ID A0A225AJT0_9EURO Unreviewed; 1130 AA.
AC A0A225AJT0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=UA08_02464 {ECO:0000313|EMBL:OKL61772.1};
OS Talaromyces atroroseus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Trachyspermi.
OX NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL61772.1, ECO:0000313|Proteomes:UP000214365};
RN [1] {ECO:0000313|EMBL:OKL61772.1, ECO:0000313|Proteomes:UP000214365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL61772.1,
RC ECO:0000313|Proteomes:UP000214365};
RA Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA Mortensen U.H., Thrane U.;
RT "Talaromyces atroroseus IBT 11181 draft genome.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA
CC mismatches thereby initiating DNA repair. MSH3 provides substrate-
CC binding and substrate specificity to the complex. When bound, the MutS
CC beta heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC 13 nucleotides in size, but can also repair base-base and single
CC insertion-deletion mismatches that occur during replication. After
CC mismatch binding, forms a ternary complex with the MutL alpha
CC heterodimer, which is thought to be responsible for directing the
CC downstream MMR events, including strand discrimination, excision, and
CC resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC repair functions. {ECO:0000256|ARBA:ARBA00025373}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with MutL alpha (MLH1-PMS1).
CC {ECO:0000256|ARBA:ARBA00025902}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000256|ARBA:ARBA00007094}.
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:OKL61772.1}.
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DR EMBL; LFMY01000003; OKL61772.1; -; Genomic_DNA.
DR RefSeq; XP_020121893.1; XM_020264509.1.
DR AlphaFoldDB; A0A225AJT0; -.
DR STRING; 1441469.A0A225AJT0; -.
DR GeneID; 31002219; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000214365; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR Gene3D; 1.10.1420.10; -; 2.
DR Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361:SF122; DNA MISMATCH REPAIR PROTEIN MSH3; 1.
DR PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 2.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037677};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR037677};
KW DNA repair {ECO:0000256|PIRNR:PIRNR037677};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037677}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000214365}.
FT DOMAIN 968..984
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 125415 MW; 6C9611671FBCA760 CRC64;
MPTMSSQSSP PSSSPALKRK QQTISSFFTK KPSPNGQKPS SQAVVQGVIQ EKNEQQGKNI
PSGKENAVFV GKSFSRIEDG QRKDDDDDDI ILPAPKRAKM GDAGKSTPTE PRADGDILQS
SQRTERFKFS SSQAVNENEQ QGGDDEHSRK EKEKMHQKFV RKLGGPDCLV GIGKSAANED
ETAAGAEDAE DDEEPVPAPT TKGRQSKKSG SKLTPMEKQV IEIKRKHMDT LLIVEVGYKF
RFFGEDARTA AKELSIVCIP GKMRFDEHPS EAHLERFASA SIPVHRLHVH VKRLVTAGHK
VGVVRQLETA ALKAAGDNRN APFVRKLTNV YTKGTYIDDA EGLSAPAVAS MGATPATGYL
LCITESNTSG SDERVHVGIV AVQPATGDII YDEFEDGFMR GEIETRLLHI APCEILIVGE
LTKATEKLVK QLSSSKMNVF GDKVRVERAP RSRTAAVESH SRVSTFYADK LKSTENADDG
KASALLEKVL QLPDQVTICL SSMIDHLSEY GLEHVFDLTK YFQSFSARSH MLLNGNTLTS
LEIYQNQTDY SSKGSLFWTM DRTRTRFGQR MLRKWVGRPL LDKSQLEERV GAVEELLNSE
QNALTDRLKD LLSKVKSDLE RSLIRIYYGK CTRPELLTVL QTLQLIANSF SHINSPADTG
FESTIISEAV AKLPTIREDV VMFLDKINMH AAKNDDKYEF FRESEESDDI TEQKLGIASV
EHDLEQHRDV AAEVMGKKKV DYVTSSGIEY LIEVENNSPQ FKRVPASWAK ISGTKKLSRF
HTPDVIKLIR QRDQHKEALA AACDKEYMRL LAEISSKYQS FRDCIQSLAL LDCLFSLAAV
ASQPGYTKPQ YTDQTRIVVE QGRHPMVEQL LLDSYVPNDT HLDSDQTRAL LVTGPNMGGK
SSYVRQVALI AIMGQIGSYV PAKSATLGML DAVFTRMGAF DNMLTGESTF MVELSETADI
LKQATSRSLV ILDELGRGTS THDGVAIAQA ILDHMVRTIR SLTLFITHYQ NLSAMAKSFP
NHELRNVHMR FTESGDRNDE EITFLYEVGE GVAHRSYGLN VARLANLPPS VLDLARQKSS
ELEEKIRRKR LVNAAKNVES ILTKESSAVN DGGAEQDLII EKLIGFAEQL
//
