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Database: UniProt
Entry: F4G3H7_METCR
LinkDB: F4G3H7_METCR
Original site: F4G3H7_METCR 
ID   F4G3H7_METCR            Unreviewed;       492 AA.
AC   F4G3H7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   OrderedLocusNames=Mcup_1242 {ECO:0000313|EMBL:AEB95347.1};
OS   Metallosphaera cuprina (strain Ar-4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=1006006 {ECO:0000313|EMBL:AEB95347.1, ECO:0000313|Proteomes:UP000007812};
RN   [1] {ECO:0000313|EMBL:AEB95347.1, ECO:0000313|Proteomes:UP000007812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar-4 {ECO:0000313|EMBL:AEB95347.1,
RC   ECO:0000313|Proteomes:UP000007812};
RX   PubMed=21551305; DOI=10.1128/JB.05038-11;
RA   Liu L.J., You X.Y., Zheng H., Wang S., Jiang C.Y., Liu S.J.;
RT   "Complete genome sequence of Metallosphaera cuprina, a metal sulfide-
RT   oxidizing archaeon from a hot spring.";
RL   J. Bacteriol. 193:3387-3388(2011).
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:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the HerA family.
CC       {ECO:0000256|ARBA:ARBA00007816}.
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DR   EMBL; CP002656; AEB95347.1; -; Genomic_DNA.
DR   RefSeq; WP_013737845.1; NC_015435.1.
DR   AlphaFoldDB; F4G3H7; -.
DR   STRING; 1006006.Mcup_1242; -.
DR   GeneID; 10493433; -.
DR   KEGG; mcn:Mcup_1242; -.
DR   PATRIC; fig|1006006.8.peg.1238; -.
DR   eggNOG; arCOG00280; Archaea.
DR   HOGENOM; CLU_023842_2_0_2; -.
DR   OrthoDB; 107033at2157; -.
DR   Proteomes; UP000007812; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR018538; HerA_barrel_dom.
DR   InterPro; IPR033186; HerA_C.
DR   InterPro; IPR002789; HerA_central.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF040937; HerA_Thermprot; 1.
DR   PANTHER; PTHR42957; HELICASE MJ1565-RELATED; 1.
DR   PANTHER; PTHR42957:SF1; HELICASE MJ1565-RELATED; 1.
DR   Pfam; PF01935; DUF87; 1.
DR   Pfam; PF09378; HAS-barrel; 1.
DR   Pfam; PF05872; HerA_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          3..73
FT                   /note="Helicase HerA barrel"
FT                   /evidence="ECO:0000259|Pfam:PF09378"
FT   DOMAIN          119..332
FT                   /note="Helicase HerA central"
FT                   /evidence="ECO:0000259|Pfam:PF01935"
FT   DOMAIN          351..447
FT                   /note="Helicase HerA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05872"
SQ   SEQUENCE   492 AA;  54694 MW;  9CB4AC66EAB92C27 CRC64;
     MIIGYVIGEA SPQEALMLAE KPVRVGRYVV LEYDGIKVLG LITYVSRGSP LLDITLNDIK
     IVQKMKDLDT SIPQFVKAVI KLLYDMRSKS IPDLPPGPGT PVRLAEEEEL LEIFSEGDIV
     IGSLIGVNIP VKIKVNSLSR HLAILAATGS GKSNTVAVLS QAIASIGGSV VVFDYHGEYY
     GSDIKPLNNI DPKLNPLYLT PKEFATLLDI RSNAHIQYRF LRQAFTTYVN EIRERMKDGN
     VNYAELNNSF VSDIEKKVDE IAADEKQRSQ KDAADEVKNK IEEFADKYGD IVDLTVSDIV
     SRLRPSSVNV VDISRMDEES MDAVVSHYLR RILDSRKEYK HRKTGLGFPV VTVIEEAHVF
     ISKNDDTLTK YYVSKISREG RKFGVSMVIV SQRPKGLDDT ILSQMTNKII LRMVEPTDKK
     YVLEASDNLT EDLVEQLSSL GVGEAIVIGN LVKLPAFIKI SKFAGNLGGS DPDILGEWNK
     FMKSINVDSE FG
//
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