ID C0P0H6_AJECG Unreviewed; 1280 AA.
AC C0P0H6;
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=3-methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000313|EMBL:EEH02796.1};
GN ORFNames=HCBG_08906 {ECO:0000313|EMBL:EEH02796.1};
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:EEH02796.1, 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};
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DR EMBL; GG663381; EEH02796.1; -; Genomic_DNA.
DR AlphaFoldDB; C0P0H6; -.
DR STRING; 447093.C0P0H6; -.
DR VEuPathDB; FungiDB:I7I50_05362; -.
DR VEuPathDB; FungiDB:I7I50_05364; -.
DR HOGENOM; CLU_006592_0_0_1; -.
DR InParanoid; C0P0H6; -.
DR OrthoDB; 1459320at2759; -.
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; 3.30.470.20; 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:UP000001631}.
FT DOMAIN 602..1050
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 718..916
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1194..1270
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 74..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1280 AA; 140034 MW; 85EFE38C3B534325 CRC64;
MSDDEEYYDD DFDAEWFWFD EGERELADDL AAGTIHSPVY MDQGAYDALD SASDWDYCTD
EYFDDDLSIL HKHDIKPQTP SKGPSVRKKN VMRKGNTMKQ GEQERDDSDN KKDTNTNSFC
RILWRPSSFL DDQGELYEPG NGEKVALLKN WREIFKDSQP KRDHKLQKYS SPSPSPSSAS
PSHLPPPSSF LKSVTGRKQP GRPRKTGKRN VVVESVDTPV FDNEGFSEEG REGGIADGDD
DGEDDGGYRT PPPTFLSASQ QGIYGKSQKT TTGPSHRPKN NGKDHNKRDG SHLKSVISAS
AQEEDLESIP IMASSPSSST ENSKQRSGRL STSSTAATSM STQSATSTSQ NGKGSGEPGT
LFQDGYGKAS GSHIIPPTGT GSSPPTQRRQ GLKRKASSPP ESTDGDYCGK TRSKRATRQK
LDSDAGDDNI DARGKRKTMN NREPPPSKSR SLRQRKKYFF PSRVTRADIV SAQSNKDDLA
RLPTRRDRHL PKSRGLALSG SAILPHAIPR HSALSIGKSY WPRTFLLAFL VCDAAAQLPV
FQHSLTELLR VCTLRTSTRM SFISRLPSTT SRLGARAVIL KPTTAAAVRA NSSLTGGPEN
KPLNSILIAN RGEIALRVGR TASQHGIRVT TLYTDPDARA QHALSSPFAF NLGETSAYLD
GDRIIEIAQK EGCQGIHPGY GFLSENSAFA QKCTQAGLVF IGPPPKAIEA MGDKSRSKEI
MTAAGVPCVP GYHGDNQSME FLEAEAEKIK FPVLIKAVKG GGGKGMRIAS SKETFRDQLI
SAKSEAMNSF GDDTMLVEKY ITTPRHIEVQ VFADKHGNCV ALGERDCSIQ RRHQKILEES
PAPHLPEATR KDIWDKARAA ALAVGYEGAG TVEFIFDNDT GEFFFMEMNT RLQVEHPVTE
MVTGQDLVHW QILVAEGAPL PLTQDEIESI MATKGHAIEA RIYAENPDQG FIPDSGRLLH
VRTPAATEDV RIDAGFVAGD EVSSHYDPMI SKLIVRGSDR TEALRNLSMA LEQYEVAGPI
TNIEFLKRVC KSPDFVSGDV ETGYIDKHRA ELFAKQPVED EVLAQVALYC LLSSSKAGGP
AGAVVGFSPA YQERQFTFVE ATAQASSELS GNAASFNVQV QQTGEATFNI VVNGTSFENV
KVQQQPHESN VVTSFFPHTR LDTTVIRDED AITAFQRGRQ YRLKIPRARW MEKALGIKDT
ANSVLAPMPC KILRVEVVEG ATVVKDQPLV VIESMKMETV IRSPQDGKIE KVVHKAGDIC
KAGTALVEFA EASDAEAKTS
//
