|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
768-1479 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 1139.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 768 TLDDPSKVKHALPFEGMLPDFGSPVIEGTKPAYKFKSLVSTLENILKGYDNQVIMNASLQQLIEVLRNPKLPYSEWKLHI 847
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDNQVIMNETLKDLIEVLRDPELPYLEWQEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 848 SALHSRLPAKLDEQMEELVARSLRRGAVFPARQLSKLIDMAVKNPEYNPDK-LLGAVVEPLADIAHKYSNGLEAHEHSIF 926
Cdd:pfam08326 81 SALSGRIPAKLEASLRQLVERAHSRSAEFPAKQLRKILDKFLAELVLKADRdLFEATLAPLVDLVERYRNGLKGHEYSVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 927 VHFLEEYYEVEKLFNGPNVREENIILKLRDENPKDLDKVALTVLSHSKVSAKNNLILAILKHYQPLCKLSSKVSAIFSTP 1006
Cdd:pfam08326 161 ASLLEEYYDVEKLFSGGNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNCPNVSNVAKELRPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1007 LQHIVELESKATAKVALQAREILIQGALPSVKERTEQIEHILKSSVVKVAYGSSNPKRSEPDLNILKDLIDSNYVVFDVL 1086
Cdd:pfam08326 241 LKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYGESGWKHREPSLEVLKELIDSKYTVFDVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1087 LQFLTHQDPVVTAAAAQVYIRRAYRAYTIGDIRVHEGVTVP-IVEWKFQLPSAAFSTF-----PTVKSKMGMNRAVSVSD 1160
Cdd:pfam08326 321 PPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPpIVSWQFQLPSSHSSEFgsplsPSSDSSPPFKRIASVSD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1161 LSYVAN-SQSSPLREGILMAVDHLDDVDEILSQSLEVIPRHQSSSNgpapdRSGSSASLSNVANVCVASTEGFESEEEIL 1239
Cdd:pfam08326 401 LSYLVNkSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESG-----ESNSSDEPINVLNVAIRDAEGSDSDEELL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1240 VRLREILDLNKQELINASIRRITFMFGFKDGSYPKYYTFNGP-NYNENETIRHIEPALAFQLELGRLSNFNIKPIFTDNR 1318
Cdd:pfam08326 476 ERLEEILKENKEELLAAGVRRITFIIGRKDGQYPKYFTFRGPdNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1319 NIHVYEAVSKTSPLDKRFFTRGIIRTGHIRDDISIQEYLTSEANRLMSDILDNLEV--TDTSNSDLNHIFINFIAVFDIS 1396
Cdd:pfam08326 556 QIHLYEAVGKENPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVasIGNSNSDLNHIFLNFVPVFNVD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1397 PEDVEAAFGGFLERFGKRLLRLRVSSAEIRIIIKDPQTGAPVPLRALINNVSGYVIKTEMYTEVKNAKGEWVFKSLGKPG 1476
Cdd:pfam08326 636 PEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDKGEWVFKSIGKPG 715
|
...
gi 6324343 1477 SMH 1479
Cdd:pfam08326 716 PMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1574-2118 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 621.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1574 PEYPRGRQFVVVANDITFKIGSFGPQEDEFFNKVTEYARKRgIPRIYLAANSGARIGMAEEIVPLFQVAWNDAANPDKGF 1653
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1654 QYLYLtsegMETLKKfdkensvltertviNGEERFVIKTIIGSEDGLGVECLRGSGLIAGATSRAYHDIFTITLVTCRSV 1733
Cdd:pfam01039 80 KILRA----MEIAIK--------------TGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1734 GIGAYLVRLGQRAIQVEG-QPIILTGAPAINKMLGrEVYTSNLQLGGTQIMYNNGVSHLTAVDDLAGVEKIVEWMSYVPA 1812
Cdd:pfam01039 142 GGGAYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1813 KRNM---PVPILETKDTWDRP---VDFTPTND-ETYDVRWMIEgretesgfeyGLFDKGSFFETLSGWAKGVVVGRARLG 1885
Cdd:pfam01039 221 PAPNnrePVPIVPTKDPPDRDaplVSIVPDDPkKPYDVREVIA----------GIVDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1886 GIPLGVIGVETRtvenlipadpanpnsaetliQEPGqVWHPNSAFKTAQAINDFNNgEQLPMMILANWRGFSGGQRDMFN 1965
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDA-FNLPLVILADVPGFLPGQRQEYG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1966 EVLKYGSFIVDALVDYKQPIIIYIPPtgELRGGSWVVVDPTINADQMeMYADVNARAGVLEPQGMVGIKFRREKLLDTMN 2045
Cdd:pfam01039 349 GILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324343 2046 RLDDKyrelrsqlsnkslapevhQQISKQLADRERELLPIYGQISLQFADLHDRSSRMVAKGVISKELEWTEA 2118
Cdd:pfam01039 426 GKDLA------------------ATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKP 480
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
59-588 |
4.56e-127 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 408.63 E-value: 4.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRT---------VAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSqsKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSgtgvdtvhvdektg 218
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACE--DAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 lvsvdddiyqKGCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANE---IPGSP-IFIMKLAG 294
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShDDGK 374
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnphsaseidfefktqdaTKKQRRPIPKGHC 454
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL-----------------------------PFTQEDIKLRGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGTLHELNFRSSSNV---WGYFSvgnNGNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELS 531
Cdd:COG4770 335 IECRINAEDPARGFLPSPGTITRLRPPGGPGVrvdSGVYE---GYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFV 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324343 532 IRGdFRTTVEYLIKLLETEDFEDNTITTGWLDdliTHKMTAEKPDPTLAVICGAATK 588
Cdd:COG4770 412 IEG-VKTNIPFLRALLAHPDFRAGDVDTGFIE---RELAELLAAAAPEELALAAAMK 464
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
59-563 |
9.84e-104 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 341.01 E-value: 9.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKT---------VAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGtgvdtvhvdektG 218
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSG--FTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSD------------G 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 LVsvdddiyqkgccTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMKLAG 294
Cdd:PRK08591 137 PV------------DDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHdDGK 374
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK-NGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnPHSASEIDFefktqdatkkqrrpipKGHC 454
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL-------------SIKQEDIVF----------------RGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGT---LHE---LNFRSSSNVW-GYFsvgnngnIHSFSDSQFGHIFAFGENRQASRKHMVVAL 527
Cdd:PRK08591 335 IECRINAEDPAKNFMPSPGKitrYHPpggPGVRVDSAVYtGYT-------IPPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510
....*....|....*....|....*....|....*.
gi 6324343 528 KELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLD 563
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
59-565 |
3.06e-90 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 302.07 E-value: 3.06e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKT---------VAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDTVhvdektg 218
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSG--FTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDE------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 lvsvdddiyqkgcctspEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMKLAG 294
Cdd:TIGR00514 142 -----------------EENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDdGK 374
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnphsaseidfefktqdaTKKQRRPIPKGHC 454
Cdd:TIGR00514 284 FYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-----------------------------SLKQEDVVVRGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGTLHE------LNFRSSSNVWGYFSvgnngnIHSFSDSQFGHIFAFGENRQASRKHMVVALK 528
Cdd:TIGR00514 335 IECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYT------VPPYYDSMIGKLITYGKTREVAIARMKRALS 408
|
490 500 510
....*....|....*....|....*....|....*..
gi 6324343 529 ELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDDL 565
Cdd:TIGR00514 409 EFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
185-412 |
1.16e-56 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 195.99 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 185 DKISSTIVAQSAKVPCIPWSGTGVDTVhvdektglvsvdddiyqkgcctspEDGLQKAKRIGFPVMIKASEGGGGKGIRQ 264
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETE------------------------EEALAAAKEIGYPVIIKAAFGGGGLGMGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 265 VEREEDFIALYHQAANEIPGSP----IFIMKLAGRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAE 340
Cdd:pfam02786 57 ARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324343 341 TFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPM 412
Cdd:pfam02786 137 ERQMLREAAVKIARHLGYVGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
457-563 |
3.44e-30 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 115.97 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 457 CRITSEDPNDGFKPSGGTLHELNFRSSSNVwgYFSVGNNGNIH--SFSDSQFGHIFAFGENRQASRKHMVVALKELSIRG 534
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEvpPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 6324343 535 dFRTTVEYLIKLLETEDFEDNTITTGWLD 563
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1579-1893 |
1.27e-18 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 92.01 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1579 GRQFVVVANDITFKIGSFGPQEDEFFNKVTEYARKRGIPRIYLAANSGARIGMaeeivplfqvawndaanpdkgfqylyl 1658
Cdd:COG4799 81 GRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQE--------------------------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1659 tsegmetlkkfdkensvltertvingeerfviktiigsedglGVECLRGSGLIAGATSRAYHDIFTITLVTCRSVGIGAY 1738
Cdd:COG4799 134 ------------------------------------------GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1739 LVRLGQRAIQVEGQPII-LTGAPAINKMLGREVytSNLQLGGTQI-MYNNGVSHLTAVDDLAGVEKIVEWMSYVPAKRNM 1816
Cdd:COG4799 172 SPALSDFVIMVKGTSQMfLGGPPVVKAATGEEV--TAEELGGADVhARVSGVADYLAEDEEEALALARRLLSYLPSNNLE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1817 PVPILETKDTWDRP---VDFTPTND-ETYDVRWMIEGretesgfeygLFDKGSFFETLSGWAKGVVVGRARLGGIPLGVI 1892
Cdd:COG4799 250 DPPRAEPAPPARDPeelYGIVPEDPrKPYDMREVIAR----------LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIV 319
|
.
gi 6324343 1893 G 1893
Cdd:COG4799 320 A 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
701-767 |
1.31e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 79.18 E-value: 1.31e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324343 701 TQLRTPSPGKLV-----KFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIVQLLKQP-GSTIVAGDIMAIM 767
Cdd:pfam00364 1 TEIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
702-767 |
1.38e-17 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 78.61 E-value: 1.38e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324343 702 QLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
698-767 |
4.35e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 59.00 E-value: 4.35e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324343 698 NDPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAGDLLVEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
698-767 |
5.41e-08 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 58.55 E-value: 5.41e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324343 698 NDPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:COG1038 1074 GNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVkEVLVKEGDQVEAGDLLIEL 1144
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1722-1989 |
7.70e-05 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 47.88 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1722 IFTITLVTCRSVGIGAYLVRLGQRAIQVEGQ-PIILTGAPAINKMLGREVYTSNLqlGGTQIMYN-NGVSHLTAVDDLAG 1799
Cdd:PLN02820 206 IPQIALVLGSCTAGGAYVPAMADESVIVKGNgTIFLAGPPLVKAATGEEVSAEDL--GGADVHCKvSGVSDHFAQDELHA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1800 VE---KIVEWMsYVPAKRNMPVPILETKDTWDRPV-------DFTPTN-DETYDVRWMIEGretesgfeygLFDKGSFFE 1868
Cdd:PLN02820 284 LAigrNIVKNL-HLAAKQGMENTLGSKNPEYKEPLydvkelrGIVPADhKQSFDVRSVIAR----------IVDGSEFDE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1869 TLSGWAKGVVVGRARLGGIPLGVIGvetrtvenlipadpanpNSAetliqepgqVWHPNSAFKTAQAInDFNNGEQLPMM 1948
Cdd:PLN02820 353 FKKNYGTTLVTGFARIYGQPVGIIG-----------------NNG---------ILFTESALKGAHFI-ELCAQRGIPLL 405
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6324343 1949 ILANWRGFSGGQRDMFNEVLKYGSFIVDALVDYKQPIIIYI 1989
Cdd:PLN02820 406 FLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITII 446
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
768-1479 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 1139.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 768 TLDDPSKVKHALPFEGMLPDFGSPVIEGTKPAYKFKSLVSTLENILKGYDNQVIMNASLQQLIEVLRNPKLPYSEWKLHI 847
Cdd:pfam08326 1 ALDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDNQVIMNETLKDLIEVLRDPELPYLEWQEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 848 SALHSRLPAKLDEQMEELVARSLRRGAVFPARQLSKLIDMAVKNPEYNPDK-LLGAVVEPLADIAHKYSNGLEAHEHSIF 926
Cdd:pfam08326 81 SALSGRIPAKLEASLRQLVERAHSRSAEFPAKQLRKILDKFLAELVLKADRdLFEATLAPLVDLVERYRNGLKGHEYSVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 927 VHFLEEYYEVEKLFNGPNVREENIILKLRDENPKDLDKVALTVLSHSKVSAKNNLILAILKHYQPLCKLSSKVSAIFSTP 1006
Cdd:pfam08326 161 ASLLEEYYDVEKLFSGGNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNCPNVSNVAKELRPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1007 LQHIVELESKATAKVALQAREILIQGALPSVKERTEQIEHILKSSVVKVAYGSSNPKRSEPDLNILKDLIDSNYVVFDVL 1086
Cdd:pfam08326 241 LKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYGESGWKHREPSLEVLKELIDSKYTVFDVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1087 LQFLTHQDPVVTAAAAQVYIRRAYRAYTIGDIRVHEGVTVP-IVEWKFQLPSAAFSTF-----PTVKSKMGMNRAVSVSD 1160
Cdd:pfam08326 321 PPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPpIVSWQFQLPSSHSSEFgsplsPSSDSSPPFKRIASVSD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1161 LSYVAN-SQSSPLREGILMAVDHLDDVDEILSQSLEVIPRHQSSSNgpapdRSGSSASLSNVANVCVASTEGFESEEEIL 1239
Cdd:pfam08326 401 LSYLVNkSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESG-----ESNSSDEPINVLNVAIRDAEGSDSDEELL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1240 VRLREILDLNKQELINASIRRITFMFGFKDGSYPKYYTFNGP-NYNENETIRHIEPALAFQLELGRLSNFNIKPIFTDNR 1318
Cdd:pfam08326 476 ERLEEILKENKEELLAAGVRRITFIIGRKDGQYPKYFTFRGPdNYEEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1319 NIHVYEAVSKTSPLDKRFFTRGIIRTGHIRDDISIQEYLTSEANRLMSDILDNLEV--TDTSNSDLNHIFINFIAVFDIS 1396
Cdd:pfam08326 556 QIHLYEAVGKENPTDKRFFVRAIIRPGRLRDDIPTAEYLISEAERLLNDILDALEVasIGNSNSDLNHIFLNFVPVFNVD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1397 PEDVEAAFGGFLERFGKRLLRLRVSSAEIRIIIKDPQTGAPVPLRALINNVSGYVIKTEMYTEVKNAKGEWVFKSLGKPG 1476
Cdd:pfam08326 636 PEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGPPIPLRLVITNVSGYVVKVELYREVKDDKGEWVFKSIGKPG 715
|
...
gi 6324343 1477 SMH 1479
Cdd:pfam08326 716 PMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1574-2118 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 621.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1574 PEYPRGRQFVVVANDITFKIGSFGPQEDEFFNKVTEYARKRgIPRIYLAANSGARIGMAEEIVPLFQVAWNDAANPDKGF 1653
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1654 QYLYLtsegMETLKKfdkensvltertviNGEERFVIKTIIGSEDGLGVECLRGSGLIAGATSRAYHDIFTITLVTCRSV 1733
Cdd:pfam01039 80 KILRA----MEIAIK--------------TGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1734 GIGAYLVRLGQRAIQVEG-QPIILTGAPAINKMLGrEVYTSNLQLGGTQIMYNNGVSHLTAVDDLAGVEKIVEWMSYVPA 1812
Cdd:pfam01039 142 GGGAYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1813 KRNM---PVPILETKDTWDRP---VDFTPTND-ETYDVRWMIEgretesgfeyGLFDKGSFFETLSGWAKGVVVGRARLG 1885
Cdd:pfam01039 221 PAPNnrePVPIVPTKDPPDRDaplVSIVPDDPkKPYDVREVIA----------GIVDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1886 GIPLGVIGVETRtvenlipadpanpnsaetliQEPGqVWHPNSAFKTAQAINDFNNgEQLPMMILANWRGFSGGQRDMFN 1965
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDA-FNLPLVILADVPGFLPGQRQEYG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1966 EVLKYGSFIVDALVDYKQPIIIYIPPtgELRGGSWVVVDPTINADQMeMYADVNARAGVLEPQGMVGIKFRREKLLDTMN 2045
Cdd:pfam01039 349 GILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324343 2046 RLDDKyrelrsqlsnkslapevhQQISKQLADRERELLPIYGQISLQFADLHDRSSRMVAKGVISKELEWTEA 2118
Cdd:pfam01039 426 GKDLA------------------ATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKP 480
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
59-588 |
4.56e-127 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 408.63 E-value: 4.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCRELGIRT---------VAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSqsKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSgtgvdtvhvdektg 218
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACE--DAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 lvsvdddiyqKGCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANE---IPGSP-IFIMKLAG 294
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREakaAFGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShDDGK 374
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnphsaseidfefktqdaTKKQRRPIPKGHC 454
Cdd:COG4770 284 FYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPL-----------------------------PFTQEDIKLRGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGTLHELNFRSSSNV---WGYFSvgnNGNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELS 531
Cdd:COG4770 335 IECRINAEDPARGFLPSPGTITRLRPPGGPGVrvdSGVYE---GYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFV 411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324343 532 IRGdFRTTVEYLIKLLETEDFEDNTITTGWLDdliTHKMTAEKPDPTLAVICGAATK 588
Cdd:COG4770 412 IEG-VKTNIPFLRALLAHPDFRAGDVDTGFIE---RELAELLAAAAPEELALAAAMK 464
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
59-563 |
9.84e-104 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 341.01 E-value: 9.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKT---------VAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGtgvdtvhvdektG 218
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSG--FTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSD------------G 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 LVsvdddiyqkgccTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMKLAG 294
Cdd:PRK08591 137 PV------------DDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPgVYMEKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHdDGK 374
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEK-NGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnPHSASEIDFefktqdatkkqrrpipKGHC 454
Cdd:PRK08591 284 FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPL-------------SIKQEDIVF----------------RGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGT---LHE---LNFRSSSNVW-GYFsvgnngnIHSFSDSQFGHIFAFGENRQASRKHMVVAL 527
Cdd:PRK08591 335 IECRINAEDPAKNFMPSPGKitrYHPpggPGVRVDSAVYtGYT-------IPPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510
....*....|....*....|....*....|....*.
gi 6324343 528 KELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLD 563
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLE 442
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
59-564 |
2.43e-99 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 349.05 E-value: 2.43e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSvrkwAYETfgDDRTVqfvAMATPEDleANAEYIRMADQYIEVpgGTNNNN---YANVDLIV 135
Cdd:PRK12999 5 IKKVLVANRGEIAIRIFRA----ATEL--GIRTV---AIYSEED--KLSLHRFKADEAYLI--GEGKHPvraYLDIDEII 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 136 DIAERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDtvhvde 215
Cdd:PRK12999 72 RVAKQAGVDAIHPGYGFLSENPEFARACAEAG--ITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPID------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 216 ktglvsvdddiyqkgcctSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMK 291
Cdd:PRK12999 144 ------------------DIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGNDeVYLEK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 292 LAGRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShD 371
Cdd:PRK12999 206 YVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVD-A 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 372 DGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGipmhrisdirtlygmnpHSASEIDFEFKTQDATKkqrrpiPK 451
Cdd:PRK12999 285 DGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG-----------------ATLHDLEIGIPSQEDIR------LR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 452 GHCTACRITSEDPNDGFKPSGGTLHElnFRSSsnvwGYFSV---GNNGN----IHSFSDSQFGHIFAFGEN-RQASRKhM 523
Cdd:PRK12999 342 GYAIQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldGGNAFagaeITPYYDSLLVKLTAWGRTfEQAVAR-M 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 6324343 524 VVALKELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDD 564
Cdd:PRK12999 415 RRALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
59-564 |
2.26e-98 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 325.44 E-value: 2.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRT---------VAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPwsgtGVDTvhvdektg 218
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEG--IVFIGPSADIIAKMGSKIEARRAMQAAGVPVVP----GITT-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 lvSVDDdiyqkgcctsPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALY----HQAANEIPGSPIFIMKLAG 294
Cdd:PRK06111 137 --NLED----------AEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFesnkKRAANFFGNGEMYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYshDDGK 374
Cdd:PRK06111 205 DPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLV--DEQK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 -FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnPHSASEIdfefktqdatkkqRRpipKGH 453
Cdd:PRK06111 283 nFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL-------------SFTQDDI-------------KR---SGH 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 454 CTACRITSEDPNDgFKPSGGTLHELNFRSSSNVWGYFSVGNNGNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELSIR 533
Cdd:PRK06111 334 AIEVRIYAEDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVE 412
|
490 500 510
....*....|....*....|....*....|.
gi 6324343 534 GdFRTTVEYLIKLLETEDFEDNTITTGWLDD 564
Cdd:PRK06111 413 G-IKTNIPLLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
59-564 |
2.79e-96 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 339.75 E-value: 2.79e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNG-IAavkeIRSVRKwAYETfgDDRTVqfvAMATPEDleANAEYiRM-ADQYIEVpgGTNNN---NYANVDL 133
Cdd:COG1038 4 IKKVLVANRGeIA----IRVFRA-ATEL--GIRTV---AIYSEED--RYSLH-RFkADEAYLI--GEGKGpvdAYLDIEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 134 IVDIAERADVDAVWAGWGHASENPLLPEKLSqsKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPwsgtgvdtvhv 213
Cdd:COG1038 69 IIRVAKEKGVDAIHPGYGFLSENPEFARACE--EAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 214 dektglvSVDDDIyqkgccTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFI 289
Cdd:COG1038 136 -------GTEGPV------DDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaafGDDeVFL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 290 MKLAGRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAP-VTIAKaETFHEMEKAAVRLGKLVGYVSAGTVEYLY 368
Cdd:COG1038 203 EKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPaPNLDE-ELREAICEAAVKLAKAVGYVNAGTVEFLV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 369 ShDDGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGipmHRISDirtlygmnphsaSEIDfeFKTQDATKKqrrp 448
Cdd:COG1038 282 D-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG---YSLDD------------PEIG--IPSQEDIRL---- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 449 ipKGHCTACRITSEDPNDGFKPSGGTLheLNFRSSSnvwGyFSV---GNNG----NIHSFSDS------QFGHIFAfgen 515
Cdd:COG1038 340 --NGYAIQCRITTEDPANNFMPDTGRI--TAYRSAG---G-FGIrldGGNAytgaVITPYYDSllvkvtAWGRTFE---- 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6324343 516 rQASRKhMVVALKELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDD 564
Cdd:COG1038 408 -EAIRK-MRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFIDE 453
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
60-608 |
9.27e-94 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 313.84 E-value: 9.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 60 SKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIAE 139
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKT---------VAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 140 RADVDAVWAGWGHASENPLLPEKLSqsKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDtvhvdektgl 219
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACE--KAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIE---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 220 vsvdddiyqkgcctSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFI-ALYHQ---AANEIPGSPIFIMKLAGR 295
Cdd:PRK08654 140 --------------DIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEdAIESTqsiAQSAFGDSTVFIEKYLEK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 296 ARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShdDGKF 375
Cdd:PRK08654 206 PRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 376 YFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnPHSASEIDFefktqdatkkqrrpipKGHCT 455
Cdd:PRK08654 284 YFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL-------------SFKQEDITI----------------RGHAI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 456 ACRITSEDPNDGFKPSGGTLheLNFRS--------SSNVW-GYfsvgnngNIHSFSDSQFGHIFAFGENRQASRKHMVVA 526
Cdd:PRK08654 335 ECRINAEDPLNDFAPSPGKI--KRYRSpggpgvrvDSGVHmGY-------EIPPYYDSMISKLIVWGRTREEAIARMRRA 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 527 LKELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDD------LITHKMTAEKPD-PTLAVICGAATKAFLASEEARHK 599
Cdd:PRK08654 406 LYEYVIVG-VKTNIPFHKAVMENENFVRGNLHTHFIEEettileEMKRYALEEEEReKTLSEKFFPGNKKVAAIAAAVNA 484
|
....*....
gi 6324343 600 YIESLQKGQ 608
Cdd:PRK08654 485 YISSAKKDN 493
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
59-568 |
2.50e-93 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 310.88 E-value: 2.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDLEAnaEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIET---------VAVYSEADKDA--LHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPllpeKLSQSKRK--VIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSgtgvdtvhvdek 216
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENS----KFAKMCKEcnIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 217 tglvsvdddiyqKGCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGS----PIFIMKL 292
Cdd:PRK05586 135 ------------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 293 AGRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShDD 372
Cdd:PRK05586 203 IENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLD-KD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 373 GKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGipmhrisdirtlygmnphsaSEIDFefkTQDATKKqrrpipKG 452
Cdd:PRK05586 282 GNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYG--------------------EKLSI---KQEDIKI------NG 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 453 HCTACRITSEDPNDGFKPSGGTLHELNFRSSSNVWGYFSVGNNGNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELSI 532
Cdd:PRK05586 333 HSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFII 412
|
490 500 510
....*....|....*....|....*....|....*.
gi 6324343 533 RGdFRTTVEYLIKLLETEDFEDNTITTGWLDDLITH 568
Cdd:PRK05586 413 EG-VNTNIDFQFIILEDEEFIKGTYDTSFIEKKLVD 447
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
59-565 |
3.06e-90 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 302.07 E-value: 3.06e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKT---------VAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDTVhvdektg 218
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSG--FTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDE------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 lvsvdddiyqkgcctspEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMKLAG 294
Cdd:TIGR00514 142 -----------------EENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDdGK 374
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKN-GE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnphsaseidfefktqdaTKKQRRPIPKGHC 454
Cdd:TIGR00514 284 FYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-----------------------------SLKQEDVVVRGHA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGTLHE------LNFRSSSNVWGYFSvgnngnIHSFSDSQFGHIFAFGENRQASRKHMVVALK 528
Cdd:TIGR00514 335 IECRINAEDPIKTFLPSPGRITRylppggPGVRWDSHVYSGYT------VPPYYDSMIGKLITYGKTREVAIARMKRALS 408
|
490 500 510
....*....|....*....|....*....|....*..
gi 6324343 529 ELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDDL 565
Cdd:TIGR00514 409 EFIIDG-IKTTIPFHQRILEDENFQHGGTNIHYLEKK 444
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
59-563 |
9.74e-87 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 291.65 E-value: 9.74e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDLEANaeYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEA---------IAIYSTADKDAL--YLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSqsKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSgtgvdtvhvdektg 218
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICS--HHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 lvsvdddiyqKGCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGS----PIFIMKLAG 294
Cdd:PRK08462 137 ----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFIN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDgK 374
Cdd:PRK08462 207 NPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNL-D 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnpHSASEIDFefktqdatkkqrrpipKGHC 454
Cdd:PRK08462 286 FYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEEL--------------PSQESIKL----------------KGHA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDgFKPSGGTLHEL------NFRSSSNVWGYFSVGnngnihSFSDSQFGHIFAFGENRQASRKHMVVALK 528
Cdd:PRK08462 336 IECRITAEDPKK-FYPSPGKITKWiapggrNVRMDSHAYAGYVVP------PYYDSMIGKLIVWGEDRNRAIAKMKRALK 408
|
490 500 510
....*....|....*....|....*....|....*
gi 6324343 529 ELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLD 563
Cdd:PRK08462 409 EFKVEG-IKTTIPFHLEMMENADFINNKYDTKYLE 442
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
61-565 |
8.15e-85 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 305.80 E-value: 8.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 61 KILIANNGIAAVKEIRSVRKwayetfgddrtVQFVAMATPEDLEANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIAER 140
Cdd:TIGR02712 3 TVLIANRGEIAVRIIRTLRR-----------MGIRSVAVYSDADAASQHVLDADEAVCLGGAPAAESYLDIDKILAAAKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 141 ADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPwsgtgvdtvhvdeKTGLV 220
Cdd:TIGR02712 72 TGAQAIHPGYGFLSENAAFAEACEAAG--IVFVGPTPEQIRKFGLKHTARELAEAAGVPLLP-------------GTGLL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 221 SvdddiyqkgcctSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALY----HQAANEIPGSPIFIMKLAGRA 296
Cdd:TIGR02712 137 S------------SLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEAFetvkRLGESFFGDAGVFLERFVENA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 297 RHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFY 376
Cdd:TIGR02712 205 RHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYDEARDEFY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 377 FLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMhrisdirtlygmnphsaseiDFEFKTQDATkkqrrpiPKGHCTA 456
Cdd:TIGR02712 285 FLEVNTRLQVEHPVTEMVTGLDLVEWMIRIAAGELP--------------------DFASLNISLT-------PRGAAIE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 457 CRITSEDPNDGFKPSGGTLHELNFRSSSNVWGYFSVGNngNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELSIRGdF 536
Cdd:TIGR02712 338 ARVYAENPAKNFQPSPGLLTDVQFPDDVRVDTWVETGT--EVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYG-I 414
|
490 500
....*....|....*....|....*....
gi 6324343 537 RTTVEYLIKLLETEDFEDNTITTGWLDDL 565
Cdd:TIGR02712 415 ETNLDYLRSILSSETFRSAQVSTRTLNSF 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
56-563 |
3.59e-84 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 285.11 E-value: 3.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 56 HTVISKILIANNGIAAVKEIRSVRKWAYetfgddRTVQFVAMATPEDLEAnaeyiRMADQYIEVPGGTNNNNYANVDLIV 135
Cdd:PRK12833 2 PSRIRKVLVANRGEIAVRIIRAARELGM------RTVAACSDADRDSLAA-----RMADEAVHIGPSHAAKSYLNPAAIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 136 DIAERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSgtgvdtvhvde 215
Cdd:PRK12833 71 AAARQCGADAIHPGYGFLSENAAFAEAVEAAG--LIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 216 ktglvsvdddiyqKGCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMK 291
Cdd:PRK12833 138 -------------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLER 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 292 LAGRARHLEVQLLADqyGTN-ISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSH 370
Cdd:PRK12833 205 FIARARHIEVQILGD--GERvVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDD 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 371 DDGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMH-RISDIRtlygMNphsaseidfefktqdatkkqrrpi 449
Cdd:PRK12833 283 ARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRfAQGDIA----LR------------------------ 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 450 pkGHCTACRITSEDPNDGFKPSGGTLHELNF------RSSSNVW-GYfsvgnngNIHSFSDSQFGHIFAFGENRQASRKH 522
Cdd:PRK12833 335 --GAALECRINAEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYpGY-------RVPPFYDSLLAKLIVHGEDRAAALAR 405
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 6324343 523 MVVALKELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLD 563
Cdd:PRK12833 406 AARALRELRIDG-MKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
61-564 |
7.49e-82 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 295.58 E-value: 7.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 61 KILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDLEANAEYirMADQ-YI--EVPGGTNNNNYANVDLIVDI 137
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRT---------VAIYSEEDKLSLHRQ--KADEsYQvgEGPDLGPIEAYLSIDEIIRV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 138 AERADVDAVWAGWGHASENPLLPEKLSqsKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDTVhvdekt 217
Cdd:TIGR01235 70 AKLNGVDAIHPGYGFLSENSEFADACN--KAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETM------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 218 glvsvdddiyqkgcctspEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGS----PIFIMKLA 293
Cdd:TIGR01235 142 ------------------EEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYVEKLI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 294 GRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShDDG 373
Cdd:TIGR01235 204 ERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD-NDG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 374 KFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMHrisdirtlygmnphsaseidfefKTQDATKKQRRPIPKGH 453
Cdd:TIGR01235 283 KFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASLP-----------------------TPQLGVPNQEDIRTNGY 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 454 CTACRITSEDPNDGFKPSGGTLHElnFRSSSNVWGYFSVGNN--GNIHS-FSDSQFGHIFAFGENRQASRKHMVVALKEL 530
Cdd:TIGR01235 340 AIQCRVTTEDPANNFQPDTGRIEA--YRSAGGFGIRLDGGNSyaGAIITpYYDSLLVKVSAWASTPEEAAAKMDRALREF 417
|
490 500 510
....*....|....*....|....*....|....
gi 6324343 531 SIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDD 564
Cdd:TIGR01235 418 RIRG-VKTNIPFLENVLGHPKFLDGSYDTRFIDT 450
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
58-589 |
8.24e-76 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 261.19 E-value: 8.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 58 VISKILIANNGIAAVKEIRSVRKWAyetfgddrtVQFVAMATpeDLEANAEYIRMADQYIEVpGGTNNNNYANVDLIVDI 137
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMG---------IRSVAIYS--EADRHALHVKRADEAYSI-GADPLAGYLNPRRLVNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 138 AERADVDAVWAGWGHASENPLLPEKLSQskRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDTVhvdekt 217
Cdd:PRK07178 69 AVETGCDALHPGYGFLSENAELAEICAE--RGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADL------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 218 glvsvdddiyqkgcctspEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIP---GSP-IFIMKLA 293
Cdd:PRK07178 141 ------------------DEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVFLEKCI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 294 GRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHdDG 373
Cdd:PRK07178 203 VNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDA-DG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 374 KFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPM-HRISDIRtlygmnpHSASEIDFefktqdatkkqrrpipkg 452
Cdd:PRK07178 282 EVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQ-------HRGFALQF------------------ 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 453 hctacRITSEDPNDGFKPSGGTLHElnfrsssnvwgYFSVGNNG-----------NIHSFSDSQFGHIFAFGENRQASRK 521
Cdd:PRK07178 337 -----RINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytgyTIPPYYDSMCAKLIVWALTWEEALD 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324343 522 HMVVALKELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDdliTH----KMTAEKPDPTLAVICGAATKA 589
Cdd:PRK07178 401 RGRRALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE---SHpeltNYSIKRKPEELAAAIAAAIAA 468
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
59-588 |
3.49e-69 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 242.03 E-value: 3.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRkwayetfgdDRTVQFVAMATPEDLEAnaEYIRMADQYIEVpGGTNNNNYANVDLIVDIA 138
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPDREC--LHVKIADEAYRI-GTDPIKGYLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLSQSKrkVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPwsGTgvdtvhvdEKTG 218
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAG--IIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVP--GT--------EKLN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 219 LVSVDDDIYQkgcctspedglqkAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANE----IPGSPIFIMKLAG 294
Cdd:PRK08463 138 SESMEEIKIF-------------ARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFESCKREalayFNNDEVFMEKYVV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 295 RARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYShDDGK 374
Cdd:PRK08463 205 NPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD-DYNR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 375 FYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGipmhRISDIrtlygmnphsaseidfefkTQDATKkqrrpiPKGHC 454
Cdd:PRK08463 284 FYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAG----EILDL-------------------EQSDIK------PRGFA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 455 TACRITSEDPNDGFKPSGGTLHEL------NFRSSSNVWGYFSvgnngnIHSFSDSQFGHIFAFGENRQASRKHMVVALK 528
Cdd:PRK08463 335 IEARITAENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYT------IPPYYDSMLAKLIVKATSYDLAVNKLERALK 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324343 529 ELSIRGdFRTTVEYLIKLLETEDFEDNTITTGWLDDLI------THKMTAEKPDPTLAVICGAATK 588
Cdd:PRK08463 409 EFVIDG-IRTTIPFLIAITKTREFRRGYFDTSYIETHMqellekTEDRHQENKEEVIAAIAAALKK 473
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
185-412 |
1.16e-56 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 195.99 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 185 DKISSTIVAQSAKVPCIPWSGTGVDTVhvdektglvsvdddiyqkgcctspEDGLQKAKRIGFPVMIKASEGGGGKGIRQ 264
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETE------------------------EEALAAAKEIGYPVIIKAAFGGGGLGMGI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 265 VEREEDFIALYHQAANEIPGSP----IFIMKLAGRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAE 340
Cdd:pfam02786 57 ARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324343 341 TFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPM 412
Cdd:pfam02786 137 ERQMLREAAVKIARHLGYVGAGTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
59-179 |
1.08e-40 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 146.09 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 59 ISKILIANNGIAAVKEIRSVRKWAYETfgddrtvqfVAMATPEDleANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIA 138
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRT---------VAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6324343 139 ERADVDAVWAGWGHASENPLLPEKLsqSKRKVIFIGPPGNA 179
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARAC--EEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
131-411 |
7.72e-40 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 149.64 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 131 VDLIVDIAERADVDAVWAGWGHASEN-PLLPEKLsqskrkvifiGPPGN---AMRSLGDKISSTIVAQSAKVPCIPWSgt 206
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVETaAELAEEL----------GLPGPspeAIRAMRDKVLMREALAAAGVPVPGFA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 207 gvdtvhvdektglvsvdddiyqkgCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEI---- 282
Cdd:COG0439 74 ------------------------LVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkags 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 283 PGSPIFIMK-LAGraRHLEVQLLADQYGTNIslfgrdCSVQRRHQK---IIE---EAPVTIaKAETFHEMEKAAVRLGKL 355
Cdd:COG0439 130 PNGEVLVEEfLEG--REYSVEGLVRDGEVVV------CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRA 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324343 356 VGYV-SAGTVEYLYsHDDGKFYFLELNPRLQVEH--PTTEMVSGVNLPAAQLQIAMGIP 411
Cdd:COG0439 201 LGYRrGAFHTEFLL-TPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
457-563 |
3.44e-30 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 115.97 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 457 CRITSEDPNDGFKPSGGTLHELNFRSSSNVwgYFSVGNNGNIH--SFSDSQFGHIFAFGENRQASRKHMVVALKELSIRG 534
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEvpPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 6324343 535 dFRTTVEYLIKLLETEDFEDNTITTGWLD 563
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
457-564 |
5.54e-28 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 109.89 E-value: 5.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 457 CRITSEDPNDGFKPSGGTLHELNFRSSSNVWGYFSVGNNGNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELSIRGdF 536
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 6324343 537 RTTVEYLIKLLETEDFEDNTITTGWLDD 564
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1579-1893 |
1.27e-18 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 92.01 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1579 GRQFVVVANDITFKIGSFGPQEDEFFNKVTEYARKRGIPRIYLAANSGARIGMaeeivplfqvawndaanpdkgfqylyl 1658
Cdd:COG4799 81 GRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQE--------------------------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1659 tsegmetlkkfdkensvltertvingeerfviktiigsedglGVECLRGSGLIAGATSRAYHDIFTITLVTCRSVGIGAY 1738
Cdd:COG4799 134 ------------------------------------------GVESFAGYGRIFYRNARSSGGIPQISVIMGPCAAGGAY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1739 LVRLGQRAIQVEGQPII-LTGAPAINKMLGREVytSNLQLGGTQI-MYNNGVSHLTAVDDLAGVEKIVEWMSYVPAKRNM 1816
Cdd:COG4799 172 SPALSDFVIMVKGTSQMfLGGPPVVKAATGEEV--TAEELGGADVhARVSGVADYLAEDEEEALALARRLLSYLPSNNLE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1817 PVPILETKDTWDRP---VDFTPTND-ETYDVRWMIEGretesgfeygLFDKGSFFETLSGWAKGVVVGRARLGGIPLGVI 1892
Cdd:COG4799 250 DPPRAEPAPPARDPeelYGIVPEDPrKPYDMREVIAR----------LVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIV 319
|
.
gi 6324343 1893 G 1893
Cdd:COG4799 320 A 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
701-767 |
1.31e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 79.18 E-value: 1.31e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324343 701 TQLRTPSPGKLV-----KFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIVQLLKQP-GSTIVAGDIMAIM 767
Cdd:pfam00364 1 TEIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
702-767 |
1.38e-17 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 78.61 E-value: 1.38e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324343 702 QLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVkEILVKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
111-411 |
1.09e-15 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 81.51 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 111 RMADQYIEVPGGTNNNNyANVDLIVDIAERADVDAVWA---GWGHA-SEN-PLLPEKlsqskrkVIFIGPPGNAMRSLGD 185
Cdd:COG3919 46 RYVDEVVVVPDPGDDPE-AFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEEH-------YRLPYPDADLLDRLLD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 186 KISSTIVAQSAKVPcIPwsgtgvDTVHVDEKTGLVSVDDDIyqkgcctspedglqkakriGFPVMIKASEG--------G 257
Cdd:COG3919 118 KERFYELAEELGVP-VP------KTVVLDSADDLDALAEDL-------------------GFPVVVKPADSvgydelsfP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 258 GGKGIRQVEREEDFIALYHQAANE---------IPGspifimklaGRARHLEVQLLADQYGTnISLFgrdCSVQRRHQKI 328
Cdd:COG3919 172 GKKKVFYVDDREELLALLRRIAAAgyelivqeyIPG---------DDGEMRGLTAYVDRDGE-VVAT---FTGRKLRHYP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 329 IEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFYFLELNPRL--QVEHPTtemVSGVNLPAAQLQI 406
Cdd:COG3919 239 PAGGNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFwrSLYLAT---AAGVNFPYLLYDD 315
|
....*
gi 6324343 407 AMGIP 411
Cdd:COG3919 316 AVGRP 320
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
233-409 |
4.73e-10 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 65.41 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 233 TSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGSPIFIMKLAGRARHLEVQLLADqyGTNI 312
Cdd:TIGR01369 691 TSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSD--GEEV 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 313 SLFGrdcsvQRRHqkiIEEA------------PVTIAkAETFHEMEKAAVRLGKLVGYVSAGTVEYLYshDDGKFYFLEL 380
Cdd:TIGR01369 769 LIPG-----IMEH---IEEAgvhsgdstcvlpPQTLS-AEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEV 837
|
170 180
....*....|....*....|....*....
gi 6324343 381 NPRLQVEHPTTEMVSGVNLPAAQLQIAMG 409
Cdd:TIGR01369 838 NPRASRTVPFVSKATGVPLAKLAVRVMLG 866
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
232-383 |
2.39e-08 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 59.12 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 232 CTSPEDGLQKAKRIGFPVMIKASE--GGGGKGIrqVEREEDFIALYHQAANEIPGSPIFIMK-LAGrARHLEVQLLADQY 308
Cdd:COG0458 135 ATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLIDEsLLG-AKEIEVDVVRDGE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 309 GTNISLfgrdCSVQrrHqkiIEEA------------PVTIAKAEtFHEMEKAAVRLGKLVGYVsaGTVEYLYSHDDGKFY 376
Cdd:COG0458 212 DNVIIV----GIME--H---IEPAgvhsgdsicvapPQTLSDKE-YQRLRDATLKIARALGVV--GLCNIQFAVDDGRVY 279
|
....*..
gi 6324343 377 FLELNPR 383
Cdd:COG0458 280 VIEVNPR 286
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
698-767 |
4.35e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 59.00 E-value: 4.35e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324343 698 NDPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVkRVLVKAGDQVEAGDLLVEL 1144
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
698-767 |
5.41e-08 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 58.55 E-value: 5.41e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324343 698 NDPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:COG1038 1074 GNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVkEVLVKEGDQVEAGDLLIEL 1144
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
205-384 |
3.62e-07 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 55.78 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 205 GTGVDTVHVDE-----KTGLVSVDDDIYQKGCCTSPEDGLQKAKRIGFPVMIKASE--GGGGKGIrqVEREEDFIALYHQ 277
Cdd:TIGR01369 116 GTPVEAIKKAEdrelfREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAER 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 278 AANEIPGSPIFIMK-LAGrARHLEVQLLADQYGTNISLfgrdCSvqrrhqkiIEEA-PV--------TIAKAET-----F 342
Cdd:TIGR01369 194 ALSASPINQVLVEKsLAG-WKEIEYEVMRDSNDNCITV----CN--------MENFdPMgvhtgdsiVVAPSQTltdkeY 260
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324343 343 HEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFYFLELNPRL 384
Cdd:TIGR01369 261 QMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRV 302
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
102-410 |
3.51e-06 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 51.84 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 102 DLEANAEYIRMADQYIEVPGGTNNNNYANVDLIVD-IAERADVDAVWAGWGHASEnpllPEKLSQSKRKVIFIGPPGNAM 180
Cdd:COG2232 32 DLFADLDTRALAERWVRLDAESCGFDLEDLPAALLeLAAADDPDGLVYGSGFENF----PELLERLARRLPLLGNPPEVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 181 RSLGDKISSTIVAQSAKVPCIPWSGTGvdtvhvdektglvsvDDDIYqkgcctspedglqkakrigfPVMIKASEGGGGK 260
Cdd:COG2232 108 RRVKDPLRFFALLDELGIPHPETRFEP---------------PPDPG--------------------PWLVKPIGGAGGW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 261 GIRQVeREEDFIA--LYHQAanEIPGSPIFIMKLA--GRARHLEV--QLLAD------QYGTNISlfgrdcsvqrrhqki 328
Cdd:COG2232 153 HIRPA-DSEAPPApgRYFQR--YVEGTPASVLFLAdgSDARVLGFnrQLIGPagerpfRYGGNIG--------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 329 ieeaPVTIAKAETfHEMEKAAVRLGK---LVGYVSAGTVEylyshDDGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQ 405
Cdd:COG2232 215 ----PLALPPALA-EEMRAIAEALVAalgLVGLNGVDFIL-----DGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLR 284
|
....*
gi 6324343 406 IAMGI 410
Cdd:COG2232 285 ACRGE 289
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
230-383 |
3.65e-06 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 52.47 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 230 GCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGSPIFIMKLAGRARHLEVQLLADQYG 309
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEG 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 310 tNISLFG--------------RDCSVQRrhQKIIEEAPVTIAKAETfhemeKAAVRLGkLVGYVSagtVEYLYSHdDGKF 375
Cdd:PLN02735 801 -NVVIGGimehieqagvhsgdSACSLPT--QTIPSSCLATIRDWTT-----KLAKRLN-VCGLMN---CQYAITP-SGEV 867
|
....*...
gi 6324343 376 YFLELNPR 383
Cdd:PLN02735 868 YIIEANPR 875
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
701-767 |
3.73e-06 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 46.32 E-value: 3.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324343 701 TQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:PRK08225 2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVkKINVQEGDFVNEGDVLLEI 69
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
232-435 |
1.18e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 50.74 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 232 CTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYhqAANEIPGSPIFIMKLAgRARHLEVQLLADqyGTN 311
Cdd:PRK12815 691 ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAISD--GED 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 312 ISLFGrdcsvqrrhqkI---IEEA------------PVTIAKAETfHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDgkFY 376
Cdd:PRK12815 766 VTIPG-----------IiehIEQAgvhsgdsiavlpPQSLSEEQQ-EKIRDYAIKIAKKLGFRGIMNIQFVLANDE--IY 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6324343 377 FLELNPRlqvehpttemvSGVNLPAaqLQIAMGIPMHRISdIRTLYGmnpHSASEIDFE 435
Cdd:PRK12815 832 VLEVNPR-----------ASRTVPF--VSKATGVPLAKLA-TKVLLG---KSLAELGYP 873
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
230-383 |
3.43e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 49.33 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 230 GCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGSPIFIMKLAGRARHLEVQLLADqyG 309
Cdd:PRK05294 688 GTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAICD--G 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 310 TNISLFGrdcsvqrrhqkI---IEEA------------PVTIAKaETFHEMEKAAVRLGKLVGYVSAGTVEYLYshDDGK 374
Cdd:PRK05294 766 EDVLIGG-----------ImehIEEAgvhsgdsacslpPQTLSE-EIIEEIREYTKKLALELNVVGLMNVQFAV--KDDE 831
|
....*....
gi 6324343 375 FYFLELNPR 383
Cdd:PRK05294 832 VYVIEVNPR 840
|
|
| PRK07051 |
PRK07051 |
biotin carboxyl carrier domain-containing protein; |
684-732 |
3.96e-05 |
|
biotin carboxyl carrier domain-containing protein;
Pssm-ID: 180811 [Multi-domain] Cd Length: 80 Bit Score: 43.85 E-value: 3.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 6324343 684 RLSVDSMTTLLEVENDPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIE 732
Cdd:PRK07051 31 AVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
107-402 |
5.81e-05 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 47.24 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 107 AEYIRMADQYIEVPGGtnnnnyanvDLIVDIAERADVDAVW--AGWGHASENPLlpEKLSQSKRKVIfigPPGNAMRSLG 184
Cdd:COG0189 30 VEVIDPDDLTLDLGRA---------PELYRGEDLSEFDAVLprIDPPFYGLALL--RQLEAAGVPVV---NDPEAIRRAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 185 DKISSTIVAQSAKVPcIPwsgtgvdtvhvdeKTGLVSvdddiyqkgcctSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQ 264
Cdd:COG0189 96 DKLFTLQLLARAGIP-VP-------------PTLVTR------------DPDDLRAFLEELGGPVVLKPLDGSGGRGVFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 265 VEREEDFIAlYHQAANEIPGSPIFimklagrarhleVQ-LLADQYGTNISLF---GRD-CSVQRRHQKiiEEAPVTIA-- 337
Cdd:COG0189 150 VEDEDALES-ILEALTELGSEPVL------------VQeFIPEEDGRDIRVLvvgGEPvAAIRRIPAE--GEFRTNLArg 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324343 338 -KAETFH---EMEKAAVRLGKLVGYVSAGtVEYLYshDDGKFYFLELNPRLQVEHptTEMVSGVNLPAA 402
Cdd:COG0189 215 gRAEPVEltdEERELALRAAPALGLDFAG-VDLIE--DDDGPLVLEVNVTPGFRG--LERATGVDIAEA 278
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1722-1989 |
7.70e-05 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 47.88 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1722 IFTITLVTCRSVGIGAYLVRLGQRAIQVEGQ-PIILTGAPAINKMLGREVYTSNLqlGGTQIMYN-NGVSHLTAVDDLAG 1799
Cdd:PLN02820 206 IPQIALVLGSCTAGGAYVPAMADESVIVKGNgTIFLAGPPLVKAATGEEVSAEDL--GGADVHCKvSGVSDHFAQDELHA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1800 VE---KIVEWMsYVPAKRNMPVPILETKDTWDRPV-------DFTPTN-DETYDVRWMIEGretesgfeygLFDKGSFFE 1868
Cdd:PLN02820 284 LAigrNIVKNL-HLAAKQGMENTLGSKNPEYKEPLydvkelrGIVPADhKQSFDVRSVIAR----------IVDGSEFDE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 1869 TLSGWAKGVVVGRARLGGIPLGVIGvetrtvenlipadpanpNSAetliqepgqVWHPNSAFKTAQAInDFNNGEQLPMM 1948
Cdd:PLN02820 353 FKKNYGTTLVTGFARIYGQPVGIIG-----------------NNG---------ILFTESALKGAHFI-ELCAQRGIPLL 405
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6324343 1949 ILANWRGFSGGQRDMFNEVLKYGSFIVDALVDYKQPIIIYI 1989
Cdd:PLN02820 406 FLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITII 446
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
233-384 |
1.07e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 47.66 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 233 TSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGSPIFIMK-LAGrARHLEVQLLADQYGTN 311
Cdd:PRK12815 150 TSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEEsIAG-WKEIEYEVMRDRNGNC 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 312 ISLfgrdCSVQRrhqkiIEeaPV--------TIAKAET-----FHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFYFL 378
Cdd:PRK12815 229 ITV----CNMEN-----ID--PVgihtgdsiVVAPSQTltddeYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLI 297
|
....*.
gi 6324343 379 ELNPRL 384
Cdd:PRK12815 298 EVNPRV 303
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
678-767 |
1.26e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 47.14 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 678 EEVAATRLSVDSMTTLLEVENdPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGS 756
Cdd:PRK09282 501 EEVVVEPLKEIVVGGRPRASA-PGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVkEILVKEGD 579
|
90
....*....|.
gi 6324343 757 TIVAGDIMAIM 767
Cdd:PRK09282 580 RVNPGDVLMEI 590
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
709-767 |
1.38e-04 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 42.36 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 709 GKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGDIMAIM 767
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLlEILVKEGDTVPVGAVIAVI 76
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
706-762 |
6.84e-04 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 42.16 E-value: 6.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324343 706 PSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIVQ-LLKQPGSTIVAGD 762
Cdd:PRK05641 90 PMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKkILVKEGDTVDTGQ 147
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
241-385 |
8.06e-04 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 42.37 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324343 241 KAKRIGFPVMIKASEGGGGKGIRQVE-REEDFIALYHQAANE-IPGSPIFIMKLAG--RARHLEV--QLLADQYGTNISL 314
Cdd:pfam02655 26 ELLREEKKYVVKPRDGCGGEGVRKVEnGREDEAFIENVLVQEfIEGEPLSVSLLSDgeKALPLSVnrQYIDNGGSGFVYA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6324343 315 FGRDCSVQRRHQKIIEEApvtiakaetfhemEKAAVRLGKLVGYVSagtVEYLYShdDGKFYFLELNPRLQ 385
Cdd:pfam02655 106 GNVTPSRTELKEEIIELA-------------EEVVECLPGLRGYVG---VDLVLK--DNEPYVIEVNPRIT 158
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
232-285 |
1.17e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 43.99 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324343 232 CTSPEDGLQKAKRIGFPVMIKASEGGGGKGIR-QVEREEDFIALYHQAANE---------IPGS 285
Cdd:PRK14016 235 VTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTvNITTREEIEAAYAVASKEssdviveryIPGK 298
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
706-762 |
2.53e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 40.18 E-value: 2.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6324343 706 PSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIV-QLLKQPGSTIVAGD 762
Cdd:PRK06549 67 PMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVtAIHVTPGQVVNPGD 124
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
704-766 |
8.24e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 38.72 E-value: 8.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324343 704 RTPSPGKlvKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENG-IVQLLKQPGSTIVAGDIMAI 766
Cdd:COG0511 73 RAPSPGA--KPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGtVVEILVENGQPVEYGQPLFV 134
|
|
| |
