ID   S7ZER6_PENO1            Unreviewed;       683 AA.
AC   S7ZER6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN   ORFNames=PDE_03715 {ECO:0000313|EMBL:EPS28769.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS28769.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS28769.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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; KB644411; EPS28769.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7ZER6; -.
DR   STRING; 933388.S7ZER6; -.
DR   eggNOG; KOG1536; Eukaryota.
DR   HOGENOM; CLU_006150_1_1_1; -.
DR   OrthoDB; 317678at2759; -.
DR   PhylomeDB; S7ZER6; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
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:UP000019376}.
FT   DOMAIN          394..602
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   683 AA;  74805 MW;  69FF093D807B4183 CRC64;
     MATPTGNNAI LTGKKLNVLV YSGTGTTVDS VRHCLYTLRR LLAPNYAVTP VTGDMILKEP
     WMATCALLVI PGGADMGYAR TLNGEGNRRI TQFVRRGGKY LGLCAGGYYG CKRCEFEVGD
     KTMEVIGDRE LGFFPGTCRG GAFPGFVYHS EAGAKAARID VSKETLSIGT VPTQFRSYYN
     GGGVFVDAPK MQDKGVEVLA SYSEKLNVDP GEGAAAVVYC KVGDGAAILT GPHPEFAAVN
     LDPQANGPEY KEIVDALAAD DKERTDFLKA CLSKLGLQVS QDSTVVPSLS SLHVSGLDTD
     DTLDILASLA PSLTNEGQKE YLKDENDTFR IERPGTWNLN DLEDALPEGS SSSHEGIVDY
     KEVIKRLVFH DEIPSSKITP YFNHHAFYAN LRQYQSDSKE GASTFGSKLM YGEVLTSTNT
     ILEKNVKLLR QLPHGFTATA TVQVAGRGRG SNVWISPAGS LMFSTIVRHP VEKIQSAPVI
     FIQYLSAMAV VKGIKSYAKG YETLPVKLKW PNDIYALDPE DPEQKRYTKI CGILINSHFM
     SNEYISVVGI GLNATNASPT TALTALAARY ATPGAAAASP ITLEKLLARI LTTFEELYTR
     FLRTGFDRAF EAMYYEDWLH MHQIVTLEEE GGARARIQGI TRDYGLLLAE ELAWDDRPTG
     RVWQLQSDSN SFDFFRGLLK RKV
//