ID A0A2H3HHZ6_FUSOX Unreviewed; 1010 AA.
AC A0A2H3HHZ6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=DNA mismatch repair protein PMS2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU210_005003 {ECO:0000313|EMBL:PCD42475.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD42475.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD42475.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD42475.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD42475.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD42475.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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:PCD42475.1}.
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DR EMBL; MABQ02000003; PCD42475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3HHZ6; -.
DR STRING; 327505.A0A2H3HHZ6; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000219602; Chromosome 4.
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:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR CDD; cd03484; MutL_Trans_hPMS_2_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
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 Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR002099; MutL/Mlh/PMS.
DR InterPro; IPR038973; MutL/Mlh/Pms-like.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00585; mutl; 1.
DR PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR PANTHER; PTHR10073:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 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.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT DOMAIN 217..357
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 786..949
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 367..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 110569 MW; 0A88B834ADAF1868 CRC64;
MATIKQIDGR TVHQIQSGQV IVDLCSVVKE LVENSIDAGA TSIDVRFKNQ GLDLIEVADN
GSGIAPANYP SVALKHHTSK LSSYSDIATL ETFGFRGEAL ASLCALSIVS ITTCQQGEAP
KGTKLSFEPS GALKGTAVVA ASKGTTVSVE RLFHNLPVRR RELERNIKRE WNKVIALLGQ
YACIQTSLKF SVSQQPTKGK RIHLFSTKGN PTTRENIINI FGAKTMTVLV PLDLTLEMHP
STGGPALQID QKHKSSSRDV RVVGHVSRPS HGDGRQTPDR QMFFVNGRPC GLPQFAKAFN
EVYKAYNSSQ APFILADIQL DTHMYDVNVS PDKRSILLHD QNQLLDNLRT SLTALFDSQD
YSVPTSQLLP FKNRTEKQST TNTPFKPLSI TPQKPLDDSQ PEVESDEDSD ESSPVAKVPL
GAVRRVGGSK SLEKNISSQH LISGWVERGS TSRPKDRSTT VSTFAQNQSP SVRPSTRREE
PSLFIGSPSP SSDSDENDAG KPLPVRDFNK QLKVNSVTKT GSSPTKKKSS ELLENEPQIP
ATKPLRRGQG GSSHTSPVKT PREKGTSEAA TIVIGNEIIQ DAASTPDRHA NNVAVSEDEM
EVDNAKPSFG SRLTQIYAAG SGATDRKISF RKEQAGEGSD GGEISDSEGT DTNTDSDTFN
ANKDGKAVSE PAIPVAGSDR PGKQTETNDL SDITPITFAE EPATTDHKTQ SLKSSVRKKE
STAQLLQHLR TDESLIKLGL DSWRNSLSPS QDSTTVDDEV TDLAAANAEE KLSLTIARKD
FLKMKIVGQF NMGFIIATRP ASTGSEEDLE VAQKNELFII DQHATDEKYN FERLQEIQTV
QSQRLVHPKR LELTALEEEI VLQNIPAIEA NGFKVHVDMT GDEPVGSRCE VLALPMSREV
TFSITDLEEL IALLGEESSE SKHIPRPSKV RKMFASRACR SSVMIGKALT HGQMETLVRH
MAELDKPWNC PHGRPTMRHL CQLDSWDAKG WRDDNLQGPS VSWRAYLNGE
//
