ID A0A257HY51_9BACT Unreviewed; 1076 AA.
AC A0A257HY51;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CFE25_10545 {ECO:0000313|EMBL:OYU55371.1};
OS Chitinophagaceae bacterium BSSC1.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX NCBI_TaxID=2015574 {ECO:0000313|EMBL:OYU55371.1, ECO:0000313|Proteomes:UP000217121};
RN [1] {ECO:0000313|EMBL:OYU55371.1, ECO:0000313|Proteomes:UP000217121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSSC1 {ECO:0000313|EMBL:OYU55371.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-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|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:OYU55371.1}.
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DR EMBL; NKJC01000002; OYU55371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257HY51; -.
DR Proteomes; UP000217121; 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; 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; 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; PF04313; HSDR_N; 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; 1.
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, ECO:0000313|EMBL:OYU55371.1};
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:UP000217121};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 334..496
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1076 AA; 124072 MW; 8073D73904B715DB CRC64;
MNTPSFKEDH ISQIPALQML QNLGYTYLTP DEADRLRGGK TSNTILEDVL RKKLKEINSD
KKISSTRSTY ISDANIENGI RALKELPMNE GYIAACETAY NLITLGKAFE QNIDGDKKSI
TLQYIDWKTI ENNDFHVTEE FSTMRSTSKD HYRPDLVLFI NGIPICIIEC KRPDMKEPLK
QAISQHLRNQ QEDGIRSLYA YSQITLSLAT QQASYATNAT PEKFWAHWEE KFLTQTEEAN
YKAELEEIKN TPLSPSQKEK LFSDRFKYVR NYFDALETEK IQPTEQDVYL YGLCRPKRLL
DIIYNFIMFD NGEKKIARYQ QFFAIKKTMQ RIVQIEGGKR RGGVIWHTQG SGKSLTMVML
AQAIAMEPSI RNPKIVLVTD RTDLDNQITD TFRKCGKFVE NASTGQRLVE LLESKSDSIV
TTIINKFVAA IKKITKPLES HDIFVLVDEG HRTQHGTFNV EMQKTLPNAC FIAMTGTPLF
KKDKSTAKQF GGIIDTYTVD QAVKDKAVVP LLYEGRLARQ VVNESPLDTF FSMVSEPLTE
YQKADFKKKF SRADQLNSAE QKIYAIAWNI SLHFRDNWQG KTPFKGQLVC DKKVNAIRYK
EFLDEIGIVT SEVLISSIDE REGEESAYEK SSEKENRFWK KMMDEHGTAK KYEKNLINRF
KNQRDPEIII VVDKLLTGFD ESKNTVLYLT RNLQGHKLLQ AIARVNRINE DKEFGYIIDY
YGVIENLDDA LEMYSTFKDF DADDLEGTLV NVIDEIKKLP QKHSELWDIF KSVANKRDAE
AYQLLLKDES IRVVFYNKLA SFAKGLKLAF SSIQFYKEVE EKIINRYKED LTMFLKLRLA
VIERYSDTID YKQYEGQIQK LIDKHITTET VETITELVNI FDKEKFQQEV ESTTGKAAKA
DKIASRTSKH ISEKMEEDPA FYKKFSQMLK ETISEYESKR INEAQYLHKV QEIMENVLAH
TDSDIPEILK DNNVAKAFFG LTVETLIEKL SDSIVRTSIA TETAMYIVEL IQKAVLDNGI
PIIDWKNKSN ITGKLVIDIG DYLIDEVRDK YKIELSFGEM DELANKCIDV ASKQYK
//
