CAS10_THEON
ID CAS10_THEON Reviewed; 777 AA.
AC B6YWB8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) {ECO:0000303|PubMed:25773141};
DE Short=ssDNase Cas10;
DE EC=3.1.-.- {ECO:0000269|PubMed:25773141};
DE AltName: Full=Cyclic oligoadenylate synthase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:A0A0A7HFE1};
DE AltName: Full=ToCsm1 {ECO:0000303|PubMed:25773141};
GN Name=csm1 {ECO:0000303|PubMed:25773141}; Synonyms=cas10 {ECO:0000305};
GN OrderedLocusNames=TON_0893;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
RN [2] {ECO:0007744|PDB:4UW2}
RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS), FUNCTION AS DNASE, COFACTOR,
RP ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH CSM4, DOMAIN, AND
RP MUTAGENESIS OF ASP-15.
RC STRAIN=NA1;
RX PubMed=25773141; DOI=10.1016/j.str.2015.01.021;
RA Jung T.Y., An Y., Park K.H., Lee M.H., Oh B.H., Woo E.;
RT "Crystal structure of the Csm1 subunit of the Csm complex and its single-
RT stranded DNA-specific nuclease activity.";
RL Structure 23:782-790(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). The
CC type III-A Csm effector complex binds crRNA and acts as a crRNA-guided
CC RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA
CC cognate to the crRNA is required for all activities.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- FUNCTION: A single-strand deoxyribonuclease (ssDNase) which digests
CC linear and circular ssDNA; has 5'-3' and 3'-5' exonuclease activity as
CC well as a less efficient endonuclease activity. Has a minimal size
CC requirement; 100 nucleotide ssDNA (nt) is more efficiently digested
CC than 50 or 25 nt ssDNA, while 14 nt ssDNA is not cleaved at all. It has
CC no activity on dsDNA or ssRNA. {ECO:0000269|PubMed:25773141}.
CC -!- FUNCTION: ssDNase activity is stimulated in the ternary Csm effector
CC complex; binding of cognate target RNA activates the ssDNase, as the
CC target RNA is degraded ssDNA activity decreases.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- FUNCTION: When associated with the ternary Csm effector complex (the
CC crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic
CC oligoadenylates (cOA) from ATP. cOAs are second messengers that
CC stimulate the ssRNase activity of Csm6, inducing an antiviral state
CC important for defense against invading nucleic acids.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:25773141};
CC Note=Ni(2+) and Mn(2+), but not Mg(2+), Ca(2+), Zn(2+), Co(2+), or
CC Cu(2+), is required for ssDNase activity.
CC {ECO:0000269|PubMed:25773141};
CC -!- ACTIVITY REGULATION: ssDNase activity is inhibited by EDTA.
CC {ECO:0000269|PubMed:25773141}.
CC -!- SUBUNIT: Probably part of the Csm effector complex, that includes
CC Cas10, Csm2, Csm3, Csm4, Csm5 and mature crRNA (By similarity). Will
CC form a homodimer in solution, interacts with Csm4, which is a tighter,
CC better association than the homodimeric Cas10 and uses the same
CC interface for interaction (PubMed:25773141).
CC {ECO:0000250|UniProtKB:A0A0A7HFE1, ECO:0000269|PubMed:25773141}.
CC -!- INTERACTION:
CC B6YWB8; B6YWB8: csm1; NbExp=3; IntAct=EBI-16149952, EBI-16149952;
CC B6YWB8; B6YWC1: csm4; NbExp=2; IntAct=EBI-16149952, EBI-16149979;
CC -!- DOMAIN: The N-terminal HD domain has ssDNase activity
CC (PubMed:25773141). The C-terminal GGDEF domain has the cOA synthesis
CC activity (By similarity). {ECO:0000250|UniProtKB:A0A0A7HFE1,
CC ECO:0000269|PubMed:25773141}.
CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus.
CC {ECO:0000305|PubMed:25773141}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Cas10/Csm1 family.
CC {ECO:0000305}.
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DR EMBL; CP000855; ACJ16381.1; -; Genomic_DNA.
DR RefSeq; WP_012571853.1; NC_011529.1.
DR PDB; 4UW2; X-ray; 2.63 A; A/B/C/D=1-777.
DR PDB; 6IQW; EM; 3.35 A; A=1-777.
DR PDB; 6KBD; X-ray; 3.00 A; A=1-500.
DR PDB; 6KC0; X-ray; 2.29 A; A=1-500.
DR PDB; 6MUA; X-ray; 2.91 A; A=1-777.
DR PDB; 6MUR; EM; 3.10 A; A=1-777.
DR PDB; 6MUS; EM; 3.60 A; A=1-777.
DR PDB; 6MUT; EM; 3.10 A; A=1-777.
DR PDB; 6MUU; EM; 3.00 A; A=1-777.
DR PDB; 6O73; X-ray; 3.00 A; A=1-777.
DR PDB; 6O74; X-ray; 2.71 A; A=1-777.
DR PDB; 6O75; X-ray; 2.60 A; A=1-777.
DR PDB; 6O78; X-ray; 2.80 A; A=1-777.
DR PDB; 6O79; X-ray; 3.00 A; A=1-777.
DR PDB; 6O7B; X-ray; 2.40 A; A=1-777.
DR PDB; 6O7D; X-ray; 2.81 A; A=1-777.
DR PDB; 6O7E; EM; 3.20 A; A=1-777.
DR PDB; 6O7H; EM; 2.90 A; A=1-777.
DR PDB; 6O7I; EM; 3.20 A; A=1-777.
DR PDBsum; 4UW2; -.
DR PDBsum; 6IQW; -.
DR PDBsum; 6KBD; -.
DR PDBsum; 6KC0; -.
DR PDBsum; 6MUA; -.
DR PDBsum; 6MUR; -.
DR PDBsum; 6MUS; -.
DR PDBsum; 6MUT; -.
DR PDBsum; 6MUU; -.
DR PDBsum; 6O73; -.
DR PDBsum; 6O74; -.
DR PDBsum; 6O75; -.
DR PDBsum; 6O78; -.
DR PDBsum; 6O79; -.
DR PDBsum; 6O7B; -.
DR PDBsum; 6O7D; -.
DR PDBsum; 6O7E; -.
DR PDBsum; 6O7H; -.
DR PDBsum; 6O7I; -.
DR AlphaFoldDB; B6YWB8; -.
DR SMR; B6YWB8; -.
DR DIP; DIP-61404N; -.
DR IntAct; B6YWB8; 1.
DR STRING; 523850.TON_0893; -.
DR EnsemblBacteria; ACJ16381; ACJ16381; TON_0893.
DR GeneID; 7017196; -.
DR KEGG; ton:TON_0893; -.
DR PATRIC; fig|523850.10.peg.901; -.
DR eggNOG; arCOG02666; Archaea.
DR HOGENOM; CLU_017487_1_0_2; -.
DR OMA; DYFFKGY; -.
DR OrthoDB; 21880at2157; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd09680; Cas10_III; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR013408; Cas10/Csm1.
DR InterPro; IPR041062; Csm1_B.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF18211; Csm1_B; 1.
DR Pfam; PF01966; HD; 1.
DR TIGRFAMs; TIGR02578; cas_TM1811_Csm1; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; Endonuclease; Exonuclease;
KW Hydrolase; Nuclease; Nucleotide-binding; Transferase.
FT CHAIN 1..777
FT /note="CRISPR system single-strand-specific
FT deoxyribonuclease Cas10/Csm1 (subtype III-A)"
FT /id="PRO_0000446114"
FT DOMAIN 1..106
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 513..660
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT MUTAGEN 15
FT /note="D->N: Loss of ssDNase activity."
FT /evidence="ECO:0000269|PubMed:25773141"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:6KC0"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:6MUU"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6MUT"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6MUU"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6O7H"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6MUU"
FT HELIX 256..281
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 304..325
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 328..338
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:6KC0"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:6KC0"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6O7H"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6O7H"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6MUR"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6O7I"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6O7H"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:6O7D"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6KBD"
FT STRAND 450..458
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 462..468
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 515..522
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 525..530
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 535..558
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 579..586
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 589..595
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 596..613
FT /evidence="ECO:0007829|PDB:6O7B"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:4UW2"
FT STRAND 620..627
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:4UW2"
FT HELIX 633..649
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 652..656
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:6O75"
FT STRAND 670..673
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 674..688
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:6O7B"
FT TURN 700..703
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 704..718
FT /evidence="ECO:0007829|PDB:6O7B"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:4UW2"
FT HELIX 724..731
FT /evidence="ECO:0007829|PDB:6O7B"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:6MUT"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:6O7H"
FT HELIX 743..745
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 750..754
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 760..762
FT /evidence="ECO:0007829|PDB:6O7B"
FT HELIX 765..775
FT /evidence="ECO:0007829|PDB:6O7B"
SQ SEQUENCE 777 AA; 88009 MW; 0F28CCAD584FB779 CRC64;
MEIDELTALG GLLHDIGKPV QRAGLYSGDH STQGARFLRD LAENTGRAEY ELLSLFSEFH
HKGHMKNDEL MIRRIKELSP ERFGLTMEDV LNALWIVYEA DNLASGEREE GQPQASRPLY
SVFNPGKAYP WAELDFEKEL PVPGDVFSIR SQDYRELVKR LWEELSKAKL RSDRLLPVLE
KYLTFVSSVT SEGNIISLYD HMRMTSAIAL AMLRAGCTAE DVRSGRCRKE KRFLLIEGDF
SGIQDFIYRV SGKGTLKYLR ARSAYLELIG WDVVLEILSR LGLTRANVVF NAGGHFMIIA
QNTPDAVKEL EEIRAKAVEW LYREFESDLY LAIEWEPVSG REFGREGGKN LFAEARKRLK
HKLTVRKLKR FGEIKGLFEH GHTERLAECP VCGRELPEGK LEPSASDPET KVCPTCNRLV
SLGGNLPKLL GFGRTAKNDA GVLVEGPFSG FVPYLQGGRP VGEQILVKNT LNPGEIPESA
QFVPYFVADY FKKDPKGGVA TFEELSMAST GTRRLGVMKG DVDRLGEFFS SMDSPSKLAT
ASRFMDYFFK GYIGAIIEGK FGYIIGDVPS LRDWPEEPDI VVVYAGGDDF FIVGAWDQIF
ELAFRVRRAF NAYTGGKLTL SVGLGYFDER TPIYRMADVV SERLDTAKDE GRNRVFVVGR
SRPLDGKHKL SYEWNHYEEL WRTYAPRIYA GNGRLKGKLE SKKGLLWKLL EIRELYVRDP
NDVRWAYLTA YLLGRHGLSD LFPELVGIDT KAVERKEPQP VYWVDGVLKI VLMAVRR
