ID   A0A1G4KCN3_9SACH        Unreviewed;       604 AA.
AC   A0A1G4KCN3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=LAMI_0G16446g1_1 {ECO:0000313|EMBL:SCV02164.1};
GN   ORFNames=LAMI_0G16446G {ECO:0000313|EMBL:SCV02164.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV02164.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCV02164.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11717 {ECO:0000313|EMBL:SCV02164.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC       family. {ECO:0000256|ARBA:ARBA00010304}.
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DR   EMBL; LT598469; SCV02164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4KCN3; -.
DR   STRING; 1230905.A0A1G4KCN3; -.
DR   OrthoDB; 23465at2759; -.
DR   Proteomes; UP000191024; Chromosome g.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR   CDD; cd16273; SNM1A-1C-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.12650; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR011084; DRMBL.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR23240:SF6; DNA CROSS-LINK REPAIR 1A PROTEIN; 1.
DR   PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR   Pfam; PF07522; DRMBL; 1.
DR   Pfam; PF12706; Lactamase_B_2; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191024}.
FT   DOMAIN          223..356
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   DOMAIN          448..579
FT                   /note="DNA repair metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF07522"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  69375 MW;  EB8EBE152A7A022D CRC64;
     MNDKKRQRKL SDFDLSQTKR ALPDSRLRPI VISLDSDDDE NDGTENCPGD VKVEVTPVTT
     PCSPAEHQET LKQRPNANYR TKIDPEEIAD TAGVAGSSSD VFTTKAVTNE ESIPDPDVVV
     IEQKSVFVDV TASKQTLVSE TLAAKVEHQE ILCPLCGLVL THMELHIRDQ HCDSCAGTDK
     LDTRRSKKPL PPLPDVKKIH FSCYSIVVDG FNYANDPSVT QYFLSHFHAD HYIGLKKSWC
     QGTVYCSKIT AELLVYKLRL SRERLVILEI GKTVNISDRV TVTCFDANHC PGAVVFLFQE
     FDSAGVVIER VLHTGDFRSN DELINSINEF TQNAVIHRVY LDTTYMYPSF HFPMQKSVLD
     VTSRFAEQIN TIGMQKLFKD RQTSILSFIA NPLTRCHRYR YVFLVGTYTI GKEKVAVALA
     ERLGTKIFLP KNTPKHRIIQ TYEETFPTHL ITHDVTKSCV HIVPLRTLSS KEGMQRYFKP
     ISHLYEDMVA FYPTGWTFKN GGKFARLYET LEEKIEHTKW LLNYEEIDTM NEGTLFRQYN
     RSSRFQVFRV PYSEHSSFKD LSNFCVKMTW QEIIPTVNLH DPYMVSQMKQ WFLAWKRAQE
     QITL
//