ID Q2NH80_METST Unreviewed; 795 AA.
AC Q2NH80;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Predicted helicase {ECO:0000313|EMBL:ABC56823.1};
GN OrderedLocusNames=Msp_0422 {ECO:0000313|EMBL:ABC56823.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC56823.1, ECO:0000313|Proteomes:UP000001931};
RN [1] {ECO:0000313|EMBL:ABC56823.1, ECO:0000313|Proteomes:UP000001931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC {ECO:0000313|Proteomes:UP000001931};
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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}.
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DR EMBL; CP000102; ABC56823.1; -; Genomic_DNA.
DR RefSeq; WP_011406023.1; NC_007681.1.
DR AlphaFoldDB; Q2NH80; -.
DR STRING; 339860.Msp_0422; -.
DR GeneID; 41324997; -.
DR KEGG; mst:Msp_0422; -.
DR eggNOG; arCOG01445; Archaea.
DR HOGENOM; CLU_010123_1_1_2; -.
DR OrthoDB; 43851at2157; -.
DR Proteomes; UP000001931; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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 NCBIfam; TIGR01587; cas3_core; 1.
DR NCBIfam; TIGR01596; cas3_HD; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF16; CRISPR-ASSOCIATED NUCLEASE_HELICASE CAS3-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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.
DR PROSITE; PS51194; HELICASE_CTER; 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:ABC56823.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001931}.
FT DOMAIN 12..215
FT /note="HD Cas3-type"
FT /evidence="ECO:0000259|PROSITE:PS51643"
FT DOMAIN 263..473
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 495..669
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 795 AA; 93436 MW; 16896654DE1E18C4 CRC64;
MLSYTDKINE LYSHPQKPLT EHLLNVAENS RSIFENLNIE NNSFYASLSF LIGLCHDFAK
CTSFFQKHLF GIENSEKAYH SFLSAIFGYY VIKKYIKENE IKEELNYPII GYICIINHHG
NLKDVYNTEK SEFNKINQIP QYLDEQIKDI KSRNISSLKE FYLKYNISID DFLEEYEEIK
SVIKKDLKII YREKRIDNYF NVLILFSVLL DSDKLDASYT ETYPRQELNA NLVDLYKQEK
FGQYEGINEI REEAYQELTS SLENIDLNNK IYSITLPTGS GKTMSAFSFA LKLRRKIKNE
KNIIPRIIYT MPFLSIVDQN EEVLRKILNY SNYDTSDILI KHNSTSELSY VVNKNGTTKI
QDDPTEKAEL DVDKAEMLLE GWYSEIVITT FYQLAYTLIS NKNKALRKFH NISNSIIIVD
EAQSIPAKYN QIFKTALDYL SKKFNVWIIF MTATQPEIFK ESDGILPLIT NEQKYFDCFD
RVNYVFHHTP MTIDDFKEKI VDIIQENNKD IMIVLNTISS STEIFEYIQG YFDEEGIELY
YLSGNIIPKE KLERIKKIKE SNNRKVIVTT QLIEAGVNID VDIIYRDFAV MDSIIQTAGR
CNRNDKKEKG TVNIIHLINE NKREYSSFIY DSTLLRLTEE LTKDYTEISE KDFNLKISKK
YYTEVNNRIS HDASHNLEKI ISTLKISNIT HEFKLIEDDI EKIDVFIEIN DEATEIWDKY
NEIYSDKNLK NYEKKLKLKK INRQFNNYVL SIPTNLIGTV NYDKFIFHVG KNDIERKYNL
NTGFIAQENE NAYMI
//
