位置:首页 > 蛋白库 > HERA_METJA
HERA_METJA
ID   HERA_METJA              Reviewed;         503 AA.
AC   Q58824;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable DNA double-strand break repair helicase HerA {ECO:0000250|UniProtKB:F2Z5Z6};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:F2Z5Z6};
GN   Name=herA {ECO:0000250|UniProtKB:F2Z5Z6};
GN   OrderedLocusNames=MJ1429 {ECO:0000312|EMBL:AAB99439.1};
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Involved in DNA double-strand break (DSB) repair (By
CC       similarity). Acts probably with NurA to stimulate resection of the 5'
CC       strand and produce the long 3' single-strand that is required for RadA
CC       loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA
CC       helicase activity (By similarity). {ECO:0000250|UniProtKB:F2Z5Z6,
CC       ECO:0000250|UniProtKB:Q8U1P0}.
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:0000250|UniProtKB:F2Z5Z6};
CC   -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}.
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; L77117; AAB99439.1; -; Genomic_DNA.
DR   PIR; D64478; D64478.
DR   AlphaFoldDB; Q58824; -.
DR   SMR; Q58824; -.
DR   STRING; 243232.MJ_1429; -.
DR   EnsemblBacteria; AAB99439; AAB99439; MJ_1429.
DR   KEGG; mja:MJ_1429; -.
DR   eggNOG; arCOG00280; Archaea.
DR   HOGENOM; CLU_023842_2_0_2; -.
DR   InParanoid; Q58824; -.
DR   OMA; EPNDQRY; -.
DR   PhylomeDB; Q58824; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR008571; HerA-like.
DR   InterPro; IPR018538; HerA_barrel_dom.
DR   InterPro; IPR033186; HerA_C.
DR   InterPro; IPR002789; HerA_central.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42957; PTHR42957; 2.
DR   Pfam; PF05872; DUF853; 1.
DR   Pfam; PF01935; DUF87; 1.
DR   Pfam; PF09378; HAS-barrel; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..503
FT                   /note="Probable DNA double-strand break repair helicase
FT                   HerA"
FT                   /id="PRO_0000107323"
FT   BINDING         122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT   BINDING         131..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97WG8"
FT   BINDING         478..479
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97WG8"
SQ   SEQUENCE   503 AA;  56697 MW;  BBDADC0E52849657 CRC64;
     MYVMKVVGKT TTTHFTFESL EKIRFGEYVI AKNVDGRDVL GVIKNVVADV EKFVGEVKVI
     GVLDGNKIIP NRTPILPNSE VRLCDDEILN NIYLTPDGLN IGHLLTRDNV RVYLDTNKLV
     SRHFAILSIT GGGKSNTASV LCRELAKKNG TVIMIDPHGE YISLYHEDME GKIKVINPII
     NPVLLAPSEF ANLIGIGDNE IEKRVYVEFA YHTVKHECPD AKGIEFIEKI ENLLYEWSKI
     ASVGWEIKYY NPLRRNYDRR KLEKEDFVIL MSLIDTISKF KLDYALNIGD RDVIEEFEIG
     KINIVNLSGL EIPQMVTFVG FIAKHLLLKR ITYLKSLKDV YSINEEIRRV AQSNLNIIES
     HYKVVTKPVL LIVEEAHIFI PVNEQNSASL WLGKIAREGR KFGVGLGLVS QRPKQLHPDV
     LSQTNTKIIL KIVEPEDQKY IQRASEELGE DLVKDLASLG IGEAVIVGAA ISLPSIVKID
     KFDGVYGGKD INIVGEWMGL DDW
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024