ID A0A165I097_9BASI Unreviewed; 687 AA.
AC A0A165I097;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Class II aaRS and biotin synthetase {ECO:0000313|EMBL:KZT59971.1};
GN ORFNames=CALCODRAFT_430158 {ECO:0000313|EMBL:KZT59971.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT59971.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT59971.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT59971.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV423935; KZT59971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I097; -.
DR STRING; 1353952.A0A165I097; -.
DR InParanoid; A0A165I097; -.
DR OrthoDB; 317678at2759; -.
DR Proteomes; UP000076842; 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:UP000076842}.
FT DOMAIN 392..600
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 687 AA; 74030 MW; 391D1BAE9EEF20EB CRC64;
MNVLVYSGPG VSTASLTHTL ASLRTALAPA YAVQPILPHA LITDPWPASC ALLVIPGGRD
LPYLSALAAA LPRIRAYVAA GGRFLGICAG AYFASERCAF ERGSPLQVLG PRDLAFFPGT
CEGCTYPGFA YESEDGARAI SITLDLPGWG PHAEGLEKDV KGVYYNGGGH FLPSSPSVLQ
SGLVTVLARY ADPPEQGKDI AAVLCRVGKG LALLTSPHVE YPLPAEPARS ALERSLPNLT
ADERTALEQA RQRLVLSCVR LLGLSPPPPT GGTTAPPPPT NPLPQFLVSS PARPELSTLV
WDLLKRISVP SPSTAPPEIR DTNDTFHLHL SSAAPALLLE ARTRFMIVGY FGGQLPGGEQ
APLFDLGAYF TELERVRRDK GLEEAEGQEG QGQGRKLGDA WGMGQVMFYG EVVTSTQTML
DRNPTLLSSL PTPFLSLATY QLTGRGRGSN IWLSPAGCLQ FSLHLRPPQN LPPSRLVFIQ
YVFGVAVVQA CRELLAELGG GKGGAGERVR LKWPNDVYGV VEGGERRKLG GILVGTNHLK
GRFEVVIGCG LNVLNTQPTT SLKHLLQLSG STPSQLASLT LEKVLAHILP TFDALWNTFL
AHRGDFRPFE AQYLASWLHS DQVVKLTTVS PPIDVRIVGI TLDYGLLRTV RAERDPWRSR
VEGEEYIDLQ PDGNSFDMIE GLIKKKV
//
