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RS2_ICTPU
ID   RS2_ICTPU               Reviewed;         277 AA.
AC   Q90YS3;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=40S ribosomal protein S2;
GN   Name=rps2;
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12095691; DOI=10.1016/s0378-1119(02)00595-4;
RA   Karsi A., Patterson A., Feng J., Liu Z.-J.;
RT   "Translational machinery of channel catfish: I. A transcriptomic approach
RT   to the analysis of 32 40S ribosomal protein genes and their expression.";
RL   Gene 291:177-186(2002).
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. Plays a role in the assembly and function of the 40S ribosomal
CC       subunit. Mutations in this protein affects the control of translational
CC       fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and
CC       ribosome assembly. {ECO:0000250|UniProtKB:P25443}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000305}.
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DR   EMBL; AF402809; AAK95183.1; -; mRNA.
DR   RefSeq; NP_001187067.1; NM_001200138.1.
DR   AlphaFoldDB; Q90YS3; -.
DR   SMR; Q90YS3; -.
DR   PRIDE; Q90YS3; -.
DR   GeneID; 100304556; -.
DR   KEGG; ipu:100304556; -.
DR   CTD; 6187; -.
DR   Proteomes; UP000221080; Chromosome 2.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01020; uS5_euk_arch; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   2: Evidence at transcript level;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..277
FT                   /note="40S ribosomal protein S2"
FT                   /id="PRO_0000131676"
FT   DOMAIN          87..150
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT   REGION          18..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   277 AA;  30408 MW;  31D1C04294FFF69C CRC64;
     MADDAVVEEG SVEVSALAAG RPSWSWQRPG ERARTPGRKA EDKEWVPVTK LGRLVKDMKI
     KSLEEIYLYS LPIKESEIID FFLGSALKDE VLKIMPVQKQ TRAGQRTRFK AFVAIGDYNG
     HVGLGVKCSK EVATAIRGAI ILAKLSIIPV RRGYWGNKIG KPHTVPCKVT GRCGSVLVRL
     IPAPRGTGIV SAPVPKKLLM MAGIDDCYTS ARGCTATLGN FAKATFDAIS KTYSYLTPDL
     WKETVFTKSP YQEFTDHLAK THTRVSVQRT QAAVQPS
 
 
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