ID   A0A094I8C7_9PEZI        Unreviewed;      1430 AA.
AC   A0A094I8C7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=V498_04757 {ECO:0000313|EMBL:KFY92787.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY92787.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY92787.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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:KFY92787.1}.
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DR   EMBL; JPKA01000978; KFY92787.1; -; Genomic_DNA.
DR   MEROPS; M20.017; -.
DR   HOGENOM; CLU_004884_0_0_1; -.
DR   Proteomes; UP000029270; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00105; KH-I; 1.
DR   CDD; cd05676; M20_dipept_like_CNDP; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 1.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS51375; PPR; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   REPEAT          511..545
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   DOMAIN          1171..1317
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          69..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1430 AA;  160409 MW;  13726038E12C5A36 CRC64;
     MAGPKSPLLR ITPPYASDMV PGSRSISICK AAVSRCSPTL HRDIREPLLF LYPTWARGFG
     SSAAEVLRNE QSTSESQQAC SPSTTPFDTH TVDTRLVATD SSIQEYKSTS KSEGTQRHSH
     ATNNKDVCNN EKPRGNLSLE GQRSDQNNPQ CQSFRMRRIV TVNDGLQIRR LKVQHIDTTP
     KLRKIRVKSS RYPPKNEHQS NAGATMMRDI VRAYPGPVIR ENSFRKVAYG QKVRTILSTT
     ERSEMRWWYE DELRRLKQEN MNEDRGFPQR GPPQVLETLI RHTPKRAEDT LLKILVPETA
     IDSLLIGPGN NIIDIKEMTG CDIELLEAEE GKSTRSLLLS GPPICISAAA AYIFRIVPTA
     VSNSTNKAFT FSQYSTRSST KDVAQSADAR DTAQIETQYY LASSKVDDIP KRADSIPRPK
     TLTQRSLELY IRSLTGITMT SPIHKMLYNK NEDHVNIVTQ RLLEVFSYGE CMDLMTITAL
     NEAVSYLAKY GRVAATREII DRARKVGFAV TSETFNILLR GCAKTQNINT FAALLGVMIH
     SGFRPNSGTW RAFMMVLRNP KAILHVFETM HERGLFHEEG LLSDVCEILL PHEMTFCLNK
     NQLVAPFLEH MTSRYGNGWL SVSGANKVFE ELGKRGLLTE CWTLVDYMVE QNVMPNAISI
     NTIFTHSTDA TDFRNNIKAL DRVSVQANFR PDGTTYEILF KLAWRWRLYS TARVIWQRAC
     LDACAKFEMR KRVSTSLQSA FLFQSTTNPS LPGPTPPADS MWDLTAGIFV VREIKPAASQ
     DRSQTPGKPP LTLWKAFHQA VETVKSELLI FKEWAPSGSL TKLMAKSVET DRTVARLMDK
     DFERGMEHLL YYAPVVKIKS RRRPHTDLED ARLRRLEQER TGPPMSRLLA SNIFKQANAR
     LSTFTTTSTS CRTSSLYPLR SIIPRPVQSK TPAIRSYSSQ LLTAEQRREH QAQKMAPQLD
     RFFKEVDAQA DHFIERLRQA VAIPSISAED ERRPDVVRMG EWLGKELEAL GAHVELRPLG
     PQPHKEHLML PPVVVARYGN DTAKRTILVY GHYDVQPAAK EDGWATEPFE LTVDDKGRMF
     GRGSTDDKGP VLGWLSAIEA HQKAGIDFPV NLLMCFEGME EYGSEGLDDF IREEAGKFFK
     DTDAVCISDN YWLGTEKPCL TYGLRGCNYY SVQISGPGQD LHSGVFGGSA QEPMTDLVRV
     LGSLVDTNGK IQIPGLAELV APVTEEERGL YKDIAFTMDN LHESLGSKTT IFEDKESTLM
     ARWRFPSLSV HGIEGAFSQP GAKTVIPAKV IGKFSIRTVP NMESEDVTRL VKEYVTDVFT
     KLGSKNTLDV SLMHDGKWWV ASPKHWNFSA AAKASERVWG VAPDLTREGG SIPVTLTFEE
     ATGKNVLLLP MGSSTDMAHS TNEKLDRSNF LEGIKTLGAY LHYAAEEPIV
//