HELS_PYRFU
ID HELS_PYRFU Reviewed; 720 AA.
AC O73946;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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};
DE AltName: Full=ATP-dependent Holliday junction unwindase Hjm;
DE AltName: Full=Holliday junction migration DNA helicase;
GN Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; Synonyms=hjm;
GN OrderedLocusNames=PF0677;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RA Kanai A., Oida H., Yabe T., Hihara S., Doi H.;
RT "Pfu helicase locus.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP IDENTIFICATION, FUNCTION, ATP-DEPENDENCE, COFACTOR, SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=15677450; DOI=10.1074/jbc.m413417200;
RA Fujikane R., Komori K., Shinagawa H., Ishino Y.;
RT "Identification of a novel helicase activity unwinding branched DNAs from
RT the hyperthermophilic archaeon, Pyrococcus furiosus.";
RL J. Biol. Chem. 280:12351-12358(2005).
RN [4]
RP FUNCTION AS AN ATPASE, FUNCTION AS A HELICASE, INTERACTION WITH PCNA,
RP SUBUNIT, DNA-BINDING, AND MUTAGENESIS OF LYS-52; ASP-145; GLU-146 AND
RP 701-LYS--SER-720.
RX PubMed=16436047; DOI=10.1111/j.1365-2443.2006.00925.x;
RA Fujikane R., Shinagawa H., Ishino Y.;
RT "The archaeal Hjm helicase has recQ-like functions, and may be involved in
RT repair of stalled replication fork.";
RL Genes Cells 11:99-110(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) WITH AND WITHOUT ATP.
RX PubMed=19159486; DOI=10.1186/1472-6807-9-2;
RA Oyama T., Oka H., Mayanagi K., Shirai T., Matoba K., Fujikane R.,
RA Ishino Y., Morikawa K.;
RT "Atomic structures and functional implications of the archaeal RecQ-like
RT helicase Hjm.";
RL BMC Struct. Biol. 9:2-2(2009).
CC -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be
CC involved in repair of stalled replication forks. Unwinds the lagging
CC strand from forked DNA structures in a 3'-5' direction. PCNA, the DNA
CC polymerase sliding clamp subunit, stimulates the helicase activity, and
CC may alter substrate specificity. Unwinds branched DNA (Holliday
CC junctions) in an ATP-dependent fashion; ss- and dsDNA stimulate ATPase
CC to the greatest extent, although it preferentially binds DNA with a
CC single-stranded region. Processes a RecA-mediated recombination
CC intermediate between gapped circular and homologous linear dsDNA.
CC {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15677450,
CC ECO:0000269|PubMed:16436047}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15677450};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15677450};
CC Note=Divalent cations, Mg(2+) and Zn(2+) are best.
CC {ECO:0000269|PubMed:15677450};
CC -!- SUBUNIT: Monomer. Interacts with PCNA. {ECO:0000255|HAMAP-
CC Rule:MF_00442, ECO:0000269|PubMed:15677450,
CC ECO:0000269|PubMed:16436047}.
CC -!- INDUCTION: Constitutively expressed (at protein level).
CC {ECO:0000269|PubMed:15677450}.
CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00442}.
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DR EMBL; AB016521; BAA32016.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80801.1; -; Genomic_DNA.
DR PIR; T43854; T43854.
DR RefSeq; WP_011011799.1; NC_018092.1.
DR PDB; 2ZJ2; X-ray; 2.40 A; A=1-720.
DR PDB; 2ZJ5; X-ray; 2.40 A; A=1-720.
DR PDB; 2ZJ8; X-ray; 2.00 A; A=1-720.
DR PDB; 2ZJA; X-ray; 2.70 A; A=1-720.
DR PDBsum; 2ZJ2; -.
DR PDBsum; 2ZJ5; -.
DR PDBsum; 2ZJ8; -.
DR PDBsum; 2ZJA; -.
DR AlphaFoldDB; O73946; -.
DR SMR; O73946; -.
DR STRING; 186497.PF0677; -.
DR PRIDE; O73946; -.
DR EnsemblBacteria; AAL80801; AAL80801; PF0677.
DR GeneID; 41712480; -.
DR KEGG; pfu:PF0677; -.
DR PATRIC; fig|186497.12.peg.713; -.
DR eggNOG; arCOG00553; Archaea.
DR HOGENOM; CLU_006553_3_0_2; -.
DR OMA; MFLNANI; -.
DR OrthoDB; 9752at2157; -.
DR PhylomeDB; O73946; -.
DR BRENDA; 3.6.4.12; 5243.
DR EvolutionaryTrace; O73946; -.
DR Proteomes; UP000001013; 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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 SMART; SM00278; HhH1; 2.
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..720
FT /note="ATP-dependent DNA helicase Hel308"
FT /id="PRO_0000102110"
FT DOMAIN 33..197
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT DOMAIN 229..422
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT MOTIF 145..148
FT /note="DEAH box"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 52
FT /note="K->A: No ATPase activity."
FT /evidence="ECO:0000269|PubMed:16436047"
FT MUTAGEN 145
FT /note="D->A: No ATPase activity."
FT /evidence="ECO:0000269|PubMed:16436047"
FT MUTAGEN 146
FT /note="E->A: No ATPase activity."
FT /evidence="ECO:0000269|PubMed:16436047"
FT MUTAGEN 701..720
FT /note="Missing: No binding to PCNA."
FT /evidence="ECO:0000269|PubMed:16436047"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 247..261
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:2ZJA"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 411..424
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 450..465
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 493..508
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 512..520
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 535..545
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT TURN 554..557
FT /evidence="ECO:0007829|PDB:2ZJA"
FT HELIX 561..581
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 586..593
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 597..621
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 627..639
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 643..648
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:2ZJ2"
FT HELIX 656..663
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 670..674
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 678..682
FT /evidence="ECO:0007829|PDB:2ZJ8"
FT HELIX 689..699
FT /evidence="ECO:0007829|PDB:2ZJ8"
SQ SEQUENCE 720 AA; 82631 MW; BA17FCE53F615688 CRC64;
MRVDELRVDE RIKSTLKERG IESFYPPQAE ALKSGILEGK NALISIPTAS GKTLIAEIAM
VHRILTQGGK AVYIVPLKAL AEEKFQEFQD WEKIGLRVAM ATGDYDSKDE WLGKYDIIIA
TAEKFDSLLR HGSSWIKDVK ILVADEIHLI GSRDRGATLE VILAHMLGKA QIIGLSATIG
NPEELAEWLN AELIVSDWRP VKLRRGVFYQ GFVTWEDGSI DRFSSWEELV YDAIRKKKGA
LIFVNMRRKA ERVALELSKK VKSLLTKPEI RALNELADSL EENPTNEKLA KAIRGGVAFH
HAGLGRDERV LVEENFRKGI IKAVVATPTL SAGINTPAFR VIIRDIWRYS DFGMERIPII
EVHQMLGRAG RPKYDEVGEG IIVSTSDDPR EVMNHYIFGK PEKLFSQLSN ESNLRSQVLA
LIATFGYSTV EEILKFISNT FYAYQRKDTY SLEEKIRNIL YFLLENEFIE ISLEDKIRPL
SLGIRTAKLY IDPYTAKMFK DKMEEVVKDP NPIGIFHLIS LTPDITPFNY SKREFERLEE
EYYEFKDRLY FDDPYISGYD PYLERKFFRA FKTALVLLAW INEVPEGEIV EKYSVEPGDI
YRIVETAEWL VYSLKEIAKV LGAYEIVDYL ETLRVRVKYG IREELIPLMQ LPLVGRRRAR
ALYNSGFRSI EDISQARPEE LLKIEGIGVK TVEAIFKFLG KNVKISEKPR KSTLDYFLKS
