ID A0A124BYU1_ASPNG Unreviewed; 1380 AA.
AC A0A124BYU1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0000313|EMBL:GAQ46611.1};
GN ORFNames=ABL_09272 {ECO:0000313|EMBL:GAQ46611.1};
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:GAQ46611.1, 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:GAQ46611.1}.
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DR EMBL; BCMY01000022; GAQ46611.1; -; Genomic_DNA.
DR PaxDb; 5061-CADANGAP00012417; -.
DR VEuPathDB; FungiDB:An16g01850; -.
DR VEuPathDB; FungiDB:An16g01860; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1108291; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1185813; -.
DR VEuPathDB; FungiDB:ATCC64974_72960; -.
DR VEuPathDB; FungiDB:ATCC64974_72970; -.
DR VEuPathDB; FungiDB:M747DRAFT_297334; -.
DR VEuPathDB; FungiDB:M747DRAFT_372093; -.
DR OMA; WIFDEMK; -.
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; IPR006771; Bys1.
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; PF04681; Bys1; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1380
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007170351"
FT DOMAIN 310..474
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 501..680
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 686..973
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 978..1158
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 390..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 155085 MW; 53FD49359D8CBE1A CRC64;
MHLTTKTLLS LLPLLPLTTA TGSAVVQNNC TSPIYLWSVG GSVSSMQTID PGSSYSETFY
YDTTSGGVAL KITTTENGLY SGAPQTDYAY TLDTSSGNVF YDISDVYGDP FSGSVVSLVS
SDASCPSICW AGGVPPAGSV LLELGGLLGW GSQTANFKYG TSLTPFTFHA GNFPQHRLRP
ERCFPATDPS FLWMPPRSPA TRRLWNSRVP LYLRSPAFRA FSKSGASAAI APPSIYPSPR
FPSPNERYSS SPALRSSHAL VSLSLPSCAR LFSHTATMGS IERLAEQLEK PELDDRSYRV
IRLPNKLEAL LVHDPDTDKA SAAVNVNVGN FSDADDMPGM AHAVEHLLFM GTMKYPKENA
YNQYLASNSG SSNAYTAATE TNYFFEVGAT TASTDDTPNG ANGTSNGTDT PAKPNHPTSP
LYGALDRFAQ FFVEPLFLES TLDRELQAVD SENKKNLQSD LWRLMQLNKS LSNPAHPYHH
FSTGNLQTLK EEPQKRGLEV RQEFIKFYQA HYSSNIMKLV VLGRDSLDEM EQWVGDLFKH
VKNQDLPQNR WDHVQPCLPE HLGKQIFAKP VMDMRSLDLY FPFMDEESLF ESQPSRYLSH
LIGHEGPGSI LAYIKAKGWA NGLSAGVMPV CPGSAFFTIS VRLTPEGLKQ YREVTKVVFE
YIGMIKEREP QQWIFDEMKN LAEVEFRFKQ KSPASRFTSR LSSVMQKPYP REWLLSGNLL
RKFEPELVKK ALSYLRPDNF RMVIVAQDYP GDWNCREKWY GTEYKVEDIP EDFMDSIRKA
VETSPESRLS ELHIPHKNEF VPTRLTVEKK EVSEPAKTPK LIRHDDHVRL WYKKDDRFWV
PKATVHVTLR NPLAYATPAN LVKTKFYCEL VRDALNEYSY DAELAGLDYS LSASLFGLDI
SVGGYNDKMS VLLEKVLTSM RDLVIKPDRF NIIKERMTRN YKNAEYQQPF YQVGDYTRYL
TAERTWLNEQ YAAELVHIEA EDVSCFFPQL LRQNHIEVLA HGNLYKEDAL RMTDLVESTL
QSRALPESQW HVRRNMILPP GANYVYERAL KDPANVNHCI EYYLFVGKLD DDALRAKLLL
FAQMTDEPAF DQLRSKEQLG YVVWSGARYS ATTMGYRVII QSERNAAYLE SRIDAFLTGF
GKSLANMSEQ EFESHKRSVI NKRLEKLKNL SSETNRFWSH IGSEYFDFVQ NESDAANVRT
LTKADLIQFY QQFVYPKSAT RAKLAIHLKA QAGAHAHATK PEEQKAQVVS FLGKQLEAAG
FAVDQERLSA AFATVDVSGG DEAQILATLK AFLESGMSLS EQQTKPVIAQ FESSLGLQLK
QAGIEAKKSD GTVQPNGTNG DLQQSTYINN VPEFKARLAV SAGPSPVTDL SEFEDFDAKL
//
