ID   A0A395MMV3_9HYPO        Unreviewed;       649 AA.
AC   A0A395MMV3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Metallo-beta-lactamase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FIE12Z_6482 {ECO:0000313|EMBL:RFN49261.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN49261.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN49261.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN49261.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RFN49261.1}.
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DR   EMBL; PXXK01000181; RFN49261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395MMV3; -.
DR   STRING; 2594813.A0A395MMV3; -.
DR   Proteomes; UP000265631; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR   PANTHER; PTHR23240:SF39; REPAIR PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G04570)-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:UP000265631}.
FT   DOMAIN          23..152
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF12706"
FT   DOMAIN          382..409
FT                   /note="DNA repair metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF07522"
FT   REGION          449..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..593
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  72654 MW;  343EC88BA9AEB373 CRC64;
     MSTFNGIVSE FPDIRIDFFR KNANAPPPLA CFLSHVHSDH LAGIESLKSP FVYCSAATRE
     ILLQLERYPC RINYAKGVLE ARQQTFKHLD KILKPLPLEA PTSIELRPGQ QIQVTLFDAN
     HCPGAVMFLV EGDGKAILYT GDIRSEPWFV NAISRNPNLV EYTSGLKTLD KIYLDTSFIE
     DVPFQTKVEG IAELLRKISD YPDDTIFHLQ AWTYGYEDVW IALSKALRSK AGCLTADINV
     RLHSCEKGNM CEVAQRPTTV FIQPIIAHLS TGEDLAEIGV GGGGDDLQRE AELEPLDQDT
     LDTLFSRVLT SSETAVDLSD TLQEGLDQLV STGRNIPLDW DLDTLSTHSA DEIITMLIQR
     LSKSSKNQKP IHEGALPKTI YFPYSRHSSL PELRHFVDVF RPKDVWPCTV SPAEWLKNGI
     TVGSLFGWLC SGKDFEHDKV MQAFATTHAL NSQHQHHDSQ TTTNSDRVPS SPVYEPQSPQ
     RQRPSILSPK FVSQLLDTQV SDYQEEIVVA LERPAEELVA QPEKSPIRHT SETSADFQSE
     GISQGLNRGI KPTERLPDNP TPRSSGQKRS FSNISQNETE DETEGETEDE EQETAYPLRE
     PPGMSMAEGC SLARREAYLQ MAQNLMGNTW TSLQLISTSN EYTSEEKEL
//