T3RH_HAEIN
ID T3RH_HAEIN Reviewed; 514 AA.
AC P44105;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable type III restriction-modification enzyme HindVIP Res subunit {ECO:0000303|PubMed:12654995};
DE EC=3.1.21.5;
DE AltName: Full=Probable type III restriction enzyme HindVIP {ECO:0000303|PubMed:12654995};
GN Name=res {ECO:0000303|PubMed:12654995}; OrderedLocusNames=HI_1055;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP NOMENCLATURE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: A type III restriction enzyme that recognizes 2 inversely
CC oriented double-stranded sequences 5'-CGAAT-3' and cleaves 25-27 base
CC pairs downstream. After binding to one recognition site undergoes
CC random one-dimensional diffusion along DNA until it collides with a
CC stationary enzyme bound to the second DNA site, which is when DNA
CC cleavage occurs. DNA restriction requires both the Res and Mod subunits
CC (By similarity). {ECO:0000250|UniProtKB:Q5ZND2,
CC ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.5;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000250|UniProtKB:P08764};
CC -!- SUBUNIT: Contains two different subunits: Res and Mod.
CC {ECO:0000250|UniProtKB:Q5ZND2}.
CC -!- DOMAIN: Has a helicase-type domain in its N-terminus and an
CC endonuclease-type domain in its C-terminus.
CC {ECO:0000250|UniProtKB:P08764}.
CC -!- SIMILARITY: Belongs to the type III restriction-modification system Res
CC protein family. {ECO:0000305}.
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DR EMBL; L42023; AAC22720.1; -; Genomic_DNA.
DR PIR; F64019; F64019.
DR AlphaFoldDB; P44105; -.
DR STRING; 71421.HI_1055; -.
DR REBASE; 203793; Ppe892ORF72P.
DR REBASE; 204713; Bso1395ORF3709P.
DR REBASE; 2820; HindVIP.
DR EnsemblBacteria; AAC22720; AAC22720; HI_1055.
DR KEGG; hin:HI_1055; -.
DR eggNOG; COG3421; Bacteria.
DR HOGENOM; CLU_016957_2_1_6; -.
DR OMA; QDNKFEF; -.
DR PRO; PR:P44105; -.
DR Proteomes; UP000000579; Chromosome.
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:0015668; F:type III site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Endonuclease; Helicase; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine.
FT CHAIN 1..514
FT /note="Probable type III restriction-modification enzyme
FT HindVIP Res subunit"
FT /id="PRO_0000077377"
SQ SEQUENCE 514 AA; 59880 MW; F7801427DB3C23C2 CRC64;
MRSIKRRKKM ANDKTLFDWV EDRKSTLEEM EQTDFFALPE FVERNLKYPF FEWQKSALEN
FLIFDRTSKL KDFPDIKNRP THLLFNMATG AGKTMMMAAL ILYYFEKGYR HFLFFVNQNN
IVDKTENNFT DPTHAKFLFT EKILQGDTVI PIRKVETFSP HSDGIEIKFT SIQKLYNDIH
TEQENQTTLT DLHDLNLVML GDEAHHLNAQ TKGKKQGELD LEKEMNDRTS KAEIERKGWE
HMVLELLLNK NGNPSENVLL EFTATLPENA EVQQKYADKI ITKFGLKEFL QKGYTKEINL
VSSTLGKKER VLHALLFAWY RHQIALKYGI ANFKPVMLFR SKTIDESKAD YLAFLNWVEN
VQAVDFSFLT TFLASLNDSD NANEQGKTRT EQALKFIQDN KFEFVHLADW VKQNYQKHNV
IITNSETNKS KTEKTDSETE KLLNNLEAAD NPIRAIFTVD RLTEGWDVLN LFDIVRLYEG
QNGGGSNKKS GKSCRHRIRK AVNWSWRALF SICV
