ID A1CHE3_ASPCL Unreviewed; 1212 AA.
AC A1CHE3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=DNA mismatch repair protein {ECO:0000256|PIRNR:PIRNR037677};
GN ORFNames=ACLA_047670 {ECO:0000313|EMBL:EAW10298.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10298.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW10298.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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.
CC {ECO:0000256|PIRNR:PIRNR037677, ECO:0000256|RuleBase:RU003756}.
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DR EMBL; DS027054; EAW10298.1; -; Genomic_DNA.
DR RefSeq; XP_001271724.1; XM_001271723.1.
DR AlphaFoldDB; A1CHE3; -.
DR STRING; 344612.A1CHE3; -.
DR EnsemblFungi; EAW10298; EAW10298; ACLA_047670.
DR GeneID; 4704255; -.
DR KEGG; act:ACLA_047670; -.
DR VEuPathDB; FungiDB:ACLA_047670; -.
DR eggNOG; KOG0217; Eukaryota.
DR HOGENOM; CLU_002472_1_0_1; -.
DR OMA; TPMMAQY; -.
DR OrthoDB; 168255at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0032301; C:MutSalpha complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000400; F:four-way junction DNA binding; IEA:EnsemblFungi.
DR GO; GO:0032137; F:guanine/thymine mispair binding; IEA:EnsemblFungi.
DR GO; GO:0032138; F:single base insertion or deletion binding; IEA:EnsemblFungi.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IEA:EnsemblFungi.
DR GO; GO:0000710; P:meiotic mismatch repair; IEA:EnsemblFungi.
DR GO; GO:0043111; P:replication fork arrest; IEA:EnsemblFungi.
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; IPR007861; DNA_mismatch_repair_MutS_clamp.
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:SF148; DNA MISMATCH REPAIR PROTEIN MSH6; 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; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR SUPFAM; SSF53150; DNA repair protein MutS, domain II; 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, ECO:0000256|RuleBase:RU003756};
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:UP000006701}.
FT DOMAIN 1042..1058
FT /note="DNA mismatch repair proteins mutS family"
FT /evidence="ECO:0000259|PROSITE:PS00486"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..195
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 135604 MW; 8792D88B3108C160 CRC64;
MARGAGAASS PTAATPPSAA LKQSTSSTQN MKNQKSILGF FQKSSPSTPS TARNAEPASS
PAQRVSEQRE ATSGKGTSKR ERKAVPKFTQ NLTPVPSSDL VVPDEEDEKV LGSTKDDLAQ
KTASPSRRAK KQVSYAESES EGEDDDDVIF APNRRNSRAS KKRKTSPEPE DEFEQAGEVG
YSDDEFDDFI VADESDEEVQ PSKKRKRPSK APTRKSSIPV PPSPGEDLDL DIPDAVGGTA
VKWTYDPENQ EPRQHRTIQA PSKSSATPAK QKAHLKEPED RYPWLANIRD MDGHPPNHPD
YDPRTIYIPP LAWSKFSPFE KQYWEIKQKF WDTVVFFKKG KFYELYENDA TIGHQLFDLK
LTDRVNMRMV GVPEMSLDHW ANQFVAKGFK IARVDQSESA LGKEMRERDG KKAGGKEDKI
IKRELSCVLT AGTLVEGSML QDDMSTYCVA IKEAIIEDHP AFGIAFVDTA TGQFSLSEFG
DDADMTKFET FVAQTRPQEL LLEKSTISTK ALRILKNNTG PTTIWNHLKP GKEFWEADIT
VKELDASDYF VSQDDDNLQA WPETLREARA KELAMSAFGA LVQYLRMLKL DRDLITIGNF
SWYDPIRKTS NLVLDGQTLI NMEIFANSFD GGSEGTLFQL LNRCITPFGK RMFKQWVCHP
LMDAKKINAR LDAVDALNAD SSIRDQFSSQ LTKMPDLERL ISRIHAANCK AQDFVRVLEG
FEQIEYTISL LKDTGSSGEG VIGQLINAMP DLGSLLEYWK TAFDRNKAKE NGILVPKLGV
EEDFDNSQES IEQLHRDLDN LLKRVRRELG STAICYRDNG KEIYQLEVPV KVKNVPKNWD
QMSATKQVKR YYFPELRSLI RKLQETQETH SHIVKEVAGR FYARFDEHYT TWLAAVRIVS
QLDCLISLAK ASSSLGHPSC RPVFVEDGRS VLEFEELRHP CLLSSVEDFI PNDVRLGGER
PNINLLTGAN AAGKSTVLRM SCVAVIMAQI GCYLPCKSAR LTPVDRIMSR LGANDNIFAA
QSTFFVELSE TKKILSEATP RSLVILDELG RGTSSYDGVA VAQAVLHHIS SHIGAMGFFA
THYHSLAAEF EGHPEITPKR MRIHVDDQER RITFLYKLED GVAEGSFGMH CASMCGIPNK
IIERAEVAAK QWEHTSRLKE SLERRKGGGF IGLGWWSDVA WALRESTGDA VSSTDSVSDL
SLEVLRKAIE TL
//
