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NOB1_PYRHO
ID   NOB1_PYRHO              Reviewed;         161 AA.
AC   O58440;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Endoribonuclease Nob1;
DE            Short=RNase Nob1;
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Endonuclease VapC6;
DE   AltName: Full=Putative toxin VapC6 {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=nob1; Synonyms=vapC6; OrderedLocusNames=PH0709;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   POSSIBLE FUNCTION.
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=15718296; DOI=10.1093/nar/gki201;
RA   Pandey D.P., Gerdes K.;
RT   "Toxin-antitoxin loci are highly abundant in free-living but lost from
RT   host-associated prokaryotes.";
RL   Nucleic Acids Res. 33:966-976(2005).
RN   [3]
RP   STRUCTURE BY NMR, FUNCTION AS AN ENDORIBONUCLEASE, COFACTOR, RNA-BINDING,
RP   DOMAIN, AND MUTAGENESIS OF ASP-12; SER-79; ASP-100 AND ARG-115.
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=22156373; DOI=10.1093/nar/gkr1186;
RA   Veith T., Martin R., Wurm J.P., Weis B.L., Duchardt-Ferner E.,
RA   Safferthal C., Hennig R., Mirus O., Bohnsack M.T., Wohnert J., Schleiff E.;
RT   "Structural and functional analysis of the archaeal endonuclease Nob1.";
RL   Nucleic Acids Res. 40:3259-3274(2012).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system
CC       (Potential). Processes pre-16S-rRNA at its 3' end (the D-site) to yield
CC       the mature 3' end. {ECO:0000269|PubMed:22156373, ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:22156373};
CC       Note=Manganese; magnesium does not support nuclease activity.
CC       {ECO:0000269|PubMed:22156373};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:22156373};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22156373};
CC   -!- DOMAIN: Has 2 structurally independent domains; the N-terminal PINc
CC       domain which binds Mn(2+), rRNA substrate and probably has
CC       endoribonuclease activity, and the C-terminal zinc ribbon domain which
CC       also binds rRNA substrate. {ECO:0000269|PubMed:22156373}.
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; BA000001; BAA29800.1; -; Genomic_DNA.
DR   PIR; F71117; F71117.
DR   RefSeq; WP_010884804.1; NC_000961.1.
DR   PDB; 2LCQ; NMR; -; A=1-161.
DR   PDBsum; 2LCQ; -.
DR   AlphaFoldDB; O58440; -.
DR   BMRB; O58440; -.
DR   SMR; O58440; -.
DR   STRING; 70601.3257117; -.
DR   EnsemblBacteria; BAA29800; BAA29800; BAA29800.
DR   GeneID; 1443039; -.
DR   KEGG; pho:PH0709; -.
DR   eggNOG; arCOG00721; Archaea.
DR   OMA; GCGREFD; -.
DR   OrthoDB; 102178at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   CDD; cd09876; PIN_Nob1-like; 1.
DR   HAMAP; MF_00265; VapC_Nob1; 1.
DR   InterPro; IPR039907; NOB1.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR033411; Ribonuclease_PIN.
DR   InterPro; IPR022907; VapC_family.
DR   PANTHER; PTHR12814; PTHR12814; 2.
DR   Pfam; PF17146; PIN_6; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; Toxin-antitoxin system;
KW   Zinc.
FT   CHAIN           1..161
FT                   /note="Endoribonuclease Nob1"
FT                   /id="PRO_0000156048"
FT   DOMAIN          7..105
FT                   /note="PINc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   REGION          120..125
FT                   /note="Flexible linker"
FT   REGION          126..161
FT                   /note="Zinc ribbon"
FT   BINDING         12
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   MUTAGEN         12
FT                   /note="D->N: No cleavage of pre-16S-rRNA."
FT                   /evidence="ECO:0000269|PubMed:22156373"
FT   MUTAGEN         79
FT                   /note="S->A: Reduced cleavage of pre-16S-rRNA."
FT                   /evidence="ECO:0000269|PubMed:22156373"
FT   MUTAGEN         100
FT                   /note="D->N: Non-specific cleavage pre-16S-rRNA, maybe due
FT                   to altered substrate-binding."
FT                   /evidence="ECO:0000269|PubMed:22156373"
FT   MUTAGEN         115
FT                   /note="R->A: Non-specific cleavage pre-16S-rRNA, maybe due
FT                   to altered substrate-binding."
FT                   /evidence="ECO:0000269|PubMed:22156373"
FT   HELIX           13..18
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   HELIX           38..48
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   HELIX           59..72
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   HELIX           101..109
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:2LCQ"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:2LCQ"
SQ   SEQUENCE   161 AA;  17972 MW;  BDB3A1AA59912AE3 CRC64;
     MLRNLKKTLV LDSSVFIQGI DIEGYTTPSV VEEIKDRESK IFLESLISAG KVKIAEPSKE
     SIDRIIQVAK ETGEVNELSK ADIEVLALAY ELKGEIFSDD YNVQNIASLL GLRFRTLKRG
     IKKVIKWRYV CIGCGRKFST LPPGGVCPDC GSKVKLIPRK R
 
 
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