ID M0JJK3_9EURY Unreviewed; 330 AA.
AC M0JJK3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01470};
GN Name=cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
GN Synonyms=cas1b {ECO:0000313|EMBL:QUJ73981.1};
GN ORFNames=C436_20688 {ECO:0000313|EMBL:EMA08154.1}, KDQ40_18595
GN {ECO:0000313|EMBL:QUJ73981.1};
OS Haloarcula sinaiiensis ATCC 33800.
OG Plasmid pHsi540 {ECO:0000313|EMBL:QUJ73981.1,
OG ECO:0000313|Proteomes:UP000682967}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA08154.1, ECO:0000313|Proteomes:UP000011659};
RN [1] {ECO:0000313|EMBL:EMA08154.1, ECO:0000313|Proteomes:UP000011659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA08154.1,
RC ECO:0000313|Proteomes:UP000011659};
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 [2] {ECO:0000313|EMBL:QUJ73981.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ73981.1};
RC PLASMID=pHsi540 {ECO:0000313|EMBL:QUJ73981.1};
RA Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT Haloarcula sinaiiensis.";
RL Submitted (APR-2021) 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 spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as
CC a dsDNA endonuclease. Involved in the integration of spacer DNA into
CC the CRISPR cassette. {ECO:0000256|HAMAP-Rule:MF_01470}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC {ECO:0000256|HAMAP-Rule:MF_01470}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000256|HAMAP-Rule:MF_01470}.
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DR EMBL; AOLR01000061; EMA08154.1; -; Genomic_DNA.
DR EMBL; CP073368; QUJ73981.1; -; Genomic_DNA.
DR RefSeq; WP_004966758.1; NZ_CP073368.1.
DR AlphaFoldDB; M0JJK3; -.
DR GeneID; 64825009; -.
DR KEGG; hsin:KDQ40_18595; -.
DR PATRIC; fig|662476.7.peg.4119; -.
DR OrthoDB; 2216at2157; -.
DR Proteomes; UP000011659; Unassembled WGS sequence.
DR Proteomes; UP000682967; Plasmid pHsi540.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004520; F:DNA endonuclease 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 Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR Gene3D; 3.100.10.20; CRISPR-associated endonuclease Cas1, N-terminal domain; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR019858; CRISPR-assoc_Cas1_HMARI/TNEAP.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR NCBIfam; TIGR00287; cas1; 1.
DR NCBIfam; TIGR03641; cas1_HMARI; 1.
DR PANTHER; PTHR43219; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR PANTHER; PTHR43219:SF2; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR Pfam; PF01867; Cas_Cas1; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01470};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01470};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_01470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01470};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01470};
KW Plasmid {ECO:0000313|EMBL:QUJ73981.1}.
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 222
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ SEQUENCE 330 AA; 38054 MW; 118D7F14E77E122F CRC64;
MTKPNHHIFA DGELSRSEST LRIDTLEGDT EYLPVESVDS LYLHGQIDFN TRTLGLLNEH
GVPLHIFGWK DYYKGSYLPK RGQVSGNTVV EQVRAYDDRR RLNIGQKMIR ASIHNMRRNL
VYYDGRRGDF SDAIASLDEF KDETADTDDI NQLRAVEGNA RSTYYDCFDQ ILRDPFELSK
REYNPPTNEA NALVSFLNGM VYTTSVSAIR KTALDPTIGF VHEPGERRFT LSLDIADIFK
PILADRLIFR LVNRQQLSLS DFESELEGCL LTESGRMTVL EAFEETLDKT IEHPRLERKV
SFKTLVQTDV YSLKKHILTG ESYHPTERWW
//
