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Database: UniProt
Entry: D3AEF2_9CLOT
LinkDB: D3AEF2_9CLOT
Original site: D3AEF2_9CLOT 
ID   D3AEF2_9CLOT            Unreviewed;       189 AA.
AC   D3AEF2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=CRISPR-associated endoribonuclease Cas2 {ECO:0000256|HAMAP-Rule:MF_01471};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01471};
GN   Name=cas2 {ECO:0000256|HAMAP-Rule:MF_01471};
GN   ORFNames=CLOSTHATH_01983 {ECO:0000313|EMBL:EFC99803.1};
OS   Hungatella hathewayi DSM 13479.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC99803.1, ECO:0000313|Proteomes:UP000004968};
RN   [1] {ECO:0000313|EMBL:EFC99803.1, ECO:0000313|Proteomes:UP000004968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC99803.1,
RC   ECO:0000313|Proteomes:UP000004968};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01471}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_01471};
CC   -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer.
CC       {ECO:0000256|HAMAP-Rule:MF_01471}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC       protein family. {ECO:0000256|ARBA:ARBA00009959, ECO:0000256|HAMAP-
CC       Rule:MF_01471}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFC99803.1}.
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DR   EMBL; ACIO01000150; EFC99803.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3AEF2; -.
DR   HOGENOM; CLU_1432763_0_0_9; -.
DR   Proteomes; UP000004968; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
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   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR   HAMAP; MF_01471; Cas2; 1.
DR   InterPro; IPR002729; CRISPR-assoc_Cas1.
DR   InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR   InterPro; IPR021127; CRISPR_associated_Cas2.
DR   InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR   NCBIfam; TIGR01573; cas2; 1.
DR   PANTHER; PTHR34405; CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS2; 1.
DR   PANTHER; PTHR34405:SF3; CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS2 3; 1.
DR   Pfam; PF01867; Cas_Cas1; 1.
DR   Pfam; PF09827; CRISPR_Cas2; 1.
DR   SUPFAM; SSF143430; TTP0101/SSO1404-like; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW   Rule:MF_01471}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01471};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01471};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01471};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01471};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01471}.
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01471"
SQ   SEQUENCE   189 AA;  21866 MW;  0CA43B6383ED271A CRC64;
     MADRFVLTLI NKQIISGDAF SVKENGAVIM DDETRKLFLS QWQMKKQETI THPFLNEKIE
     WGMVPYVQSM LLARYIRGDL DEYPSFLWKQ VLMMLVLITY DVNTETAAGR SRLRRVAKQC
     VNYGQRVQNS VFESNMDAAK CRAVKGILEG IIDKNVDSLR FYYLSDNYKH KVEHIGAKPG
     FDVTEPLIF
//
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