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Database: UniProt
Entry: A0A1S8W969_9FUNG
LinkDB: A0A1S8W969_9FUNG
Original site: A0A1S8W969_9FUNG 
ID   A0A1S8W969_9FUNG        Unreviewed;       655 AA.
AC   A0A1S8W969;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   03-MAY-2023, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OON10663.1};
GN   ORFNames=BSLG_00562 {ECO:0000313|EMBL:OON10663.1};
OS   Batrachochytrium salamandrivorans.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON10663.1, ECO:0000313|Proteomes:UP000189906};
RN   [1] {ECO:0000313|EMBL:OON10663.1, ECO:0000313|Proteomes:UP000189906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS {ECO:0000313|EMBL:OON10663.1,
RC   ECO:0000313|Proteomes:UP000189906};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OON10663.1}.
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DR   EMBL; LYON01000042; OON10663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8W969; -.
DR   STRING; 1357716.A0A1S8W969; -.
DR   VEuPathDB; FungiDB:BSLG_00562; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000189906; 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; 3.30.700.30; -; 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; IPR041265; PCC_BT.
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   Pfam; PF18140; PCC_BT; 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:UP000189906}.
FT   DOMAIN          1..425
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          97..294
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          574..649
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   655 AA;  71975 MW;  23B2EF6ABC425B1E CRC64;
     MGIKTVAIYS DADVNSLHVR LADEAVNVGP PATSKSYLNI PNIIGAIQKT GAQAVHPGYG
     FLSENSQFVH ALDAIGAVFI GPNESAMAAM GDKIQSKIIA KKANVTTIPG FDGVVNDVDH
     AIQIANEIGY PVMVKASAGG GGKGMRIAWN DKEAREAFKI SSSEALSSFG DSRLLVEKFI
     EDPRHIEIQL IGDQHGNVIY LPERECSIQR RNQKVIEEAP SMHIDAATRK AMGEQAVALA
     QNVGYYSAGT CEFLVDPRRN FYFLEMNTRL QVEHPITEYI TGLDLVEQMI RVAAKQKLDF
     KQSDIKINGW AFESRVYAED PEKYLPSIGR LNKYIEPIIP ASGSVRCDSG IVEGSEISIY
     YDPLICKLCT HGPTREDAMN EMKHALDTYV IKGVTHNVPL LRDVMSHPRF ESGKISTAFL
     AEVYPNGFKG HQLSDQSRFE LLSVAGYIFA RRDLRNRSWI EGGGSIASGI RPKQTWDLHI
     STGDNLYHDI SVVKKGDSFV ISANGESVTV AADWALDSPL INASFTQGGA ESKVVVQYLD
     SLPLGFRLQH YGTKFDVQVR TKTQHELSVH MKEREKIDLT RMILSPMPGS VVSVSVKVDD
     VVAEGSELAV VEAMKMQNVI RAPRSGKVKK VNVQAGASVA GDEIMIEFYD DQIKK
//
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