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CAS3_HALVD
ID   CAS3_HALVD              Reviewed;         937 AA.
AC   D4GQN8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=CRISPR-associated nuclease/helicase Cas3 {ECO:0000303|PubMed:22767603};
DE            EC=3.1.-.-;
DE            EC=3.6.4.-;
GN   Name=cas3; OrderedLocusNames=HVO_A0209; ORFNames=C498_09721;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DS70 / H26;
RX   PubMed=22767603; DOI=10.1074/jbc.m112.377002;
RA   Fischer S., Maier L.K., Stoll B., Brendel J., Fischer E., Pfeiffer F.,
RA   Dyall-Smith M., Marchfelder A.;
RT   "An archaeal immune system can detect multiple protospacer adjacent motifs
RT   (PAMs) to target invader DNA.";
RL   J. Biol. Chem. 287:33351-33363(2012).
CC   -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC       repeat), is an adaptive immune system that provides protection against
CC       mobile genetic elements (viruses, transposable elements and conjugative
CC       plasmids). CRISPR clusters contain sequences complementary to
CC       antecedent mobile elements and target invading nucleic acids. CRISPR
CC       clusters are transcribed and processed into CRISPR RNA (crRNA). This
CC       protein plus Cascade participate in CRISPR interference, the third
CC       stage of CRISPR immunity (By similarity). Plasmid targeted by CRISPR
CC       locus P1 transform wild-type cells very poorly (PubMed:22767603).
CC       {ECO:0000250|UniProtKB:P38036, ECO:0000269|PubMed:22767603}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q53VY2};
CC   -!- DISRUPTION PHENOTYPE: Loss of the 8 Cas genes in this locus (cas1,
CC       cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR
CC       interference against plasmid targeted by this CRISPR locus, i.e.
CC       plasmid is not destroyed by CRISPR. Disruption of this single gene also
CC       leads to loss of CRISPR interference. {ECO:0000269|PubMed:22767603}.
CC   -!- MISCELLANEOUS: There are 3 CRISPR RNA loci in this organism and a
CC       single cas gene locus. A CRISPR-Cas type I-B system.
CC       {ECO:0000303|PubMed:20333302, ECO:0000303|PubMed:22767603}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC       nuclease Cas3-HD family. {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC       helicase Cas3 family. {ECO:0000305}.
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DR   EMBL; CP001955; ADE02249.1; -; Genomic_DNA.
DR   EMBL; AOHU01000052; ELY32095.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GQN8; -.
DR   STRING; 309800.C498_09721; -.
DR   EnsemblBacteria; ADE02249; ADE02249; HVO_A0209.
DR   EnsemblBacteria; ELY32095; ELY32095; C498_09721.
DR   KEGG; hvo:HVO_A0209; -.
DR   PATRIC; fig|309800.29.peg.1899; -.
DR   eggNOG; arCOG01445; Archaea.
DR   HOGENOM; CLU_010123_1_1_2; -.
DR   OMA; EGWNSEI; -.
DR   Proteomes; UP000008243; Plasmid pHV4.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3210.30; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR035011; Cas3.
DR   InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR   InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24031:SF539; PTHR24031:SF539; 2.
DR   Pfam; PF18019; HD_6; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01596; cas3_HD; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
PE   3: Inferred from homology;
KW   Antiviral defense; ATP-binding; Helicase; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Nucleotide-binding; Plasmid; Reference proteome.
FT   CHAIN           1..937
FT                   /note="CRISPR-associated nuclease/helicase Cas3"
FT                   /id="PRO_0000432150"
FT   DOMAIN          24..232
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53VY2"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q53VY2"
SQ   SEQUENCE   937 AA;  103679 MW;  6281AB8C2C38D003 CRC64;
     MTYPLISHPE ANDGERTYPD EQLTDDGSLR LTAHNTVVSE YATRLFRGPE TQRRFLCVAA
     SLHDFGKATP QFQAYVRDEY EGPEKEKNHA RLGALATWFV LDQRDAPARD KLAATLAVAR
     HHQALPDAAQ YTAESLADAF ETSNSVLTAQ LEAISERWPQ KATELLQRSG ETDSTWDEFR
     TWVQSGTVVG ELHEVSARRE LTGPKATSDK LPRKLYDRTL HYWAAITLAD KSHAMAVPES
     HVFDVETLDR ETLEEYISGL RAEPPDDELE RALNDERERA RRQAIDGVHE WLGGDAQTPP
     IATLTLPTGL GKTFTGLSAA FEARGILESD GGPTRPIVYA LPYTSIIEQT RSIFERPELW
     GADPTKSALT VHHYLSETVV YRNERESEDV ASTDQEEHAS FLGEAWRDGT VLTTFVQLFE
     SLVGPSNRQG LKLSALDDGL VILDEPQALP KEWWDGITRL IELLTTEYQT RVIAMTATQP
     TLLRDVETTS LLDVGREHDK TGCLRCEVGP DYPVRLEPAR KETYFENAER VRYRIDESAL
     SFHLSADERY LSHETAAARV VAATAAGEGG STLAICNTIN SSATLTQELC GHDGVTHLGE
     AIDSVLGAND VDATKQENNV SAIVDAILRR SGLRGVDGEL SVPAGTDIVV ATLNSRYRPF
     DRRLLIEIAD TLSGSEIPFV LISTQAIEAG VDLSFKRVFR DIAPLDSIVQ AGGRCNRSYE
     WGRNGGQVVV WTLADPDEEN PGDPTKSPPA HWVYERGSSD AGIQTHLQLI SSILAQFEDE
     EVPDAEISHH AVNEYFDALR EKSLSSTKIR TLIDDAKAGK LARESLIGGY QTVDVLVATT
     QAERKRLNEL TELFTSDDPT DRSTGYKKLE QAAGIRVSLP LNSIEQLPDV SRVDGKERNE
     DGVQVFRYTG TESLEYDLQT GGLRGKEDTV AGRFTTF
 
 
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