ID A0A1Y2DRX3_9PEZI Unreviewed; 679 AA.
AC A0A1Y2DRX3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Biotin-protein ligase {ECO:0000313|EMBL:ORY61435.1};
GN ORFNames=BCR38DRAFT_411308 {ECO:0000313|EMBL:ORY61435.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY61435.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY61435.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY61435.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY61435.1}.
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DR EMBL; MCFJ01000010; ORY61435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2DRX3; -.
DR STRING; 1141098.A0A1Y2DRX3; -.
DR InParanoid; A0A1Y2DRX3; -.
DR OrthoDB; 317678at2759; -.
DR Proteomes; UP000193689; 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 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:ORY61435.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689}.
FT DOMAIN 396..598
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT REGION 334..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 74325 MW; A3C0AF04407F6ED9 CRC64;
MAPRKLNVLV YTGAGSTVES VKHAVYSLRR LLSPNYAVIP ITDTVLLKEP WAPTCALLVF
PGGADLGYCR VLNGAGNILI SQYVRRGGAY LGFCAGGYYG STKCEFEVGN KPMEVVGSRE
LAFFPGTCRG AAFQGFQYQS EKGARAVKLI VKKDAFKSAG VVPDEVTSYY NGGGVFVPFG
DARDYEVLAS YASPPNVDGG DENPALVMCK VGMGSALLTG PHPEFSPANL EQHCDIPGYD
DLIASLRATD EARTNFFKAC LGKLGLDVNQ ETSSVPSLSR LHLSSLGNGD VDDLLHSWEE
IITRENGEEF IKGENDTFHL EKRETRWGVV DLKESLPSDK TSAQPPTEQG LGASPGSGIV
DYNTVTKRMV IHDSSWPGTQ ETPYFNHHAF YGNLKAYRDI DTEAEEWGDF LLYGEVVTST
NTLLDKNHNL LSKAPSGFTL TATTQIAGRG RGSNVWVSPA GSLVFSTVIN HPAHLAPSRP
IVFIQYISAI AIVEAIKTYD KGYTELPVKL KWPNDIYAVD PSKPASPPTY VKIGGILSNC
AYSSGSYQIV LGIGLNTTNG RPTTSLDALL PSHLPPFRIE KLLARILTRI EVLYKQFLRQ
GFSKELEELY YSYWLHGRQI VTLEAHGGVK ARIMGITTDW GLLKAEELGS DDRPTGKMWA
LQSDENSFDF FRNLVKRKL
//