ID   A0A2L2TBZ6_9HYPO        Unreviewed;       669 AA.
AC   A0A2L2TBZ6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI60476.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|ARBA:ARBA00009934}.
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; LN649230; CEI60476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2TBZ6; -.
DR   STRING; 56646.A0A2L2TBZ6; -.
DR   OrthoDB; 317678at2759; -.
DR   Proteomes; UP000245910; Chromosome ii.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   CDD; cd16442; BPL; 1.
DR   CDD; cd03144; GATase1_ScBLP_like; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR019197; Biotin-prot_ligase_N.
DR   InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   NCBIfam; TIGR00121; birA_ligase; 1.
DR   PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF09825; BPL_N; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245910}.
FT   DOMAIN          388..588
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   669 AA;  73728 MW;  E6AC732B7DBFF735 CRC64;
     MAPAKLNVLV YTGLGTTVES VKHCIWSLRR LLGPNYAVIP ITETIILKEP WQATCALLVF
     PGGGDLGYCQ ALNGEGNRRI GDYVRRGGSY LGFCAGGYYG TQRCEFEVGN KPMEVIGRRE
     LGFFPGTCRG GAFKGFEYKS ERGARAVRLS VPKDAFEQEV ASEIISYYNG GGVFVDAASV
     KDRKVEVLAT YDEEIDVDGG DGKAAVVLCT VGDGKALLTG PHPEFAASNL NSQPSLPDYD
     ELISQLAAAD KDRATFLKGC LTKLGLEVSS HDNGVPSLSR LHLSSISDTG VSELLSDWSD
     IINKEDGEEW IRAETDNFHI QNEETIWNLE GLQQSLPDTT EASISENGSI DYSKITKKIV
     PHEKGLPHPK LTPHFNHGLF FSSLKRYRQI EPTARAWGDL LMYGEVVTST NTMLEKNPKL
     MPKLPSGFTV SATTQVAGRG RGSNVWIAPP GMLIFSTIIN HPAHLAVSHP VVFIQYIASI
     AIVEAVQSYD RGYDKIPIKI KWPNDIYALD PTRSQEKPHY SKVGGMLSQC VYFDGKYQII
     LGIGLNTLNS RPTMSISDLV PAGAPELHLE TLLARVLTRI EAIYAQFLRE GFSSGLEARY
     YRHWLHTRQE VSLEAEGGVK ARVLGITRDW GMLKVEEIDA SGRAIGKTWA LQSDENSFDF
     WKGLVRRKT
//