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Database: UniProt
Entry: J4W956_9FIRM
LinkDB: J4W956_9FIRM
Original site: J4W956_9FIRM 
ID   J4W956_9FIRM            Unreviewed;       330 AA.
AC   J4W956;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ECO:0000313|EMBL:EJU22271.1};
GN   ORFNames=HMPREF1152_1399 {ECO:0000313|EMBL:EJU22271.1};
OS   Mogibacterium sp. CM50.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis; Mogibacterium.
OX   NCBI_TaxID=936375 {ECO:0000313|EMBL:EJU22271.1, ECO:0000313|Proteomes:UP000003142};
RN   [1] {ECO:0000313|EMBL:EJU22271.1, ECO:0000313|Proteomes:UP000003142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM50 {ECO:0000313|EMBL:EJU22271.1,
RC   ECO:0000313|Proteomes:UP000003142};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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}.
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:EJU22271.1}.
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DR   EMBL; ALNL01000019; EJU22271.1; -; Genomic_DNA.
DR   RefSeq; WP_009643621.1; NZ_ALNL01000019.1.
DR   AlphaFoldDB; J4W956; -.
DR   STRING; 936375.HMPREF1152_1399; -.
DR   PATRIC; fig|936375.3.peg.609; -.
DR   eggNOG; COG1518; Bacteria.
DR   OrthoDB; 9803119at2; -.
DR   Proteomes; UP000003142; Unassembled WGS sequence.
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:SF1; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 2; 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:UP000003142}.
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;  39224 MW;  B1D6B36FA31CEA14 CRC64;
     MNRNYYIFKS GTLQRKDNSI RVVTEDKIKK DIPCETVSDL YVFGEINLNT KLLNFLAQKE
     ILLHVFNYYG FYSGSFSPRD KNVSGFLLVK QVGHYSEYEK RLMLAKKFID AASYNIYRNV
     RYYNGRGVNL EGVLKEIALL REKLNRTNSI EELMGIEGNI RKKYYESWND IIKQNVNFTK
     RIKHPPENMI NTLLSFANSL VYTTALAEIY KTQLNPTVSY LHEPGVARFS LSLDIAEIFK
     PLIAERMIFS LLNKNMISED DFEKESNYLY LKESARKIIV EEYDKRLQRT IKHKELNRDV
     SYRYLFRLEC YKLIKHLTEE KEYEGFKIWW
//
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