HELS_THEKO
ID HELS_THEKO Reviewed; 1125 AA.
AC Q5JGV6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Contains:
DE RecName: Full=Endonuclease PI-PkoHel;
DE EC=3.1.-.-;
DE AltName: Full=Pko Hel intein;
GN Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; OrderedLocusNames=TK1332;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=21178304; DOI=10.1266/ggs.85.243;
RA Fujikane R., Ishino S., Ishino Y., Forterre P.;
RT "Genetic analysis of DNA repair in the hyperthermophilic archaeon,
RT Thermococcus kodakaraensis.";
RL Genes Genet. Syst. 85:243-257(2010).
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}.
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:0000255|HAMAP-Rule:MF_00442}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Not essential, it can be disrupted. Slightly more
CC sensitive to UV and mitomycin C than wild-type cells.
CC {ECO:0000269|PubMed:21178304}.
CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00442}.
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DR EMBL; AP006878; BAD85521.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5JGV6; -.
DR SMR; Q5JGV6; -.
DR STRING; 69014.TK1332; -.
DR EnsemblBacteria; BAD85521; BAD85521; TK1332.
DR KEGG; tko:TK1332; -.
DR PATRIC; fig|69014.16.peg.1304; -.
DR eggNOG; arCOG00553; Archaea.
DR eggNOG; arCOG03145; Archaea.
DR HOGENOM; CLU_279743_0_0_2; -.
DR InParanoid; Q5JGV6; -.
DR PhylomeDB; Q5JGV6; -.
DR Proteomes; UP000000536; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_00442; Helicase_Hel308; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR022965; Helicase_Hel308.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00305; HintC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; DNA damage; DNA repair; DNA-binding;
KW Endonuclease; Helicase; Hydrolase; Intron homing; Nuclease;
KW Nucleotide-binding; Protein splicing; Reference proteome.
FT CHAIN 1..331
FT /note="ATP-dependent DNA helicase Hel308, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013302"
FT CHAIN 332..734
FT /note="Endonuclease PI-PkoHel"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013303"
FT CHAIN 735..1125
FT /note="ATP-dependent DNA helicase Hel308, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000013304"
FT DOMAIN 33..197
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT DOMAIN 226..440
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT DOMAIN 500..640
FT /note="DOD-type homing endonuclease"
FT MOTIF 1..29
FT /note="Q motif"
FT MOTIF 145..148
FT /note="DEAH box"
FT BINDING 28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
SQ SEQUENCE 1125 AA; 129202 MW; 1208EEC7AD1045FE CRC64;
MKVDELPIDE RIKRVIKERG IEELYPPQAE ALKSGVLEGK NLVLAIPTAS GKTLVSEIVM
VNKLLSEGGK AVYLVPLKAL AEEKYREFKE WEVLGLRVAA TTGDYDSTDE WLGRYDIIVA
TAEKFDSLLR HGASWIKDVK LVVADEVHLI GSYDRGATLE MILTHMLGKA QILALSATVG
NAEELAEWLD ASLVVSDWRP VELRKGVFHL GQLFWEDGKI DHYPENWESL VLDAVKKGKQ
ALVFVNTRRS AEKEAISLSS KVSKLLTKPE TRRLEELISS IEDNPTTEKL KRALKGGVAF
HHAGLSRAER TLIEDAFRNG LIKVITATPT LCMHPDTYVV TKSGAKKVSE LTEGDEVLTH
TGTFKKVIQP LRREHKGRLL VIKAYGTVPV KITPEHMVWV VKQIRHKSHY SDGRQVIWWE
FEGPEWMTAQ ELKERLESET DPKVSYMLLQ PIPEPSVDAD KIPLRKEVYV VNQHGKTDKL
HPSVKRTPEY LPLNFETARL IGLWIAEGST SKNGVIKFDI SSNEEDLTEF ITGTIRKYFP
HAKIVVKDHE RNRRTVRFCN KRFAEWLREN IGHGADNKSI PPLLLLNKNR EVRLGLLRGL
IEGDGYVRRE SQRRANYISY STVSPSLAYQ LQLLVASLGY TSSIHRSIRT EGIGKTRKPI
YDVKVSGKSY YSLLEELGFE VPQRGNRTYN VNRTWKNYLL LKVRSIEEEE YEGDVYNLEV
EGDESYSVGF IVHNSAGINL PAFRVIIRDT KRYANFGWTD IPVLEIQQMM GRAGRPKYDK
VGEAIIVART EDPKKLIDRY IHGKPEKLFS MLANEQAFRS QVLALITNFG VEDFRELVDF
LSRTFYAHQR GDTSSLEYKA KDIVYFLIEN EFIDMDVENR FIALPFGRRT SQLYIDPLTA
KKFKDAFPAI ERNPNPFGIF QLLASTPDMA TLTARRREME DYLDLAYEME EHLYSSIPYY
EDSRFQGFLG QVKTAKVLLD WINEVPEARI YETYNIDPGD LYRILELADW LMYSLIELYK
LFEPKEDVLQ YLRDLHLRLR HGVREELLEL VKLPNIGRRR ARALYNAGFR SVEDILRAKP
KDLLQVEGIG LKIIEGIYRH LGVEYTISEK EKPKKRKGNL YDFLK
