ID A0A0J0XU96_9TREE Unreviewed; 693 AA.
AC A0A0J0XU96;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 22-FEB-2023, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KLT44640.1};
GN ORFNames=CC85DRAFT_242131 {ECO:0000313|EMBL:KLT44640.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT44640.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT44640.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT44640.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) 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; KQ087185; KLT44640.1; -; Genomic_DNA.
DR RefSeq; XP_018281131.1; XM_018420239.1.
DR AlphaFoldDB; A0A0J0XU96; -.
DR STRING; 879819.A0A0J0XU96; -.
DR GeneID; 28980842; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000053611; 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; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; PS00866; CPSASE_1; 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:UP000053611}.
FT DOMAIN 24..470
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 143..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 610..686
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 693 AA; 74246 MW; 8E655486B77F7355 CRC64;
MATAAPSTLS PNAQGFEPRT DAKKLNKVLI ANRGEIACRV IKTARKLGVK TVAVYSDADK
DCLHVEMADE AYHIGPAPAA ESYLVAEKLL QVAAASGADG IHPGYGFLSE SPAFAAAVGK
AGIAFIGPPA EAIRAMGSKR ESKEIMVAAG VPCVPGYHGA NQDEDVLVKA ASDVGFPLLI
KPTHGGGGKG MRVVRKLDDF VEELRSAKRE AAKSFGNDEV LLERWLERPR HIEVQVFADS
QGNCVSLWER DCSVQRRHQK IIEEAPAPGL SAAIKKDLAD KAVAAAKAVN YVGAGTVEFI
MDADSGEFFF MEMNTRLQVE HPVTEEVTGV DLVQWQLSVA AGNPLPVTQD DIPCIGHAFE
ARIYAERPEA NFLPDAGRLI HTAAPRDAPH RLDTGFREGD DVSSYYDPMI AKLIVHGRDR
NEALALLRSA LDQYQVVGPS TNVEFLRTVA SHPTFAAGPV ETNFIEQHHA ELFPPKKVPA
EILAQAALSI AHHEPGAGAW AALPGRRFSD VNEHTYHFDE GEVVVRQNPD RSYDLSVVVG
DHADAHKAED QGEAVRLHAR ATRTGPNDLV VQFGNSRAEA TIIPHGPKLV VFTPEGSHTL
RRRGAEVEAE GEGGAAADAL VSPMPATVID VRVKPGDKVT EGQVCAVLES MKMEINIRAE
RDGVIAAVSA EKGQAVEEGA VLVALEPAEA EAK
//
