CS4F1_LEPIN
ID CS4F1_LEPIN Reviewed; 541 AA.
AC Q8F1F5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=LA_3181;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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; AE010300; AAN50379.2; -; Genomic_DNA.
DR RefSeq; NP_713361.2; NC_004342.2.
DR RefSeq; WP_002068643.1; NC_004342.2.
DR AlphaFoldDB; Q8F1F5; -.
DR SMR; Q8F1F5; -.
DR STRING; 189518.LA_3181; -.
DR EnsemblBacteria; AAN50379; AAN50379; LA_3181.
DR KEGG; lil:LA_3181; -.
DR PATRIC; fig|189518.3.peg.3158; -.
DR HOGENOM; CLU_466793_0_0_12; -.
DR InParanoid; Q8F1F5; -.
DR Proteomes; UP000001408; Chromosome I.
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:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
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; IPR023844; CRISPR-assoc_Cas1_MYXAN.
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; TIGR03983; cas1_MYXAN; 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..541
FT /note="CRISPR-associated exonuclease Cas4/endonuclease Cas1
FT fusion"
FT /id="PRO_0000417115"
FT REGION 1..179
FT /note="CRISPR-associated exonuclease Cas4"
FT REGION 204..541
FT /note="CRISPR-associated endonuclease Cas1"
FT BINDING 9
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
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"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 365
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 448
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
SQ SEQUENCE 541 AA; 61580 MW; 24D7EA1EF144CD52 CRC64;
MGIHSLLYCE RLFYLEEVEG ILVADDRVYA GRTLHEELEP NEDSSGRIES FHYTSEKLEV
SGKVDRIQKR DGDWIPYEHK RGRARIGTNG PEAWESDQCQ VTVYALLLEE ATGRNISEGK
IRYHGSKDLV KIEIDEELRS KALKTIDRAK GLSTSTNRPP VAQNENLCKN CSLAPVCLPE
ETRVITENEY EPIRLFPEKR EKTTLHVFGH DSRIKKSDNV LLVEKVTETG EKSKSEKIPI
QEIESVNIHG NCQISSQMIK FLVSEEIPVH WFSGGGNYIG GININPSGVQ RRIRQFKALT
KETIRLNLAK KLVSAKCESQ LRYLLRATRG KDETRNETES YLATIRSGLK NIESADSPSQ
LLGIEGSSAR AYFSGLPALL KNSDPFLVPN GRSKRPPKDP FNATLSFLYS LLYKSVRQAI
IAVGLDPSFG FYHTPRSSAE PLVLDLMELF RVSLCDMTLI GSINRKSWID EDFEITKNKV
WLSESGRKKA TQLYETRLDD TWKHPVVNYS LSYYRMIELE VRLLEKEWSG EANIFAQARL
R
