ID   G8Y216_PICSO            Unreviewed;       434 AA.
AC   G8Y216;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Piso0_005386 protein {ECO:0000313|EMBL:CCE86869.1};
GN   Name=Piso0_005386 {ECO:0000313|EMBL:CCE86869.1};
GN   ORFNames=GNLVRS01_PISO0N14005g {ECO:0000313|EMBL:CCE86869.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS   10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE86869.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; FO082046; CCE86869.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8Y216; -.
DR   STRING; 559304.G8Y216; -.
DR   eggNOG; ENOG502QPR4; Eukaryota.
DR   HOGENOM; CLU_024588_2_0_1; -.
DR   InParanoid; G8Y216; -.
DR   OMA; FGKAHPY; -.
DR   Proteomes; UP000005222; Chromosome N.
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:UP000005222}.
FT   DOMAIN          225..318
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   434 AA;  47450 MW;  44AFCC14779D448E CRC64;
     MSKGLSIVQG RLLKSIHFTA QYGAKGVWGG ASTETGVCRL ALSDLDKMVR DWFVSETKKL
     GCEIKVDAIG NIFSIYPGKN DGVPTAIGSH LDTQPTGGRY DGVYGVLAGL EVLKIFRENS
     FVPNYPVAVV NWTNEEGARF PKATMASSLW AENVSEESIM NLESITDQKP VTVEQELTRI
     GYRGEIPASY KENPLAAHFE LHIEQGPILE SENKKIGIVT GAQAYDWYKV TIQGNSSHTG
     TTPLGARSDA LLAASRMITK CNEVAHKHNG LVSVGVIDIE PAVVNVIPKK VSFIYDARHA
     SDNELSKMHA DLTQEFEEIV RTSQGPLSIK PLELSIEHLF HSKAVHFDPD CISSVKDESI
     HLYGESNVKE IMSGAGHDSC STSFRCPTSM IFIPSRNGIS HSPEEYSTPE SIDEGLSVLL
     GAVIRYDELR KIKG
//