ID H1L0A9_9EURY Unreviewed; 334 AA.
AC H1L0A9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-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=MetfoDRAFT_1483 {ECO:0000313|EMBL:EHP85066.1};
OS Methanotorris formicicus Mc-S-70.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=647171 {ECO:0000313|EMBL:EHP85066.1, ECO:0000313|Proteomes:UP000003706};
RN [1] {ECO:0000313|EMBL:EHP85066.1, ECO:0000313|Proteomes:UP000003706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mc-S-70 {ECO:0000313|EMBL:EHP85066.1,
RC ECO:0000313|Proteomes:UP000003706};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sieprawska-Lupa M., Takai K., Miyazaki J.,
RA Whitman W., Woyke T.J.;
RT "The draft genome of Methanotorris formicicus Mc-S-70.";
RL Submitted (SEP-2011) 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:EHP85066.1}.
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; AGJL01000040; EHP85066.1; -; Genomic_DNA.
DR RefSeq; WP_007044911.1; NZ_AGJL01000040.1.
DR AlphaFoldDB; H1L0A9; -.
DR STRING; 647171.MetfoDRAFT_1483; -.
DR PATRIC; fig|647171.4.peg.1446; -.
DR OrthoDB; 2216at2157; -.
DR Proteomes; UP000003706; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
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; cd09634; Cas1_I-II-III; 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; IPR042211; CRISPR-assoc_Cas1_N.
DR NCBIfam; TIGR00287; cas1; 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}.
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ SEQUENCE 334 AA; 38856 MW; 39A105722D716772 CRC64;
MDIVLKSYGF FISKKGDRFV FEVKENGEVK KVEISANKVE RIILGKDGTI TTSAINLAIE
NNIPIIFLKN EEPTAMVWHC KLGKTGKIRR NQIKFSETVE GIKYASKWIE RKMKNQISYL
KELKKNHNHK GDFDGLVEGI KGCIDDLNDY LSKIDGNIQK RTIKDTIIGI EGLASKYYFE
GINYALPEKY KFKERSRRPA KDEFNALLNY DYGMLYPIVE KCCIVAGLDP YVGFIHSDGY
NKTTLVYDII EMYRVYVDRG VVNFINKKKV KNEFFVPLHN GISLSEIGIG EFASFMNESV
FNKEFEFKRK KYKLPDFIQK ECYEIANYIR ERYL
//