ID   A0A166UXY0_9HYPO        Unreviewed;      1073 AA.
AC   A0A166UXY0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=A-pheromone processing metallopeptidase Ste23 {ECO:0000313|EMBL:OAA33084.1};
GN   ORFNames=AAL_00549 {ECO:0000313|EMBL:OAA33084.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:OAA33084.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:OAA33084.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:OAA33084.1,
RC   ECO:0000313|Proteomes:UP000078544};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(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:OAA33084.1}.
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DR   EMBL; AZGY01000001; OAA33084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166UXY0; -.
DR   STRING; 1081109.A0A166UXY0; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000078544; 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   Reference proteome {ECO:0000313|Proteomes:UP000078544};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          46..194
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          221..404
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          411..699
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          703..885
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1073 AA;  122545 MW;  F9F25B39CCF06587 CRC64;
     MPSLQSSGLT AGRHAPVILL TNQLEKPSVD NRDYRVVRLE NDLEALLVHD PETDKASAAL
     DVNVGNFSDE DGMPGMAHAV EHLLFMGTKK FPVENEYSQY LSANSGSSNA YTASTSTNYY
     FEVAAKAAND EEPSDANPSP LLGALDRFAQ FFIEPLFLPN TLDRELRAVD SENKKNLQND
     MWRLHQLDKS LSNPRHPYCH YSTGNLETLK NIPEKQGVNV REKFIEFHEK HYSANRMKLV
     VLGREPLDVL QKWVVELFSG IQNKNLPPNR WTEEEPFRES ELGTQCFAKP VMDSRELHLS
     FPFIDEETLY ESQPSRYISH LIGHEGPGSI MSYVKSKGWA NSLSAGAYAL CSGTPGIFEA
     QVRLTEESDI QGLKHYPEIV KIFFQYVGML RESPPQEWIF QEQKGMADVD FKFRQKTPAS
     RFTSGTSSVM QKPLPREWLL SGNSRLRVFD SNAIARALDQ LQPEKLRMTV VSRAFPGDWN
     QKEKWYGTEF RYEKIPAELM AELKAASEMP KGKRLAELHL PHKNNFIPSK LEVEKKDVSQ
     PALAPRVLRN DQRVRAWWKK DDTFWVPKAN VIVSLINPIT YASAENSVKA RLFTELVRDA
     LEEYSYDAEL AGLQYSVTLD ERGLYLQISG YNDKLPVLLE QVAVTMRDIE IKDDRFDIIK
     ERLARGYENW QLQSSYQQVG DYMSWLTAER DYLVEEMAAE LQNVSVDAIR LFHKQMLSQL
     FVEVYAHGNL YRGDALKVAD MVESTFQARA LPPSQWHITR SLILPPGSNY VFKKDLRDPA
     NVNHCIETWF FVGYRGDRLS RAQTLLVDQM IHEPAFDQLR TKEQLGYIVF SGMRNFATTC
     GLRFLVQSEK TPEYLDRRIE AFLAQFGKTL ESMSESDFEG HKRSLINKRL EKVRNLEQES
     SRHWLQISTE YYDFEQAQQD AAHVKTLTKA EMLKFYNVYF NPASLARARL SVHLIARGAG
     ELDSKIIKLL EENGVTDVPQ EKRQSVNLLR EYLEAGNLIP KEKLSNIIDE MKEIGLSQDP
     DGEPSNGLSN GLSAVDEAEV ITNVREYKAK LAVSSGAWPV KEISEFEDAD PKL
//