ID   A0A2I1GZT9_9GLOM        Unreviewed;      1000 AA.
AC   A0A2I1GZT9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Ste23p {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RhiirA4_546998 {ECO:0000313|EMBL:PKY52153.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY52153.1, ECO:0000313|Proteomes:UP000234323};
RN   [1] {ECO:0000313|EMBL:PKY52153.1, ECO:0000313|Proteomes:UP000234323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY52153.1,
RC   ECO:0000313|Proteomes:UP000234323};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:PKY52153.1}.
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DR   EMBL; LLXI01001150; PKY52153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I1GZT9; -.
DR   VEuPathDB; FungiDB:FUN_001191; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1789635; -.
DR   VEuPathDB; FungiDB:RhiirA1_537874; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000234323; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR   PROSITE; PS00143; INSULINASE; 1.
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:UP000234323};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          51..187
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          213..390
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          396..677
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          680..860
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1000 AA;  116231 MW;  E8657DEC2117600F CRC64;
     MATTSIFKNL PSNFTISEDK SHAVLSVPIE QSDNDDRSYK LIRLSNELEA LLIHDANTDK
     SSASLDVNVG YFCDPESLSG LAHFCEHLLF MGTEKYPKEN EYLDYLSQHN GNANAFTSTN
     DTNYHFGVGP EFLEGALDRF AQFFIAPLFD PNCVDREICA VDSENNKNLQ LDGWRLYQLE
     KALSNPKHPY SRFGTGNLET LKENPIKQGL NIRDELLKFH EKYYSANIMK LVVLGKESLD
     QLTQWVIEKF SAIKNKNVPI PTFDGHPLTE NELLKQVFAK PVKDNRSLKI KFPFPDLSSL
     YRFMPERYLS HLIGHEGSGS LFTLLKKKGW VNSLGAYYQG DIGFGFFIVS IDLTESGLAN
     YEDVVVHIFQ YIEMLKQVGI QEWTYHEIKK IREISFRFRE KYAPTGYTTN LSMMMQKPYP
     REWILSTSLI REFDSKLINE LLDLLRHDNF VLRLSSQSFT GLDQKEKWYG TEYKVEPLSD
     KLIQALKNIT THSELKLPEI NEFIPTDFET YKKEISTPAK RPDIIKDTQI SRLWYKKDDT
     FWVPKANIYV LLNSPLAYAT PLYHVKTRLY SELIKDALNE YLYNAQMAGV YYGINYRSQG
     LSLSISGYND KLPVLLEKVV NKMKNLKVDP ERFSLIKEKV QRSYKNFLLN SPSQHSEYYL
     DYLTIDRLWL NEEKLEALES IKYEDIEIFY PKLLDQLYIE ILIHGNILKD NAIKISQKIE
     EILQPKALLP SQSIRSRSIM IPKGKKFTYQ RDVFDSDNVN SAVEYYIQIC DFTNRELRIR
     SNIMSKLAHE PCFDQLRTKE QLGYLVSSGL RLESGSTGLR IRVQSIKDTV HLENRIENFL
     YGLQKIIEDM SEQEYQTRVQ ALIDRKLEKP KNLSQETSRH WGQIKSGYYD FEQDVKDVEE
     IRKVSKQDLL EFYKKFISPD SPRHKKLSVH LRSQKLNKSN DIVNGEKKGD DEEVKSEELE
     LELKGYNEII NDMVLWKSRM NLGPSATPID DDIISKARVI
//