HELS_ARCFU
ID HELS_ARCFU Reviewed; 691 AA.
AC P0DMI1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=ATP-dependent DNA helicase Hel308 {ECO:0000255|HAMAP-Rule:MF_00442};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00442};
GN Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; OrderedLocusNames=AF_2245;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN APO FORM AND IN COMPLEX WITH DNA,
RP FUNCTION AS A HELICASE, FUNCTION AS AN ATPASE, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF GLU-146.
RX PubMed=17558417; DOI=10.1038/nsmb1246;
RA Buttner K., Nehring S., Hopfner K.P.;
RT "Structural basis for DNA duplex separation by a superfamily-2 helicase.";
RL Nat. Struct. Mol. Biol. 14:647-652(2007).
CC -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be
CC involved in repair of stalled replication forks. {ECO:0000255|HAMAP-
CC Rule:MF_00442, ECO:0000269|PubMed:17558417}.
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:0000255|HAMAP-Rule:MF_00442};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:17558417}.
CC -!- DOMAIN: The N-terminal region (1-400) has DNA-dependent ATPase activity
CC but no helicase activity. {ECO:0000269|PubMed:17558417}.
CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00442}.
CC -!- CAUTION: This open reading frame is annotated as an authentic
CC frameshift in the genome. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AE000782; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE000782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 2P6R; X-ray; 3.00 A; A=1-691.
DR PDB; 2P6U; X-ray; 3.14 A; A=1-691.
DR PDBsum; 2P6R; -.
DR PDBsum; 2P6U; -.
DR AlphaFoldDB; P0DMI1; -.
DR SMR; P0DMI1; -.
DR PRIDE; P0DMI1; -.
DR BRENDA; 3.6.4.12; 414.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00442; Helicase_Hel308; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022965; Helicase_Hel308.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..691
FT /note="ATP-dependent DNA helicase Hel308"
FT /id="PRO_0000429029"
FT DOMAIN 34..200
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT DOMAIN 230..421
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT REGION 400..691
FT /note="Required for helicase but not ATPase activity"
FT MOTIF 145..148
FT /note="DEAH box"
FT BINDING 30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT MUTAGEN 146
FT /note="E->Q: Loss of DNA-stimulated ATP hydrolysis, almost
FT complete loss of DNA unwinding."
FT /evidence="ECO:0000269|PubMed:17558417"
SQ SEQUENCE 691 AA; 77835 MW; 2E5B2D3E69D6A38E CRC64;
MKVEELAESI SSYAVGILKE EGIEELFPPQ AEAVEKVFSG KNLLLAMPTA AGKTLLAEMA
MVREAIKGGK SLYVVPLRAL AGEKYESFKK WEKIGLRIGI STGDYESRDE HLGDCDIIVT
TSEKADSLIR NRASWIKAVS CLVVDEIHLL DSEKRGATLE ILVTKMRRMN KALRVIGLSA
TAPNVTEIAE WLDADYYVSD WRPVPLVEGV LCEGTLELFD GAFSTSRRVK FEELVEECVA
ENGGVLVFES TRRGAEKTAV KLSAITAKYV ENEGLEKAIL EENEGEMSRK LAECVRKGAA
FHHAGLLNGQ RRVVEDAFRR GNIKVVVATP TLAAGVNLPA RRVIVRSLYR FDGYSKRIKV
SEYKQMAGRA GRPGMDERGE AIIIVGKRDR EIAVKRYIFG EPERITSKLG VETHLRFHSL
SIICDGYAKT LEELEDFFAD TFFFKQNEIS LSYELERVVR QLENWGMVVE DHHLAPTKLG
SLVSRLYIDP LTGFIFHDVL SRMELSDIGA LHLICRTPDM ERLTVRKTDS WVEEEAFRLR
KELSYYPSDF SVEYDWFLSE VKTALCLKDW IEEKDEDEIC AKYGIAPGDL RRIVETAEWL
SNAMNRIAEE VGNTSVSGLT ERIKHGVKEE LLELVRIRHI GRVRARKLYN AGIRNAEDIV
RHREKVASLI GRGIAERVVE GISVKSLNPE S
