MSH3_USTMA
ID MSH3_USTMA Reviewed; 1154 AA.
AC Q4P6I8; A0A0D1DYZ2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; ORFNames=UMAG_04275;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) 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 (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; CM003151; KIS67780.1; -; Genomic_DNA.
DR RefSeq; XP_011390736.1; XM_011392434.1.
DR AlphaFoldDB; Q4P6I8; -.
DR SMR; Q4P6I8; -.
DR STRING; 5270.UM04275P0; -.
DR PRIDE; Q4P6I8; -.
DR EnsemblFungi; KIS67780; KIS67780; UMAG_04275.
DR GeneID; 23564507; -.
DR KEGG; uma:UMAG_04275; -.
DR VEuPathDB; FungiDB:UMAG_04275; -.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR InParanoid; Q4P6I8; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR Proteomes; UP000000561; Chromosome 12.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006298; P:mismatch repair; IEA:InterPro.
DR GO; GO:0043504; P:mitochondrial DNA repair; IBA:GO_Central.
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; 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; PTHR11361; 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; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53150; SSF53150; 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..1154
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000338531"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..342
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 929..936
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1154 AA; 127005 MW; 0AA4C08AC31CA16D CRC64;
MPPPPSQKPG QASISAFFKP KSSQRPITKS CQPDRAQVSN GYARTSNLLD TDTGASSSAQ
PPHKRSKLNN KDGPRRETID RMSKWKFTAL QPSDNVSSEL DEAASQATPT ERSQHDQARH
DAFRKTLLGP NFAIDRHASN QMQIDDMSSA HTFSHSESRT STGTKVDAMV VDDDDDDDDN
QHEQAAQSVP GTWNRFTGLA APESTPAPCS HRDSSMNKTK GKPKASGAGT GPSYTPLEKQ
ILELKAEHPG VLLIIEVGYK LKFYGEDARI ASKELSIMCF PERNLLTAMI PVHRLHIHVK
RLIQAGHKVG VVRQIETRAL KAASKNAYTP FVRKLTALYT ASTWVDDLSS LDDLAANMGD
AYTNQPKSLM AIVEQSERGN AQADRVSIGI VSVEVNTGHL TYDQFSDGHA RSELETRIAH
LAPAEVLIPP QLTKPTEKVI SYLLGNGADG GVRIERLAAM PDYNQAFQSV TRFYRDRGLE
SPEVPEVPEV PGSSEADTTR LATTLADGAD KRSSPLISLI VSLPQLSLIA LAQIIQHLQA
FQLESICTLS TNFRSFSSRT TMLLNSNTLA NLEIFRTANE QTERGSLIWL LDKCKSAMGR
RLLRKWVSRP LTDIDKLQER LDAVEALRDG KSYVLRRLDS VLHGLPDLER GLARMTYGRA
TPTELATVLL SLNRVTQEFK ADEAATWKTQ SSLIDTHLLS LASGKQVVQT YLNQISIKEA
RANNKADLYL DADVFPAIQA SKDNMAIIDG ELREHLREIR KLLHRPSLDY VSVAGVDYLV
EVRVADAKKV PVEWLRVSAT KSMVRFHTPE VMRLSKIRDQ HKETLDAAAQ EAFARFVREL
CKSEYVVLRN VVASLAVLDV LLSLAHVARA AGYTRPVFLR QPQDAEASVP VEIIGMRHAI
LEVVSAMPYI PNDVSLSTGD SGAAILLSGC NMGGKSSVVR ALGLVIIMAQ IGSFVAADVA
RIGVHDAVYV RMGARDRMFS GRSTYMVEVS ETADILGSLT SRSMVILDEL GRGTSSRDGY
CLAAGVLEYL LTLGCPPNTV FITHYLQLAS MQRRYPHLRN MHMAFTSNSR NLLDPIHLVY
KLRPGIAHSF GIHAAHLARL PLQIIHSAST ISSALYAKHT NRSAFLVLKH AFANPPQLAT
VSTLQHLLFT HPPT
