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ORN_NEIMF
ID   ORN_NEIMF               Reviewed;         187 AA.
AC   A1KS35;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=NMC0355;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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}.
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DR   EMBL; AM421808; CAM09665.1; -; Genomic_DNA.
DR   RefSeq; WP_002221521.1; NC_008767.1.
DR   AlphaFoldDB; A1KS35; -.
DR   SMR; A1KS35; -.
DR   PRIDE; A1KS35; -.
DR   EnsemblBacteria; CAM09665; CAM09665; NMC0355.
DR   KEGG; nmc:NMC0355; -.
DR   HOGENOM; CLU_064761_2_0_4; -.
DR   OMA; AFFHYRN; -.
DR   Proteomes; UP000002286; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN           1..187
FT                   /note="Oligoribonuclease"
FT                   /id="PRO_1000004267"
FT   DOMAIN          7..170
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
SQ   SEQUENCE   187 AA;  21791 MW;  BA75A63BFF32BFA3 CRC64;
     MQDKNNLCWL DMEMTGLNPE TDRIIEVAMI ITDSDLNVLA QSEVYAVHQS DELLDNMDEW
     NTATHGRTGL TQRVRESLHT EAEVEQKLLD FMSEWVPGRA TPMCGNSIHQ DRRFMVKYMP
     KLENYFHYRN LDVSTLKELA KRWNPSVAKS VVKRGSHKAL DDILESIEEM RHYREHFLIS
     APRAEAQ
 
 
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