DN7A_SACS2
ID DN7A_SACS2 Reviewed; 64 AA.
AC P61991; O59631; P80170; Q9UWI8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DNA-binding protein 7a {ECO:0000305};
DE AltName: Full=7 kDa DNA-binding protein a;
DE AltName: Full=Endoribonuclease P2 {ECO:0000303|PubMed:8425540};
DE EC=3.1.27.-;
DE AltName: Full=p7ss;
GN Name=sso7a1; Synonyms=sso7d-2; OrderedLocusNames=SSO9180;
GN and
GN Name=sso7a2; Synonyms=sso7d-3; OrderedLocusNames=SSO9535;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP PROTEIN SEQUENCE OF 2-63, FUNCTION AS A RNASE, METHYLATION AT LYS-5 AND
RP LYS-7, AND SUBUNIT.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8425540; DOI=10.1111/j.1432-1033.1993.tb19899.x;
RA Fusi P., Tedeschi G., Aliverti A., Ronchi S., Tortora P., Guerritore A.;
RT "Ribonucleases from the extreme thermophilic archaebacterium S.
RT solfataricus.";
RL Eur. J. Biochem. 211:305-310(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-40.
RX PubMed=7887965; DOI=10.1006/bbrc.1995.1304;
RA Faraone-Mennella M.R., Farina B.;
RT "In the thermophilic archaeon Sulfolobus solfataricus a DNA-binding protein
RT is in vitro (ADPribosyl)ated.";
RL Biochem. Biophys. Res. Commun. 208:55-62(1995).
CC -!- FUNCTION: Can constrain negative DNA supercoils. May be involved in
CC maintaining the integrity of the genome at high temperature (By
CC similarity). Has RNase activity. Has a narrow substrate specificity;
CC the cleavage products are 3'-phosphooligonucleotides (PubMed:8425540).
CC {ECO:0000250|UniProtKB:P61990, ECO:0000269|PubMed:8425540}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8425540}.
CC -!- PTM: Lys-5 and Lys-7 were found to be 60% monomethylated.
CC {ECO:0000269|PubMed:8425540}.
CC -!- SIMILARITY: Belongs to the 7 kDa DNA-binding/endoribonuclease P2
CC family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42090.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK42212.1; -; Genomic_DNA.
DR PIR; E90369; E90369.
DR RefSeq; WP_009992021.1; NC_002754.1.
DR PDB; 1B4O; NMR; -; A=2-63.
DR PDB; 1JIC; NMR; -; A=2-63.
DR PDB; 1SSO; NMR; -; A=2-63.
DR PDB; 2CVR; NMR; -; A=2-63.
DR PDB; 6QBA; X-ray; 1.80 A; B=2-62.
DR PDBsum; 1B4O; -.
DR PDBsum; 1JIC; -.
DR PDBsum; 1SSO; -.
DR PDBsum; 2CVR; -.
DR PDBsum; 6QBA; -.
DR AlphaFoldDB; P61991; -.
DR BMRB; P61991; -.
DR SMR; P61991; -.
DR iPTMnet; P61991; -.
DR EnsemblBacteria; AAK42090; AAK42090; SSO9180.
DR EnsemblBacteria; AAK42212; AAK42212; SSO9535.
DR GeneID; 7812726; -.
DR KEGG; sso:SSO9180; -.
DR KEGG; sso:SSO9535; -.
DR PATRIC; fig|273057.12.peg.1957; -.
DR eggNOG; arCOG05888; Archaea.
DR HOGENOM; CLU_2929990_0_0_2; -.
DR OMA; MATKIKF; -.
DR BRENDA; 4.6.1.18; 6163.
DR EvolutionaryTrace; P61991; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR003212; DNA-bd_7kDa_arc.
DR Pfam; PF02294; 7kD_DNA_binding; 1.
DR PIRSF; PIRSF036912; Sac7; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Hydrolase;
KW Methylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7887965,
FT ECO:0000269|PubMed:8425540"
FT CHAIN 2..64
FT /note="DNA-binding protein 7a"
FT /id="PRO_0000213077"
FT MOD_RES 5
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:8425540"
FT MOD_RES 7
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:8425540"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6QBA"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:6QBA"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:6QBA"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:6QBA"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6QBA"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1B4O"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6QBA"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6QBA"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:6QBA"
SQ SEQUENCE 64 AA; 7279 MW; 0E4BA126FCCF84DD CRC64;
MATVKFKYKG EEKQVDISKI KKVWRVGKMI SFTYDEGGGK TGRGAVSEKD APKELLQMLE
KQKK
