CAS2_HALVD
ID CAS2_HALVD Reviewed; 86 AA.
AC D4GQP1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=CRISPR-associated endoribonuclease Cas2 {ECO:0000255|HAMAP-Rule:MF_01471};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01471};
GN Name=cas2 {ECO:0000255|HAMAP-Rule:MF_01471}; OrderedLocusNames=HVO_A0212;
GN ORFNames=C498_09741 {ECO:0000312|EMBL:ELY32099.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70 / H26;
RX PubMed=22767603; DOI=10.1074/jbc.m112.377002;
RA Fischer S., Maier L.K., Stoll B., Brendel J., Fischer E., Pfeiffer F.,
RA Dyall-Smith M., Marchfelder A.;
RT "An archaeal immune system can detect multiple protospacer adjacent motifs
RT (PAMs) to target invader DNA.";
RL J. Biol. Chem. 287:33351-33363(2012).
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. Plasmid targeted by
CC CRISPR locus P1 transform wild-type cells very poorly
CC (PubMed:22767603). {ECO:0000255|HAMAP-Rule:MF_01471,
CC ECO:0000269|PubMed:22767603}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01471};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC {ECO:0000255|HAMAP-Rule:MF_01471}.
CC -!- DISRUPTION PHENOTYPE: Loss of the 8 Cas genes in this locus (cas1,
CC cas2, cas3, cas4, cas5, cas6, cas7 and cas8b) leads to loss of CRISPR
CC interference against plasmid targeted by this CRISPR locus, i.e.
CC plasmid is not destroyed by CRISPR. {ECO:0000269|PubMed:22767603}.
CC -!- MISCELLANEOUS: There are 3 CRISPR RNA loci in this organism and a
CC single cas gene locus. A CRISPR-Cas type I-B system.
CC {ECO:0000303|PubMed:20333302, ECO:0000303|PubMed:22767603}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC protein family. {ECO:0000255|HAMAP-Rule:MF_01471}.
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DR EMBL; CP001955; ADE02207.1; -; Genomic_DNA.
DR EMBL; AOHU01000052; ELY32099.1; -; Genomic_DNA.
DR RefSeq; WP_004043133.1; NZ_AOHU01000052.1.
DR AlphaFoldDB; D4GQP1; -.
DR SMR; D4GQP1; -.
DR STRING; 309800.C498_09741; -.
DR EnsemblBacteria; ADE02207; ADE02207; HVO_A0212.
DR EnsemblBacteria; ELY32099; ELY32099; C498_09741.
DR GeneID; 8923341; -.
DR KEGG; hvo:HVO_A0212; -.
DR PATRIC; fig|309800.29.peg.1902; -.
DR eggNOG; arCOG04194; Archaea.
DR HOGENOM; CLU_161124_0_0_2; -.
DR OMA; KRTRIYR; -.
DR OrthoDB; 118787at2157; -.
DR Proteomes; UP000008243; Plasmid pHV4.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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 Pfam; PF09827; CRISPR_Cas2; 1.
DR TIGRFAMs; TIGR01573; cas2; 1.
PE 3: Inferred from homology;
KW Antiviral defense; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Plasmid; Reference proteome.
FT CHAIN 1..86
FT /note="CRISPR-associated endoribonuclease Cas2"
FT /id="PRO_0000432149"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01471"
SQ SEQUENCE 86 AA; 9978 MW; 1BBF57944CFFA09E CRC64;
MQVIVVYDVP AKRTRIYRKL LRRRLEHLQY SVFFGELTAG QVTAMKNEIE SELEPTDSIV
VFEFDNPHAF DHTTFGDADE PGSRFT
