HCS1_YEAST
ID HCS1_YEAST Reviewed; 683 AA.
AC P34243; D6VXR9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA polymerase alpha-associated DNA helicase A;
DE EC=3.6.4.12;
GN Name=HCS1; Synonyms=DIP1; OrderedLocusNames=YKL017C;
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 [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 9-22, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9341217; DOI=10.1021/bi9712910;
RA Biswas S.B., Chen P.H., Biswas E.E.;
RT "Purification and characterization of DNA polymerase alpha-associated
RT replication protein A-dependent yeast DNA helicase A.";
RL Biochemistry 36:13270-13276(1997).
RN [5]
RP FUNCTION, AND ASSOCIATION WITH DNA POLYMERASE ALPHA.
RX PubMed=7681325; DOI=10.1021/bi00063a012;
RA Biswas E.E., Chen P.H., Gray W., Li Y.H., Ray S., Biswas S.B.;
RT "Purification and characterization of a yeast DNA polymerase alpha complex
RT with associated primase, 5'-->3' exonuclease, and DNA-dependent ATPase
RT activities.";
RL Biochemistry 32:3013-3019(1993).
RN [6]
RP FUNCTION, AND ASSOCIATION WITH DNA POLYMERASE ALPHA.
RX PubMed=8384485; DOI=10.1021/bi00063a013;
RA Biswas E.E., Ewing C.M., Biswas S.B.;
RT "Characterization of the DNA-dependent ATPase and a DNA unwinding activity
RT associated with the yeast DNA polymerase alpha complex.";
RL Biochemistry 32:3020-3026(1993).
RN [7]
RP FUNCTION, AND ASSOCIATION WITH DNA POLYMERASE ALPHA.
RX PubMed=8257676; DOI=10.1021/bi00212a003;
RA Biswas E.E., Chen P.H., Biswas S.B.;
RT "DNA helicase associated with DNA polymerase alpha: isolation by a modified
RT immunoaffinity chromatography.";
RL Biochemistry 32:13393-13398(1993).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9341218; DOI=10.1021/bi971292s;
RA Biswas E.E., Fricke W.M., Chen P.H., Biswas S.B.;
RT "Yeast DNA helicase A: cloning, expression, purification, and enzymatic
RT characterization.";
RL Biochemistry 36:13277-13284(1997).
RN [9]
RP INDUCTION.
RX PubMed=10077188;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<219::aid-yea349>3.0.co;2-3;
RA Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.;
RT "Systematic identification, classification, and characterization of the
RT open reading frames which encode novel helicase-related proteins in
RT Saccharomyces cerevisiae by gene disruption and Northern analysis.";
RL Yeast 15:219-253(1999).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
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: DNA polymerase alpha-associated DNA helicase which may be
CC involved in DNA replication. {ECO:0000269|PubMed:7681325,
CC ECO:0000269|PubMed:8257676, ECO:0000269|PubMed:8384485,
CC ECO:0000269|PubMed:9341217, ECO:0000269|PubMed:9341218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for ATP {ECO:0000269|PubMed:9341217,
CC ECO:0000269|PubMed:9341218};
CC Vmax=14 umol/min/mg enzyme {ECO:0000269|PubMed:9341217,
CC ECO:0000269|PubMed:9341218};
CC -!- SUBUNIT: Associates with the hexameric DNA polymerase alpha.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000305|PubMed:14562095}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:10077188}.
CC -!- MISCELLANEOUS: Present with 1040 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
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DR EMBL; X74152; CAA52266.1; -; Genomic_DNA.
DR EMBL; Z28017; CAA81852.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09139.1; -; Genomic_DNA.
DR PIR; S34700; S34700.
DR RefSeq; NP_012908.1; NM_001179583.1.
DR AlphaFoldDB; P34243; -.
DR SMR; P34243; -.
DR BioGRID; 34115; 125.
DR DIP; DIP-1383N; -.
DR IntAct; P34243; 2.
DR MINT; P34243; -.
DR STRING; 4932.YKL017C; -.
DR MaxQB; P34243; -.
DR PaxDb; P34243; -.
DR PRIDE; P34243; -.
DR EnsemblFungi; YKL017C_mRNA; YKL017C; YKL017C.
DR GeneID; 853852; -.
DR KEGG; sce:YKL017C; -.
DR SGD; S000001500; HCS1.
DR VEuPathDB; FungiDB:YKL017C; -.
DR eggNOG; KOG1803; Eukaryota.
DR GeneTree; ENSGT00930000151035; -.
DR HOGENOM; CLU_001666_8_2_1; -.
DR InParanoid; P34243; -.
DR OMA; YKRMEST; -.
DR BioCyc; YEAST:G3O-31826-MON; -.
DR SABIO-RK; P34243; -.
DR PRO; PR:P34243; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P34243; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004483; SMUBP-2/Hcs1-like.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00376; TIGR00376; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..683
FT /note="DNA polymerase alpha-associated DNA helicase A"
FT /id="PRO_0000080726"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 683 AA; 78273 MW; FCD02680757377B8 CRC64;
MNKELASKFL SSIKHEREQD IQTTSRLLTT LSIQQLVQNG LAINNIHLEN IRSGLIGKLY
MELGPNLAVN DKIQRGDIKV GDIVLVRPAK TKVNTKTKPK VKKVSEDSNG EQAECSGVVY
KMSDTQITIA LEESQDVIAT TFYSYSKLYI LKTTNVVTYN RMESTMRKLS EISSPIQDKI
IQYLVNERPF IPNTNSFQNI KSFLNPNLND SQKTAINFAI NNDLTIIHGP PGTGKTFTLI
ELIQQLLIKN PEERILICGP SNISVDTILE RLTPLVPNNL LLRIGHPARL LDSNKRHSLD
ILSKKNTIVK DISQEIDKLI QENKKLKNYK QRKENWNEIK LLRKDLKKRE FKTIKDLIIQ
SRIVVTTLHG SSSRELCSLY RDDPNFQLFD TLIIDEVSQA MEPQCWIPLI AHQNQFHKLV
LAGDNKQLPP TIKTEDDKNV IHNLETTLFD RIIKIFPKRD MVKFLNVQYR MNQKIMEFPS
HSMYNGKLLA DATVANRLLI DLPTVDATPS EDDDDTKIPL IWYDTQGDEF QETADEATIL
GSKYNEGEIA IVKEHIENLR SFNVPENSIG VISPYNAQVS HLKKLIHDEL KLTDIEISTV
DGFQGREKDV IILSLVRSNE KFEVGFLKEE RRLNVAMTRP RRQLVVVGNI EVLQRCGNKY
LKSWSEWCEE NADVRYPNID DYL
