ID A0A5B1QYH0_9AGAM Unreviewed; 643 AA.
AC A0A5B1QYH0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE SubName: Full=Class II aaRS and biotin synthetase {ECO:0000313|EMBL:KAA1474395.1};
GN ORFNames=DENSPDRAFT_840972 {ECO:0000313|EMBL:KAA1474395.1};
OS Dentipellis sp. KUC8613.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Hericiaceae; Dentipellis.
OX NCBI_TaxID=1883078 {ECO:0000313|EMBL:KAA1474395.1, ECO:0000313|Proteomes:UP000322482};
RN [1] {ECO:0000313|EMBL:KAA1474395.1, ECO:0000313|Proteomes:UP000322482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8613 {ECO:0000313|EMBL:KAA1474395.1,
RC ECO:0000313|Proteomes:UP000322482};
RX PubMed=31482283; DOI=.1007/s00253-019-10089-6;
RA Park H., Min B., Jang Y., Kim J., Lipzen A., Sharma A., Andreopoulos B.,
RA Johnson J., Riley R., Spatafora J.W., Henrissat B., Kim K.H.,
RA Grigoriev I.V., Kim J.J., Choi I.G.;
RT "Comprehensive genomic and transcriptomic analysis of polycyclic aromatic
RT hydrocarbon degradation by a mycoremediation fungus, Dentipellis sp.
RT KUC8613.";
RL Appl. Microbiol. Biotechnol. 103:8145-8155(2019).
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:KAA1474395.1}.
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DR EMBL; NSJX01000027; KAA1474395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B1QYH0; -.
DR FunCoup; A0A5B1QYH0; 362.
DR InParanoid; A0A5B1QYH0; -.
DR OrthoDB; 10250105at2759; -.
DR Proteomes; UP000322482; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0004077; F:biotin--[biotin carboxyl-carrier protein] ligase activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000322482}.
FT DOMAIN 369..559
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 643 AA; 67768 MW; 41F8154F5EC7887C CRC64;
MDVLVYTQPA AGSTATDPPA LVTLLRAILH PFYTVQAITA SSLASHPWEK SCALLVLQPT
GSAVTGLPMP PKAGEAVQRY VENGGRVLTL GLDMLVGARR SGEGQLQLYD PRSRRHISPT
APAGVPELRS GNVRLRTGEL LSDVVGLSSP FSDAASGSAL ARWEQASSDG TETEGQNVAA
VELPVGEGRI SAWAVNFTED TIQSSNNQLR LFLQSIVAST GLSVPSGSAE IEKETGGAAA
APPHRPLPQF LVTAKLITTE IILASLGVPT PESFSTTSSA ASPSFVLKDT ADTFGFHFCT
PEAALGLLQQ ARADDAHAGG DTIKSVIVLP PAVIPSLAVT PKFDLQLYFN NLEKARKANG
LPDVSQEGSC GMGEALFYGE AVTSTQTMLD KNQHLASRLP PPILSLATHQ LAGRGRGRNT
WLSPAGCLQF SLLLRAAPPA LPAPRLVFVQ YLFGLAVVRA CRDAAVLGPE AGAGVRLKWP
NDVYVVRGGE KKKIGGVLVN TSFSGGKVDI VIGCGLNVST PPPIASLSLL SPAQQPPLRP
ETVLPVILAK FEALWAAFVQ GRGSWAPFAD AYLDAWMHSD QLVTLTTLTP PRPVRILGIT
PDHGLLRTLP ERAAWGGAEE GYIDLQPDGN SFDLMAGLIR SKT
//
