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Database: UniProt
Entry: L0L3C3_METHD
LinkDB: L0L3C3_METHD
Original site: L0L3C3_METHD 
ID   L0L3C3_METHD            Unreviewed;       752 AA.
AC   L0L3C3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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   OrderedLocusNames=Metho_2674 {ECO:0000313|EMBL:AGB50804.1};
OS   Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1).
OG   Plasmid pMETHO01 {ECO:0000313|EMBL:AGB50804.1,
OG   ECO:0000313|Proteomes:UP000010866}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanomethylovorans.
OX   NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB50804.1, ECO:0000313|Proteomes:UP000010866};
RN   [1] {ECO:0000313|Proteomes:UP000010866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15978 / NBRC 107637 / DMS1
RC   {ECO:0000313|Proteomes:UP000010866};
RC   PLASMID=Plasmid pMETHO01 {ECO:0000313|Proteomes:UP000010866};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of plasmid of Methanomethylovorans hollandica DSM
RT   15978.";
RL   Submitted (FEB-2012) 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; CP003363; AGB50804.1; -; Genomic_DNA.
DR   RefSeq; WP_015313936.1; NC_019972.1.
DR   AlphaFoldDB; L0L3C3; -.
DR   GeneID; 14401636; -.
DR   KEGG; mhz:Metho_2674; -.
DR   HOGENOM; CLU_006553_3_0_2; -.
DR   OrthoDB; 371946at2157; -.
DR   Proteomes; UP000010866; Plasmid pMETHO01.
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:0004386; F:helicase activity; 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; -; 1.
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; 1.
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}; Plasmid {ECO:0000313|EMBL:AGB50804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010866}.
FT   DOMAIN          38..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          289..448
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00442"
SQ   SEQUENCE   752 AA;  84309 MW;  68C40AA8B527DFC4 CRC64;
     MNESPCYIKS LPLPEKIQQF YIDSGIKQLY PPQGEVVQKG LLEGKNTLAA IPTASGKTLL
     AELAMLKHII DGGKALYIVP LIALANEKYQ RFKEFEKFGI LTGISTGELE SKSEGLGKND
     IVVCTSEKTD SMLRNGTQWL QTLSIVVVDE VHLLDEKSRG PTLEIVMTKL RKIPNLQIVA
     LSATIGNTQV LADWLKAELT VSDWRPTKLQ EGVVFGKSMN FLSEDPVIQK EIVHDTKEPA
     ADVALDTIKE GGQCLVFESS RRTCMAFAKR FSNPKNREHK QINILLSQDE KNKLAEISEE
     IEYSSDTTES NNLAECIRNG VAFHHAGLNA AQRRLVEDGF KENKIKVISC TPTLAAGLNL
     PARRVVIRSF LRYDANEGNI PIPVLDYKQM VGRAGRPHLD PYGQSLLIAK SSDKIDFLET
     KYIHAKAEDI SSKLGSEKAL RSHILAIISS GIATSQKGVI DFLSETFYAH TSDLSYFIET
     INECLYFLEE NDLIVTDNNY LQATPLGQLV SRIYIDPLTA VVIVEDLKKA SQSNMEITAF
     SLLQVICKTP DIRTLYLKGN EYFENLIYAD DHKNEIINFP DLDEISEISA ESFIESIKNA
     RILLDWIEEC ETKEIVENYV IGEGDLHSLS ESASWISHAV QRISKLKGFD IQNIFLEQRL
     KYGASKELVS LLSIKNIGRK RARKLYDNGI GSVDKIKSTP FSEVSKLFGN KITIKIFHEL
     ELPIPSDEID TSPEVPENNK KEINQQKNLF DF
//
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