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
//