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Database: UniProt
Entry: C5FVB5_ARTOC
LinkDB: C5FVB5_ARTOC
Original site: C5FVB5_ARTOC 
ID   C5FVB5_ARTOC            Unreviewed;       712 AA.
AC   C5FVB5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:EEQ33849.1};
GN   ORFNames=MCYG_06668 {ECO:0000313|EMBL:EEQ33849.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33849.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; DS995706; EEQ33849.1; -; Genomic_DNA.
DR   RefSeq; XP_002844704.1; XM_002844658.1.
DR   AlphaFoldDB; C5FVB5; -.
DR   STRING; 554155.C5FVB5; -.
DR   GeneID; 9227102; -.
DR   VEuPathDB; FungiDB:MCYG_06668; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_000395_3_1_1; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT   DOMAIN          37..485
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          153..351
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          626..704
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   712 AA;  77303 MW;  BC5D738870E0C9FB CRC64;
     MSFLLRASAS RIPQRALFAA PSLRHSSSTA TGKGTTSLHS ILIANRGEIA LRVGRTAGQH
     GIRVTTLYTD PDAHAQHALS SPFAFNLGET SAYLDGDRII EIAKREGCKG IHPGYGFLSE
     NAGFAKKCTD AGLIFIGPPP SAIDAMGDKS RSKEIMTAAG VPCVPGYHGT NQDVNFLAAE
     AEKIKYPVLI KAVKGGGGKG MRIARSAAEF QDQLKSAKSE AMSSFGDDTM LIEKYIITPR
     HIEVQVFADQ HGNSVALGER DCSVQRRHQK VLEESPAPHL PEATRKDLWA KARDAALAVG
     YEGAGTVEFI FDNDTGEFFF MEMNTRLQVE HPVTEMVTGQ DLVHWQLLVA EGAPLPLTQE
     EVEAKMATMG HAIEARIYAE NPEQNFVPDS GKLIHVRTPQ PTEDVRIDAG FVAGDEVSSH
     YDPMISKLIV RGADRTEALR NLSMALEQYE VAGPITNIEF LKRVCKSPDF VAGEVETGYI
     EKHREELFAK APVEPELWAQ VALSTFISGT SLSNPVGNTG AGVGFSPGYQ QRQFTFVEAT
     APNTPEATPA TVQIHQTGPS SYDVTVNNEK TFSNVTASLS ADGKALTSFF PHTRLDTTVI
     RDEDSITAFQ HGRQYRLKVP RAKWMEKALG IKELANSVLA PMPCKILRVE VAEGAVVEKD
     QPLVVIESMK METVIRSPIK GVVEKIVHKQ GDICKAGTAL VEFAAEPKAP ES
//
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