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Database: UniProt
Entry: U1FZC6_ENDPU
LinkDB: U1FZC6_ENDPU
Original site: U1FZC6_ENDPU 
ID   U1FZC6_ENDPU            Unreviewed;       266 AA.
AC   U1FZC6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=EPUS_06328 {ECO:0000313|EMBL:ERF70287.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF70287.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA   Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; KE721344; ERF70287.1; -; Genomic_DNA.
DR   RefSeq; XP_007804049.1; XM_007805858.1.
DR   AlphaFoldDB; U1FZC6; -.
DR   GeneID; 19241271; -.
DR   eggNOG; ENOG502QPR4; Eukaryota.
DR   HOGENOM; CLU_024588_5_0_1; -.
DR   OMA; AYIEAHI; -.
DR   OrthoDB; 5491171at2759; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR   PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          53..150
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   266 AA;  28442 MW;  84152F23D58EB142 CRC64;
     MGVGRAGEAG VVEASWDTGV KMAAHFELHI EQGPHLVGAG EKIGVVEGVQ AYRWYEVEFH
     GRDCHTGTTS FPHRADALLA AAEAIVDIRA LAEELGNGAL ASVGIIEAKP GSVNTVPGFV
     SMSLDLRCPD EKILDELEKR VMESLRSAAA HSGAGRRPVQ TSIKETFRSG AVRFQREAVD
     CVEAAARNVL ESAGASQGGK TLMRRMSSGA GHDSVFASKR CPTAMIFVPC KDGVSHHPEE
     WCEKEDCAMG ASVLIQALLR YDRTRG
//
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