ID   A0A0F4GJB0_9PEZI        Unreviewed;      1007 AA.
AC   A0A0F4GJB0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   SubName: Full=DNA mismatch repair protein {ECO:0000313|EMBL:KJX97162.1};
GN   ORFNames=TI39_contig541g00011 {ECO:0000313|EMBL:KJX97162.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX97162.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX97162.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX97162.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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:KJX97162.1}.
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DR   EMBL; LAFY01000533; KJX97162.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GJB0; -.
DR   STRING; 1047168.A0A0F4GJB0; -.
DR   OrthoDB; 9570at2759; -.
DR   Proteomes; UP000033647; Unassembled WGS sequence.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR037198; MutL_C_sf.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF47; DNA MISMATCH REPAIR PROTEIN MLH3; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT   DOMAIN          807..972
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          337..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1007 AA;  109364 MW;  DE374CA525F5CD0A CRC64;
     MPSADNQRQR ILPLPPDVIA QIHSSKHITT LQGVILSLLE NSLDAASTKV DITVDWKRGS
     CTIDDNGDGI SPDEFAEDGG LGKMYCTSKP SLASTHLHGS HGIFLAELSS MSLLTISSTH
     SSNQQSASLT FHMAKCITRS LPESTQAHST VPARPGTNIA VHDLFGNMPV RLKHRALATS
     APSSDDTSWQ DLKRGVVALL LAWPKPCSVK LRDATSASKV VNISGLHTYF APELTSKSLR
     RLAGSKSSAS TYDPTDVLPI LFQSGFASPD SRSSWVPLSA NTSAISLKGI ICEDPVPTKQ
     CQFLSLGVMP CGAADGHGEW YDCVNRIFAN SGFGIEEDDG APSSKKEDRE HGRLARQTAK
     DKPRKGVDRY PMFCLQLQFK EMPGRFSDPS RLNEASLKVV EDILEAAVTA WLEAHHFRPR
     RKRAGRRRNE EQESPARAKR SWKNGTNSVP ATPVVGTDAA SASITTDSGR KNRVTDIFGR
     PVSRDTTQLC GDTEELKALS RMRSGRPHSG VQSLRQNLAM RSTTEDSRPC TADDAVTSQK
     RLRLQAPPID AGQYSGLRSH KSSHHDSTTR SHPRLHVPQL SERHSDISSV PQPDAPSSED
     FGSINSEDLT AIAHHLELAA GVEAEETIPW TDPSTGQVHR VSSRTGIVMP FAFESRTDSD
     RPTTRGQKVF LDAGSLSSAG RPLSLSRRGI MAAKYAILSR PETAPPSIPT SGFDSGGIAD
     GTAKTPAETQ GQQEKWLPGF LREWNNPVFA LRKEPPIPTA SHHGPGILLP TVDSTHHACH
     SHADGTNLHS TDKGIALSKN ALKHARIIAQ VDRKFILAVL PATVPSSSSS AGTFELSGPS
     QSDTLVLIDQ HAASERVMLE DLLVDLCTPA LAPKTQSEAA LTINHAQTGV QTVPLESTLE
     FDIPSSEQAV LEKFKTWFLR WGIVYSLYAP PAPLQTAQKP LHPLAHAHVH GTDSESWTTP
     GKRNKKVQEA RLKITHLPPC IVARCQKEPR LAIELPLFEN QFMISKK
//