CAS4_RHORT
ID CAS4_RHORT Reviewed; 333 AA.
AC Q2RRV2;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=CRISPR-associated exonuclease Cas4;
DE EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9};
GN Name=cas4; OrderedLocusNames=Rru_A2343;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(2011).
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 may be a 5' to 3' ssDNA exonuclease (By similarity).
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; CP000230; ABC23143.1; -; Genomic_DNA.
DR RefSeq; WP_011390096.1; NC_007643.1.
DR RefSeq; YP_427430.1; NC_007643.1.
DR AlphaFoldDB; Q2RRV2; -.
DR SMR; Q2RRV2; -.
DR STRING; 269796.Rru_A2343; -.
DR EnsemblBacteria; ABC23143; ABC23143; Rru_A2343.
DR KEGG; rru:Rru_A2343; -.
DR PATRIC; fig|269796.9.peg.2445; -.
DR eggNOG; COG1468; Bacteria.
DR HOGENOM; CLU_833874_0_0_5; -.
DR OrthoDB; 1594787at2; -.
DR PhylomeDB; Q2RRV2; -.
DR Proteomes; UP000001929; 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..333
FT /note="CRISPR-associated exonuclease Cas4"
FT /id="PRO_0000417891"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 70
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 212
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ SEQUENCE 333 AA; 35537 MW; 3C8A9642488FCD57 CRC64;
MAPSDTPPSA EDLPSQGELA LFAPPATAED ALVPASMVNA WIYCPRLAVL EWGRGEKARS
VDLIAGLRAH QATESGPTPA LPDPMVLRED QSLKTRKLSL SSERLGLTAE LDLLDVEEGV
VIPVEIKVGK RPSVDEGAYL PERAQVCAQA LLLREAGYTC LEGALWFAES RERVTVDLTE
ALVTATLVAT SDLRLTVASG RLPPPLDHSA KCPRCSLLPI CLPDEIAWFR KGSIARTPPP
PASPALPLYG QTPGARIGKK DRGGSVCLDR MAAWLSSRPV PCYAAIGMLN TASGASHPSV
ARHADGGASA RSFRLPTAFR RPVRRSLPCY AAR
