MSH3_ASPFU
ID MSH3_ASPFU Reviewed; 1123 AA.
AC Q4WGB7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; ORFNames=AFUA_7G04480;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer consisting of msh2-msh3 (MutS beta). Forms a
CC ternary complex with MutL alpha (mlh1-pms1) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000009; EAL87024.1; -; Genomic_DNA.
DR RefSeq; XP_749062.1; XM_743969.1.
DR AlphaFoldDB; Q4WGB7; -.
DR SMR; Q4WGB7; -.
DR STRING; 746128.CADAFUBP00008751; -.
DR EnsemblFungi; EAL87024; EAL87024; AFUA_7G04480.
DR GeneID; 3506462; -.
DR KEGG; afm:AFUA_7G04480; -.
DR VEuPathDB; FungiDB:Afu7g04480; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_0_1; -.
DR InParanoid; Q4WGB7; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IEA:EnsemblFungi.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IEA:EnsemblFungi.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR11361; 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; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1123
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000338509"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..331
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 894..901
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1123 AA; 124367 MW; B64ACCA03C5C0DB3 CRC64;
MTLSSSQSSP PSTQNLKRKQ QTISSFFTKR APSAEKRSND IEDGRATTQK GAEMPLRETA
GDQNNLEDDE DGDVVVRAPK RVKTNGVDPE NGFGRNIKEA SNIARRPDPP LSSSQRTNLY
KFASSQADDA GIEKTDDPEA RQRQLEREKL HKLFVKKLGG ADCLIGIGRD ATTEAPSGTE
DVAEGDEDDE SPPQPRSKGK GLSKKGGSKL TPLEKQVIEI KRKHMDTILV VEVGYKFRFF
GEDARIAAKE LSIVCIPGKM RFDEHPSEAH LDRFASASIP VHRLHVHVKR LVSAGYKVGV
VRQLETAALK AAGDNRNAPF SRKLTNLYTK GTYVDDVEGL DGATPAASGG ASPATGYMLC
ITETNAKGWG NDEKVHVGIV AVQPNTGDVI YDDFDDGFMR SEVETRLLHI APCELVIVGE
LSKATEKLVQ HLSGSKLNTF GDKVRVDRVA KKKTAVAESH SHVANFYAAK LKAANTADDA
PASNLLQKVL NLPEQVTVCL SAMIQHLTEY GLEHIFELTK YFQHFSSRSH MLLNANTLVS
LEIYQNQTDH SAKGSLFWTL DRTQTRFGQR LLRKWVGRPL LDKERLEERV NAVEELKSPE
RTVQAERLKI MLGKIKSDLE KNLIRIYYGK CTRPELLTVL QTLQTIAQEY VDVKTPQDSG
FTSPILGEAI ARVPSILGDV VKFLNKINMH AARNDDKYEF FRESEETEGI SEHKCGIASV
EHELEEHRSV AAGILKWPKV TYVTSSGIEY LIEVENSAAA IKRVPASWVK VSGTKKVSRF
HTPEVIQLLR QRDQHKEALA AACDQAFAAL LAEIASNYQS FRDCVQSLAT LDCLLSLAAI
ASQPGYVKPE YTDQTCIHVE QGRHPMVEQL LLDSYVPNDI DLDSDKTRAL LVTGPNMGGK
SSYVRQIALI AIMAQIGSYV PARSAKLGML DAVFTRMGAF DNMLAGESTF MVELSETADI
LKQATPRSLV ILDELGRGTS THDGVAIAQA VLDYMVRTIR SLTLFITHYQ HLSNMAQSFP
DHELRNVHMR FTESGSGKDE EITFLYEVGE GVAHRSYGLN VARLANLPAP LLEVARQKSS
ELEERIRRRR LARLLADVGG LIEDPAKGDE NFFQRLISNA EQL
