MSH1_SCHPO
ID MSH1_SCHPO Reviewed; 941 AA.
AC O13921; O13700; Q9USD9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=MutS protein homolog 1;
GN Name=msh1; ORFNames=SPAC13F5.01c, SPAC23C11.18c;
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]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 623-792, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- FUNCTION: Involved in mitochondrial DNA repair. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}.
CC Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11169.1; -; Genomic_DNA.
DR EMBL; AB027833; BAA87137.1; -; Genomic_DNA.
DR PIR; T38256; T37626.
DR RefSeq; NP_593649.2; NM_001019080.3.
DR AlphaFoldDB; O13921; -.
DR SMR; O13921; -.
DR BioGRID; 279280; 19.
DR STRING; 4896.SPAC13F5.01c.1; -.
DR iPTMnet; O13921; -.
DR MaxQB; O13921; -.
DR PaxDb; O13921; -.
DR EnsemblFungi; SPAC13F5.01c.1; SPAC13F5.01c.1:pep; SPAC13F5.01c.
DR GeneID; 2542833; -.
DR KEGG; spo:SPAC13F5.01c; -.
DR PomBase; SPAC13F5.01c; msh1.
DR VEuPathDB; FungiDB:SPAC13F5.01c; -.
DR eggNOG; ENOG502QUUG; Eukaryota.
DR HOGENOM; CLU_002472_4_0_1; -.
DR InParanoid; O13921; -.
DR OMA; MQCGDFY; -.
DR PhylomeDB; O13921; -.
DR PRO; PR:O13921; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:PomBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; 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:0030983; F:mismatched DNA binding; ISM:PomBase.
DR GO; GO:0006298; P:mismatch repair; ISM:PomBase.
DR GO; GO:0043504; P:mitochondrial DNA repair; ISO: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; 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; SSF53150; SSF53150; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..941
FT /note="MutS protein homolog 1"
FT /id="PRO_0000115180"
FT BINDING 747..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 941 AA; 106933 MW; 7A1D8F477E1140AB CRC64;
MPTWRYIFSL RSKSSFTKTW VPFTQIRNSS KSPKVGQKPI LQGALGPPLD FIRPKEKVTL
PPLLKEVSFQ QKKFADCVLL TKVGNFYEMY FEQAEKIGPL LNLRVSKKKT SKSDVSMAGF
PFFKLDRYLK ILVEDLKKCV ALSEEVIRPV DDLSSKNMYI RSVTRVITPG TLIDENFMNP
YESNYILTVV FDPNFFSSDI SNQGTAEDKD CFADCKIGLS WLDLSTGEFF TQDSNLQRLA
GDLTRISPRE IVLDESLKSF TTHPIYSFIQ ERKYFLSYVE NRYQSLDCWN KFLEKEIDPS
FIKYCTKLEV TAGCTLISYI ADRLQNSHPN IQPPIRVSLN EYMIIGESAM KGLEIRSSLY
QNRYTGSLLH AINKTVTKSG SRLLTRRLCA PSTNIVEINN RLDLVEKFKL LPELCSKVIN
LLKKSNDTHR ILQHLLMGRG NSYDLLKMAD NFSITKEIHS LLSPLESSSA FRLLLLNMHP
HDELKQLINN AVDENALMKQ KINEEEETEV IAQEAEEILQ DENAQVEIVK KSLSSEFDIR
QSFKENWVVK SNFNNNLRKL HEKLQSLFAS YDKLQEDLSK RLGKKATLRK SPAKLYYVHL
KLSGNETIER FIKKFTQAVL FQSTKSTASF QLPGWTSLGM DLENTKLHIH QEEQRVLKSI
TDEIVSHHKT LRSLANALDE LDISTSLATL AQEQDFVRPV VDDSHAHTVI QGRHPIVEKG
LSHKLIPFTP NDCFVGNGNV NIWLITGPNM AGKSTFLRQN AIISILAQIG SFVPASNARI
GIVDQIFSRI GSADNLYQQK STFMVEMMET SFILKNATRR SFVIMDEIGR GTTASDGIAI
AYGCLKYLST INHSRTLFAT HAHQLTNLTK SFKNVECYCT NLSIDRDDHT FSFDYKLKKG
VNYQSHGLKV AEMAGIPKNV LLAAEEVLTL LPNTSKPTSM K