ID   A0A1V8SQ21_9PEZI        Unreviewed;       616 AA.
AC   A0A1V8SQ21;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN   ORFNames=B0A48_12810 {ECO:0000313|EMBL:OQO01257.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO01257.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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:OQO01257.1}.
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DR   EMBL; NAJO01000031; OQO01257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SQ21; -.
DR   STRING; 1507870.A0A1V8SQ21; -.
DR   InParanoid; A0A1V8SQ21; -.
DR   OrthoDB; 317678at2759; -.
DR   Proteomes; UP000192596; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        409..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          341..535
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   616 AA;  66974 MW;  0C4989F24AFEABAC CRC64;
     MPGGADMGYC RILNGKGNRR IKQYVEMGGR YLGLCAGGYY GCAKCEFEVG VKGMEVIGER
     ELAFFPGMCK GLAFPGFVYH SEAGMRAAEL KVATKQLTDV EAAVPERLKA YYNGGGFFVD
     AMKYADKGVE ILATYEDQVA TADEQKSNKA AIVYCKVGEG SVILTGPHPE FSGTNLNRDE
     PTGPQGYDKL VDALVEDEQY RILFMTACLR KLGLDIRAET QHSVPSLSGL HLTASQPIVV
     SELLQSWQEA GLIADNVIKG ENDTFLIGSA LQSDAFDLGR VKAAVATASD PVGGLEPEDP
     PKTLMAHETS LPQSKDTPNF DHHAFYTHLR NYHSQQKESE ATFGKILIYG EVVTSTSTML
     EKNPTWLAEV PNGLTATATT QLAGRGRGTN VWVSPPGSLM FSTVMRHSLA LSTSAPVVFV
     QYLAALAIVA GIQTYDKGYA RLPVRLKWPN DIYALDPTRP ASENAYVKIG GILVNSSYAG
     GDYTLIVGVG LNVLNAAPTT SLAQLAAKAA LPAPSLERLL ASILANFEGL YLRFCRTGFD
     TVFEQSYYRS WLHSEQIVTL ETQGGVKARI KGISTDWGLL VAEELGFGDR ETGKRWELQS
     DSNSFDFFRG LVRRKI
//