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Database: UniProt
Entry: V5GCR1_BYSSN
LinkDB: V5GCR1_BYSSN
Original site: V5GCR1_BYSSN 
ID   V5GCR1_BYSSN            Unreviewed;       687 AA.
AC   V5GCR1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Biotin apo-protein ligase, putative {ECO:0000313|EMBL:GAD98702.1};
GN   ORFNames=PVAR5_7402 {ECO:0000313|EMBL:GAD98702.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD98702.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD98702.1}.
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DR   EMBL; BAUL01000256; GAD98702.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5GCR1; -.
DR   eggNOG; KOG1536; Eukaryota.
DR   HOGENOM; CLU_006150_1_1_1; -.
DR   InParanoid; V5GCR1; -.
DR   OrthoDB; 317678at2759; -.
DR   Proteomes; UP000018001; 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, ECO:0000313|EMBL:GAD98702.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT   DOMAIN          400..606
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
SQ   SEQUENCE   687 AA;  75792 MW;  D060035DC9EA98E0 CRC64;
     MSAVNANLAS KKLNVLVYSG DGSTVESVRH CLYTLRRLLA PNYAVTPVTS DMIIKEPWTS
     SCALFVMPGG ADLGYSRVLN GAGNRRISTF VQTGGAYLGF CAGGYYGTKR CEFEVGDKTM
     EVIGERELGF FPGTCRGCAF PGFVYHSEAG ARAVELKVSK TALITGTVPD LFRSYYNGGG
     VFVDAPSYAD RGVEVLASYT EELNVDPGQG AAAVVYCKVG EGAAILTGPH PEFAAANLDK
     KAGGPEYAKV VDALAQDDKV RTDFLKACLS KLGLQVTQET TTVPSLSTLH LSALRAEDTT
     ELLSSLRETV TQEDGREYLK DENDTFFIEA PNVWKMQELE KSLPEGEIKE EAKEETPESV
     EGIVDYNKII KHVVIHDELP SSKATPYFNH YAFFSNLQNY RSKSSEPLFQ FGSQILYGEV
     VTSTSTILEK NPKLLRHLPT GFTATATVQV AGRGRGSNVW VSPAGALIFS TVVRHPIEKM
     QSAPIVLIQY LAAMAVVKGI KSYDKGYEDM PVKLKWPNDI YALDPERADE KRYTKICGIL
     VNSQYTSKEY IAVVGIGLNA TNASPTTSLN ALVEHFLKGR RAEPITLEKL LARILTVFEE
     LYARFLRVGF DKTFEDMYYS DWLHMNQVVT LEEEGGARAR IKGITRDYGL LLAEELGWED
     RPTGRVWQLQ SDSNSFDFFR GLVKRKV
//
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