T2CX_CITFR
ID T2CX_CITFR Reviewed; 285 AA.
AC P56200;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Type II restriction enzyme Cfr10I {ECO:0000303|PubMed:12654995};
DE Short=R.Cfr10I;
DE EC=3.1.21.4;
DE AltName: Full=Endonuclease Cfr10I;
DE AltName: Full=Type-2 restriction enzyme Cfr10I;
GN Name=cfr10IR;
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), FUNCTION, AND SUBUNIT.
RC STRAIN=RFL10;
RX PubMed=8568865; DOI=10.1006/jmbi.1996.0015;
RA Bozic D., Grazulis S., Siksnys V., Huber R.;
RT "Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I
RT at 2.15-A resolution.";
RL J. Mol. Biol. 255:176-186(1996).
RN [2]
RP NOMENCLATURE, AND SUBTYPES.
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: An F and P subtype restriction enzyme that recognizes the
CC double-stranded sequence 5'-RCCGGY-3' and cleaves after R-1.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8568865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8568865}.
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DR PDB; 1CFR; X-ray; 2.15 A; A=1-285.
DR PDBsum; 1CFR; -.
DR AlphaFoldDB; P56200; -.
DR SMR; P56200; -.
DR EvolutionaryTrace; P56200; -.
DR PRO; PR:P56200; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR012415; Restrct_endonuc_II_Cfr10I.
DR Pfam; PF07832; Bse634I; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Restriction system.
FT CHAIN 1..285
FT /note="Type II restriction enzyme Cfr10I"
FT /id="PRO_0000077295"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1CFR"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1CFR"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 35..53
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 59..84
FT /evidence="ECO:0007829|PDB:1CFR"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1CFR"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:1CFR"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:1CFR"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:1CFR"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1CFR"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 195..218
FT /evidence="ECO:0007829|PDB:1CFR"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1CFR"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:1CFR"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:1CFR"
SQ SEQUENCE 285 AA; 32016 MW; 5F95F49ED058D743 CRC64;
MDIISKSGEG NKYTINSAIA FVAYASHIDI NTTEFSKVLS GLRDFINDEA IRLGGKISDG
SFNKCNGDWY EWLIGIRAIE FFLESETNFI VVKMPNATSF DVMSIYKSCL SEFIYDLRSK
LSLNNVNLIT SNPDFSIIDI RGRREELKSM LKDISFSNIS LSTISEIDNL YKNFIDYAEL
EHIKSFLSVK TTFRPDRRLQ LAHEGSLMKA LYTHLQTRTW TINPTGIRYY AAATSIGNAD
VIGLKTVATH SITDVKSLPQ SAVDEIFKIN SVLDVDSCLS HILSS
