CS4F1_RHORT
ID CS4F1_RHORT Reviewed; 580 AA.
AC Q2RY11;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=CRISPR-associated exonuclease Cas4/endonuclease Cas1 fusion;
DE EC=3.1.-.-;
DE EC=3.1.12.1;
GN Name=cas4-cas1; OrderedLocusNames=Rru_A0179;
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 spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA) (By
CC similarity). The Cas4 region acts as a ssDNA exonuclease, while the
CC Cas1 region acts as a dsDNA endonuclease. Involved in the integration
CC of spacer DNA into the CRISPR cassette (By similarity). {ECO:0000250,
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC exonuclease Cas4 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the CRISPR-associated
CC endonuclease Cas1 family. {ECO:0000305}.
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DR EMBL; CP000230; ABC20984.1; -; Genomic_DNA.
DR RefSeq; WP_011387938.1; NC_007643.1.
DR RefSeq; YP_425271.1; NC_007643.1.
DR AlphaFoldDB; Q2RY11; -.
DR SMR; Q2RY11; -.
DR STRING; 269796.Rru_A0179; -.
DR EnsemblBacteria; ABC20984; ABC20984; Rru_A0179.
DR KEGG; rru:Rru_A0179; -.
DR PATRIC; fig|269796.9.peg.233; -.
DR eggNOG; COG1468; Bacteria.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_466793_0_0_5; -.
DR OMA; FAYCPRL; -.
DR OrthoDB; 464161at2; -.
DR PhylomeDB; Q2RY11; -.
DR Proteomes; UP000001929; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.920; -; 1.
DR Gene3D; 3.100.10.20; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR InterPro; IPR013343; CRISPR-assoc_prot_Cas4.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR Pfam; PF01867; Cas_Cas1; 1.
DR Pfam; PF01930; Cas_Cas4; 1.
DR TIGRFAMs; TIGR00287; cas1; 1.
DR TIGRFAMs; TIGR00372; cas4; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Antiviral defense; DNA-binding; Endonuclease; Exonuclease;
KW Hydrolase; Iron; Iron-sulfur; Magnesium; Manganese; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..580
FT /note="CRISPR-associated exonuclease Cas4/endonuclease Cas1
FT fusion"
FT /id="PRO_0000417116"
FT REGION 1..223
FT /note="CRISPR-associated exonuclease Cas4"
FT REGION 248..580
FT /note="CRISPR-associated endonuclease Cas1"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
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"
FT BINDING 401
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 472
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 487
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
SQ SEQUENCE 580 AA; 63240 MW; 735871744BE4D7D3 CRC64;
MAPSDTPPSA EDLPSQGELA LFAPPATAED ALVPASMVNA WIYCPRLAVL EWGRGEKARS
VDLIAGLRAH QATESGPTPA LPDPMVLRED QSLKTRRLSL SSERLGLTAE LDLLDVEEGM
VIPVEIKVGK RPSVDEGAYL PERAQVCAQA LLLREAGYTC LEGALWFAES RERVTVDLTE
ALVTATLVAT SDLRLTVASG RLPPPLDHSA KCPRCSLLPI CLPDEIAWFR KGSIARTPPP
PASPALPLYG QTPGARIGKK DYTLVIQVEG EADRSLALDE ISEVVLAGPV SLTTPAIHEL
LRREIPVAWM SSGFWFLGST GGQGPRSAAV RTAQYALAGD ERRRQAFARD LVSAKIRNGR
TLLRRNWRGA EAERQIALDR LARLAERATT AETTACLLGI EGEAAAVYFR AFPQLFTQAV
TTLPAFAFER RNRRPPADPV NACLSLCYAV LTRTLSSALS IAGLDPWKGF YHTERPGRPA
LALDLIESFR PVLADSTVLM VLNNGEIGTN DFLYAGGGCA LKPNARRGLI AAYERRLDQE
TTHPVFGYQL SMRRLIQVQA RLLARFVSGD IPRYPHYCPR
