ID A0A1W1VFX2_9BACT Unreviewed; 574 AA.
AC A0A1W1VFX2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
GN ORFNames=SAMN00120144_2123 {ECO:0000313|EMBL:SMB92252.1};
OS Hymenobacter roseosalivarius DSM 11622.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=645990 {ECO:0000313|EMBL:SMB92252.1, ECO:0000313|Proteomes:UP000192266};
RN [1] {ECO:0000313|EMBL:SMB92252.1, ECO:0000313|Proteomes:UP000192266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11622 {ECO:0000313|EMBL:SMB92252.1,
RC ECO:0000313|Proteomes:UP000192266};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|RuleBase:RU364115}.
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DR EMBL; FWWW01000058; SMB92252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1VFX2; -.
DR STRING; 645990.SAMN00120144_2123; -.
DR Proteomes; UP000192266; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR021810; T1RH-like_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR Pfam; PF11867; T1RH-like_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|RuleBase:RU364115};
KW Hydrolase {ECO:0000256|RuleBase:RU364115};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364115};
KW Reference proteome {ECO:0000313|Proteomes:UP000192266};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 66..252
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 574 AA; 62870 MW; E0FA78CDF837DCB8 CRC64;
MKKVAAYHQY YAVNAAVQST LRAAGHTPAE VAAATPPTGR GYGRGTPPPA LAHEAPETYG
VPGVSAQPFG DRKGGVVWHT QGSPKSLSMV FYTGKIVQAL DNPTVVVITD RNDLDDQLFD
TFAACTQLLR QEPKQVESRE QLKELLRVAS GGVVFSTIQK FQPEEGNVYE ELSARRNIIV
IADEAHRTQY GFKAKEVDVK EEGQVIGKRT VYGFAKYLRD ALPQATYLGF TGTPIEQTDV
NTPAVFGNYI DIYDIAQAVE DGATVRIYYE SRLAKVSLSE EGKKLVADLD EELDADDLTN
TQKAKAKWTQ LEALIGSERR IATIAADVVA HFEQRQEVFE GKGMIVAMSR RIAAELYAAI
IALRPAWHSS DLTQGKLKVV MTSASTDGPS IAKHHTTKEQ RRALAERMKD PADELQLVIV
RDMWLTGFDA PSMHTLYIDK PMQGHNLMQA IARVNRVYKD KPGGLVVDYL GIASDLKKAL
SFYSDAGGKG DPAVAQKQAV ALMAEKLEVV QALYHGFGYD SSYDAATSTK LSMILAAEEH
ILGLPDGKKR YINEVTALSQ AFAGFFLQTG GFTR
//
