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Database: UniProt
Entry: G7G150_9GAMM
LinkDB: G7G150_9GAMM
Original site: G7G150_9GAMM 
ID   G7G150_9GAMM            Unreviewed;       322 AA.
AC   G7G150;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   ORFNames=P20495_1619 {ECO:0000313|EMBL:GAA79123.1};
OS   Pseudoalteromonas sp. BSi20495.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA79123.1, ECO:0000313|Proteomes:UP000003050};
RN   [1] {ECO:0000313|Proteomes:UP000003050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX   PubMed=22275105; DOI=10.1128/JB.06427-11;
RA   Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT   ice.";
RL   J. Bacteriol. 194:908-909(2012).
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:GAA79123.1}.
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DR   EMBL; BADY01000054; GAA79123.1; -; Genomic_DNA.
DR   RefSeq; WP_008135456.1; NZ_BADY01000054.1.
DR   AlphaFoldDB; G7G150; -.
DR   Proteomes; UP000003050; 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   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; IPR019857; CRISPR-assoc_Cas1_YPEST-subtyp.
DR   NCBIfam; TIGR00287; cas1; 1.
DR   NCBIfam; TIGR03637; cas1_YPEST; 1.
DR   PANTHER; PTHR34353:SF3; CRISPR-ASSOCIATED ENDONUCLEASE CAS1; 1.
DR   PANTHER; PTHR34353; 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|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}.
FT   BINDING         186
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         248
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         262
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   322 AA;  36563 MW;  10BD9B21221517AE CRC64;
     MDDFSPSNLK TILHSKRANM YYLEYCRVMQ KDGRVLYLTE AKNENQYFNI PIANTTVLLL
     GNGTSITQAA MRMLAQAGVL VGFSGGGGTP LYMGNNIEWL TPQSEYRPTE YLQGWMSFWF
     DDKKRLAVAK QFQQARIEYL NKIWNKDRSL KSEGFTTQNN SIETALTRFN ERMLVATKQS
     ELLLTEAQLT KALYKFAANI TKAEGFTRQH TSTDLANDFL NHGNYLAYGL AASCLWVLGI
     PHGFAVMHGK TRRGALVFDI ADLIKDAIVL PWAFICAQEN ATEQEFRQQI LQAFTDNKAL
     DFMFDEVKKA ALQTEHKTGE NQ
//
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