ID Q4UBT8_THEAN Unreviewed; 847 AA.
AC Q4UBT8;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE SubName: Full=DNA mismatch repair protein, putative {ECO:0000313|EMBL:CAI75713.1};
GN ORFNames=TA04865 {ECO:0000313|EMBL:CAI75713.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI75713.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI75713.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; CR940352; CAI75713.1; -; Genomic_DNA.
DR RefSeq; XP_955189.1; XM_950096.1.
DR AlphaFoldDB; Q4UBT8; -.
DR STRING; 5874.Q4UBT8; -.
DR GeneID; 3864931; -.
DR KEGG; tan:TA04865; -.
DR VEuPathDB; PiroplasmaDB:TA04865; -.
DR eggNOG; KOG1978; Eukaryota.
DR InParanoid; Q4UBT8; -.
DR OMA; HACDERY; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000001950; Chromosome 3.
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:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd16926; HATPase_MutL-MLH-PMS-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; 2.
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 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:UP000001950}.
FT DOMAIN 201..325
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 573..804
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
SQ SEQUENCE 847 AA; 95779 MW; BA891BE50974DED6 CRC64;
MSLQSLDHQH SCISRSFQVI NGISCVIREL VENAIDAHST NIGFFIIFIQ FLEIKLYNAG
VDLIKVTDNG TGISEINFDN LGSKHSTSKI RKFEDLFTSL TTFGFRGEAL YSMCNLSNVE
IETRTPNSDN GWLLKFDSLG NIINKSPIAS NIGTCVKVRE LFGEYPVRRK LLVKNSKSQI
SKSVSQIQQY ALINPHISFN FTTVTNNKKF SNIFATSGSK DEIRGVVEEI FEGLVSNPYN
ERGYREMEYF YINKRPITKV QKFKNAISAI FSHFSSRAKP SFILNLTMNC DNVDVNISPD
KRSAYIYSED YIIRTFKENL YEILKPKTNL LQINSEILTQ FISNSINIKQ EKRQLDTIDT
NSIKKQTITH TNGDTNEEHI SDTMSTGMVT DSMGINAITD TVDNTITTDT SAITYGALNL
PEILDTKDTT RAITNSTVNI PTTTSISTKS ISTDIITTES FSTENISNRI STNSITDCMS
DSITDYMSDS ITNCMSDGIN LDRINTLEEY LELVEDECCS SISRRIKICE RRLFERNMKK
LLPEESIMKC KLTNEDLMEH NFLNPQVFEK MELIGQFNKS FIITKLTFPD IKTKYNFSLY
VIDQHAADEK AKYHVTVLAQ AAPITIISIQ LFSSLSGSTL HSYRISSLSR GYWLVIYPLR
GLINMSEINR IDTIFNTSKF FKINNVQVAE NSMNVLLSNG FDIKVCREKE FLVFNDGDVC
MSSVLTEKIG RGVYVNTLPQ ILGKVLGEDD FIDFLNELST IDYIENNQQS DYIWGLGNIP
RPHKIWSILA SKACKSSVRA GDGLTNGQMK NIIKKMGTLI HPWNCPHGRP SIKCLVSHQQ
LQELLSN
//