ID   HELS_METAC              Reviewed;         730 AA.
AC   Q8TL39;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=MA_3203;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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   -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00442}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE010299; AAM06574.1; -; Genomic_DNA.
DR   RefSeq; WP_011023138.1; NC_003552.1.
DR   AlphaFoldDB; Q8TL39; -.
DR   SMR; Q8TL39; -.
DR   STRING; 188937.MA_3203; -.
DR   EnsemblBacteria; AAM06574; AAM06574; MA_3203.
DR   GeneID; 1475096; -.
DR   KEGG; mac:MA_3203; -.
DR   HOGENOM; CLU_006553_3_0_2; -.
DR   InParanoid; Q8TL39; -.
DR   OMA; MFLNANI; -.
DR   OrthoDB; 9752at2157; -.
DR   PhylomeDB; Q8TL39; -.
DR   Proteomes; UP000002487; 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   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..730
FT                   /note="ATP-dependent DNA helicase Hel308"
FT                   /id="PRO_0000102106"
FT   DOMAIN          33..199
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   DOMAIN          232..433
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00442"
FT   REGION          707..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           144..147
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   730 AA;  80958 MW;  CB557279E92BD889 CRC64;
     MKIESLDLPD EVKRFYENSG IPELYPPQAE AVEKGLLEGK NLLAAIPTAS GKTLLAELAM
     LKSVLAGGKA LYIVPLRALA SEKFRRFQDF SELGIRVGIS TGDYDRRDEG LGINDIIVAT
     SEKTDSLLRN ETAWMQEISV VVVDEVHLID SADRGPTLEV TLAKLRKMNP FCQILALSAT
     VGNADELAAW LDAELVLSEW RPTDLMEGVF FDGTFFCKDK EKLIEQPTKD EAINLVLDTL
     REGGQCLVFE SSRKNCMGFA KKATSAVKKT LSAEDKEKLA GIADEILENS ETDTASVLAS
     CVRAGTAFHH AGLTSPLREL VETGFREGYV KLISSTPTLA AGLNLPARRV IIRSYRRYSS
     DSGMQPIPVL EYKQMAGRAG RPRLDPYGEA VLLAKSYEEL LFLFEKYIEA GAEDIWSKLG
     TENALRTHVL STISNGFART KEELMDFLEA TFFAYQYSNF GLSVVVDECL NFLRQEGMLE
     QDSDALISTM FGKLVSRLYI DPLSAALIAK GLREAGTLTE LTLLHLVCST PDMRLMYMRS
     QDYQDINDFV MAHAEEFSKV PSPFNIVEYE WFLSEVKTSL LLMDWIHEKP ENEICLKFGT
     GEGDIHTTAD IAEWIMHVAT QLARLLDLKG AKEAAELEKR IHYGAGPELM DLLDIRGIGR
     VRARKLYGAG FKSTADLAGA TPEKVAALVG PKIAERIFRQ IGRREAVSEI SDSERLEKSS
     QDGQSTISDF