ID C7GNZ7_YEAS2 Unreviewed; 1188 AA.
AC C7GNZ7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=HFM1 {ECO:0000313|EMBL:EEU07470.1};
GN ORFNames=C1Q_01988 {ECO:0000313|EMBL:EEU07470.1};
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961 {ECO:0000313|EMBL:EEU07470.1, ECO:0000313|Proteomes:UP000008073};
RN [1] {ECO:0000313|EMBL:EEU07470.1, ECO:0000313|Proteomes:UP000008073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291 {ECO:0000313|EMBL:EEU07470.1,
RC ECO:0000313|Proteomes:UP000008073};
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.,
RA Missawa S.K., Galzerani F., Costa G.G., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
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 Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEU07470.1}.
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DR EMBL; ACFL01000079; EEU07470.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GNZ7; -.
DR Proteomes; UP000008073; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 149..323
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 361..543
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 135159 MW; 04EFAD63D6B34D33 CRC64;
MKTKFDRLGT GKRSRPSPNS NIDFNDQSAT FKRNKKNSRQ PSFKVGLSYN SLLDDCDDEN
ETEEIFEGRG LQFFDKDDNF SITADDTQVT SKLFDHDLEQ TPDEEAKKPK KVTIRKSAKK
CLSTTILPDS FRGVFKFTEF NKMQSEAFPS IYESNENCII SSPTGSGKTV LFELAILRLI
KETNSDTNNT KIIYIAPTKS LCYDMYKNWF PSFVNLSVGM LTSDTSFLET EKAKKCNIII
TTPEKWDLLT RRWSDYSRLF ELVKLVLVDE IHTIKEKRGA SLEVILTRMN TMCQNIRFVA
LSATVPNIED LALWLKTNNE LPANILSFDE SYRQVQLTKF VYGYSFNCKN DFQKDAIYNS
KLIEIIEKHA DNRPVLIFCP TRASTISTAK FLLNNHIFSK SKKRCNHNPS DKILNECMQQ
GIAFHHAGIS LEDRTAVEKE FLAGSINILC STSTLAVGVN LPAYLVIIKG TKSWNSSEIQ
EYSDLDVLQM IGRAGRPQFE THGCAVIMTD SKMKQTYENL IHGTDVLESS LHLNLIEHLA
AETSLETVYS IETAVNWLRN TFFYVRFGKN PAAYQEVNRY VSFHSVEDSQ INQFCQYLLD
TLVKVKIIDI SNGEYKSTAY GNAMTRHYIS FESMKQFINA KKFLSLQGIL NLLATSEEFS
VMRVRHNEKK LFKEINLSPL LKYPFLTEKK QSQIIDRVSQ KVSLLIQYEL GGLEFPSYEG
ASKLHQTLVQ DKFLVFRHCF RLLKCMVDTF IEKSDGTSLK NTLFLLRSLN GHCWENTPMV
LRQLKTIGLV SVRRLIRHGI TNLEEMGHLS DTQIEYYLNL KIGNGIKIKN DISLLPCLNI
RTKLENCKIE NEELWLTFKV EISATFKSSI WHGQHLSLDI ETEKSSGELI DFRRLQLNKL
QSPRGFRISA KISPKLEKIE FSIHCQEIAG LGKTIVYSTD HLASQFSAKT PNIRKDLNSL
EKCLFYESSS DGEVGKTSRV SHKDGLEESL SSDDSILDYL NERKKSSKAV ESAAVIHPEA
HSSSHFSNGR QVRSNGNYEC FHSCKDKTQC RHLCCKEGIP VKYIKEKGPS SIKPVSKPDQ
IRQPLLAKNI NTTPHLEKRL NSKPKQWQEE NTDIATVHTL PSKIYNLSQQ MSSMEAGEQV
LKSGPENCPE IIPIDLESSD SYSSNTAASS ISDPNGDLDF LGSDIEFE
//
