ID   A0A0A8L5L2_9SACH        Unreviewed;       454 AA.
AC   A0A0A8L5L2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=WGS project CCBQ000000000 data, contig 00098 {ECO:0000313|EMBL:CDO93540.1};
GN   ORFNames=KLDO_g1836 {ECO:0000313|EMBL:CDO93540.1};
OS   Kluyveromyces dobzhanskii CBS 2104.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93540.1, ECO:0000313|Proteomes:UP000031516};
RN   [1] {ECO:0000313|EMBL:CDO93540.1, ECO:0000313|Proteomes:UP000031516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA   Nystedt B., Astrom S.;
RT   "The genome of Kluyveromyces dobzhanskii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:CDO93540.1}.
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DR   EMBL; CCBQ010000025; CDO93540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8L5L2; -.
DR   OrthoDB; 5491171at2759; -.
DR   Proteomes; UP000031516; 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;
FT   DOMAIN          249..341
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   454 AA;  49625 MW;  AAB18B7BB858D08A CRC64;
     MSATTTTTSA GTEFPSSINA TGSVALSIES GRLNETILST GSEFGGVARW GTEAHEFGMR
     RLAGTELDGK MRDWFVNECK GLGCTIKVDK IGNIFAIYPG KKSGTKPTAT GSHLDTQPEA
     GKYDGILGVL AGLEVLRTFK DNNYVPNFDV CVVVWFNEEG ARFSRSCTGS SVWSHDLSLE
     EAYGLVSVGE EHPETVKESL TNIGYIGETA ASYQENEIDA HFELHIEQGP ILEDEQRRIG
     IVTGVQAYNW SKVTVHGVGA HAGTTPWRLR KDSLLMSSKM IVAASEIAES HDGLFTTGII
     DAKPYSVNII PGEVSFTLDI RHQDDDVLEQ IIKEVTAKFD ELITKNKGGA LSYEREILQI
     SPAVKFNDIC IDCVSRSAYS QFAKEEVRTM WSGAGHDSCQ TAPHVPTSMI FIPSKDGLSH
     NYYEYSSPQE IADGFKVLLQ AIVNYDNDRA SRGH
//