ID   CAS2_DESVH              Reviewed;         102 AA.
AC   Q72WF4;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=CRISPR-associated endoribonuclease Cas2;
DE            EC=3.1.-.-;
GN   Name=cas2; OrderedLocusNames=DVUA0135;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OG   Plasmid pDV.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), AND SUBUNIT.
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=21139194; DOI=10.1107/s1744309110039801;
RA   Samai P., Smith P., Shuman S.;
RT   "Structure of a CRISPR-associated protein Cas2 from Desulfovibrio
RT   vulgaris.";
RL   Acta Crystallogr. F 66:1552-1556(2010).
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).
CC       Functions as a ssRNA-specific endoribonuclease. Involved in the
CC       integration of spacer DNA into the CRISPR cassette (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Forms a heterotetramer with a Cas1 homodimer (By similarity).
CC       Homodimer. {ECO:0000250, ECO:0000269|PubMed:21139194}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC       protein family. {ECO:0000305}.
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DR   EMBL; AE017286; AAS94461.1; -; Genomic_DNA.
DR   RefSeq; YP_009175.1; NC_005863.1.
DR   PDB; 3OQ2; X-ray; 1.35 A; A/B=1-102.
DR   PDBsum; 3OQ2; -.
DR   AlphaFoldDB; Q72WF4; -.
DR   SMR; Q72WF4; -.
DR   EnsemblBacteria; AAS94461; AAS94461; DVUA0135.
DR   KEGG; dvu:DVUA0135; -.
DR   PATRIC; fig|882.5.peg.3225; -.
DR   HOGENOM; CLU_161124_3_1_7; -.
DR   OMA; SVFECEV; -.
DR   PhylomeDB; Q72WF4; -.
DR   EvolutionaryTrace; Q72WF4; -.
DR   Proteomes; UP000002194; Plasmid pDV.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
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   CDD; cd09725; Cas2_I_II_III; 1.
DR   HAMAP; MF_01471; Cas2; 1.
DR   InterPro; IPR021127; CRISPR_associated_Cas2.
DR   InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR   PANTHER; PTHR34405; PTHR34405; 1.
DR   Pfam; PF09827; CRISPR_Cas2; 1.
DR   PIRSF; PIRSF032582; Cas2; 1.
DR   TIGRFAMs; TIGR01573; cas2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Plasmid; Reference proteome.
FT   CHAIN           1..102
FT                   /note="CRISPR-associated endoribonuclease Cas2"
FT                   /id="PRO_0000416943"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   STRAND          7..14
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   HELIX           20..33
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   HELIX           51..64
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   TURN            67..69
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:3OQ2"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:3OQ2"
SQ   SEQUENCE   102 AA;  11843 MW;  321FBD021277DDAE CRC64;
     MYGNDAMLVL ISYDVSFEDP GGQRRLRRIA KACQDYGQRV QYSVFECVVD PAQWAKLKHR
     LLSEMDKEKD CLRFYYLGAN WRNKVEHVGA KPAYDPEGPL IL