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Database: UniProt
Entry: S3C1T3_OPHP1
LinkDB: S3C1T3_OPHP1
Original site: S3C1T3_OPHP1 
ID   S3C1T3_OPHP1            Unreviewed;       782 AA.
AC   S3C1T3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   05-JUN-2019, entry version 31.
DE   SubName: Full=Methylcrotonoyl-carboxylase subunit alpha {ECO:0000313|EMBL:EPE07509.1};
GN   ORFNames=F503_00231 {ECO:0000313|EMBL:EPE07509.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Ophiostomatales; Ophiostomataceae;
OC   Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE07509.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE07509.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE07509.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S.,
RA   Docking R., Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma
RT   piceae, and a comparison with the bark beetle-associated pine pathogen
RT   Grosmannia clavigera.";
RL   BMC Genomics 14:373-373(2013).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|SAAS:SAAS00197451};
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DR   EMBL; KE148150; EPE07509.1; -; Genomic_DNA.
DR   STRING; 61273.S3C1T3; -.
DR   EnsemblFungi; EPE07509; EPE07509; F503_00231.
DR   OrthoDB; 254436at2759; -.
DR   Proteomes; UP000016923; 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   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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234148};
KW   Biotin {ECO:0000256|SAAS:SAAS00296904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016923};
KW   Ligase {ECO:0000256|SAAS:SAAS00232059};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00234082};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923}.
FT   DOMAIN       50    503       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      163    363       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      695    770       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   REGION       23     50       Disordered. {ECO:0000256|MobiDB-lite:
FT                                S3C1T3}.
SQ   SEQUENCE   782 AA;  84438 MW;  0D39A2208FA2D85F CRC64;
     MRPLKRAAHT RLPLRYPVRY LASTTTTTTT TTTSSTTLPN NASSSSGPAP LPSLLIANRG
     EIALRIHRTA TRMGIPTTTL YTAVDASAQH AKASPRSLAL GSYLDGDRII DLATKHNIRA
     LHPGYGFLSE NAAFAERCAE AGITFVGPPA QAMNEMGDKA RSKAIMLAAG VPCVPGYHGT
     DQTPEQLAAH ADAVGYPVLL KSVRGGGGKG MRIVSTPDEF PAQLTSARAE ARASFGEGGE
     VMLVERYIVR PRHVEVQVFA DTHGACVALG ERDCSVQRRH QKILEESPAP DLDNGLRHDL
     WDKARTAALT VGYVGAGTVE FILDRDTDEF FFMEMNTRLQ VEHPVSELVT GTDLVEWQLR
     VAAGEKLPLT QDEIEARIDS RGHAIEARIY AENPEANFMP DSGKLVHLTT PQPQANNDEN
     SDVRIDAGFV QGDTVSEAYD GMIAKLIVRG DDRQQAIRKL ELALEEYEVV GLHTNIEFLK
     RLCRSEAFQE ADVETGFIDK WRDQLFETKE VSDEVYIQAA LGVLASDVHS DTASSSSIPF
     SGQLHGQPLG FGNSNGGGIS ERSFAFEVLD PYSNRAGDIV EVALTQTGRQ LYNARVSWKK
     KDAKSAKGSV DDTATEVREY DGIVLDTAST HQPTTDATTT KLASFFPLSH VASTVVQQHP
     EGLDEGPVRV TVFQTGSKTD LALVPPPWHA KVLGIDTSSA AASVVAPMPC KILRNEVSVG
     QTVDKGAPLV VIESMKMETV IRSPQAGVVK KLAHKEGDIC KAGTVLVLFE EGEGQGEGED
     KV
//
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