位置:首页 > 蛋白库 > ORN_XANCP
ORN_XANCP
ID   ORN_XANCP               Reviewed;         194 AA.
AC   Q8P8S1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Oligoribonuclease {ECO:0000255|HAMAP-Rule:MF_00045};
DE            EC=3.1.15.- {ECO:0000255|HAMAP-Rule:MF_00045};
GN   Name=orn {ECO:0000255|HAMAP-Rule:MF_00045}; OrderedLocusNames=XCC2168;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC       oligoribonucleotides. {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC       {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008922; AAM41448.1; -; Genomic_DNA.
DR   RefSeq; NP_637524.1; NC_003902.1.
DR   RefSeq; WP_011037314.1; NC_003902.1.
DR   PDB; 2GBZ; X-ray; 2.30 A; A=1-194.
DR   PDBsum; 2GBZ; -.
DR   AlphaFoldDB; Q8P8S1; -.
DR   SMR; Q8P8S1; -.
DR   STRING; 340.xcc-b100_2013; -.
DR   EnsemblBacteria; AAM41448; AAM41448; XCC2168.
DR   KEGG; xcc:XCC2168; -.
DR   PATRIC; fig|190485.4.peg.2315; -.
DR   eggNOG; COG1949; Bacteria.
DR   HOGENOM; CLU_064761_2_0_6; -.
DR   OMA; AFFHYRN; -.
DR   EvolutionaryTrace; Q8P8S1; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd06135; Orn; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00045; Oligoribonuclease; 1.
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; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Exonuclease; Hydrolase; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..194
FT                   /note="Oligoribonuclease"
FT                   /id="PRO_0000111084"
FT   DOMAIN          11..174
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
FT   STRAND          10..19
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   STRAND          28..37
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           55..59
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           74..80
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           85..96
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           112..122
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           124..129
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           137..147
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           163..178
FT                   /evidence="ECO:0007829|PDB:2GBZ"
FT   HELIX           182..185
FT                   /evidence="ECO:0007829|PDB:2GBZ"
SQ   SEQUENCE   194 AA;  21808 MW;  729559F4AD0740AB CRC64;
     MADNVAGNDR LIWIDLEMTG LDTDRDSIIE IATIVTDAQL NVLAEGPELA IAHSLETLEA
     MDEWNRNQHR RSGLWQRVLD SQVTHAQAEA QTVAFLSEWI RAGASPMCGN SICQDRRFLH
     RQMSRLERYF HYRNLDVSTI KELARRWAPA VASGFAKSSA HTALSDVRDS IDELRHYRQF
     MGTLGGDNGG GVQN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024