GenomeNet

Database: UniProt
Entry: K1WME0_TRIAC
LinkDB: K1WME0_TRIAC
Original site: K1WME0_TRIAC 
ID   K1WME0_TRIAC            Unreviewed;       408 AA.
AC   K1WME0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   ORFNames=A1Q2_03436 {ECO:0000313|EMBL:EKD02289.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD02289.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD02289.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD02289.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKD02289.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AMBO01000294; EKD02289.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1WME0; -.
DR   STRING; 1220162.K1WME0; -.
DR   eggNOG; ENOG502QPR4; Eukaryota.
DR   HOGENOM; CLU_024588_2_1_1; -.
DR   InParanoid; K1WME0; -.
DR   OMA; WTLDTDS; -.
DR   OrthoDB; 5491171at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
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:UP000006757}.
FT   DOMAIN          205..298
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   408 AA;  43158 MW;  2BDDA19D98A05715 CRC64;
     MIWSPAKANA SGATETGMAR LALGDDDKKA RDWFCEEMSS LGCDVKVDAM GNTFAVRPGK
     NAGPPTAMGS HLDTQPTGGC YDGILGIHAA VEAMRTMRDA GYEAKYPVAV VNWTNEEGAR
     FPKSLHGSSV WAGDLNLEAA YALKDVADPS KTAGAELERI GYKGTLPADA RQNPLAAHFE
     LHIEQGPILE GEDAAIGVVS GGQAYKWLRC KISGRDSHAG TTPLAYRADA MLGAARIIAA
     CHDVAAKHSG VATTGILTLE PGSINTIPHT VEFTIDIRHP DPAAVRAMEA DIRTLSSSLL
     QTGNKWECKV DFEEMFDAPA AIFAMECRDA IREAAIASVG EGKVRELVSG AGHDSCSTSK
     HCPTGMVFVP CKDGASHTPV EYASPEACAN GAQVLMDAAL LFDSRREK
//
DBGET integrated database retrieval system