ID A0A0D1XDK6_9PEZI Unreviewed; 429 AA.
AC A0A0D1XDK6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=PV09_08203 {ECO:0000313|EMBL:KIW00316.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00316.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00316.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00316.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847565; KIW00316.1; -; Genomic_DNA.
DR RefSeq; XP_016210185.1; XM_016362065.1.
DR AlphaFoldDB; A0A0D1XDK6; -.
DR STRING; 253628.A0A0D1XDK6; -.
DR GeneID; 27316176; -.
DR VEuPathDB; FungiDB:PV09_08203; -.
DR HOGENOM; CLU_024588_2_0_1; -.
DR InParanoid; A0A0D1XDK6; -.
DR OrthoDB; 5491171at2759; -.
DR Proteomes; UP000053259; 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 CDD; cd03884; M20_bAS; 1.
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 NCBIfam; TIGR01879; hydantase; 1.
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 PIRSF; PIRSF001235; Amidase_carbamoylase; 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:UP000053259};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 222..321
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 429 AA; 46549 MW; C270B45B75D41938 CRC64;
MTMISLSAEY AALKIDALRT NQTLDAACTW GNTPDGGMNR LASNIDDKHV RDWFISETAK
CGCSHLIDEM GNIFAIRPGK NNNLPPIALG SHLDTQPTGG RYDGILGVVS AMEVLKVIHT
NCITTYAPLA VVNWTNEEGA RFPPAMLCSG VWGGAFTVEW AQSRADSEGL TLGEELKRIG
YLGTTPCSYE ANPLLAHFEV HIEQGPILDQ EEQPAAVVKG VQSIRWYNIS VRGREAHTGT
TPMDRRSDAL LGAAKIIVET NKCVTEGEIA ARGGRATIAV INSSPQSINT IAGSVHLALD
IRAPADSDVE LIEQNCQNRF EGICIEHGLT MSMDNFWVSP AVKFDATMVD CVRQSANENG
CKLELTSGAG HDSVYTSKKV PTAMIFVRCR DGISHNPAEF SRPEDCAVGA QVLLGAYLRY
DQYVQGLYR
//
