DMO1_DESMO
ID DMO1_DESMO Reviewed; 194 AA.
AC P21505;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Homing endonuclease I-DmoI {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:9092657};
DE EC=3.1.-.- {ECO:0000269|PubMed:9092657};
OS Desulfurococcus mucosus (Desulfurococcus mobilis).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=2275;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3136929; DOI=10.1016/s0092-8674(88)80014-x;
RA Kjems J., Garrett R.A.;
RT "Novel splicing mechanism for the ribosomal RNA intron in the
RT archaebacterium Desulfurococcus mobilis.";
RL Cell 54:693-703(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RA Kjems J., Garrett R.A.;
RT "An intron in the 23S ribosomal RNA gene of the archaebacterium
RT Desulfurococcus mobilis.";
RL Nature 318:675-677(1985).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP DNA-BINDING.
RX PubMed=9092657; DOI=10.1093/nar/25.8.1523;
RA Aagaard C., Awayez M.J., Garrett R.A.;
RT "Profile of the DNA recognition site of the archaeal homing endonuclease I-
RT DmoI.";
RL Nucleic Acids Res. 25:1523-1530(1997).
RN [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=10047486; DOI=10.1006/jmbi.1998.2519;
RA Silva G.H., Dalgaard J.Z., Belfort M., Van Roey P.;
RT "Crystal structure of the thermostable archaeal intron-encoded endonuclease
RT I-DmoI.";
RL J. Mol. Biol. 286:1123-1136(1999).
CC -!- FUNCTION: Endonuclease involved in intron homing (Probable). Recognizes
CC DNA in the 23S rRNA gene intron (minimally 5'-CCGGGTAAGTTCCGG-3'),
CC cutting after A-8 on the top and C-11 on the bottom strand. Has a slow
CC turnover rate, cuts the coding strand with a slight preference over the
CC non-coding strand (PubMed:9092657). {ECO:0000269|PubMed:9092657,
CC ECO:0000305}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:9092657};
CC Note=Mn(2+), Co(2+) and Mg(2+) enable equal cleavage, Zn(2+) is less
CC active and Ni(2+) is essentially inactive.
CC {ECO:0000269|PubMed:9092657};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 nM for a 25-bp DNA substrate {ECO:0000269|PubMed:9092657};
CC Temperature dependence:
CC Not extremely thermostable, has lost significant activity after 90
CC minues at 65 degreees Celsius, has no activity after 4 hours.
CC {ECO:0000269|PubMed:9092657};
CC -!- MISCELLANEOUS: Translated from a circularized intron.
CC {ECO:0000269|PubMed:3136929}.
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DR EMBL; X03263; CAA27018.1; -; Genomic_DNA.
DR PIR; A31224; A31224.
DR PDB; 1B24; X-ray; 2.20 A; A=1-188.
DR PDB; 1MOW; X-ray; 2.40 A; A/D/G/J=-.
DR PDB; 2VS7; X-ray; 2.05 A; A/D/G=2-188.
DR PDB; 2VS8; X-ray; 2.10 A; A/F/K=2-188.
DR PDB; 4D6N; X-ray; 2.35 A; A/F/K=2-188.
DR PDB; 4D6O; X-ray; 2.20 A; A/D/G=2-188.
DR PDB; 4UN7; X-ray; 2.70 A; A/D/G=2-188.
DR PDB; 4UN8; X-ray; 2.60 A; A/D/G=2-188.
DR PDB; 4UN9; X-ray; 2.73 A; A/D/G=2-188.
DR PDB; 4UNA; X-ray; 2.30 A; A/D/G=2-188.
DR PDB; 4UNB; X-ray; 2.55 A; A/D/G=2-188.
DR PDB; 4UNC; X-ray; 2.30 A; A/D/G=2-188.
DR PDB; 4UT0; X-ray; 2.40 A; A/F/K=2-188.
DR PDB; 5A0W; X-ray; 2.20 A; A/D/G=2-188.
DR PDB; 5AK9; X-ray; 2.60 A; A/E/J=2-188.
DR PDB; 5AKF; X-ray; 2.45 A; A/E/I=2-188.
DR PDB; 5AKM; X-ray; 2.40 A; A/F/K=2-188.
DR PDB; 5AKN; X-ray; 2.75 A; A/F/K=2-188.
DR PDB; 5O6G; X-ray; 2.75 A; A/D/G=2-188.
DR PDB; 5O6I; X-ray; 2.25 A; A/F/K=2-188.
DR PDBsum; 1B24; -.
DR PDBsum; 1MOW; -.
DR PDBsum; 2VS7; -.
DR PDBsum; 2VS8; -.
DR PDBsum; 4D6N; -.
DR PDBsum; 4D6O; -.
DR PDBsum; 4UN7; -.
DR PDBsum; 4UN8; -.
DR PDBsum; 4UN9; -.
DR PDBsum; 4UNA; -.
DR PDBsum; 4UNB; -.
DR PDBsum; 4UNC; -.
DR PDBsum; 4UT0; -.
DR PDBsum; 5A0W; -.
DR PDBsum; 5AK9; -.
DR PDBsum; 5AKF; -.
DR PDBsum; 5AKM; -.
DR PDBsum; 5AKN; -.
DR PDBsum; 5O6G; -.
DR PDBsum; 5O6I; -.
DR AlphaFoldDB; P21505; -.
DR SMR; P21505; -.
DR REBASE; 2542; I-DmoI.
DR EvolutionaryTrace; P21505; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 2.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR004860; LAGLIDADG_2.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR PRINTS; PR00379; INTEIN.
DR SUPFAM; SSF55608; SSF55608; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Intron homing; Magnesium; Nuclease.
FT CHAIN 1..194
FT /note="Homing endonuclease I-DmoI"
FT /id="PRO_0000192791"
FT DOMAIN 14..147
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT ACT_SITE 21
FT ACT_SITE 117
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2VS7"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2VS7"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:2VS7"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2VS7"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4UN8"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2VS7"
SQ SEQUENCE 194 AA; 22609 MW; 99ED3354907F35A3 CRC64;
MHNNENVSGI SAYLLGLIIG DGGLYKLKYK GNRSEYRVVI TQKSENLIKQ HIAPLMQFLI
DELNVKSKIQ IVKGDTRYEL RVSSKKLYYY FANMLERIRL FNMREQIAFI KGLYVAEGDK
TLKRLRIWNK NKALLEIVSR WLNNLGVRNT IHLDDHRHGV YVLNISLRDR IKFVHTILSS
HLNPLPPERA GGYT
