ID A2R108_ASPNC Unreviewed; 755 AA.
AC A2R108;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Contig An12c0370, genomic contig {ECO:0000313|EMBL:CAK41398.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:CAK41398.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:CAK41398.1};
GN ORFNames=An12g10510 {ECO:0000313|EMBL:CAK41398.1};
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:CAK41398.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK41398.1, 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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; AM270293; CAK41398.1; -; Genomic_DNA.
DR RefSeq; XP_001396097.1; XM_001396060.1.
DR AlphaFoldDB; A2R108; -.
DR EnsemblFungi; CAK41398; CAK41398; An12g10510.
DR GeneID; 4986404; -.
DR KEGG; ang:An12g10510; -.
DR VEuPathDB; FungiDB:An12g10510; -.
DR HOGENOM; CLU_021802_8_4_1; -.
DR OrthoDB; 5487978at2759; -.
DR Proteomes; UP000006706; Chromosome 3L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR CDD; cd08013; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR42937; -; 1.
DR PANTHER; PTHR42937:SF1; DIAMINOPROPIONATE AMMONIA-LYASE; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CAK41398.1};
KW Lyase {ECO:0000313|EMBL:CAK41398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 33..341
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT DOMAIN 549..652
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 80308 MW; E326DB51059B38BE CRC64;
MSAFRRPIYV NPSSSTTSSA GSPGALAFHQ QFPGYGPSPL VALPAMAEEL GVRAVYLKQE
SNRFGLPSFK VLGASWAIYQ AIRSFVELPE GTPLDILIER VRAQSAPITL LAATEGNHGR
AVARVAQQMS LQCRIYVPCT MHTYTQEKIR SEGAEVVVVD GDYDHAVETA ATAANQLSQG
ILVQDTALEG YEEIPAWVVE GYATLLQEAD TQLHALGLQN SLVVAPVGVG SFAQAVATYY
KSRDTPATVV AVEPDTAPCL THSLQQGHPT SVVTSPSIMA GMNCGTVSSA AWLLLKKLVD
VSLTVSDWES HCAVQDLAAQ SIDSGPCGAA SLAAIRRLKA EATSPSAFFS PESVILLLST
EGSRPYEVPM DVSMDEPVSL TQVLTRINSS NPTLSKTQGA GEAAITNYLC AWFAHRAIEH
HRIETAPGRP SVVGIIRGTG GGASVMLDGH VDTVSLTTYD GDALTGHLGV KDGKEAVFGR
GTLDMKGGLA AGLSALLVAR EQRLAGDVMV AAVADEEDAS QGTQDVIAAG WRADAGIVLE
PTNMAIAHAH KGFVWVEVEI LGRAAHGSQP ADGVDAILNM GHLLQALRQY QAQLPVDPVL
GPGSLHCGVI QGGEEVSSYP ASCTLTLEYR TVPVQTNEKI LAELGAILQR LSQEHPDFQY
REPRITLWRP SQHVPKDHPV VQQLVQLGAG VLEKPPQVES APFWCDAALL TEAGTPSVVF
GPSGAGLHSR EEWVEVDSVR QLREILGQFI QQFCK
//
