ID A0A127VAE6_9SPHI Unreviewed; 319 AA.
AC A0A127VAE6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AY601_1217 {ECO:0000313|EMBL:AMP98141.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP98141.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMP98141.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP98141.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) 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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014504; AMP98141.1; -; Genomic_DNA.
DR RefSeq; WP_068397883.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127VAE6; -.
DR KEGG; pcm:AY601_1217; -.
DR PATRIC; fig|188932.3.peg.1259; -.
DR OrthoDB; 9803119at2; -.
DR Proteomes; UP000071561; 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 HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR019855; CRISPR-assoc_Cas1_NMENI.
DR NCBIfam; TIGR00287; cas1; 1.
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:UP000071561}.
FT BINDING 154
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 319 AA; 36177 MW; E107988EA5D35A70 CRC64;
MIKRTLHFSN PAYLSLQQNQ LSIDLPHLKS LGEKESRKLV PIEDIGIIIL DNQQITITHG
CIAALLSNNA AIITCNKSRH PTGMMLPIDG HNTQSERFRY QIDASQPLKK QLWQQTVQAK
ILNQAAILFN RDIPCKNMIH WAKSVRSGDP DNYEGRAAVY YWKNVFPEKI DFFRGRDGDP
PNNLLNYGYA ILRAIVARGL VCSGLLPTLG IHHRNKYNAY CLADDIMEPY RPYVDEIVLG
IIDRGENFLE LGKDIKTQLL GIATVDVQFE KNRSPLLVGL QTTTSSLAKC YEGTIRRINY
PIMKNFETKR GSGFDESED
//
