ID   A0A094CSA2_9PEZI        Unreviewed;       685 AA.
AC   A0A094CSA2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN   ORFNames=V491_01758 {ECO:0000313|EMBL:KFY25402.1};
OS   Pseudogymnoascus sp. VKM F-3775.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY25402.1, ECO:0000313|Proteomes:UP000029338};
RN   [1] {ECO:0000313|EMBL:KFY25402.1, ECO:0000313|Proteomes:UP000029338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY25402.1,
RC   ECO:0000313|Proteomes:UP000029338};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|ARBA:ARBA00009934}.
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:KFY25402.1}.
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; JPJT01000920; KFY25402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CSA2; -.
DR   HOGENOM; CLU_006150_1_1_1; -.
DR   Proteomes; UP000029338; 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:UP000029338}.
FT   DOMAIN          403..604
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   685 AA;  74939 MW;  71CB1B8EFE333F22 CRC64;
     MVTKKLNVLV YAGTGSTDGA VRHALFTLRR LLSPNYAVFP VSDSVIIKEP WTSSCALLVF
     PGGADLGYCR ILNGAGNDRI SQYVRRGGSY LGFCAGGYYG SQKCEFEVGD KKMEVIGKRE
     LSFFPGICRG CAFNGFVYQS EAGACAAELT VETESFAGID CPKSFKSYYN GGGVFVDAAN
     FKTEGVEVLA TYSKDTDVDG GDCGTRAAAV YCKIGDGCAV LTGPHPEFAA ANLDAKSGGP
     DYSKMIESLI EGDNLRESFM KACLTKMGLL VATIETNTVP PVLSALHISS LHNVEVSELF
     EDLKSDMTLE EGENFVKGEN DTFLIEKNGS PLSLHSLGVS LPQANSQAKE EAETDELRSG
     QDKKNIDYNK LIKRLVFHDG GWPQNTETPN FNHDVFYSEL VDYQDESGSR AEDFGKVLMY
     GDIVTSTNTL LEKNQKLLSH LPNGFTATAT TQVAGRGRGT NVWVSPVGSL IFSTCIRHSL
     ELSAKAPVIF VQYLAAIAIA EGIKSYGKGY QDIPVKLKWP NDIYALDPAK PGNNEYVKIG
     GILVNSSYSS GNYNLVVGIG INTTNPAPTT SLNALRPQHL PEFTIEKLLA RILTRFEDIY
     IKFCRSGFDK QLEETYYKLW LHSEQIITLE AEGGVRARVV GITRDWGFLK VQELGWEDKP
     TGKIIELQTD SNSFDFFRGL VKRKV
//