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Database: UniProt
Entry: A0A0C7ND72_9SACH
LinkDB: A0A0C7ND72_9SACH
Original site: A0A0C7ND72_9SACH 
ID   A0A0C7ND72_9SACH        Unreviewed;       455 AA.
AC   A0A0C7ND72;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=LALA0S08e04764g1_1 {ECO:0000313|EMBL:CEP63537.1};
GN   ORFNames=LALA0_S08e04764g {ECO:0000313|EMBL:CEP63537.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP63537.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP63537.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP63537.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; LN736367; CEP63537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7ND72; -.
DR   STRING; 1245769.A0A0C7ND72; -.
DR   HOGENOM; CLU_024588_2_0_1; -.
DR   OrthoDB; 5491171at2759; -.
DR   Proteomes; UP000054304; 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:UP000054304}.
FT   DOMAIN          248..342
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   455 AA;  49776 MW;  425A4D916458849A CRC64;
     MTSHSTSGTA TIDLPSTGTF SIPAVAPLSI VNGRLNTTVL ETGTTYGGVA RWGDEPHEFG
     MRRLAGTKED GAMRNWFLNE CKTLGCEIKI DQIGNIFAVF PGKNPGKPTA TGSHLDTQPE
     AGKYDGILGV LAGLEVLRTF KDNNYVPHYD VCVVVWFNEE GARFARSCTG SSVWSHDLPL
     KEAYELMSIG ETESESVFDS LSKIGYIGDV PASYKDNEID AHFELHIEQG PILEDEQKSI
     GIVTGVQAYK WEKITVSGEG AHAGTTPWRC RKDALLVSAK MIVVASEIAK KHQGLFTCGV
     IDAKPYSVNI IPGEVSFTLD FRHPSDETLE AILAEAHGEF DRIVKDNTAG ALDYRTEVLQ
     VSPAVKFDQT CIECVTRSAL AQFPESEVRQ IWSGAGHDSC QTAPHVATSM IFIPSKDGLS
     HNYHEYSSPE EVENGFKVLL HAIVNYDNFR AMRGH
//
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