ID G3Y6E9_ASPNA Unreviewed; 682 AA.
AC G3Y6E9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN ORFNames=ASPNIDRAFT_48905 {ECO:0000313|EMBL:EHA22164.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA22164.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA22164.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA22164.1}.
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DR EMBL; ACJE01000013; EHA22164.1; -; Genomic_DNA.
DR AlphaFoldDB; G3Y6E9; -.
DR STRING; 380704.G3Y6E9; -.
DR HOGENOM; CLU_006150_1_1_1; -.
DR Proteomes; UP000009038; 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}.
FT DOMAIN 396..601
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 682 AA; 74995 MW; 048B2C405754D184 CRC64;
MATPNMTGKK VNVLVYSGAP LSPLLPAQHQ RYPSLCTQRI IRNGTTVESV RHTLYSLRRL
LAPHYAVIPV TSDALLHEPW TATCALLVIP GGADLGYGRV LNGPGNRRIE QFVKRGGAYL
GFCAGGYYGS QRCEFEVGDK TLQVIGEREL AFYPGTCRGG AFAGFVYHSE AGARAAEISV
NKDILNAGIV PERFRCYYNG GGVFVDAPTL ADKGVEVLAS FEEELNVDPG EGKAAGGLFL
RDRIRSKALY PPWSNCLGDV CADGCRWPRI YKSAHGLPQG MSGQAGPAGD AEHDHRAVAV
IAASTADLVA SWQEIITKDG NEEIIKDEND TFRIERPGAW NLSQLEDSLP ESSQSTEGIV
DYNAIVKRLV VHDDVPSSKL TPYFNHHAFY SNLHQYQSQS REGASEFGAH LVYGEVVTST
NTILEKNPKL LRKLPNGFTA SATTQVAGRG RGSNVWVSPA GALIFSTVLR HPLEKIQSAP
VVFIQYLAAM AVVQGIKNYD AGYSELPVKL KWPNDVYALD PEHPEKKQYS KICGILVNSH
YCANEYISVV GIGINATNAS PTTSLTALAA RFLGPRAAPI TLEKLLARIL TTFEELYTRF
LRSGFDRSFE EMYYADWLHM HQVVTLEEEG GVRARIKGIT RDYGLLLAEE LGWNDRPTGR
VWQLQSDSNS FDFFRGLVRR KV
//
