CAS4_METJA
ID CAS4_METJA Reviewed; 170 AA.
AC Q57822;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=CRISPR-associated exonuclease Cas4;
DE EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9};
GN Name=cas4; OrderedLocusNames=MJ0377;
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: 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.
CC {ECO:0000250|UniProtKB:Q97TX9}.
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. It may be important for
CC protein stability, since mutation of the Cys that bind the cofactor
CC leads to a colorless, insoluble protein.
CC {ECO:0000250|UniProtKB:Q97TX9};
CC -!- SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98366.1; -; Genomic_DNA.
DR PIR; A64347; A64347.
DR RefSeq; WP_010869876.1; NC_000909.1.
DR AlphaFoldDB; Q57822; -.
DR SMR; Q57822; -.
DR STRING; 243232.MJ_0377; -.
DR EnsemblBacteria; AAB98366; AAB98366; MJ_0377.
DR GeneID; 1451234; -.
DR KEGG; mja:MJ_0377; -.
DR eggNOG; arCOG00794; Archaea.
DR HOGENOM; CLU_133784_0_0_2; -.
DR InParanoid; Q57822; -.
DR OMA; ICKTKLW; -.
DR OrthoDB; 115986at2157; -.
DR PhylomeDB; Q57822; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
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; Reference proteome.
FT CHAIN 1..170
FT /note="CRISPR-associated exonuclease Cas4"
FT /id="PRO_0000106840"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 49
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 68
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 159
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 168
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ SEQUENCE 170 AA; 20420 MW; 10CEBC592550AA4B CRC64;
MENYLEEELI IGGIEINYLY VCKTKLWYFV RGITMEQESD FVDLGKFLHE KSYFGEEKEV
QIGSIKIDFI KKRDVIEIHE VKRGKQMEKA HIMQVLYYIY YLNSLGIKSK AILHYPKLKE
IKEIELKENN KEEIKRAIKE IEYIKSLKEP PEPIYQKICK NCAYYELCFI
