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
//