WRIP1_YEAST
ID WRIP1_YEAST Reviewed; 587 AA.
AC P40151; D6W0X2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=DNA-dependent ATPase MGS1;
DE AltName: Full=Maintenance of genome stability protein 1;
GN Name=MGS1; OrderedLocusNames=YNL218W; ORFNames=N1302;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-587.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7762305; DOI=10.1002/yea.320110111;
RA Coster F., van Dyck L., Jonniaux J.-L., Purnelle B., Goffeau A.;
RT "The sequence of a 13.5 kb DNA segment from the left arm of yeast
RT chromosome XIV reveals MER1; RAP1; a new putative member of the DNA
RT replication complex and a new putative serine/threonine phosphatase gene.";
RL Yeast 11:85-91(1995).
RN [5]
RP FUNCTION.
RX PubMed=11301316; DOI=10.1074/jbc.c100035200;
RA Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F.,
RA Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.;
RT "A novel protein interacts with the Werner's syndrome gene product
RT physically and functionally.";
RL J. Biol. Chem. 276:20364-20369(2001).
RN [6]
RP FUNCTION, AND COFACTOR.
RX PubMed=11459965; DOI=10.1073/pnas.121009098;
RA Hishida T., Iwasaki H., Ohno T., Morishita T., Shinagawa H.;
RT "A yeast gene, MGS1, encoding a DNA-dependent AAA(+) ATPase is required to
RT maintain genome stability.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8283-8289(2001).
RN [7]
RP FUNCTION.
RX PubMed=12436259; DOI=10.1007/s00438-002-0757-3;
RA Branzei D., Seki M., Onoda F., Enomoto T.;
RT "The product of Saccharomyces cerevisiae WHIP/MGS1, a gene related to
RT replication factor C genes, interacts functionally with DNA polymerase
RT delta.";
RL Mol. Genet. Genomics 268:371-386(2002).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Involved in the maintenance of proper DNA topology and
CC chromosome integrity via annealing of single-stranded DNA breaks.
CC Modulates DNA polymerase delta during replication or replication-
CC associated repair. May function as a modulator for SGS1 when DNA is
CC damaged. {ECO:0000269|PubMed:11301316, ECO:0000269|PubMed:11459965,
CC ECO:0000269|PubMed:12436259}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11459965};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000305}.
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DR EMBL; Z71493; CAA96120.1; -; Genomic_DNA.
DR EMBL; Z71494; CAA96121.1; -; Genomic_DNA.
DR EMBL; AY693190; AAT93209.1; -; Genomic_DNA.
DR EMBL; X78898; CAA55489.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10338.1; -; Genomic_DNA.
DR PIR; S63176; S63176.
DR RefSeq; NP_014181.1; NM_001183056.1.
DR AlphaFoldDB; P40151; -.
DR SMR; P40151; -.
DR BioGRID; 35618; 81.
DR DIP; DIP-1638N; -.
DR IntAct; P40151; 9.
DR MINT; P40151; -.
DR STRING; 4932.YNL218W; -.
DR MaxQB; P40151; -.
DR PaxDb; P40151; -.
DR PRIDE; P40151; -.
DR EnsemblFungi; YNL218W_mRNA; YNL218W; YNL218W.
DR GeneID; 855503; -.
DR KEGG; sce:YNL218W; -.
DR SGD; S000005162; MGS1.
DR VEuPathDB; FungiDB:YNL218W; -.
DR eggNOG; KOG2028; Eukaryota.
DR GeneTree; ENSGT00390000008538; -.
DR HOGENOM; CLU_017985_0_1_1; -.
DR InParanoid; P40151; -.
DR OMA; RIILSQC; -.
DR BioCyc; YEAST:G3O-33224-MON; -.
DR PRO; PR:P40151; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40151; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IDA:SGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; IGI:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006642; Rad18_UBZ4.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..587
FT /note="DNA-dependent ATPase MGS1"
FT /id="PRO_0000084788"
FT ZN_FING 11..38
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 35..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 179..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P55072"
SQ SEQUENCE 587 AA; 66544 MW; A7464BF94FCC23EA CRC64;
MSNKRTSVEQ LISCPICSRK VFFSLINSHL DICGKEKSKP SSRPQTVSSL LAGPKKRKQA
NSEKFIDLEN KDHEIKPGLK SESDDIEIVE NESKRFKAAP STDFAKSIVE PASSRDQLHN
DYESRWLQKI SHLPLSEKLR PKELRDYVGQ QHILSQDNGT LFKYIKQGTI PSMILWGPPG
VGKTSLARLL TKTATTSSNE SNVGSRYFMI ETSATKANTQ ELRGIFEKSK KEYQLTKRRT
VLFIDEIHRF NKVQQDLLLP HVENGDIILI GATTENPSFQ LNNALISRCL IFVLEKLNVN
ELCIVLSRGI ALLNKCRKQV WNIENPLKLS RSILEYVVDL SVGDTRRALN MLEMIEVSTR
ERKADEEELS IDDVRDIIKN NSSNGLNTYY DPKGDNHYDT ISAFHKSIRG GDENASLYYL
ARMLQGGEDP LYVARRMIRI ASEDIGLRDS SLLPLAVAAH DAVMKVGLPE ADLALAQCCV
ALARAPKSVE LYRAWKKLRA MMSENMYSLA SSEIPMHIRN APTKLMEELG YHKGYKYNPD
YIEGKVQQDY FPKEVLEKCP NKTDLKFLDG KHLGDKEDPD LRQSYQG
