ID HFM1_YEAST Reviewed; 1187 AA.
AC P51979; D6VV84;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 27-MAR-2024, entry version 191.
DE RecName: Full=ATP-dependent DNA helicase MER3;
DE EC=3.6.4.12;
DE AltName: Full=Protein HFM1;
GN Name=HFM1; Synonyms=MER3; OrderedLocusNames=YGL251C; ORFNames=NRE1046;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8972578;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1555::aid-yea43%3e3.0.co;2-q;
RA Coissac E., Maillier E., Robineau S., Netter P.;
RT "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT VII of Saccharomyces cerevisiae.";
RL Yeast 12:1555-1562(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-1187.
RA West R.W. Jr., Thomas S., Ma J.L., Finley R.L. Jr.;
RT "Saccharomyces cerevisiae Hfm1p (HFM1) gene.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION.
RX PubMed=10523314; DOI=10.1093/emboj/18.20.5714;
RA Nakagawa T., Ogawa H.;
RT "The Saccharomyces cerevisiae MER3 gene, encoding a novel helicase-like
RT protein, is required for crossover control in meiosis.";
RL EMBO J. 18:5714-5723(1999).
RN [6]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLY-166.
RX PubMed=11376001; DOI=10.1074/jbc.m104003200;
RA Nakagawa T., Flores-Rozas H., Kolodner R.D.;
RT "The mer3 helicase involved in meiotic crossing over is stimulated by
RT single-stranded DNA-binding proteins and unwinds DNA in the 3' to 5'
RT direction.";
RL J. Biol. Chem. 276:31487-31493(2001).
CC -!- FUNCTION: DNA-dependent ATPase. Required in the control of double
CC strand breaks transition and crossover during meiosis. Unwinds DNA in
CC the 3' TO 5' direction. Prefers single-stranded DNA.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA93159.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA64136.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA96971.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X94357; CAA64136.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z72773; CAA96971.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U22156; AAA93159.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006941; DAA07868.1; -; Genomic_DNA.
DR RefSeq; NP_011263.2; NM_001181117.1.
DR AlphaFoldDB; P51979; -.
DR SMR; P51979; -.
DR BioGRID; 33028; 46.
DR DIP; DIP-2604N; -.
DR IntAct; P51979; 3.
DR MINT; P51979; -.
DR STRING; 4932.YGL251C; -.
DR PaxDb; 4932-YGL251C; -.
DR PeptideAtlas; P51979; -.
DR EnsemblFungi; YGL251C_mRNA; YGL251C; YGL251C.
DR GeneID; 852641; -.
DR KEGG; sce:YGL251C; -.
DR AGR; SGD:S000003220; -.
DR SGD; S000003220; HFM1.
DR VEuPathDB; FungiDB:YGL251C; -.
DR eggNOG; KOG0952; Eukaryota.
DR GeneTree; ENSGT00940000176293; -.
DR HOGENOM; CLU_000335_0_1_1; -.
DR InParanoid; P51979; -.
DR OMA; VYGYQSH; -.
DR OrthoDB; 57056at2759; -.
DR BioCyc; YEAST:G3O-30721-MONOMER; -.
DR BRENDA; 3.6.4.12; 984.
DR BioGRID-ORCS; 852641; 1 hit in 10 CRISPR screens.
DR PRO; PR:P51979; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P51979; Protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IDA:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR CDD; cd18023; DEXHc_HFM1; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02889; Sec63; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1187
FT /note="ATP-dependent DNA helicase MER3"
FT /id="PRO_0000102090"
FT DOMAIN 148..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 360..542
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 616..922
FT /note="SEC63"
FT ZN_FING 1039..1054
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 268..271
FT /note="DEIH box"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 166
FT /note="G->D: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11376001"
FT CONFLICT 552
FT /note="T -> TAA (in Ref. 4; AAA93159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1187 AA; 135072 MW; 6B804F1E3D12A5B9 CRC64;
MKTKFDRLGT GKRSRPSPNN IDFNDQSATF KRNKKNSRQP SFKVGLSYNS LLDDCDDENE
TEEIFEGRGL QFFDKDDNFS ITADDTQVTS KLFDHDLEQT PDEEAKKPKK VTIRKSAKKC
LSTTILPDSF RGVFKFTEFN KMQSEAFPSI YESNENCIIS SPTGSGKTVL FELAILRLIK
ETNSDTNNTK IIYIAPTKSL CYEMYKNWFP SFVNLSVGML TSDTSFLETE KAKKCNIIIT
TPEKWDLLTR RWSDYSRLFE LVKLVLVDEI HTIKEKRGAS LEVILTRMNT MCQNIRFVAL
SATVPNIEDL ALWLKTNNEL PANILSFDES YRQVQLTKFV YGYSFNCKND FQKDAIYNSK
LIEIIEKHAD NRPVLIFCPT RASTISTAKF LLNNHIFSKS KKRCNHNPSD KILNECMQQG
IAFHHAGISL EDRTAVEKEF LAGSINILCS TSTLAVGVNL PAYLVIIKGT KSWNSSEIQE
YSDLDVLQMI GRAGRPQFET HGCAVIMTDS KMKQTYENLI HGTDVLESSL HLNLIEHLAA
ETSLETVYSI ETAVNWLRNT FFYVRFGKNP AAYQEVNRYV SFHSVEDSQI NQFCQYLLDT
LVKVKIIDIS NGEYKSTAYG NAMTRHYISF ESMKQFINAK KFLSLQGILN LLATSEEFSV
MRVRHNEKKL FKEINLSPLL KYPFLTEKKQ SQIIDRVSQK VSLLIQYELG GLEFPSYEGA
SKLHQTLVQD KFLVFRHCFR LLKCMVDTFI EKSDGTSLKN TLFLLRSLNG HCWENTPMVL
RQLKTIGLVS VRRLIRHGIT NLEEMGHLSD TQIEYYLNLK IGNGIKIKND ISLLPCLNIR
TKLENCKIEN EELWLTFKVE ISATFKSSIW HGQHLSLDIE TEKSSGELID FRRLQVNKLQ
SPRGFRISAK ISPKLEKIEF SIHCQEIAGL GKTIVYSTDH LASQFSAKTP NIRKDLNSLE
KCLFYESSSD GEVGKTSRVS HKDGLEESLS SDDSILDYLN ERKKSSKAVE SAAVIHPEAH
SSSHFSNGRQ VRSNGNYECF HSCKDKTQCR HLCCKEGIPV KYIKEKGPSS IKPVSKPDQI
RQPLLAKNIN TTPHLEKRLN SKPKQWQEEN TDIATVHTLP SKIYNLSQQM SSMEAGEQVL
KSGPENCPEI IPIDLESSDS YSSNTAASSI SDPNGDLDFL GSDIEFE
//
