MSH6_SCHPO
ID MSH6_SCHPO Reviewed; 1254 AA.
AC O74502;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=DNA mismatch repair protein msh6;
GN Name=msh6; ORFNames=SPCC285.16c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tornier C., Bessone S., Varlet I., Rudolph C., Darmon M., Fleck O.;
RT "Major role of msh6 in the mismatch repair system of S. pombe both towards
RT base-base mispairs and insertion-deletion loops, contrasting with minor
RT role of the msh3 ortholog swi4.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-299; SER-307 AND
RP SER-309, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in post-replicative DNA-mismatch repair. Has a role
CC towards base-base mispairs and insertion-deletion loops.
CC -!- SUBUNIT: Heterodimer of msh2 and msh6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; AF207839; AAF20943.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20855.1; -; Genomic_DNA.
DR PIR; T41262; T41262.
DR RefSeq; NP_588344.1; NM_001023335.2.
DR AlphaFoldDB; O74502; -.
DR SMR; O74502; -.
DR BioGRID; 275785; 43.
DR STRING; 4896.SPCC285.16c.1; -.
DR iPTMnet; O74502; -.
DR MaxQB; O74502; -.
DR PaxDb; O74502; -.
DR PRIDE; O74502; -.
DR EnsemblFungi; SPCC285.16c.1; SPCC285.16c.1:pep; SPCC285.16c.
DR GeneID; 2539215; -.
DR KEGG; spo:SPCC285.16c; -.
DR PomBase; SPCC285.16c; msh6.
DR VEuPathDB; FungiDB:SPCC285.16c; -.
DR eggNOG; KOG0217; Eukaryota.
DR HOGENOM; CLU_002472_1_0_1; -.
DR InParanoid; O74502; -.
DR OMA; TPMMAQY; -.
DR PhylomeDB; O74502; -.
DR Reactome; R-SPO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR PRO; PR:O74502; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0032301; C:MutSalpha complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISO:PomBase.
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:0032137; F:guanine/thymine mispair binding; ISO:PomBase.
DR GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:PomBase.
DR GO; GO:0006298; P:mismatch repair; IMP:PomBase.
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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1254
FT /note="DNA mismatch repair protein msh6"
FT /id="PRO_0000115212"
FT REGION 1..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1024..1031
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1254 AA; 141512 MW; 7A28EC8DD8D2845B CRC64;
MSVGNVGKQR EKTKDSSAKT KQKTLFGFFS KIPNVKQEKS DSTLSSSSNH DSNHDTPADV
DNSSNVNKNS SSPERELPTS PSHHANTEID SSSSMLPPPS SDPFSSPLSS SLHRSSPKRP
HDSLGEESPG KLLRTSVKQE PDSEEEIDSP TKKKSFKSLD TSIFQAEDQF RHPVSSKLEN
SELSEVDKPF IASRRSRKPV SYAESDEDED FDDAPTKGSR HKRIVSDDES DDYVEPDHIS
EASSEASLPI DEVESMDEDV DGYSDHSVSV AAPIPKKESR KESSNSLYES YRLGSQIASP
SPSVSGSASP TKSNKNGVLN REEKRRQRME AFKKENNERY EWLLDVRDAD QNRVGDPNYD
PRTLYIPPSA WATFKPFEKQ FWKIKKDLMD TVVFFQKGKF YELYENDAAI GHQVFSLKLT
DRVNMKMVGI PEASFDYWAS QFIAKGYRIA RVDQLETALG KEIKDRQRTQ KEEKVVQRGL
TQVLTSGTLV DEAMLTSDLS TYCMAIKESL QSDNEEPSFG ICFIDTSTGG FHMCEFTDDI
HRTKLDTLLT QVRPKELILE KSKISQKSIR AIKYCVSSSS IWNFIKPYTE FWDNERVERE
IIAGDYFKNG LEGAPKILKS YLSEKPLAIS AFGALFWYLR QLKLDKDMCS MGNFDEYDAS
QQSTSLLMNG QTLKNLEIFS NSFDGGSEGT LFHLLCRCVT PFGKRLFHTW LCHPLRSGTA
INARLDVVEL IADNPVIRDT IWGFLHKLPD LERLISRVHA GRSKPADFVR VLEGFQRINS
AFDQLREEFM EVAEGTLLGE IIQSAPNMKE ELEAWTRAFN WQKASEEGVF EPEIGFEAEY
DTSQKYQSEL KNELYALLEQ YKKQLRCSSL NFKNIGKEVY QVEVPSDVKV PVNWCKMSGT
KKTNRYYNDE LRKKIKKLLE AEELHLAIMS RMQEKFYIRF DSNYEQWLAL IKYTASIDCF
FSLSQAAAAL GEPYCRPEII EQKDGHLYFE ELRHPCINAS AASTFVPNDV VLGGESPNMI
VLTGPNMAGK STLLRQVCIA VIMAQLGCWV PAKRASITPM TSIYTRLGAN DDIMSARSTF
MVELSETKKI LDECGPKSLV ILDELGRGTS TYDGHAIAYA VLHHLVSNIG CLGFFSTHYQ
SLCVDFMHHR QVRLMQMAAA VDEKIRRVTF LYKLEDGICP KSYGMNVASM AGLPEKVIDA
AEEKASELEQ ASASFINASD DIALMSDFLQ VLRISKSIEP LTAVNIPLIL DSFE
