CAS3_STRTR
ID CAS3_STRTR Reviewed; 926 AA.
AC F2XG53;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=CRISPR-associated nuclease/helicase Cas3;
DE EC=3.1.-.-;
DE EC=3.6.4.-;
GN Name=cas3;
OS Streptococcus thermophilus.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ATPASE, FUNCTION AS A
RP NUCLEASE, FUNCTION AS A HELICASE, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP ASP-77; ASP-227; GLN-290; LYS-316; ASP-452; GLU-453; ARG-663 AND ARG-666.
RC STRAIN=DGCC7710;
RX PubMed=21343909; DOI=10.1038/emboj.2011.41;
RA Sinkunas T., Gasiunas G., Fremaux C., Barrangou R., Horvath P., Siksnys V.;
RT "Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the
RT CRISPR/Cas immune system.";
RL EMBO J. 30:1335-1342(2011).
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 sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3
CC plus Cascade participate in CRISPR interference, the third stage of
CC CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do
CC not stimulate ATPase activity, while other nucleotides (aside from
CC dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does
CC not require ATP. Functions as an ATP-dependent helicase; helicase
CC activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and
CC RNA/DNA hybrids, moving mostly in a 3' to 5' direction.
CC {ECO:0000269|PubMed:21343909}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Mn(2+) or Mg(2+) or Ca(2+). ATPase and nuclease activities are
CC dependent on divalent cations, for ATPase Mn(2+) is marginally
CC preferred over Mg(2+) or Ca(2+).;
CC -!- ACTIVITY REGULATION: Nuclease activity is inhibited by EDTA.
CC {ECO:0000269|PubMed:21343909}.
CC -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain and
CC a C-terminal helicase/ATPase domain. In some CRISPR/Cas systems the
CC domains are swapped, in others they are encoded separately.
CC -!- MISCELLANEOUS: Found in the E.coli-type CRISPR4/cas system.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC nuclease Cas3-HD family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC helicase Cas3 family. {ECO:0000305}.
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DR EMBL; HQ453272; ADV90802.1; -; Genomic_DNA.
DR RefSeq; WP_037623090.1; NZ_QFLC01000003.1.
DR AlphaFoldDB; F2XG53; -.
DR SMR; F2XG53; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004536; F:deoxyribonuclease activity; IDA:CACAO.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3210.30; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR035011; Cas3.
DR InterPro; IPR041372; Cas3_C.
DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47959:SF5; PTHR47959:SF5; 1.
DR Pfam; PF18395; Cas3_C; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF18019; HD_6; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01587; cas3_core; 1.
DR TIGRFAMs; TIGR01596; cas3_HD; 1.
DR PROSITE; PS51643; HD_CAS3; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Helicase; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding.
FT CHAIN 1..926
FT /note="CRISPR-associated nuclease/helicase Cas3"
FT /id="PRO_0000417607"
FT DOMAIN 17..229
FT /note="HD Cas3-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00974"
FT DOMAIN 297..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 551..745
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 452..455
FT /note="DEAH box"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 310..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 77
FT /note="D->A: Loss of ssDNA nuclease activity, no effect on
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 227
FT /note="D->A: Loss of ssDNA nuclease activity."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 290
FT /note="Q->A: Loss of ssDNA-dependent ATPase."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 316
FT /note="K->A: Loss of ssDNA-dependent ATPase."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 452
FT /note="D->A: Loss of ssDNA-dependent ATPase, loss of
FT helicase activity."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 453
FT /note="E->A: Loss of ssDNA-dependent ATPase."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 663
FT /note="R->A: Loss of ssDNA-dependent ATPase."
FT /evidence="ECO:0000269|PubMed:21343909"
FT MUTAGEN 666
FT /note="R->A: Loss of ssDNA-dependent ATPase."
FT /evidence="ECO:0000269|PubMed:21343909"
SQ SEQUENCE 926 AA; 105760 MW; CFBD0C7E1300FEF3 CRC64;
MKHINDYFWA KKTEENSRLL WLPLTQHLED TKNIAGLLWE HWLSEGQKVL IENSINVKSN
IENQGKRLAQ FLGAVHDIGK ATPAFQTQKG YANSVDLDIQ LLEKLERAGF SGISSLQLAS
PKKSHHSIAG QYLLSHYGVD EDIATIIGGH HGRPVDDLDG LNSQKSYPSN YYQDEKKDSL
VYQKWKSNQE AFLNWALTET GFNSVSQLPK IKQPAQVILS GLLIMSDWIA SNEHFFPLLS
LDETDVKNKS QRIETGFKKW KKSNLWQPET FVDLVTLYQE RFGFSPRNFQ LILSQTIEKT
TNPGIVILEA PMGIGKTEAA LAVSEQLSSK KGCSGLFFGL PTQATSNGIF KRIEQWTENI
KGNNSDHFSI QLVHGKAALN TDFIELLKGN TINMDDSENG SIFVNEWFSG RKTSALDDFV
VGTVDQFLMV ALKQKHLALR HLGFSKKVIV IDEVHAYDAY MSQYLLEAIR WMGAYGVPVI
ILSATLPAQQ REKLIKSYMA GMGVKWRDIE NIDQIKIDAY PLITYNDGPD IHQVKMFEKQ
EQKNIYIHRL PEEQLFDIVK EGLDNGGVVG IIVNTVRKSQ ELARNFSDIF GDDMVDLLHS
NFIATERIRK EKDLLQEIGK KAIRPPKKII IGTQVLEQSL DIDFDVLISD LAPMDLLIQR
IGRLHRHKIK RPQKHEVARF YVLGTFEEFD FDEGTRLVYG DYLLARTQYF LPDKIRLPDD
ISPLVQKVYN SDLTITFPKP ELHKKYLDAK IEHDDKIKNK ETKAKSYRIA NPVLKKSRVR
TNSLIGWLKN LHPNDSEEKA YAQVRDIEDT VEVIALKKIS DGYGLFIENK DISQNITDPI
IAKKVAQNTL RLPMSLSKAY NIDQTINELE RYNNSHLSQW QNSSWLKGSL GIIFDKNNEF
ILNGFKLLYD EKYGVTIERL DKNESV
