ID A0A2N7DCZ3_9VIBR Unreviewed; 1074 AA.
AC A0A2N7DCZ3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=BCU68_13645 {ECO:0000313|EMBL:PMH42636.1};
OS Vibrio sp. 10N.286.49.B3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1880855 {ECO:0000313|EMBL:PMH42636.1, ECO:0000313|Proteomes:UP000235563};
RN [1] {ECO:0000313|Proteomes:UP000235563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10N.286.49.B3 {ECO:0000313|Proteomes:UP000235563};
RA Kauffman K., Hussain F., Yang J., Arevalo P., Brown J., Cutler M.,
RA Kelly L., Polz M.F.;
RT "Nontailed viruses are major unrecognized killers of bacteria in the
RT ocean.";
RL Submitted (JUL-2016) 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:PMH42636.1}.
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DR EMBL; MCUV01000026; PMH42636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7DCZ3; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000235563; 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:0004386; F:helicase activity; 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; 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 Helicase {ECO:0000313|EMBL:PMH42636.1};
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:UP000235563};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 303..494
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1074 AA; 122087 MW; E7447AD63204CF69 CRC64;
MITEDQLEQE CIRWFTDQGY LYKNGYDIAP DGDDAERDDY HQVVLKQRLL NQLTIINPEL
PIEALNDVVN TVSSPDTPIL IKNNRAFHKF VIEGVPVEYT DVEDGESKTK HTHAQLMDFT
TPDNNEFLIV NQFTITGTKG NRRPDVVVFI NGLPISVIEL KNPADDHADI WNAFNQLQTY
KDEISDLFVF NEALIVSDGW TARVGSLTAN KERFLPWKTV ATEDDRPLLE FQLETMVRGF
FKQDLLLDYI RYFVLFETDN DKIIKKIAGY HQFHAVRAAV EATVRAANTS GNFLESTIPA
LEKIKQGSGK AGVVWHTQGS GKSISMVCYA SKLLQQASMN NPTIVVVTDR NDLDGQLYNT
FGMAQETLKQ IPQQADDRDA LRELLLNRQS GGIIFTTIQK FALLDEETEH PRLSERSNIV
VVSDEAHRSQ YGNKSKMVEV KDKNGTVTGH KYVYGYSKYM RDALPNASFI GFTGTPIAMD
DKDTRGVFGE YVSIYDIQDA VDDGATVPIY YESRLAKLDI NQDEIEQLND KVEGEIGEDE
ETADREKVKS EWATLEKLVG AEPRIEQVAK DLVEHFTTRT STFPGKAMIV SMSREICVDL
YNAIVAIKPE WHHPDTDKGA IKIVMTGSAS DKEKMQPHIH DKKTKKLFEK RYKDTDDELQ
LVIVRDMWLT GFDAPCCHTM YIDKPMKGHN LMQAIARVNR VFKDKPGGLV VDYIGIANEL
KNALKTYTNS QGKGQPTVDT AEAFAVLMEK VDIIRGMFAT PVDTKVFNYR PDFESDALRL
LPGAVNHLSG LSHTDANGKQ VRDGKRRFLD VMAALAKAYS LCSTMDETHC YKNEIAFYSA
IKTAFIKHST VDKKRTDEER NTALKQILNN AVVADGVDDI FTMVGLDKPN IGLLSEEFLE
DVKNMKEKNL AVELLEKLLR DEVKSRMKND VVQEKKYSER IMSTLQKYHN RSIETAQVIE
ELIQWAKEMQ EDGELLDKLN LSVDEIAFYR ALVDNESSVR ELGDDNLRKL AIELTHQLRK
SATVDWQKRD SVRARMRNLV RRLLRRWKYP PDAAEEAIKL VLEQAEVLAD GWYK
//
