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Conserved domains on  [gi|24586065|ref|NP_652724|]
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Methylcrotonoyl-CoA carboxylase 2 [Drosophila melanogaster]

Protein Classification

carboxyltransferase domain-containing protein( domain architecture ID 1001328)

carboxyltransferase domain-containing protein catalyzes the transcarboxylation from biotin to an acyl-CoA acceptor molecule; similar to methylcrotonyl-CoA carboxylase subunit beta

CATH:  3.90.226.10
Gene Ontology:  GO:0016740|GO:0009374
PubMed:  8102604

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Carboxyl_trans super family cl47203
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
27-578 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.


The actual alignment was detected with superfamily member PLN02820:

Pssm-ID: 481543 [Multi-domain]  Cd Length: 569  Bit Score: 931.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   27 ANVLHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHE 106
Cdd:PLN02820  29 LGVLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  107 LYGEEVvNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPD 186
Cdd:PLN02820 109 LYGEDL-PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  187 KLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHC 266
Cdd:PLN02820 188 RDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHC 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  267 KTSGVTDHYALDDEHALYLARQIVSNLNLSATNSyndqlmhsSQVNFQTATPPSavEEPRYDAEELYGIVGPNLTKSFDV 346
Cdd:PLN02820 268 KVSGVSDHFAQDELHALAIGRNIVKNLHLAAKQG--------MENTLGSKNPEY--KEPLYDVKELRGIVPADHKQSFDV 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  347 REVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGR 426
Cdd:PLN02820 338 RSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGS 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  427 DAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRK 506
Cdd:PLN02820 418 RSEASGIAKAGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKK 497
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24586065  507 RAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM 578
Cdd:PLN02820 498 RQGIQWSKEEEEAFKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
27-578 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 931.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   27 ANVLHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHE 106
Cdd:PLN02820  29 LGVLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  107 LYGEEVvNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPD 186
Cdd:PLN02820 109 LYGEDL-PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  187 KLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHC 266
Cdd:PLN02820 188 RDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHC 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  267 KTSGVTDHYALDDEHALYLARQIVSNLNLSATNSyndqlmhsSQVNFQTATPPSavEEPRYDAEELYGIVGPNLTKSFDV 346
Cdd:PLN02820 268 KVSGVSDHFAQDELHALAIGRNIVKNLHLAAKQG--------MENTLGSKNPEY--KEPLYDVKELRGIVPADHKQSFDV 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  347 REVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGR 426
Cdd:PLN02820 338 RSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGS 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  427 DAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRK 506
Cdd:PLN02820 418 RSEASGIAKAGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKK 497
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24586065  507 RAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM 578
Cdd:PLN02820 498 RQGIQWSKEEEEAFKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
47-576 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 790.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  47 EMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSpFLELSALAGHELYGE-EVVNSGGIVTGVGRV 125
Cdd:COG4799   1 AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDDdDRVPGDGVVTGIGTV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 126 CGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPdklHFGRIFYNQAnMSAQGI 205
Cdd:COG4799  80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFA---GYGRIFYRNA-RSSGGI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 206 PQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYL 285
Cdd:COG4799 156 PQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALAL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 286 ARQIVSNLNlsatnSYNDQLmhssqvnfqtaTPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKL 365
Cdd:COG4799 236 ARRLLSYLP-----SNNLED-----------PPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPL 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 366 YGETLVCGFAKLYGHTVGIVGNN-----GVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKM 440
Cdd:COG4799 300 YGPNIVTGFARIDGRPVGIVANQpmvlaGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKL 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 441 VTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQrkragkefsEEEAQKL 520
Cdd:COG4799 380 LYAVAEATVPKITVILRKAYGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAA---------AEDPEAL 450
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24586065 521 KAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNN--AGQETKFGVF 576
Cdd:COG4799 451 RAELIAEYEEQANPYYAAARGWIDDVIDPRDTRRVLARALEAAANKpeERPPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
73-576 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: 547.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065    73 RHTSRGKLLARERINLLLDKGSpFLELSALAGHEL--YGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVK 150
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGS-FGELEDLFFHRAteFGRKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   151 KHLRAQEIAQENRLPCIYLVDSGGAnlpRQADVFPDKLHFGRIFYNQANMSaQGIPQIAVVMGSCTAGGAYVPAMADESI 230
Cdd:pfam01039  80 KILRAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLAS-GVIPQISLIMGPCAGGGAYLPALGDFVI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   231 IVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNsyndqlmhssq 310
Cdd:pfam01039 156 MVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPN----------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   311 vNFQTATPPSAVEEPRYDAEeLYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNN-- 388
Cdd:pfam01039 225 -NREPVPIVPTKDPPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQpr 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   389 ---GVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNY 465
Cdd:pfam01039 303 vgaGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYV 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   466 GMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKapivEMFEAEGSPYYSTARLWDDG 545
Cdd:pfam01039 383 VMDSKINGADINFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRGKDLAATRKQKIA----EYEEELSPPYVAAARGFADA 458
                         490       500       510
                  ....*....|....*....|....*....|...
gi 24586065   546 IIDPANTRQILGLSLKAALNNAGQ--ETKFGVF 576
Cdd:pfam01039 459 VIDPGRTRAKLVIALAALWTKPRFfpWRKHGNI 491
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
27-578 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 931.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   27 ANVLHSEVDKQSAEYKENAREMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSPFLELSALAGHE 106
Cdd:PLN02820  29 LGVLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  107 LYGEEVvNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPD 186
Cdd:PLN02820 109 LYGEDL-PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  187 KLHFGRIFYNQANMSAQGIPQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHC 266
Cdd:PLN02820 188 RDHFGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHC 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  267 KTSGVTDHYALDDEHALYLARQIVSNLNLSATNSyndqlmhsSQVNFQTATPPSavEEPRYDAEELYGIVGPNLTKSFDV 346
Cdd:PLN02820 268 KVSGVSDHFAQDELHALAIGRNIVKNLHLAAKQG--------MENTLGSKNPEY--KEPLYDVKELRGIVPADHKQSFDV 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  347 REVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNNGVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGR 426
Cdd:PLN02820 338 RSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGS 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  427 DAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRK 506
Cdd:PLN02820 418 RSEASGIAKAGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKK 497
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24586065  507 RAGKEFSEEEAQKLKAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNNAGQETKFGVFRM 578
Cdd:PLN02820 498 RQGIQWSKEEEEAFKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
47-576 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 790.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  47 EMASLVGDLRNFTSQVLKGGGQKAIERHTSRGKLLARERINLLLDKGSpFLELSALAGHELYGE-EVVNSGGIVTGVGRV 125
Cdd:COG4799   1 AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDDdDRVPGDGVVTGIGTV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 126 CGTECLVVANDATVKGGSYYPITVKKHLRAQEIAQENRLPCIYLVDSGGANLPRQADVFPdklHFGRIFYNQAnMSAQGI 205
Cdd:COG4799  80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFA---GYGRIFYRNA-RSSGGI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 206 PQIAVVMGSCTAGGAYVPAMADESIIVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYL 285
Cdd:COG4799 156 PQISVIMGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALAL 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 286 ARQIVSNLNlsatnSYNDQLmhssqvnfqtaTPPSAVEEPRYDAEELYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKL 365
Cdd:COG4799 236 ARRLLSYLP-----SNNLED-----------PPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPL 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 366 YGETLVCGFAKLYGHTVGIVGNN-----GVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKM 440
Cdd:COG4799 300 YGPNIVTGFARIDGRPVGIVANQpmvlaGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKL 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065 441 VTAVACANVPKFTVIIGGSYGAGNYGMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQrkragkefsEEEAQKL 520
Cdd:COG4799 380 LYAVAEATVPKITVILRKAYGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAA---------AEDPEAL 450
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24586065 521 KAPIVEMFEAEGSPYYSTARLWDDGIIDPANTRQILGLSLKAALNN--AGQETKFGVF 576
Cdd:COG4799 451 RAELIAEYEEQANPYYAAARGWIDDVIDPRDTRRVLARALEAAANKpeERPPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
73-576 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: 547.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065    73 RHTSRGKLLARERINLLLDKGSpFLELSALAGHEL--YGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVK 150
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGS-FGELEDLFFHRAteFGRKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   151 KHLRAQEIAQENRLPCIYLVDSGGAnlpRQADVFPDKLHFGRIFYNQANMSaQGIPQIAVVMGSCTAGGAYVPAMADESI 230
Cdd:pfam01039  80 KILRAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLAS-GVIPQISLIMGPCAGGGAYLPALGDFVI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   231 IVKKQGTIFLAGPPLVKAATGEEVSAEDLGGADLHCKTSGVTDHYALDDEHALYLARQIVSNLNLSATNsyndqlmhssq 310
Cdd:pfam01039 156 MVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPN----------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   311 vNFQTATPPSAVEEPRYDAEeLYGIVGPNLTKSFDVREVIARIVDGSRFTEFKKLYGETLVCGFAKLYGHTVGIVGNN-- 388
Cdd:pfam01039 225 -NREPVPIVPTKDPPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQpr 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   389 ---GVLFSESALKGAHFIQLCAQRKIPLVFLQNITGFMVGRDAEANGIAKNGAKMVTAVACANVPKFTVIIGGSYGAGNY 465
Cdd:pfam01039 303 vgaGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYV 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   466 GMCGRAYSPRFLYMWPNSRISVMGGTQAANVMAQITEDQRKRAGKEFSEEEAQKLKapivEMFEAEGSPYYSTARLWDDG 545
Cdd:pfam01039 383 VMDSKINGADINFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRGKDLAATRKQKIA----EYEEELSPPYVAAARGFADA 458
                         490       500       510
                  ....*....|....*....|....*....|...
gi 24586065   546 IIDPANTRQILGLSLKAALNNAGQ--ETKFGVF 576
Cdd:pfam01039 459 VIDPGRTRAKLVIALAALWTKPRFfpWRKHGNI 491
PRK07189 PRK07189
malonate decarboxylase subunit beta; Reviewed
82-297 1.61e-03

malonate decarboxylase subunit beta; Reviewed


Pssm-ID: 235954  Cd Length: 301  Bit Score: 40.66  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065   82 ARERINLLLDKGSpFLEL-----SALAGH-ELYGEEVVNSGGIVTGVGRVCGTECLVVANDATVKGGSYYPITVKKHLRA 155
Cdd:PRK07189  17 ARERAAALLDAGS-FRELlgpfeRVMSPHlPLQGIPPQFDDGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEVHGAKLAGA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  156 QEIAQENRL-----PCIYLVDSGGAnlprqadvfpdKLHfgrifynQAN---------MSA-----QGIPQIAVVMGS-- 214
Cdd:PRK07189  96 LELAAEDNRngiptAVLLLFETGGV-----------RLQ-------EANaglaaiaeiMRAivdlrAAVPVIGLIGGRvg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586065  215 CTAGGAYVPAMADeSIIVKKQGTIFLAGPPLVKAATG-EEVSAED-------LGGAdlHCKTSGVTDHYALDDEHAL--- 283
Cdd:PRK07189 158 CFGGMGIAAALCS-YLIVSEEGRLGLSGPEVIEQEAGvEEFDSRDralvwrtTGGK--HRYLSGLADALVDDDVAAFraa 234
                        250
                 ....*....|....*..
gi 24586065  284 ---YLARQIVSNLNLSA 297
Cdd:PRK07189 235 alaLLARGPFPAAHRSA 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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