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RRP4_AERPE
ID   RRP4_AERPE              Reviewed;         235 AA.
AC   Q9YC02;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Exosome complex component Rrp4 {ECO:0000255|HAMAP-Rule:MF_00623};
GN   Name=rrp4 {ECO:0000255|HAMAP-Rule:MF_00623}; OrderedLocusNames=APE_1448;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS).
RA   Murayama K., Kato-Murayama M., Takemoto C., Terada T., Shirouzu M.,
RA   Yokoyama S.;
RT   "Crystal structure of putative exosome complex RNA-binding protein.";
RL   Submitted (MAY-2007) to the PDB data bank.
CC   -!- FUNCTION: Non-catalytic component of the exosome, which is a complex
CC       involved in RNA degradation. Increases the RNA binding and the
CC       efficiency of RNA degradation. Confers strong poly(A) specificity to
CC       the exosome. {ECO:0000255|HAMAP-Rule:MF_00623}.
CC   -!- SUBUNIT: Component of the archaeal exosome complex. Forms a trimer of
CC       Rrp4 and/or Csl4 subunits. The trimer associates with a hexameric ring-
CC       like arrangement composed of 3 Rrp41-Rrp42 heterodimers.
CC       {ECO:0000255|HAMAP-Rule:MF_00623}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00623}.
CC   -!- SIMILARITY: Belongs to the RRP4 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00623}.
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DR   EMBL; BA000002; BAA80446.1; -; Genomic_DNA.
DR   PIR; H72623; H72623.
DR   PDB; 2Z0S; X-ray; 3.20 A; A=1-235.
DR   PDBsum; 2Z0S; -.
DR   AlphaFoldDB; Q9YC02; -.
DR   SMR; Q9YC02; -.
DR   STRING; 272557.APE_1448; -.
DR   EnsemblBacteria; BAA80446; BAA80446; APE_1448.
DR   KEGG; ape:APE_1448; -.
DR   eggNOG; arCOG00678; Archaea.
DR   OMA; NWFVDIN; -.
DR   EvolutionaryTrace; Q9YC02; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR   GO; GO:0008143; F:poly(A) binding; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   HAMAP; MF_00623; Exosome_Rrp4; 1.
DR   InterPro; IPR026699; Exosome_RNA_bind1/RRP40/RRP4.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR023474; Rrp4.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR21321; PTHR21321; 1.
DR   Pfam; PF15985; KH_6; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   PROSITE; PS50126; S1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Exosome; Reference proteome; RNA-binding.
FT   CHAIN           1..235
FT                   /note="Exosome complex component Rrp4"
FT                   /id="PRO_0000050144"
FT   DOMAIN          67..139
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   DOMAIN          149..205
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00623"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           96..100
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          120..128
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          148..153
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           168..177
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           196..211
FT                   /evidence="ECO:0007829|PDB:2Z0S"
FT   HELIX           219..232
FT                   /evidence="ECO:0007829|PDB:2Z0S"
SQ   SEQUENCE   235 AA;  26061 MW;  70A79A5EB0BF8CE7 CRC64;
     MSSERQLAGR IVVPGEPLPE EVEASPPYVI DYKGVKRATV VGLLREKGDG GGRAFVKLKE
     IYVPQAGDVV IGLIQSVGIM NWFVDINSPY VAVLSVQDFL GRPFNPAVDD MQSLLKVGDY
     IKAKVVAFDK TRSPLLTVQG EGLGRIVRGK IVEISPAKVP RVIGRKMSML KTLEEKTECK
     IFVARNGRIH LECPNEDLEA IAVMAIKIID EEAYTSGLTK RIIKFIEEER RIREV
 
 
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