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Database: UniProt
Entry: A9A9R8_METM6
LinkDB: A9A9R8_METM6
Original site: A9A9R8_METM6 
ID   A9A9R8_METM6            Unreviewed;       751 AA.
AC   A9A9R8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=ERCC4 domain protein {ECO:0000313|EMBL:ABX02091.1};
GN   OrderedLocusNames=MmarC6_1278 {ECO:0000313|EMBL:ABX02091.1};
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158 {ECO:0000313|EMBL:ABX02091.1};
RN   [1] {ECO:0000313|EMBL:ABX02091.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 {ECO:0000313|EMBL:ABX02091.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000867; ABX02091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A9R8; -.
DR   STRING; 444158.MmarC6_1278; -.
DR   KEGG; mmx:MmarC6_1278; -.
DR   eggNOG; arCOG00872; Archaea.
DR   HOGENOM; CLU_002513_3_1_2; -.
DR   OrthoDB; 9764at2157; -.
DR   PhylomeDB; A9A9R8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd12089; Hef_ID; 1.
DR   CDD; cd20075; XPF_nuclease_XPF_arch; 1.
DR   Gene3D; 3.40.50.10130; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 1.20.1320.20; hef helicase domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR041755; Hef_ID.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR010994; RuvA_2-like.
DR   PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR   Pfam; PF02732; ERCC4; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF21210; RNA_helicase_helical; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          22..186
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          337..504
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          521..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          479..509
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        523..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  85603 MW;  2742EAD60638C90D CRC64;
     MHVNHPLIKP ESIEARIYQQ LVVASALKQN TLCVLGTGLG KTAIAALTIA GILSKQDGKV
     LIIAPSRPLV DQHFKSMNQF LNIDSEKIVI LNGKISPKKR EAMWESGKIF IATPQVAEND
     IISKMLKPSQ FSLLIADEAH HTTGNHSYTF VANKFKKKSH VLGLTASPGS NIERIIEICG
     NLGIEHVEIK TEEDPDVAPY VAKVKMRPKR VELPEEFEIN LTLLKNALKD RLRDLKENRV
     IHTINVNKSE LLGLNKKIMT MDDNIKYEML RISSEAVKLE HAIEMLETQG RSTFLNYYQK
     LLTQNTKSAK EITNDPRFIQ VVKNLNELDI EHPKYEKMLE ILKEILKENE KIIIFAQYRD
     TVQKIVDLLS ENGIEAIMFV GQSNKDGKGM SQTEQAKAIE RFKSDVNVLV STSVSEEGID
     ISGVNYVLFY EPVPSEIRMI QRRGRAARGE GGQVIVLIAE KTRDEGYYRA GLAKEKNMKN
     ILKNMQTSLN KKLKELTEER EEVEKTENKD HYMDLRSVVG SKTSVKSEEK KPTKLDKKSK
     SGAPNKATII LDSRERHIGR YLSEKAEVEF KTLEIGDYIL SDRVAVERKT AEDFENSIID
     KRLFNQVMDL KKYERPLMII EGNEFVRIHE NAIRGMMFSI MIDYQIPIMF SRDIEDTADI
     LVKLAEREQI KEKREISIRY GKRPMSLKER QKFLVEGLPD VGPVMAENLL DNFNSVENIF
     TASEEELKSV DGVGPITAKK IKEVVTKKYR E
//
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