CAS1B_SACS2
ID CAS1B_SACS2 Reviewed; 307 AA.
AC Q97Y84;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=CRISPR-associated endonuclease Cas1 2 {ECO:0000255|HAMAP-Rule:MF_01470};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470};
GN Name=cas1-2 {ECO:0000255|HAMAP-Rule:MF_01470}; OrderedLocusNames=SSO1450;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, SUBUNIT, DNA-BINDING, AND RNA-BINDING.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=19427858; DOI=10.1016/j.febslet.2009.04.047;
RA Han D., Lehmann K., Krauss G.;
RT "SSO1450--a CAS1 protein from Sulfolobus solfataricus P2 with high affinity
RT for RNA and DNA.";
RL FEBS Lett. 583:1928-1932(2009).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF GLU-142.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=26284603; DOI=10.7554/elife.08716;
RA Rollie C., Schneider S., Brinkmann A.S., Bolt E.L., White M.F.;
RT "Intrinsic sequence specificity of the Cas1 integrase directs new spacer
RT acquisition.";
RL Elife 4:0-0(2015).
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:0000255|HAMAP-Rule:MF_01470}.
CC -!- FUNCTION: In vitro catalyzes a concerted transesterification reaction
CC on branched DNA, as would be expected during integration of
CC protospacers into the CRISPR leader sequence; Cas2 is not required in
CC vitro. This reaction requires a 3'-OH group at the branch point
CC (PubMed:26284603). Binds ss- and dsDNA and ss- and dsRNA with
CC approximately equal affinity. May be able to anneal complementary DNA
CC strands (PubMed:19427858). {ECO:0000269|PubMed:19427858,
CC ECO:0000269|PubMed:26284603}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer (By
CC similarity). Forms oligomers, probably binds nucleic acids as a
CC homodimer (PubMed:19427858). {ECO:0000255|HAMAP-Rule:MF_01470,
CC ECO:0000269|PubMed:19427858}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01470}.
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DR EMBL; AE006641; AAK41681.1; -; Genomic_DNA.
DR PIR; B90303; B90303.
DR AlphaFoldDB; Q97Y84; -.
DR SMR; Q97Y84; -.
DR STRING; 273057.SSO1450; -.
DR PRIDE; Q97Y84; -.
DR EnsemblBacteria; AAK41681; AAK41681; SSO1450.
DR KEGG; sso:SSO1450; -.
DR PATRIC; fig|273057.12.peg.1480; -.
DR eggNOG; arCOG01452; Archaea.
DR HOGENOM; CLU_052779_0_0_2; -.
DR InParanoid; Q97Y84; -.
DR OMA; FIRLECY; -.
DR PhylomeDB; Q97Y84; -.
DR Proteomes; UP000001974; Chromosome.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 3.100.10.20; -; 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 Pfam; PF01867; Cas_Cas1; 2.
DR TIGRFAMs; TIGR00287; cas1; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..307
FT /note="CRISPR-associated endonuclease Cas1 2"
FT /id="PRO_0000417111"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470,
FT ECO:0000305|PubMed:26284603"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT BINDING 221
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01470"
FT MUTAGEN 142
FT /note="E->A: No longer catalyzes a transesterification
FT reaction on branched DNA."
FT /evidence="ECO:0000269|PubMed:26284603"
SQ SEQUENCE 307 AA; 34895 MW; A179E60F2BBB6410 CRC64;
MISVRTLVIS EYGAYVYVKK NMLVIKKGDK KVEISPSEVD EILITVSCSI STSALSLALT
HGISVMFLNS RETPWGILLP SIVTETVKTK KAQYEAIVVR KDNRYGEEII SSKIYNQSVH
LKYWARVTGT KNDYKELLDK DEPAAARVYW QNISQLLPKD IGFDGRDVDG TDQFNMALNY
SYAILYNTIF KYLVIAGLDP YLGFIHKDRP GNESLVYDFS EMFKPYIDFL LVRALRSGFR
LKVKGGLIEE NSRGDLAKLI RKGMEENVKE ESDHNPKTLI QAIRAHAVKL ASSIREGKEY
RGFKLVM
