ID A0A1H1ERJ9_9EURY Unreviewed; 836 AA.
AC A0A1H1ERJ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ATP-dependent DNA helicase Hel308 {ECO:0000256|HAMAP-Rule:MF_00442};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_00442};
GN Name=hel308 {ECO:0000256|HAMAP-Rule:MF_00442};
GN ORFNames=DWB78_08960 {ECO:0000313|EMBL:RDI71842.1}, SAMN05216278_3008
GN {ECO:0000313|EMBL:SDQ90746.1};
OS Halopelagius longus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1236180 {ECO:0000313|EMBL:SDQ90746.1, ECO:0000313|Proteomes:UP000199289};
RN [1] {ECO:0000313|EMBL:SDQ90746.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|EMBL:SDQ90746.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000199289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|Proteomes:UP000199289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDI71842.1, ECO:0000313|Proteomes:UP000255421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC12-B1 {ECO:0000313|EMBL:RDI71842.1,
RC ECO:0000313|Proteomes:UP000255421};
RA Zhang X.;
RT "Genome sequence of extremly halophilic archaeon Halopelagius longus strain
RT BC12-B1.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be
CC involved in repair of stalled replication forks. {ECO:0000256|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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_00442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617, ECO:0000256|HAMAP-
CC Rule:MF_00442};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00442}.
CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00442}.
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DR EMBL; QQST01000001; RDI71842.1; -; Genomic_DNA.
DR EMBL; FNKQ01000003; SDQ90746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1ERJ9; -.
DR OrthoDB; 371946at2157; -.
DR Proteomes; UP000199289; Unassembled WGS sequence.
DR Proteomes; UP000255421; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd18028; DEXHc_archSki2; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00442; Helicase_Hel308; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR048772; Hel308-like_dom4.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022965; Helicase_Hel308.
DR InterPro; IPR046931; HTH_61.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961:SF10; ATP-DEPENDENT DNA HELICASE HEL308; 1.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21280; Helicase_dom4_arc; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF20470; HTH_61; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00442};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00442};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00442};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00442};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00442};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00442};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00442}.
FT DOMAIN 34..200
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 242..444
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 540..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..590
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..836
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00442"
SQ SEQUENCE 836 AA; 91370 MW; 88C16A11A3B3C56F CRC64;
MKTADLAGLP PGVPEHLRDE GIEELYPPQA EAVEAGVTAG ESLVASVPTA SGKTLVAELA
MLSAVERGGK ALYIVPLRAL ASEKKAEFER WEEYGIDVGV STGNYDSSGE WLASQDIIVA
TSEKVDSLVR NNAPWVDDLS CVVADEVHLV DDSHRGPTLE VTLGKLRKIN PGLQVVALSA
TVGNPEDIAE WLDAELVESE WRPIDLKMGV HYGNAITFDD GSQREVRVGK GDRQTPALVA
DILDDDGDGE DDDGGGSSLV FVNSRRNAEA SAKRLADVTE KRLTSEERGE LAEIAQEIRD
VSDTETSDTL ANCVAKGAAF HHAGLAADHR SLVEDAFRER LIKVISATPT LAAGVNTPSR
RVIVRDWQRY DGDFGGMKPL DVLEVHQMMG RAGRPGLDPY GEAVLLAKNA DTRDELFERY
IWADAEPVRS KLAAEPALRT HLLATVASGF AHTREGLLEF LDQTLYATQT DEPGRLERVT
DNVLDYLEAN GFVERDGDGV TATSVGHTVS RLYLDPMSAA EIIDGLRWAS DHREEKLREL
EGEADGSARE NRADAEVDAD AGFQRASEMV PEEGTDADGD GGGDAESDDD VEFETDRTYP
TALGLFHLVC RTPDMYQLYL KSGDREEYTE LCYEREPELL GNTPSEYEDV RFEEWLSALK
TARLLEDWAD EVDEDRITER YGVGPGDIRG KVETAEWLLG AAEQLAGEID ASATVPVREA
KMRVQYGVRD ELIDLAGIRG VGRKRARRLF EAGIQTRADL READKSVVLA ALRGRRKTAE
NVLEAAGRKD PSMDDVREAD AEDLPEATFE TAKDRREDGD GEADDPEEQA SLGDFG
//
