ID B2W1G0_PYRTR Unreviewed; 968 AA.
AC B2W1G0;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=DNA mismatch repair protein {ECO:0000313|EMBL:EDU47133.1};
GN ORFNames=PTRG_04295 {ECO:0000313|EMBL:EDU47133.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU47133.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; DS231617; EDU47133.1; -; Genomic_DNA.
DR RefSeq; XP_001934628.1; XM_001934593.1.
DR AlphaFoldDB; B2W1G0; -.
DR STRING; 426418.B2W1G0; -.
DR EnsemblFungi; EDU47133; EDU47133; PTRG_04295.
DR GeneID; 6342533; -.
DR eggNOG; KOG1977; Eukaryota.
DR eggNOG; KOG1978; Eukaryota.
DR HOGENOM; CLU_005415_0_0_1; -.
DR InParanoid; B2W1G0; -.
DR OMA; NKWPMFY; -.
DR OrthoDB; 9570at2759; -.
DR Proteomes; UP000001471; 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; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 698..902
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 410..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 107576 MW; 6B2F2ACBFB6619C7 CRC64;
MTTVRGPSIL PLPEDVVAQI KSSTAILSLT DVLTELVKNS LDAKATKIEA TVDFARGGCT
VEDNGLGISP LEFREDGGLG KLYCTSKYHA RESLLGRNGT FLASLAAVSL LTIASRHHEY
RSHNSLTFHH SNTVERQLPA SAHQELHAKH GTRVTVRNLF GNLPVRVKQR SMGSGQRAEH
DRLWDQLKRD ITRLLLSWQG ELSLRVRDSE NRVLINFNTS SSSPSVGQDR EAVTPRSTQL
SSLLNILTQA NYIAIDEWPS WVPASASTSA ISINGAISLD PAPSKHVQFI SLGVRPLSPD
CGHNELFDQV NRLFALSSFG TVEDDAVVDE HEKIRRQSDK RFKQGGYTNR QLKARKDVDR
YPMFHLRISM KDPHTSRASE DEFVGDEANL QNVTEVLGAM VTQWLSVHHF RPRQPRKRRE
RPSTACSLLD NSSETPAPTT TEHGSTKPIT SSTSVASKKR KRLKDPISNK SSEKEHRQAF
ADWSRIKSGK PDFFNAVSKS KSPLANNSPD SQRNEADTCH RTKTDNFASF NIEPIDQGAL
NEHRDGSVAS ATTSSADNKE NDDTIIWTDP CTKKTHLLNA RTGCVMPDAR ARPDTDPTAS
IFGTHTRNKS VRLPSRPSTA VARKTPWLDN VLDTWENPVF KPTEKRIQQA NIHEDGLDPS
HHPSRHGCSR FDIDRAFNQA STGGSSRLSK EGLKNAQVIS QVDKKFILVK MQSFASEQEA
KAGLLVLIDQ HAADERVQVE SLFRELCTPL PQARAYKSQL GHGVLVVSTM LEKPMQFAIS
SRERTHFTTH AARFAAWGIL YDILVSAFSS SSLEKDKHVL SVTTLPPAIS ERCKADPKVL
ISFLRSTVWK YVEDAHLPPL PQHGYSANKD DWVRRLATCP PGLVDLVNSR ACRSAIMFND
TLEIEECIEL VRKLADCVFP FMCAHGRPSM VPLVDLGTSG DAGSVLSSST KNVENKTTFV
QAWRKWQK
//
