ID A0A0D1ZTD5_9EURO Unreviewed; 430 AA.
AC A0A0D1ZTD5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=PV08_06063 {ECO:0000313|EMBL:KIW16012.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW16012.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW16012.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW16012.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; KN847495; KIW16012.1; -; Genomic_DNA.
DR RefSeq; XP_016236228.1; XM_016380401.1.
DR AlphaFoldDB; A0A0D1ZTD5; -.
DR STRING; 91928.A0A0D1ZTD5; -.
DR GeneID; 27333146; -.
DR VEuPathDB; FungiDB:PV08_06063; -.
DR HOGENOM; CLU_021802_0_0_1; -.
DR OrthoDB; 5487978at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03895; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR033687; YodQ-like.
DR NCBIfam; TIGR01910; DapE-ArgE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-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 Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 208..320
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 430 AA; 46734 MW; B28172A90FBB777F CRC64;
MPPLTAEQID AITKSVHDNF AAQLSYTQQL IRFGGQRGEE GAVQDFVFDA FATRGYAPVK
FDMDESALGK HEGAGKFSPT HSRAPVVVGV HKPKAQCEGG KSLILNGHID IVPLGPVDMW
ADDPYSGKIE GDKLYGRGAA DMRSGHASNI FALDALRNIG LQPASEVIIQ SVPEEESTGN
GTMMTHLKGY KADAVLIPEP VQEQLVRANV GVLWFQIEVR GRPVHVRTMG TGVNAVDACW
GVVGALRELE AEWNQRHAKT KYFEEENHPL NLNIAIVNAG DWASSVPAWC KIDCRVAITP
GTTAKSAADE IETKVATYAA SHPYLSNNPP KVIWNGFFAE GYALEPGTEA ENILRKAHKQ
ATGSELTTQT STAYLDARVH SLYDKIPALV YGPIGEDVHG FDEWVSIESV KKVTVAMALF
IAEWCGVEKI
//
