PMS1_DICDI
ID PMS1_DICDI Reviewed; 1022 AA.
AC Q54QA0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Mismatch repair endonuclease pms1;
GN Name=pms1; ORFNames=DDB_G0283981;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with mlh1 to form MutL alpha. DNA repair is
CC initiated by MutS alpha (msh2-msh6) or MutS beta (msh2-msh3) binding to
CC a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex.
CC Assembly of the MutL-MutS-heteroduplex ternary complex in presence of
CC rfc and pcna is sufficient to activate endonuclease activity of pms1.
CC It introduces single-strand breaks near the mismatch and thus generates
CC new entry points for the exonuclease exo1 to degrade the strand
CC containing the mismatch (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of pms1 and mlh1 (MutL alpha). Forms a ternary
CC complex with MutS alpha (msh2-msh6) or MutS beta (msh2-msh3) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000058; EAL65478.1; -; Genomic_DNA.
DR RefSeq; XP_638844.1; XM_633752.1.
DR AlphaFoldDB; Q54QA0; -.
DR SMR; Q54QA0; -.
DR STRING; 44689.DDB0232417; -.
DR PaxDb; Q54QA0; -.
DR EnsemblProtists; EAL65478; EAL65478; DDB_G0283981.
DR GeneID; 8624368; -.
DR KEGG; ddi:DDB_G0283981; -.
DR dictyBase; DDB_G0283981; pms1.
DR eggNOG; KOG1978; Eukaryota.
DR HOGENOM; CLU_004131_0_2_1; -.
DR InParanoid; Q54QA0; -.
DR OMA; HIPRPSK; -.
DR PhylomeDB; Q54QA0; -.
DR Reactome; R-DDI-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR PRO; PR:Q54QA0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0032389; C:MutLalpha complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:dictyBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISS:dictyBase.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006298; P:mismatch repair; ISS:dictyBase.
DR Gene3D; 3.30.1370.100; -; 1.
DR Gene3D; 3.30.1540.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR002099; DNA_mismatch_repair_N.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; PTHR10073; 2.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF118116; SSF118116; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00585; mutl; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 3: Inferred from homology;
KW Cell cycle; DNA damage; DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..1022
FT /note="Mismatch repair endonuclease pms1"
FT /id="PRO_0000331656"
FT REGION 251..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1022 AA; 114606 MW; 5E44C6FB26C1C32F CRC64;
MIKAIDKESI NNICSGQVIF DLSIAVKELI ENSIDAGATT VEIRLKEYGE EFIEVIDNGS
GVEPSNFVAL TMKHCTSKLE SFSDLLSIET YGFRGEALSS LCSLSNCIIT TRTKNQVTAQ
RLVFDKEGKI QTQTPVAREV GTTVQLSNLF KGLPVRYQEF KRNIKKEYAK LLTILQAYAL
ISTNTRITCY NQAGKSPRSC VLSTTSGSTI RDNLINVFGT KMSQSLDEFT ASDSLFKVNG
LISKIGIGSG TGQSISNSSS SSSQSSSQLS SSSSSSSSSQ SSQLSIGSLS RSCADRQFFF
VNSRPFEHSK LAKEINSLYQ SFHKRGSYPV VIFNIEMPTN NYDVNVTPDK RTIFIQKEQQ
LLLLITDGLK TMWETAQSVF DTNQLGQFTF NDENENDNSN NNKQSKISSF PNLYTLKTEE
DENNNKITTP IKKHSTTTTT SSLNSPSSNK KSSNSTSSSS SSNNKNNRNN LEEDGDDSFD
ITDQQPLKRA KYDGNYNNSN KKPELPKTPY PNKKKNNENE DEDEDEDNYV QPVFSNVNKS
KNSSNSGSSN SLDDIIDDNE FISRSNGNSS NFMDDFEFKG SSNNIGSSSN GIKLKTISNN
NNSNNSNNSN KIIDDINKTI DKMKQQQQPQ QKMGLNDDGD DEEQQKQKQQ QQQQKRKQQQ
QQQQIEEEEE ETIDGYKQKN SKTFDITIKT DLNTISKQYL IRNGTFDKDN NPIIPNTALV
VSNDDMVVNN NNSNEFDQNS IITTTSEKCC IVDKSIPQLD GKFSTSLGGI GAKQQQKAAT
QVTSQLQQQP SQTNQKTAEE ELTKFFKKEY FKQMIVIGQF NLGFIIAKLG NDLFIIDQHA
ADEKYNFEIL SKSVESSINS QPLLKPDTLS DLTSEEELII IENVDLFKKN GFKFIIDHDA
PTRFKIKLSA FPIIHGQSFG IKDIYEWIFM IKESSIPGSV NKIPRLNSLL ASKACRKSIM
VGTTLTHKEM KDVLNNLSTL DNPWCCPHGR PTMRHLVDLS IKDKLKQQQQ QQQQKQQQQQ
QQ
