ID A2QNP2_ASPNC Unreviewed; 1037 AA.
AC A2QNP2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Contig An07c0180, genomic contig {ECO:0000313|EMBL:CAK39494.1};
DE EC=3.4.24.56 {ECO:0000313|EMBL:CAK39494.1};
GN ORFNames=An07g06490 {ECO:0000313|EMBL:CAK39494.1};
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:CAK39494.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK39494.1, 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 -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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DR EMBL; AM270135; CAK39494.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QNP2; -.
DR MEROPS; M16.008; -.
DR EnsemblFungi; CAK39494; CAK39494; An07g06490.
DR VEuPathDB; FungiDB:An07g06490; -.
DR HOGENOM; CLU_004639_1_1_1; -.
DR Proteomes; UP000006706; Chromosome 4L.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAK39494.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..196
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 225..400
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 410..694
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 703..881
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 1037 AA; 118055 MW; AE208DB5D62268C0 CRC64;
MGEAPPFGSI KLISDRMEKP LLDNRSYRVI QLSNQLEVLL IHDPDTDKAA AAMDVNVGSF
SDPDDLPGTA HAVEHLCFMG TKKYPAESEY STYLAKHGGY SNAYTASTST NYFFELSASS
MSNSPGSVAT VEQSNVTITK DKTPLYGALD RFSQFFIQPL FLPDTLDREL RAVDSENKKN
LQSDTWRLEQ LGRSTSSEKH PIRKFATGNY QCLHEEPVSR GIDIRKRFIE FHEAHYSANR
MKLVVLGREA LQELESWVQE LFSDVPNKSL HRLRWDNIPV LNESELMTQI FVKPVTEQRQ
LNIDFTYPDE EELVDSHPSQ YLAHLVSHGG PGSALAYLKE LGLAVSLSAG ASALCPGTAL
FCIDVMLTEK GVRQYRDVLK VVFQYIAMLK ENPPSAWISD EMSRLAEMDF KFRQKSPPSR
TVSDLAQLMQ NACIPREHLL SPFLVRKFDP ESIQSGLSHL RPDKFRFFLV DQQFPGNWDA
KEKWYGTEYK LEKIRKDFMQ ELWKAAQAPI TERHSILHLP AVNEFIPRRL GVDRKDVTEP
ARHPTLVRHD DHVRVWFKQD DQFWVPKANI KILLRSPIVS LTPMHAVMTR LYVELVEDSL
IEYAYNADKA GLSYAISESS QGLNIELKGF NDKMSVLLEK VLLAVRDLKI KQEQFDVAKD
RVWKAYKNFD YMEPYRQINA FSRMLINERS WTPFLLVEEL PAVTAEDINL YYPHLLRQMH
IEILVHGNLN KEDALNLTGL VESTLRPRRL PESQWLSRRT IALPSGANYL YERELRNPDN
VNNCLEYTIS VGSVSDRSQR AKLLLFSQIA EVPCFSTLRT KEQLGYIVNS AIGVYVTTGT
WRILVQSERD CKHLEERCDA FLVNFEHHLR AMTDETFEEH KVGLINKRME KLKNLDQETS
RFWTHITSEA LDFEQVYHDV EHIEPLTKED ILQFFDQHIH PSSPTRAKLA IHLIAQASAT
ADAASGDSAV AVGNPDALGL PETQDAVAAN AYEPSVSPAI IPIKIDNVRT WKASLPLSRA
AAPVKGRAEF GESNSES
//
