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Database: UniProt
Entry: D7DSV7_METV3
LinkDB: D7DSV7_METV3
Original site: D7DSV7_METV3 
ID   D7DSV7_METV3            Unreviewed;       321 AA.
AC   D7DSV7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   OrderedLocusNames=Mvol_0558 {ECO:0000313|EMBL:ADI36217.1};
OS   Methanococcus voltae (strain ATCC BAA-1334 / A3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36217.1, ECO:0000313|Proteomes:UP000007722};
RN   [1] {ECO:0000313|EMBL:ADI36217.1, ECO:0000313|Proteomes:UP000007722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanococcus voltae A3.";
RL   Submitted (MAY-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 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; CP002057; ADI36217.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7DSV7; -.
DR   STRING; 456320.Mvol_0558; -.
DR   KEGG; mvo:Mvol_0558; -.
DR   eggNOG; arCOG01452; Archaea.
DR   HOGENOM; CLU_052779_2_0_2; -.
DR   InParanoid; D7DSV7; -.
DR   OrthoDB; 2216at2157; -.
DR   Proteomes; UP000007722; Chromosome.
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   CDD; cd09722; Cas1_I-B; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000007722}.
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         213
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         228
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   321 AA;  38413 MW;  033E02F4923F0132 CRC64;
     MKYNKYLNSE GKLYRKENTV YFMDTKGKKT PIPVEKIYAL YCYKEVSFTS SVVILLAKYN
     IPIHYFGRYG NYVGTFYPKG ENYSGKVIVQ QSENYLNSDK RHYIAKEFVK GSILNISKNL
     SRYKLDYDKE KYITALQKVN RITDIMNVEA LMRNDYYNNF DNIFKNFKYE KRSRRPPENE
     INALISFGNS LLYSTVISEI FNTHLNPSVS YLHEPYERRY SLALDIADVF KPIFVDRLIF
     NLVNKKIINE NHFEKDLNSC LLNDEGRAIF LSKYNERLQK TIKHRKLNRN VSYQRLLRLE
     CYKLEKHIMG IEQYEPFVIW W
//
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