ID A0A3N4JDU4_9PEZI Unreviewed; 672 AA.
AC A0A3N4JDU4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Class II aaRS and biotin synthetase {ECO:0000313|EMBL:RPA96445.1};
GN ORFNames=L873DRAFT_1694267 {ECO:0000313|EMBL:RPA96445.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA96445.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA96445.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA96445.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|ARBA:ARBA00009934}.
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DR EMBL; ML120414; RPA96445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4JDU4; -.
DR STRING; 1336337.A0A3N4JDU4; -.
DR Proteomes; UP000276215; 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; 2.
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:UP000276215}.
FT DOMAIN 388..592
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 672 AA; 74567 MW; 72CA3FA4B8064BA4 CRC64;
MGRMNVLVYS GTGTTVESVR HCLYSLRRLL SPNYAVIPTT ADTLLKEPWE TSCALLIIPG
GADLGYCRVL NGEGNRKIAQ FVRKGGAFIG FCAGGYYGCK MVEFEVGNGK MEVVGSRELQ
FFPGACRGAA FAGFQYASEK GARAPKIKVE KEALGNNELE GFNSYYNGGG LFVDADKYAD
RGVEVLARFE ETEKLSVEGG DAAVVYCKIG NGGAILTGPH PEFAAVNLDK SARDYAYRER
IELIEHTDNQ REAFLRACLV KLGLNISEEI GAIPSLSLLH LSSTSPADVG LLADRLRDIS
VTDGDKQKII GENDTFILER NSAPFSMGSL ADALAGEQDS PHKIIDYNKV VKHVQIHDSG
LPPTKDTPYF DHAAYFEHLK RYRSRSRSSP ENFGSFLLYG EVVTSTNTML DKNFELLQRL
PSGLTAVATL QVAARGRGSN VWVSPMGALV FSTCIRHPRE LSVQAPVVFV QYLVALAIVE
AIKSYDIGFE DMPVRLKWPN DIYAENPKNE KEFLKIAGIL VNSSYANNQF LLVVGCGINT
TNNAPTTSLN HILDKLNRTR KSKNLSRLPS FEQERLLAKI LVVFEEMYYQ FCRSGFAPFE
ELYYRHWLHS GQIVRLEMEG GRKARIRGIT PDYGLLTADE LDESDRLTGR SFTLQSDNNS
FDFFKGLLRR KT
//
