GenomeNet

Database: UniProt
Entry: C0NSM2_AJECG
LinkDB: C0NSM2_AJECG
Original site: C0NSM2_AJECG 
ID   C0NSM2_AJECG            Unreviewed;       600 AA.
AC   C0NSM2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Carboxylase:pyruvate/acetyl-CoA/propionyl-CoA {ECO:0000313|EMBL:EEH05888.1};
GN   ORFNames=HCBG_06152 {ECO:0000313|EMBL:EEH05888.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05888.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG663370; EEH05888.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NSM2; -.
DR   STRING; 447093.C0NSM2; -.
DR   VEuPathDB; FungiDB:I7I50_01840; -.
DR   VEuPathDB; FungiDB:I7I50_06502; -.
DR   HOGENOM; CLU_000395_3_2_1; -.
DR   InParanoid; C0NSM2; -.
DR   OrthoDB; 2785982at2759; -.
DR   Proteomes; UP000001631; 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; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
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; PTHR45007; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-RELATED; 1.
DR   PANTHER; PTHR45007:SF1; CARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G07570)-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:UP000001631}.
FT   DOMAIN          9..405
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          114..350
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          504..585
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          88..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  64724 MW;  D0FDDA70271392D2 CRC64;
     MSPPPPARPI KRLLVANRGE IAVRILQAAR ELPNIETFAL YTADDRSHCD LGAPHHAVAL
     PSPSSYMDIA LLVQLALEHS IDTIHPGIRP ANVGGSRGQS HRSRLGGTGK DRRQAASEDA
     GGGMSRADFE SDENATSDIG LIRQFVAEVG YPVMVKAVDG GGGRGIRFVK GPDELQSAID
     RATGESPSKK VFVEKAAVGG FHHVEVQVVG DGTGEIKYLS LGTFEFLASE KLSKFYFLEI
     NPRLQVEHTI TECISTVDLV QTQLLLAQGV SLRDMGLGDI ENPEQPPATY SIQLRLCAED
     PTADFALSIG KITEFHVPGG NSVRVDTHVS GSSSVVIGSD FDNMMAKIIV TSTSWDGVVR
     KACRVLNDAR ISEVKTNIDV LKGIIGNIEF QEWQIRDAMD GKEFGRYHST WKAAASSLGS
     SSVLFRKGDA WSIELAPLNS TKGSGSQAPH HLLLSKLFRN EFPTSLSAEI EYTTPATATQ
     TARTTPYRVT LARTLASSSS LSSTHRRGNP NNSSHITLPM SGKLTEMLVE EGDDIQENSV
     IAFVKQMKME LEVRSPKAGR VTWALELEDG DGEGVPEGIL LAEVTPIDPP EQGVEVKGKL
//
DBGET integrated database retrieval system