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Database: UniProt
Entry: V5RI93_SPIAP
LinkDB: V5RI93_SPIAP
Original site: V5RI93_SPIAP 
ID   V5RI93_SPIAP            Unreviewed;       313 AA.
AC   V5RI93;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, 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   ECO:0000313|EMBL:AHB36274.1};
GN   ORFNames=SAPIS_v1c04280 {ECO:0000313|EMBL:AHB36274.1};
OS   Spiroplasma apis B31.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276258 {ECO:0000313|EMBL:AHB36274.1, ECO:0000313|Proteomes:UP000018550};
RN   [1] {ECO:0000313|EMBL:AHB36274.1, ECO:0000313|Proteomes:UP000018550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B31 {ECO:0000313|EMBL:AHB36274.1};
RX   PubMed=24407648;
RA   Ku C., Lo W.S., Chen L.L., Kuo C.H.;
RT   "Complete Genome Sequence of Spiroplasma apis B31T (ATCC 33834), a
RT   Bacterium Associated with May Disease of Honeybees (Apis mellifera).";
RL   Genome Announc. 2:e01151-13(2014).
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|ARBA:ARBA00038592, 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; CP006682; AHB36274.1; -; Genomic_DNA.
DR   RefSeq; WP_023789211.1; NC_022998.1.
DR   AlphaFoldDB; V5RI93; -.
DR   STRING; 1276258.SAPIS_v1c04280; -.
DR   KEGG; sapi:SAPIS_v1c04280; -.
DR   PATRIC; fig|1276258.3.peg.428; -.
DR   eggNOG; COG1518; Bacteria.
DR   HOGENOM; CLU_055263_1_0_14; -.
DR   OrthoDB; 9803119at2; -.
DR   Proteomes; UP000018550; 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   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; IPR042211; CRISPR-assoc_Cas1_N.
DR   InterPro; IPR019855; CRISPR-assoc_Cas1_NMENI.
DR   NCBIfam; TIGR03639; cas1_NMENI; 1.
DR   PANTHER; PTHR34353; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR   PANTHER; PTHR34353:SF2; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 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|ARBA:ARBA00023211, 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:UP000018550}.
FT   BINDING         153
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         209
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         224
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   313 AA;  36285 MW;  D007FB9942F29B83 CRC64;
     MSWKTIIINK YDKLSLKNNL LKIENTKQES DKSLTFSLSD INCVILENNY TLISTQLISK
     LLDNNVFLVV CNDSYEPNGI MLSYHNHWKP LAIIEKQISI NSEYKKIIWK QIIEKKIENS
     LNVMVMIGCS DRSIEMVSNF QKTVKLNDTT NREGLAAKVF FRELYGSNFI RFSDDIINKT
     LNYGYTILAS AISRTLVKYG LLCFLGIFHI GKTNNWNLSY DLLEPFRPLV DLWVIKNLDG
     LEGENISYNK RLELINLLNQ FVSVDGKFQT ITNAIDIMVR SYVTVLKTTS SLKLKLPTII
     YYEEKVDDIY EYE
//
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