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Y1683_ARCFU
ID   Y1683_ARCFU             Reviewed;         156 AA.
AC   O28590;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=VapC ribonuclease AF_1683;
DE            Short=RNase AF_1683;
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Putative toxin AF_1683;
GN   OrderedLocusNames=AF_1683;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RG   Midwest center for structural genomics (MCSG);
RT   "The structure of gene product AF1683 from Archaeoglobus fulgidus.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An
CC       RNase. {ECO:0000255|HAMAP-Rule:MF_00265}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; AE000782; AAB89566.1; -; Genomic_DNA.
DR   PIR; B69460; B69460.
DR   RefSeq; WP_010879179.1; NC_000917.1.
DR   PDB; 1W8I; X-ray; 2.10 A; A=1-156.
DR   PDBsum; 1W8I; -.
DR   AlphaFoldDB; O28590; -.
DR   SMR; O28590; -.
DR   STRING; 224325.AF_1683; -.
DR   EnsemblBacteria; AAB89566; AAB89566; AF_1683.
DR   GeneID; 24795426; -.
DR   KEGG; afu:AF_1683; -.
DR   eggNOG; arCOG04502; Archaea.
DR   HOGENOM; CLU_1682583_0_0_2; -.
DR   OrthoDB; 96415at2157; -.
DR   EvolutionaryTrace; O28590; -.
DR   Proteomes; UP000002199; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   HAMAP; MF_00265; VapC_Nob1; 1.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR022907; VapC_family.
DR   Pfam; PF01850; PIN; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..156
FT                   /note="VapC ribonuclease AF_1683"
FT                   /id="PRO_0000128047"
FT   DOMAIN          4..125
FT                   /note="PINc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         6
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           7..14
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           21..32
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   TURN            33..36
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           43..55
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           60..67
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   STRAND          71..76
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           101..113
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   TURN            131..136
FT                   /evidence="ECO:0007829|PDB:1W8I"
FT   HELIX           139..151
FT                   /evidence="ECO:0007829|PDB:1W8I"
SQ   SEQUENCE   156 AA;  17841 MW;  F6B4286D1C96A6B4 CRC64;
     MAALIDTGIF FGFYSLKDVH HMDSVAIVVH AVEGKWGRLF VTNHILDETL TLLKYKKLPA
     DKFLEGFVES GVLNIIYTDD EVERKALEVF KARVYEKGFS YTDAISEVVA EELKLKLISY
     DSRFSLPTIG RDYWKSLDES ERKRISAILR EKGIDG
 
 
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