF------EDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
47-252 |
5.18e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEELlevrrQKM-SMVFQ------------N 113
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL-----QKLvSDEWQrnntdmlspgedD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 114 FGLFPQRTVLEnteyglevqGVDKAERQARAEKALDNANLLA--FKdqypsQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:PRK10938 98 TGRTTAEIIQD---------EVKDPARCEQLAQQFGITALLDrrFK-----YLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 192 SALDPLIRRDMQDELLELQeSQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDIL 252
Cdd:PRK10938 164 DGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-247 |
9.31e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 9.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGedistmdkeellevrrqKMSMVFQNFGLFPQrTVLE 124
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVQGVdKAERQARAEKALDNANLLAFKDQYP-----SQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIR 199
Cdd:TIGR01271 506 NIIFGLSYDEY-RYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 682099688 200 RDMQDE-LLELQESqqKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGT 247
Cdd:TIGR01271 585 KEIFEScLCKLMSN--KTRILVTSKL-EHLKKADKILLLHEGVCYFYGT 630
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-252 |
1.20e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 61.46 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 3 KVKIEHLTKIFGKKVKPALKMVQENVskteileKTGATVGvydanieieegeifvIMGLSGSGKSTLIRLLNRLIEPTSG 82
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYI-------KPGQKVG---------------ICGRTGSGKSSLSLAFFRMVDIFDG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 83 SIYLDGEDISTMDkeelLEVRRQKMSMVFQN---------FGLFPQRTVLENTEY-GLEVQGVDKaerqarAEKALDnAN 152
Cdd:cd03288 77 KIVIDGIDISKLP----LHTLRSRLSIILQDpilfsgsirFNLDPECKCTDDRLWeALEIAQLKN------MVKSLP-GG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 153 LLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDelLELQESQQKTIIFISHDLNEALRiGD 232
Cdd:cd03288 146 LDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQK--VVMTAFADRTVVTIAHRVSTILD-AD 222
|
250 260
....*....|....*....|
gi 682099688 233 RIAIMKDGKVVQVGTGEDIL 252
Cdd:cd03288 223 LVLVLSRGILVECDTPENLL 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-235 |
1.77e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKvkpalkMVQENVSKTeiLEKtGATVGVYDANieieegeifvimglsGSGKSTLIRLLNRLIEPTSGS 83
Cdd:TIGR03719 323 IEAENLTKAFGDK------LLIDDLSFK--LPP-GGIVGVIGPN---------------GAGKSTLFRMITGQEQPDSGT 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLdGEDIstmdkeellevrrqKMSMVFQNF-GLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNanllaFK--DQ- 159
Cdd:TIGR03719 379 IEI-GETV--------------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFN-----FKgsDQq 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 160 -YPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESqqktIIFISHD---LnealrigDRIA 235
Cdd:TIGR03719 439 kKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGC----AVVISHDrwfL-------DRIA 507
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-243 |
1.89e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 20 ALKMVQENVSKTEILEKTGATVgVYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPT---SGSIYLDGEDIstmdK 96
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPI-LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 97 EELLEVRRQkMSMVFQNFGLFPQRTVLENTEYGLEVQGvdkaerqaraekaldnanllafkDQYPSQLSGGMQQRVGLAR 176
Cdd:cd03233 76 EFAEKYPGE-IIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 177 ALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIF-ISHDLNEALRIGDRIAIMKDGKVV 243
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
53-249 |
1.95e-10 |
|
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: 58.54 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGS-IYLDGEDISTMDKEELLEVRRqkmsmvfqnfglfpqrtvlenteygle 131
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 132 vqgvdkaerqaraekaldnanllafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDE-----L 206
Cdd:smart00382 55 --------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 682099688 207 LELQESQQKTIIFISHDLNEalrIGDRIAIMKDGKVVQVGTGE 249
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIVLLLIL 148
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
45-247 |
2.62e-10 |
|
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: 60.64 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGedistmdkeellevrrqKMSMVFQNFGLFPQrTVLE 124
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEVqgvDKAERQARAEKALDNANLLAF--KDQYPS-----QLSGGMQQRVGLARALANNPEILLMDEAFSALDPL 197
Cdd:cd03291 117 NIIFGVSY---DEYRYKSVVKACQLEEDITKFpeKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 682099688 198 IRRDMQDE-LLELQESqqKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGT 247
Cdd:cd03291 194 TEKEIFEScVCKLMAN--KTRILVTSKM-EHLKKADKILILHEGSSYFYGT 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
53-227 |
3.27e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIstmDKEelLEVRRQKMSMVFQNFGLFPQRTVLENTEYGLEV 132
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKD--LCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 133 Q----GVDKAERQARAEKALDnanllafkdqYP-SQLSGGMQQRVGLARALANNPEILLMDEAFSALDpliRRDMQDELL 207
Cdd:PRK13540 102 SpgavGITELCRLFSLEHLID----------YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIIT 168
|
170 180
....*....|....*....|....*
gi 682099688 208 ELQESQQK--TIIFISHD---LNEA 227
Cdd:PRK13540 169 KIQEHRAKggAVLLTSHQdlpLNKA 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-252 |
4.60e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.50 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEdistmdkeeLLEVRRQKMsmvFQNfglfpqRTVLENT 126
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------VAYVPQQAW---IQN------DSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 127 EYGlevqgvdKAERQARAEKALDNANLLAFKDQYPS-----------QLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:TIGR00957 720 LFG-------KALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 196 PLIRRDMQDELLELQES-QQKTIIFISHDLNEALRIgDRIAIMKDGKVVQVGTGEDIL 252
Cdd:TIGR00957 793 AHVGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-304 |
6.06e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEpTSGSIYLDGediSTMDKEELLEVRRQkmsmvfqnFGLFPQRTVLE 124
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG---VSWNSVTLQTWRKA--------FGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NteyGLEVQGVDKAERQARAE--KALDNANLLAFKDQYPSQL-----------SGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:TIGR01271 1305 S---GTFRKNLDPYEQWSDEEiwKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 192 SALDP----LIRRDMQdellelQESQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQVGTGEDILtNPANDYVRAFTEdI 267
Cdd:TIGR01271 1382 AHLDPvtlqIIRKTLK------QSFSNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSA-A 1452
|
250 260 270
....*....|....*....|....*....|....*....
gi 682099688 268 DRSKVLTAE--NIMIQPLTTNISvdgpnvALKKMATEEV 304
Cdd:TIGR01271 1453 DRLKLFPLHrrNSSKRKPQPKIT------ALREEAEEEV 1485
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-249 |
9.48e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 21 LKMVQENVSKTEILEktgatvGVydaNIEIEEGEIFVIMGLSGSGKSTLIRLL--NRLIEPTSGSIYLDGEDISTMDKEE 98
Cdd:CHL00131 10 IKNLHASVNENEILK------GL---NLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 99 llevrRQKMSmVFQNFglfpqrtvlentEYGLEVQGVDKAE------RQARAEKALDNANLLAFKDQYPSQL-------- 164
Cdd:CHL00131 81 -----RAHLG-IFLAF------------QYPIEIPGVSNADflrlayNSKRKFQGLPELDPLEFLEIINEKLklvgmdps 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 165 ----------SGGMQQRVGLARALANNPEILLMDEAFSALDplirrdmQDELLELQES------QQKTIIFISH--DLNE 226
Cdd:CHL00131 143 flsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLD-------IDALKIIAEGinklmtSENSIILITHyqRLLD 215
|
250 260
....*....|....*....|...
gi 682099688 227 ALrIGDRIAIMKDGKVVQVGTGE 249
Cdd:CHL00131 216 YI-KPDYVHVMQNGKIIKTGDAE 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
45-255 |
1.11e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.56 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDgedistmdkeellevrrqkmsmvfQNFGLFPQR---- 120
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------------------RSIAYVPQQawim 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 --TVLENTEYGLEvqgvdkaERQARAEKALDNANLLAFKDQYPS-----------QLSGGMQQRVGLARALANNPEILLM 187
Cdd:PTZ00243 734 naTVRGNILFFDE-------EDAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 682099688 188 DEAFSALDPLIRRDMQDELLeLQESQQKTIIFISHDLNeALRIGDRIAIMKDGKVVQVGTGEDILTNP 255
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVH-VVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
50-244 |
1.43e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 58.33 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 50 IEEGEIFVIMGLSGSGKSTLIRLLNRLIEpTSGSIYLDGEDISTMdkeELLEVRRQkmsmvfqnFGLFPQRTVLENteyG 129
Cdd:cd03289 27 ISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSV---PLQKWRKA--------FGVIPQKVFIFS---G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 130 LEVQGVDKAERQARAE--KALDNANLLAFKDQYPSQL-----------SGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:cd03289 92 TFRKNLDPYGKWSDEEiwKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 682099688 197 L----IRRDMQdellelQESQQKTIIFISHDLnEALRIGDRIAIMKDGKVVQ 244
Cdd:cd03289 172 ItyqvIRKTLK------QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQ 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
135-253 |
3.39e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 135 VDKAERQARAEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESqQ 214
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-G 194
|
90 100 110
....*....|....*....|....*....|....*....
gi 682099688 215 KTIIFISHDLNEALRIGDRIAIMKDGKVVQVGTGEDILT 253
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
58-195 |
4.91e-09 |
|
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: 58.02 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLlnrlieptsgsiyldgedISTMDKEELLEVRRQ---KMSMVFQNFGLFPQRTVLENTEYGL-EVQ 133
Cdd:TIGR03719 36 VLGLNGAGKSTLLRI------------------MAGVDKDFNGEARPQpgiKVGYLPQEPQLDPTKTVRENVEEGVaEIK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 134 GV------------------DK-AERQARAEKALDNANL---------------LAFKDQYPSQLSGGMQQRVGLARALA 179
Cdd:TIGR03719 98 DAldrfneisakyaepdadfDKlAAEQAELQEIIDAADAwdldsqleiamdalrCPPWDADVTKLSGGERRRVALCRLLL 177
|
170
....*....|....*.
gi 682099688 180 NNPEILLMDEAFSALD 195
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD 193
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
40-236 |
1.24e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 40 TVGVYDANIE---IEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDIStmdkeellevrrqkmsmvfqnfgl 116
Cdd:cd03222 9 RYGVFFLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 117 fpqrtvlenteyglevqgvdkaerqaraekaldnanllaFKDQYPSqLSGGMQQRVGLARALANNPEILLMDEAFSALDP 196
Cdd:cd03222 65 ---------------------------------------YKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 682099688 197 LIRRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAI 236
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
49-224 |
1.32e-08 |
|
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: 56.72 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDgEDIS----------TMDKEELLEvrrqkmSMVFQNFGlfp 118
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISykpqyispdyDGTVEEFLR------SANTDDFG--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 119 qrTVLENTEYGlevqgvdkaerqaraeKALDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD--- 195
Cdd:COG1245 432 --SSYYKTEII----------------KPLGLEKLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveq 490
|
170 180 190
....*....|....*....|....*....|....
gi 682099688 196 -----PLIRRDMqdellelqESQQKTIIFISHDL 224
Cdd:COG1245 491 rlavaKAIRRFA--------ENRGKTAMVVDHDI 516
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-250 |
1.75e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 3 KVKIEHLtKIFGKKVKPALKMVQENVSKTEILEKTGATVGVYDAnieIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTS- 81
Cdd:PLN03211 48 RVKFENM-KNKGSNIKRILGHKPKISDETRQIQERTILNGVTGM---ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNf 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 82 -GSIYLDGEDIStmdKEELlevrrQKMSMVFQNFGLFPQRTVLENTEY--------GLEVQGVDKAERQARAEKALDNAN 152
Cdd:PLN03211 124 tGTILANNRKPT---KQIL-----KRTGFVTQDDILYPHLTVRETLVFcsllrlpkSLTKQEKILVAESVISELGLTKCE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 153 LLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESQQKTIIFISHDLNEALRIGD 232
Cdd:PLN03211 196 NTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFD 275
|
250
....*....|....*...
gi 682099688 233 RIAIMKDGKVVQVGTGED 250
Cdd:PLN03211 276 SVLVLSEGRCLFFGKGSD 293
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
49-224 |
2.09e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDgEDISTmdKEELLEVrrqKMSMVFQNFgLFPQRTVLENTEY 128
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISY--KPQYIKP---DYDGTVEDL-LRSITDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 129 GLEVQgvdkaerqaraeKALDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALD--------PLIRR 200
Cdd:PRK13409 434 KSEII------------KPLQLERLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaKAIRR 498
|
170 180
....*....|....*....|....
gi 682099688 201 DMqdellelqESQQKTIIFISHDL 224
Cdd:PRK13409 499 IA--------EEREATALVVDHDI 514
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
43-222 |
2.94e-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: 52.44 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 43 VYDANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDgedistmdkeellevRRQKMSMVfqnfglfPQR-- 120
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFYV-------PQRpy 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 ----TVLENTEYGLEV-QGVDKAERQARAEKALDNANLL----------AFKDqYPSQLSGGMQQRVGLARALANNPEIL 185
Cdd:TIGR00954 526 mtlgTLRDQIIYPDSSeDMKRRGLSDKDLEQILDNVQLThilereggwsAVQD-WMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*..
gi 682099688 186 LMDEAFSALDPlirrDMQDELLELQESQQKTIIFISH 222
Cdd:TIGR00954 605 ILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| COG3448 |
COG3448 |
CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
273-393 |
3.64e-07 |
|
CBS-domain-containing membrane protein [Signal transduction mechanisms];
Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 49.09 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 273 LTAENIMIQPLTTnISVDGP-NVALKKMATEEVSGLVAVDRNRQFKGFLT-----------SDAAIKARRDQIPLTDVLV 340
Cdd:COG3448 2 MTVRDIMTRDVVT-VSPDTTlREALELMREHGIRGLPVVDEDGRLVGIVTerdllrallpdRLDELEERLLDLPVEDVMT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 682099688 341 -DMQTVSQDMLVADLMPLISDSP-SPLAVVDG-GRLKGVVIRGRVLEALTDNLEEE 393
Cdd:COG3448 81 rPVVTVTPDTPLEEAAELMLEHGiHRLPVVDDdGRLVGIVTRTDLLRALARLLEEE 136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-235 |
4.67e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 4 VKIEHLTKIFGKKVkpalkmVQENVSKTeiLEKtGATVGVYDANieieegeifvimglsGSGKSTLIRLLNRLIEPTSGS 83
Cdd:PRK11819 325 IEAENLSKSFGDRL------LIDDLSFS--LPP-GGIVGIIGPN---------------GAGKSTLFKMITGQEQPDSGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 84 IYLdGEDIstmdkeellevrrqKMSMVFQNF-GLFPQRTVLENTEYGLEVQGVDKAERQARAEKALDNanllaFK--DQ- 159
Cdd:PRK11819 381 IKI-GETV--------------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSRAYVGRFN-----FKggDQq 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 160 -YPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIRRDMQDELLELQESqqktIIFISHD---LnealrigDRIA 235
Cdd:PRK11819 441 kKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGC----AVVISHDrwfL-------DRIA 509
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
58-195 |
7.31e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLLnrlieptSGsiyldgedistMDKEELLEVRRQ---KMSMVFQNFGLFPQRTVLENTEYGL-EVQ 133
Cdd:PRK11819 38 VLGLNGAGKSTLLRIM-------AG-----------VDKEFEGEARPApgiKVGYLPQEPQLDPEKTVRENVEEGVaEVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 134 GV------------------DK-AERQARAEKALDNANL---------------LAFKDQYPSQLSGGMQQRVGLARALA 179
Cdd:PRK11819 100 AAldrfneiyaayaepdadfDAlAAEQGELQEIIDAADAwdldsqleiamdalrCPPWDAKVTKLSGGERRRVALCRLLL 179
|
170
....*....|....*.
gi 682099688 180 NNPEILLMDEAFSALD 195
Cdd:PRK11819 180 EKPDMLLLDEPTNHLD 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
60-223 |
2.49e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 60 GLSGSGKSTLIRLLNRLIEPTSGSIYLD-GE------------------DISTMDKEELLEVRRQKmSMVFQNfglfPQR 120
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDpNErlgklrqdqfafeeftvlDTVIMGHTELWEVKQER-DRIYAL----PEM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 121 TV--------LEnTEYGlEVQGVDkAErqARAEKALDNANL-LAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAF 191
Cdd:PRK15064 109 SEedgmkvadLE-VKFA-EMDGYT-AE--ARAGELLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190
....*....|....*....|....*....|..
gi 682099688 192 SALDPLIRRDMQDELLElqesQQKTIIFISHD 223
Cdd:PRK15064 184 NNLDINTIRWLEDVLNE----RNSTMIIISHD 211
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
48-224 |
5.26e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 48 IEIEEGeIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGEDISTMDKEEL---LE----------VRRQKMsmvFQNF 114
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEAsveLEfehggkryriERRQGE---FAEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 GLFPQRTVLENTEYGLEVQGVDKA-----ERQARAEKALDNAN-LLAFKDQY---------PSQLSGGMQQRVGLARALA 179
Cdd:COG0419 95 LEAKPSERKEALKRLLGLEIYEELkerlkELEEALESALEELAeLQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 682099688 180 nnpeiLLMDeaFSALDPLIRRDMQDELLELQesqqktiiFISHDL 224
Cdd:COG0419 175 -----LILD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
47-195 |
8.99e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 47 NIEIEEGEIFVIMGLSGSGKSTLIRLL--NRLIEPTSGSIYLDGEDISTMDKEELLEvrrQKMSMVFQnfglfpqrtvle 124
Cdd:PRK09580 21 NLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAG---EGIFMAFQ------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 nteYGLEVQGVD---------KAERQARAEKALDNANLLAFKD------QYPSQL---------SGGMQQRVGLARALAN 180
Cdd:PRK09580 86 ---YPVEIPGVSnqfflqtalNAVRSYRGQEPLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
|
170
....*....|....*
gi 682099688 181 NPEILLMDEAFSALD 195
Cdd:PRK09580 163 EPELCILDESDSGLD 177
|
|
| COG2524 |
COG2524 |
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
265-386 |
1.03e-05 |
|
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 46.03 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 265 EDIDRSKVLTAENIMIQPLTTnISVDGP-NVALKKMATEEVSGLVAVDRNRqFKGFLTSDAAIKARRDQIPLTDVLV--- 340
Cdd:COG2524 78 KELGLVLKMKVKDIMTKDVIT-VSPDTTlEEALELMLEKGISGLPVVDDGK-LVGIITERDLLKALAEGRDLLDAPVsdi 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 682099688 341 ---DMQTVSQDMLVADLMPLISDSPSP-LAVVD-GGRLKGVVIRGRVLEAL 386
Cdd:COG2524 156 mtrDVVTVSEDDSLEEALRLMLEHGIGrLPVVDdDGKLVGIITRTDILRAL 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
44-240 |
1.38e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 44 YDANIEIEEGEIFVIMGLSGSGKSTLIRLL---------NRL-------------------IEPTSGSIYLDGEdISTmd 95
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgrrrgsgetiwdikkhIGYVSSSLHLDYR-VST-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 96 keellEVRRQKMSMVFQNFGLFpqrtvlenteyglevQGVDKAERQaRAEKALDNANLLAFKDQYPSQ-LSGGmQQRVGL 174
Cdd:PRK10938 354 -----SVRNVILSGFFDSIGIY---------------QAVSDRQQK-LAQQWLDILGIDKRTADAPFHsLSWG-QQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 682099688 175 -ARALANNPEILLMDEAFSALDPLIR---RDMQDELLELQESQqktIIFISHDLNEALR-IGDRIAIMKDG 240
Cdd:PRK10938 412 iVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLISEGETQ---LLFVSHHAEDAPAcITHRLEFVPDG 479
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
45-234 |
1.38e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIrllnrlieptsgsiyldgedistmdKEELLEVRRQKMSMVFQNFglFPQRTVLe 124
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV-------------------------NEGLYASGKARLISFLPKF--SRNKLIF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 nteyglevqgVDKAerqaraeKALDNANLLAFK-DQYPSQLSGGMQQRVGLARALANNPE--ILLMDEAFSALDPLIRRD 201
Cdd:cd03238 65 ----------IDQL-------QFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|...
gi 682099688 202 MQDELLELQeSQQKTIIFISHDLnEALRIGDRI 234
Cdd:cd03238 128 LLEVIKGLI-DLGNTVILIEHNL-DVLSSADWI 158
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-224 |
1.46e-05 |
|
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: 46.21 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 51 EEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSiyLDGED-----ISTMDKEELLE----VRRQKMSMVF--QNFGLFPq 119
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNyftkLLEGDVKVIVkpQYVDLIP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 120 RTVLENTEYGLEvqGVDKAERQARAEKALDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFSALDPLIR 199
Cdd:cd03236 101 KAVKGKVGELLK--KKDERGKLDELVDQLELRHVL---DRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....*
gi 682099688 200 RDMQDELLELQEsQQKTIIFISHDL 224
Cdd:cd03236 176 LNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
49-106 |
1.86e-05 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 44.66 E-value: 1.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIR-LLNRLIEPTSGSIYLDGEDI------STMDKEELLEVRRQK 106
Cdd:PRK05541 3 MKPNGYVIWITGLAGSGKTTIAKaLYERLKLKYSNVIYLDGDELreilghYGYDKQSRIEMALKR 67
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-195 |
6.55e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 50 IEEGEIFVIMGLSGSGKSTLIRLLNRLIE----PTSGSIYLDGedistMDKEELLEVRRQKMSMVFQNFGLFPQRTVLEN 125
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDG-----ITPEEIKKHYRGDVVYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 126 TEY-------GLEVQGVDKAERQAR------AEKALDNANLLAFKDQYPSQLSGGMQQRVGLARALANNPEILLMDEAFS 192
Cdd:TIGR00956 159 LDFaarcktpQNRPDGVSREEYAKHiadvymATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
...
gi 682099688 193 ALD 195
Cdd:TIGR00956 239 GLD 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
58-242 |
1.04e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 58 IMGLSGSGKSTLIRLLNRLIEPTSGSIY--------------LDGEDISTmdkEELLEVRRqkmsmvfqnfgLFPqrtvl 123
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSS---NPLLYMMR-----------CFP----- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 124 enteyglevqGVdkAERQARAE-KALDNANLLAFKDQYpsQLSGGMQQRVGLARALANNPEILLMDEAFSALDplirRDM 202
Cdd:PLN03073 601 ----------GV--PEQKLRAHlGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDA 662
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 682099688 203 QDELLELQESQQKTIIFISHDlnEALRIG--DRIAIMKDGKV 242
Cdd:PLN03073 663 VEALIQGLVLFQGGVLMVSHD--EHLISGsvDELWVVSEGKV 702
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
49-240 |
1.14e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 49 EIEEGEIFVIMGLSGSGKSTLIRLLNRLI---EPTSGSIYLDGEDISTMDKEelLEV-----RRQKMSMVFQNFGL---- 116
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITYALygkTPRYGRQENLRSVFAPGEDT--AEVsftfqLGGKKYRVERSRGLdydq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 117 FPQRTVLenteyglevqgvdkaeRQARAEKALDNAnllafkdqyPSQLSGGMQQRVGLARALA----------NNPEILL 186
Cdd:cd03279 102 FTRIVLL----------------PQGEFDRFLARP---------VSTLSGGETFLASLSLALAlsevlqnrggARLEALF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 187 MDEAFSALDPLIrRDMQDELLELQESQQKTIIFISHDLNEALRIGDRIAIMKDG 240
Cdd:cd03279 157 IDEGFGTLDPEA-LEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTP 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
48-238 |
1.77e-04 |
|
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: 41.58 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 48 IEIEEGEIFVIMGLSGSGKSTLIRllnrlieptsgsiyldgeDIStmdkeellevrrqkmsmvfqnFGLFpQRTVLENTE 127
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILD------------------AIG---------------------LALG-GAQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 128 YGLevqgvdkaerQARAEKALDNANLLAFKDQypsqLSGGMQQRVGLARALAN---NPEIL-LMDEAFSALDPLIRRDMQ 203
Cdd:cd03227 56 SGV----------KAGCIVAAVSAELIFTRLQ----LSGGEKELSALALILALaslKPRPLyILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 682099688 204 DELLELqeSQQK-TIIFISHDLNEALRIgDRIAIMK 238
Cdd:cd03227 122 EAILEH--LVKGaQVIVITHLPELAELA-DKLIHIK 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
45-252 |
2.77e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 45 DANIEIEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIyldgedistmdkeellevrrqKMSMVfQNFGLFPQrtvle 124
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---------------------KWSEN-ANIGYYAQ----- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 125 NTEYGLEvQGVDKAE--RQARAEKALDNA------NLLAFKDQYPSQ---LSGGMQQRVGLARALANNPEILLMDEafsa 193
Cdd:PRK15064 390 DHAYDFE-NDLTLFDwmSQWRQEGDDEQAvrgtlgRLLFSQDDIKKSvkvLSGGEKGRMLFGKLMMQKPNVLVMDE---- 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 194 ldPLIRRDMQD-ELLELQ-ESQQKTIIFISHDLNEALRIGDRIAIMKDGKVVQV-GTGEDIL 252
Cdd:PRK15064 465 --PTNHMDMESiESLNMAlEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFsGTYEEYL 524
|
|
| COG2905 |
COG2905 |
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
295-390 |
3.94e-04 |
|
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];
Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 39.81 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 295 ALKKMATEEVSGLVAVDRNRQFKGFLT-SDAAIKARRDQIPLTDVLV------DMQTVSQDMLVADLMPLISDSP-SPLA 366
Cdd:COG2905 21 AARLMTEKGVGSLVVVDDDGRLVGIITdRDLRRRVLAEGLDPLDTPVsevmtrPPITVSPDDSLAEALELMEEHRiRHLP 100
|
90 100
....*....|....*....|....
gi 682099688 367 VVDGGRLKGVVIRGRVLEALTDNL 390
Cdd:COG2905 101 VVDDGKLVGIVSITDLLRALSEEL 124
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
51-224 |
5.38e-04 |
|
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: 42.08 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 51 EEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSIYLDGedistmDKEELLE-------------VRRQKMSMVF--QNFG 115
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEP------SWDEVLKrfrgtelqdyfkkLANGEIKVAHkpQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 116 LFPQ------RTVLENTEyglevqgvdkaERQARAE--KALDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILLM 187
Cdd:COG1245 171 LIPKvfkgtvRELLEKVD-----------ERGKLDElaEKLGLENIL---DRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 682099688 188 DEAFSALDPLIRRDMQDELLELQESqQKTIIFISHDL 224
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| CBS_pair_SF |
cd02205 |
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
295-383 |
8.64e-04 |
|
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 38.76 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 295 ALKKMATEEVSGLVAVDRNRQFKGFLTSDAAIKARRDQIPLTDVLV------DMQTVSQDMLVADLMPLISDS-PSPLAV 367
Cdd:cd02205 16 ALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVaevmtpDVITVSPDTDLEEALELMLEHgIRRLPV 95
|
90
....*....|....*..
gi 682099688 368 VDG-GRLKGVVIRGRVL 383
Cdd:cd02205 96 VDDdGKLVGIVTRRDIL 112
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
50-282 |
8.68e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 50 IEEGEIFVIMGLSGSGKSTLIRLLNRLIEPTSGSiyLDGEDistmDKEELLE-------------VRRQKMSMVF--QNF 114
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEP----SWDEVLKrfrgtelqnyfkkLYNGEIKVVHkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 115 GLFPQ------RTVLENTEyglevqgvdkaERQARAE--KALDNANLLafkDQYPSQLSGGMQQRVGLARALANNPEILL 186
Cdd:PRK13409 170 DLIPKvfkgkvRELLKKVD-----------ERGKLDEvvERLGLENIL---DRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 187 MDEAFSALDPLIRRDMQDELLELQESqqKTIIFISHDlneaLRIGDRIAimkdgKVVQVGTGED----ILTNPA------ 256
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEG--KYVLVVEHD----LAVLDYLA-----DNVHIAYGEPgaygVVSKPKgvrvgi 304
|
250 260
....*....|....*....|....*.
gi 682099688 257 NDYVRAFtedidrskvLTAENIMIQP 282
Cdd:PRK13409 305 NEYLKGY---------LPEENMRIRP 321
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
55-108 |
1.23e-03 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 39.16 E-value: 1.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 682099688 55 IFVIMGLSGSGKSTLIRLLNRLIeptsGSIYLDGEDISTMdkeelleVRRQKMS 108
Cdd:cd02021 1 IIVVMGVSGSGKSTVGKALAERL----GAPFIDGDDLHPP-------ANIAKMA 43
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
53-195 |
1.59e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 53 GEIFVIMGLSGSGKSTLIRLLNRliEPTSGsiYLDGE-DISTMDKEEllEVRRQKMSMVFQNFGLFPQRTVLENTEYGLE 131
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDiRISGFPKKQ--ETFARISGYCEQNDIHSPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 682099688 132 VQ---GVDKAERQARAEKALDNANLLAFKDQ---YP--SQLSGGMQQRVGLARALANNPEILLMDEAFSALD 195
Cdd:PLN03140 980 LRlpkEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| YtoI |
COG4109 |
Predicted transcriptional regulator containing CBS domains [Transcription]; |
273-386 |
1.67e-03 |
|
Predicted transcriptional regulator containing CBS domains [Transcription];
Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 38.35 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 273 LTAENIMIQP----LTTNISVDGpnvALKKMATEEVSGLVAVDRNRQFKGFLTSDAAIKARRDqIPLTDVLV-DMQTVSQ 347
Cdd:COG4109 16 LLVEDIMTLEdvatLSEDDTVED---ALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDD-TPIEDVMTkNPITVTP 91
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 682099688 348 DMLVADLMPLISDSPSPLA-VVDG-GRLKGVVIRGRVLEAL 386
Cdd:COG4109 92 DTSLASAAHKMIWEGIELLpVVDDdGRLLGIISRQDVLKAL 132
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
55-90 |
2.77e-03 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 38.19 E-value: 2.77e-03
10 20 30
....*....|....*....|....*....|....*..
gi 682099688 55 IFVIMGLSGSGKSTLIRLL-NRLieptsGSIYLDGED 90
Cdd:COG3265 3 VIVVMGVSGSGKSTVGQALaERL-----GWPFIDGDD 34
|
|
| CBS |
COG0517 |
CBS domain [Signal transduction mechanisms]; |
273-391 |
3.17e-03 |
|
CBS domain [Signal transduction mechanisms];
Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 37.54 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682099688 273 LTAENIMIQPLTTnISVDGP-NVALKKMATEEVSGLVAVDRNRQFKGFLT-SDAAIKARRDQIPLTDVLVD--MQ----T 344
Cdd:COG0517 1 MKVKDIMTTDVVT-VSPDATvREALELMSEKRIGGLPVVDEDGKLVGIVTdRDLRRALAAEGKDLLDTPVSevMTrppvT 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 682099688 345 VSQDMLVADLMPLISDSPSP-LAVVDG-GRLKGVVIRGRVLEALTDNLE 391
Cdd:COG0517 80 VSPDTSLEEAAELMEEHKIRrLPVVDDdGRLVGIITIKDLLKALLEPLA 128
|
|
| |
