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Database: UniProt
Entry: A0A100IDE4_ASPNG
LinkDB: A0A100IDE4_ASPNG
Original site: A0A100IDE4_ASPNG 
ID   A0A100IDE4_ASPNG        Unreviewed;      1034 AA.
AC   A0A100IDE4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAQ39210.1};
GN   ORFNames=ABL_03012 {ECO:0000313|EMBL:GAQ39210.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ39210.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ39210.1}.
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DR   EMBL; BCMY01000004; GAQ39210.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IDE4; -.
DR   VEuPathDB; FungiDB:An07g06490; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1105159; -.
DR   VEuPathDB; FungiDB:ATCC64974_47820; -.
DR   VEuPathDB; FungiDB:M747DRAFT_328795; -.
DR   OMA; VGHQWLE; -.
DR   Proteomes; UP000068243; 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          39..197
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          225..401
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          410..699
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          703..883
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1034 AA;  118034 MW;  0F853868F77DD87C CRC64;
     MGEALRFDSV ELISDTMEKP LLDNRSYRVI QLPNQLEALL IHDPDTDKAA AAMDVNVGSF
     SDPDDLPGTA HAVEHLCFMG TKKYPEETEY STYLAKYGGS SNAYTASTST NYYFELSASS
     TSNSSGSSAN KKGPNVSISK NMSPLYGALD RFSQFFIQPL FLADTLDREL RAVDSENKKN
     LQSDTWRLEQ LGRTTSNENH PIHKFATGNY QCLFEEPLSR GVDVRKRFIE FYDTHYSANC
     MKLVVLGIEL LQDLESWVQE FFSNVPNKDL HRLRWDGIPV LTESELTTQI FVKPVTEQRQ
     LNIDFTYPDE EDLVDSHPSL YLEHLISHGG PGSALAYLKE LGLADSLSAG ASALCPGSAL
     FCIDVRLTDK GVRQHREVLK IIFQYISMLK ENPPSAWISD EISRLAEVEF KFKQKGPPSR
     TVSGLAQLMQ NTCIPREQLL SYPLIRKFNP ESIQHGLSHL RPENFRFFLV DQQFPVDWNK
     REKWYGTEYK LEKIPRDLIQ ELGIIAQAST PERPPRLHLP ALNEFIPQQL DVERKDVTEP
     ARQPTLIRHD DHVRVWFKKD DQFWVPKANI KILLRSPMVA LTPMYAVMTR LYVDLVEDSL
     DEYAYNADKA GLNYNLSENA QGLIIELKGF NDKMSVLLEK VLLAIRDLEI KQEQFDVAKE
     RVWKAYKNFD YLEPYRQINT FSRLMINERS WTPSQLLEEL PAVTAEDIRS FFPQLLQGMH
     IEILVHGNLY REDALSITKL VESTLRPRQF PKSQWPPRRT IALPSGANYL YERVLKNLDN
     VNHCLEYIIS VGSVSDRSQR AKLLLFSQVV AEPCFSTLRT KEQLGYIVNS AIGVYVTTGT
     WRILVQSERD CKYLEERCDA FLETFAHELR AMTDEVFEEH KIGLINRLLE KLKNLDQETS
     RFWTHIMSEV LDFEQVYQEV EHIEPLTKKD ILEFFNQYIH PSSSTRAKLS IHLIAQASTG
     DSAAAGYIAA AEENIDSALK RDQDAVVVNG HRRSVPPATI PIDNVRKWKA SLPLSPAAAP
     VKGLAEFEGL KSKS
//
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