EX1_HAEIN
ID EX1_HAEIN Reviewed; 473 AA.
AC P45188;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Exodeoxyribonuclease I;
DE Short=ExoI;
DE Short=Exonuclease I;
DE EC=3.1.11.1 {ECO:0000250|UniProtKB:P04995};
DE AltName: Full=DNA deoxyribophosphodiesterase;
DE Short=dRPase;
GN Name=sbcB; OrderedLocusNames=HI_1377;
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).
CC -!- FUNCTION: Degrades single-stranded DNA (ssDNA) in a highly processive
CC manner. Also functions as a DNA deoxyribophosphodiesterase that
CC releases deoxyribose-phosphate moieties following the cleavage of DNA
CC at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or
CC AP lyase. {ECO:0000250|UniProtKB:P04995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.1;
CC Evidence={ECO:0000250|UniProtKB:P04995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P04995};
CC Note=Binds 2 Mg(2+) ions per monomer. {ECO:0000250|UniProtKB:P04995};
CC -!- SUBUNIT: Monomer. Interacts with ssb (via C-terminus); this interaction
CC stimulates the exonuclease activity by recruiting the enzyme to its
CC substrate. {ECO:0000250|UniProtKB:P04995}.
CC -!- DOMAIN: The N-terminal exonuclease domain and the exonuclease C-
CC terminal domain form a central positively charged groove which binds
CC the DNA. {ECO:0000250|UniProtKB:P04995}.
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DR EMBL; L42023; AAC23023.1; -; Genomic_DNA.
DR PIR; E64120; E64120.
DR RefSeq; NP_439529.1; NC_000907.1.
DR RefSeq; WP_010869196.1; NC_000907.1.
DR STRING; 71421.HI_1377; -.
DR EnsemblBacteria; AAC23023; AAC23023; HI_1377.
DR KEGG; hin:HI_1377; -.
DR PATRIC; fig|71421.8.peg.1432; -.
DR eggNOG; COG2925; Bacteria.
DR HOGENOM; CLU_043508_1_1_6; -.
DR OMA; RDRPAQF; -.
DR PhylomeDB; P45188; -.
DR BioCyc; HINF71421:G1GJ1-1403-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0008852; F:exodeoxyribonuclease I activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1520.20; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR023607; Exodeoxyribonuclease_I.
DR InterPro; IPR034748; EXOI_C.
DR InterPro; IPR034747; EXOI_SH3.
DR InterPro; IPR038649; EXOI_SH3_sf.
DR InterPro; IPR013620; Exonuc_1_C.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR022894; Oligoribonuclease.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR11046; PTHR11046; 1.
DR Pfam; PF08411; Exonuc_X-T_C; 1.
DR Pfam; PF00929; RNase_T; 1.
DR PIRSF; PIRSF000977; Exodeoxyribonuclease_I; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS51785; EXOI_C; 1.
DR PROSITE; PS51784; EXOI_SH3; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..473
FT /note="Exodeoxyribonuclease I"
FT /id="PRO_0000087111"
FT DOMAIN 9..188
FT /note="Exonuclease"
FT /evidence="ECO:0000255"
FT DOMAIN 198..353
FT /note="ExoI SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01120"
FT DOMAIN 356..472
FT /note="ExoI C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01121"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 109
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 120
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 124
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 138
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 144
FT /note="Important for interaction with ssb"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 177
FT /note="Important for activity"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 210
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 253
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 302
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 366
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
FT SITE 369
FT /note="Interaction with single-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P04995"
SQ SEQUENCE 473 AA; 54388 MW; 734EA59A4F583965 CRC64;
MVKDFSFFIY DYESFGVNPA TDRPAQFAGI RTDADFNIIG EPIMFYCKQT NDYLPAPEAV
MVTGITPQEC NEKGLSEPEF AANILAEFSQ PNTCVMGYNN IRYDDEMTRY TFYRNFIEPY
EYSWKNGNSR WDLLDLVRAC YALRPEGINW AYDDDGMPSF RLEKLTKANS IEHENAHDAM
ADVYATIAMA KLIKEKQPKL FQYFFENRGK KEIEKLVDTG AMTPLVHVSG MLGNYRGNCT
WVAPLAWHPT NQNALIVCDL TGDIDNLLAK SADELRADLY TKKLELEERG VSSVPLKLVH
INKCPILAPA KTLLPETANR LGIDRQLCLD NLAKLRASFD IREKVADIFN EERQFASNDN
VETELYNGFF SNADKNNMAI LRSLPAEKLS EHGLAFEDKR ILELLFHYRA RHFYKTLTRA
EQIKWKKYRQ NKLEKSAVEF EASLQRLVEX HSDNSEKLSL LQQVYEYGIK LLG
