ID A2QGQ6_ASPNC Unreviewed; 372 AA.
AC A2QGQ6;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Contig An03c0120, genomic contig {ECO:0000313|EMBL:CAK47853.1};
DE EC=3.5.1.- {ECO:0000313|EMBL:CAK47853.1};
GN ORFNames=An03g04140 {ECO:0000313|EMBL:CAK47853.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK47853.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47853.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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DR EMBL; AM270053; CAK47853.1; -; Genomic_DNA.
DR RefSeq; XP_001390295.1; XM_001390258.2.
DR AlphaFoldDB; A2QGQ6; -.
DR EnsemblFungi; CAK47853; CAK47853; An03g04140.
DR GeneID; 4980403; -.
DR KEGG; ang:An03g04140; -.
DR VEuPathDB; FungiDB:An03g04140; -.
DR HOGENOM; CLU_009854_1_1_1; -.
DR OrthoDB; 297364at2759; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR039703; Nta1.
DR PANTHER; PTHR11750; PROTEIN N-TERMINAL AMIDASE; 1.
DR PANTHER; PTHR11750:SF26; PROTEIN N-TERMINAL AMIDASE; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CAK47853.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 1..332
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
FT REGION 309..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 40905 MW; AE49AF93CC0C033F CRC64;
MKVATLQFAP RLGDVDGNIK RANELLKNGK VVRGVGIGVG LDLLKPDVLI LPELALTGYN
FPSLEAIRPF LEPVGQGPSA QWARETAKCF NCKVCVGYPE VYRGDDAQQA DSSNPTETCY
NSLLVVDETG DIILNYRKSF LYYTDETWAA EGNPQQGYHQ LSFPNSSQSS VESQIATSFG
ICMDINPYRF EAPFTAWEFA NRVLDTNSEL VILSMAWLTL LERNELDSLG DEPDLDTFNY
WIQRFMPLIR KKMGHETNFD GDDASHGKKI IIVFANRAGE EPGAEGTNPA RYAGTSAIVA
ITQKPTIRTW SKETSIEEGD PGADTDAAET DAPSFDTKIL CWDMMGATTE GICFADTTAD
PSMVFGLVKA SK
//