ID A0A0D2IUT8_9EURO Unreviewed; 438 AA.
AC A0A0D2IUT8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=Z518_04902 {ECO:0000313|EMBL:KIX06926.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX06926.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX06926.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX06926.1,
RC ECO:0000313|Proteomes:UP000053617};
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 Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847477; KIX06926.1; -; Genomic_DNA.
DR RefSeq; XP_013274062.1; XM_013418608.1.
DR AlphaFoldDB; A0A0D2IUT8; -.
DR STRING; 1442369.A0A0D2IUT8; -.
DR GeneID; 25292973; -.
DR VEuPathDB; FungiDB:Z518_04902; -.
DR HOGENOM; CLU_021802_3_0_1; -.
DR OrthoDB; 2875217at2759; -.
DR Proteomes; UP000053617; 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; cd05652; M20_ArgE_DapE-like_fungal; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..438
FT /note="Peptidase M20 dimerisation domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002255612"
FT DOMAIN 243..352
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 438 AA; 47176 MW; 33B3ADB06E2E8E19 CRC64;
MKLFWSGAPI LLATCASQAL VTMHEQHPVP FQPSESSTHQ KLSDVIAASP LLSLHRAICE
VESITDNELA VGRLIISILE AHNFTVQTQN VPRPNSTKER LNVYAYPDVS KYGGAETPKS
ETSPQVLLSS HIDTVPPHIP YSLSLPKKSE ASPSSRRDIV IAGRGTVDDK ACVAVQIQTL
LDLLADPRAK INPSDVALLF VVGEEKYGDG MRHFSDSGLY SRTNSDYKAI LFGEPTEGKL
AAGHKGIIML TIKAHGKAAH SGYPWLGRSA NSMILPALAV LDKLGDIPEE KGGLPRSEKY
GKSTVNIGYM QGGVAANVVP EFAMANIAFR LAGGTVEGVK EIIKHAVRSI DPDERLELEF
SQGYGPIPLD ADVDGFDTIT VNYGTDVPNL EVADGVKRYL YGPGSILVAH GKDEALTVGD
MEEALEGYKK LVMHSLKS
//
