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Database: UniProt
Entry: A0A150J3C0_9EURY
LinkDB: A0A150J3C0_9EURY
Original site: A0A150J3C0_9EURY 
ID   A0A150J3C0_9EURY        Unreviewed;       803 AA.
AC   A0A150J3C0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=CRISPR-associated nuclease/helicase Cas3 {ECO:0000313|EMBL:KYC51692.1};
DE            EC=3.1.-.- {ECO:0000313|EMBL:KYC51692.1};
GN   Name=cas3_1 {ECO:0000313|EMBL:KYC51692.1};
GN   ORFNames=AMQ74_01028 {ECO:0000313|EMBL:KYC51692.1};
OS   Candidatus Methanofastidiosum methylthiophilus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Methanofastidiosa;
OC   Methanofastidiosum.
OX   NCBI_TaxID=1705564 {ECO:0000313|EMBL:KYC51692.1, ECO:0000313|Proteomes:UP000075578};
RN   [1] {ECO:0000313|EMBL:KYC51692.1, ECO:0000313|Proteomes:UP000075578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U1lsi0528_Bin089 {ECO:0000313|EMBL:KYC51692.1};
RX   PubMed=26943620;
RA   Nobu M.K., Narihiro T., Kuroda K., Mei R., Liu W.T.;
RT   "Chasing the elusive Euryarchaeota class WSA2: genomes reveal a uniquely
RT   fastidious methyl-reducing methanogen.";
RL   ISME J. 0:0-0(2016).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC       nuclease Cas3-HD family. {ECO:0000256|ARBA:ARBA00006847}.
CC   -!- SIMILARITY: In the central section; belongs to the CRISPR-associated
CC       helicase Cas3 family. {ECO:0000256|ARBA:ARBA00009046}.
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:KYC51692.1}.
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DR   EMBL; LNGD01000057; KYC51692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150J3C0; -.
DR   PATRIC; fig|1705564.3.peg.1060; -.
DR   Proteomes; UP000075578; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd09641; Cas3''_I; 1.
DR   CDD; cd17930; DEXHc_cas3; 1.
DR   Gene3D; 1.10.3210.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006483; CRISPR-assoc_Cas3_HD.
DR   InterPro; IPR038257; CRISPR-assoc_Cas3_HD_sf.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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   NCBIfam; TIGR01587; cas3_core; 1.
DR   NCBIfam; TIGR01596; cas3_HD; 1.
DR   Pfam; PF18019; Cas3_HD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51643; HD_CAS3; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KYC51692.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KYC51692.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          11..236
FT                   /note="HD Cas3-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51643"
FT   DOMAIN          285..483
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   803 AA;  94890 MW;  2B5E88B2886462CC CRC64;
     MEQKLFQFKL YSHPNKTLVS HLEEVGKKSK DILLQKNLNI GDYVDTEVLS EIIYLIGATH
     DFGKASKYFQ EYLLEKDLTK KRELKSYKET RHGLFSSIFT YYIIKTYLKN IPKDKDEHYS
     FLPIISFFVV KRHHGNLANS VKEINEIHEI LNDKKLISVI NSQIYSIDEN EIQNILDKLF
     GCNKYLFSDF KENYLNILRE IDREFINLLK IQKNKILFYY FLTLLLYSIL IDSDKADAIG
     SLNILRENIP SRLVDQYKIN KFNNNLNFID KIRTEIYEEV NSKLENLDVQ DKIYLLNVPT
     GTGKTITSFS FAVKLKNKIQ TEKGYNPRII YSLPFLSIID QNYSVIEDII VSQFENIRSN
     ILLKHHHLSE ISYTTSEEEY ESDKSLFLIE GWNSELIITS FIQLFHGLIS NKNRLLRKFH
     NITNSIVILD EIQTIPHKYW KLLNESLYFL SKYFNTYFII VTATAPLIFD SEKNEINNLI
     EDSQKYYSQL NRIKLNLYLE KEVNFEDFKN IVLNDIITRD DKSFLIVLNT ITSSKELFNF
     IKKNTNNDCN EYYYLSSNII PFDRLDRIRK IKTSKKRKII VSTQVIEAGV DIDIDIIYRD
     LAPLDSINQV AGRCNRNFSF KSQGEVNVYI LKDNNERKFC TYIYEGFLIN KTLETLKNVK
     VVEEKDFFKL LNKYFLLVNE SSTDQISREI LENLYKLEFQ ETGNFKLIED DYEKIDIFIE
     INENAKKIWN EFVKILDIDD PILKRKKFLN IKKSFYDYII SIPKNKANDV LYNERIGYVS
     LGKINSKYDL ETGYKSEKIP LII
//
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