ID G3XZ14_ASPNA Unreviewed; 1037 AA.
AC G3XZ14;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHA24109.1};
GN ORFNames=ASPNIDRAFT_180100 {ECO:0000313|EMBL:EHA24109.1};
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:EHA24109.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA24109.1, 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 peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:EHA24109.1}.
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DR EMBL; ACJE01000009; EHA24109.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XZ14; -.
DR STRING; 380704.G3XZ14; -.
DR HOGENOM; CLU_004639_1_1_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
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; 118023 MW; AFC143330553BD79 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 LFSDVPNKNL 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 WKASLPLSPA
AAPVKGRAEF GESNSES
//
