ID G0S651_CHATD Unreviewed; 1018 AA.
AC G0S651;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=DNA mismatch repair protein pms1-like protein {ECO:0000313|EMBL:EGS21559.1};
GN ORFNames=CTHT_0034200 {ECO:0000313|EMBL:EGS21559.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS21559.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; GL988041; EGS21559.1; -; Genomic_DNA.
DR RefSeq; XP_006693855.1; XM_006693792.1.
DR AlphaFoldDB; G0S651; -.
DR STRING; 759272.G0S651; -.
DR GeneID; 18257458; -.
DR KEGG; cthr:CTHT_0034200; -.
DR eggNOG; KOG1978; Eukaryota.
DR HOGENOM; CLU_004131_0_0_1; -.
DR OMA; RMRIIGQ; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000008066; 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: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:UP000008066}.
FT DOMAIN 220..359
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 863..1011
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 376..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 111923 MW; C20776969EB754A7 CRC64;
MASSATIKAI DSNTIHQIQS GQVIVDLCSV AKELVENSID AGATAIEVRF KNQGLDSIEV
QDNGSGIAPH NYETVALKHY TSKLSSYDDL ETLQTFGFRG EALSSLCALS RLSIVTCTQE
QAPRAARLEF EPSGKLKSTT VVSGQRGTTV IVEDLFRSLP VRRRELERNI KREWGKVINL
LNQYACIQTG VKFTVTQQPT KGKRMVMFST KGNSTTRENI INVFGVKTMN ALVPMDLTLE
LIPTAGPLTK GKARTDRKST EVRVVGHISR PTHGEGRSTP DRQMFYVNGR PCGLPQFAKV
FNEVYRLYNS SQSPFIFADI QLDTHLYDVN VSPDKRTILL HDQGQMLDNL RESLIELFET
QDVIIPMSRV AALKQTSSKI STARPSPSTS PQETGSKSAA ADSRLSKATT SFRAMENTGD
NANEESANTE DNVDDVEKED TRPRQQPKMH FRHSKPQAQF KGFTTLSNWL RNELPRPSHT
SSPLSEEQAT EASTRDKGMS SSVTSAGDRG DRIPQSQVTG DTNVRDDERS LLPDVGKDDE
IAPNEPESPI RALCPPSQPP TLRMSSTPSK PLKRATQEMA TITIGDHTVR SAIGNPSKKP
RVDEPAKPVV KTGVLKGGMR STQLPSFGIR LSQLFSASTQ PEGDLELIED AGKGIEEHEV
IEEKKGEEGR EEDDGHDSSD DDADGLFVSQ DGNKDAEDEG SGEGQPEEIL KPMETDQPQS
MSDADVPMES LGTHLASCDQ EHGDNDFEYV DEEEKVAREN QKVQAMIQEA EIATAESTEE
TEKRSETFVK GRPKRKDMTC NLVQRVKANC SEIRRRIEYL SSRLPQEACQ TTAGVRLESI
ESEDAEAKLS LKISKSDFTK MRIVGQFNLG FILAVREAVS ASSSTSCSRD SGTKDDDELF
IIDQHASDEK YNFERLQATT TVQSQRLVQP KTLSLTALEE EIILANLPAL ERNGFSVSVD
TSGASPVGSR IQLLTLPLSR ETTFSIADLE ELIFLLADNP TSNATTVPRP SKADGKGS
//
