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CAS4_HALVD
ID   CAS4_HALVD              Reviewed;         183 AA.
AC   D4GQN9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=CRISPR-associated exonuclease Cas4;
DE            EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9};
GN   Name=cas4; OrderedLocusNames=HVO_A0210;
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   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 may be a 5' to 3' ssDNA exonuclease. Plasmid targeted by CRISPR
CC       locus P1 transform wild-type cells very poorly (PubMed:22767603).
CC       {ECO:0000250|UniProtKB:Q97TX9, ECO:0000269|PubMed:22767603}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC         nucleoside 3'-phosphates.; EC=3.1.12.1;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Note=Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also
CC       utilise Cu(2+). {ECO:0000250|UniProtKB:Q97TX9};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:Q97TX9};
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. {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: Belongs to the CRISPR-associated exonuclease Cas4 family.
CC       {ECO:0000305}.
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DR   EMBL; CP001955; ADE02138.1; -; Genomic_DNA.
DR   RefSeq; WP_013035187.1; NZ_AOHU01000052.1.
DR   AlphaFoldDB; D4GQN9; -.
DR   SMR; D4GQN9; -.
DR   STRING; 309800.C498_09726; -.
DR   PRIDE; D4GQN9; -.
DR   EnsemblBacteria; ADE02138; ADE02138; HVO_A0210.
DR   GeneID; 8923865; -.
DR   KEGG; hvo:HVO_A0210; -.
DR   eggNOG; arCOG00794; Archaea.
DR   HOGENOM; CLU_133784_0_0_2; -.
DR   OMA; CKRELWF; -.
DR   OrthoDB; 115986at2157; -.
DR   Proteomes; UP000008243; Plasmid pHV4.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.320.10; -; 1.
DR   InterPro; IPR013343; CRISPR-assoc_prot_Cas4.
DR   InterPro; IPR022765; Dna2/Cas4_DUF83.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   Pfam; PF01930; Cas_Cas4; 1.
DR   TIGRFAMs; TIGR00372; cas4; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Antiviral defense; Exonuclease; Hydrolase; Iron; Iron-sulfur;
KW   Manganese; Metal-binding; Nuclease; Plasmid; Reference proteome.
FT   CHAIN           1..183
FT                   /note="CRISPR-associated exonuclease Cas4"
FT                   /id="PRO_0000432151"
FT   BINDING         36
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         83
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         92
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         172
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         175
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT   BINDING         181
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ   SEQUENCE   183 AA;  21152 MW;  C950B4602A5DC16B CRC64;
     MSSTDVVEEY VQDERDPSRS PNVPITGLMV QYYHVCKREL WFMANGIDID RETTNIQRGT
     HVDETSYGTS RRSFMIDNRI QLDILDSGDV MEVKVSSALE KPARMQLLFY LWYLREIHDI
     DKDGVLAYPT ERKRESVVLD ETTTAEVEST VRGVLDVVGR DSPPQLEKKP YCGTCLYQDL
     CWM
 
 
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