ID A0A0X7BFP9_9FLAO Unreviewed; 957 AA.
AC A0A0X7BFP9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=hsdR_3 {ECO:0000313|EMBL:KVV16184.1};
GN ORFNames=AP058_00242 {ECO:0000313|EMBL:KVV16184.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV16184.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV16184.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV16184.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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|ARBA:ARBA00000851,
CC 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. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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:KVV16184.1}.
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DR EMBL; LLWK01000025; KVV16184.1; -; Genomic_DNA.
DR RefSeq; WP_066305873.1; NZ_LLWK01000025.1.
DR AlphaFoldDB; A0A0X7BFP9; -.
DR STRING; 1729581.AP058_00242; -.
DR REBASE; 151971; Fsp87ORF254P.
DR PATRIC; fig|1729581.3.peg.265; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000059935; 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; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 1.
DR Gene3D; 1.20.58.910; -; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115};
KW Reference proteome {ECO:0000313|Proteomes:UP000059935};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 251..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 957 AA; 110363 MW; 5B3701C638E37CE2 CRC64;
MAHQSEAQLE NNLIKQLRDL GYASVKIADG DALVDNLKKQ LEGFNQTTFS QKEFDSILNH
LAKGNVFEKA KTLRDRFQLN KDDGTSFYVR FFNTEDSAQN IYQVSNQISL EGSYKNRFDV
TILVNGLPLV QIELKRSGIE IKEAFNQINR YQLHSFWSNH GLFQYVQLFV ISNGVNTKYL
ANNKLQSVKQ TFFWADANNK NVTDLTEFTA AFLNTAHLGN MIAHYIVINE THKVMMVLRP
YQYFATEAII KQVKTSSDNA YIWHTTGSGK TLTSFKASQI LMELPEVHKV VFVVDRKDLD
YQTMNEFNAF KKGSVNGSSD TQSLLKQLTD NTKLVLTTIQ KLNNAISDRF KNSIDTLRDK
KIVFIFDECH RSQFGETHGR ITTFFEKSQL IGFTGTPIFA ENASKNDLGK RTTKDLFGNC
LHKYVITDAI RDENVLRFGI EYVGKYKNKS KSFIDIDVED IDKQEVLDSE NRITKIVDYI
IAYHNQKTFN REYSALFAVS SIKNVIKYYD IFQQKKLAGE HDLRIATIFT FGANEESEDA
QDFLPGDYEF DMAAEPGTNY QASHSRDKLD QYIADYNGMF GTSFSTKDGQ QFENYFKNIS
QRLKDREKQT FNHDKDRLDI VLVVNMMLTG FDAKKVNTLY VDKNLKQHGL IQAYSRTNRI
LGEQKSQGNI LSFRNLKKAT DEAITLFSNK DAVEVVTMPD YEHIAEKFDD ALTSLREITP
TFQSVDDLQS EEDEAQFVLA FRKLLRAMNV LQSYTDFDWE DLHIDEEEFK GFETKYLDLK
DKVQRDTQKE KTSILDDIDF ELELIHRDKI GVAYILKLVA QMKGANTSEA KAQRKAIIDL
LGGDIKLRSK RELIQKFIDE NMPFIKDGDS IEDEFEKFWQ DEKILALGKI CEDEHLDKAQ
FKSLIDAYIY SGREPIKDEV FQCLDNRPSI LQARSIGDRI IAKMKEYVEV FVRGMMA
//