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RSSA_MACHI
ID   RSSA_MACHI              Reviewed;         308 AA.
AC   A2I3Z2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03015};
OS   Maconellicoccus hirsutus (Pink hibiscus mealybug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Coccoidea;
OC   Pseudococcidae; Maconellicoccus.
OX   NCBI_TaxID=177089;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hunter W.B., Hunnicutt L.E.;
RT   "Ribosomal proteins of the pink hibiscus mealybug, Maconellicoccus
RT   hirsutus.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC       ribosomal subunit. Required for the processing of the 20S rRNA-
CC       precursor to mature 18S rRNA in a late step of the maturation of 40S
CC       ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (28S, 5.8S and 5S). Interacts with ribosomal protein S21.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR   EMBL; EF070495; ABM55561.1; -; mRNA.
DR   AlphaFoldDB; A2I3Z2; -.
DR   SMR; A2I3Z2; -.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd01425; RPS2; 1.
DR   HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR   InterPro; IPR032281; 40S_SA_C.
DR   InterPro; IPR001865; Ribosomal_S2.
DR   InterPro; IPR018130; Ribosomal_S2_CS.
DR   InterPro; IPR027498; Ribosomal_S2_euk.
DR   InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR   InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR   PANTHER; PTHR11489; PTHR11489; 1.
DR   Pfam; PF16122; 40S_SA_C; 1.
DR   Pfam; PF00318; Ribosomal_S2; 2.
DR   PRINTS; PR00395; RIBOSOMALS2.
DR   SUPFAM; SSF52313; SSF52313; 1.
DR   TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR   PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR   PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT   CHAIN           2..308
FT                   /note="40S ribosomal protein SA"
FT                   /id="PRO_0000371592"
FT   REGION          283..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   308 AA;  33871 MW;  73322BB253C6CB6A CRC64;
     MSGGLEILKL TEGDITKMLS ANTHLGAENT NFQMEQYIYK RRSDGINIFN LRKTWEKLLL
     AARAIAAVEH AAEIFVISSR PFGQRAVLKF AAHTGATPIA GRFTPGAFTN QIQAAFREPR
     LLVVTDPAED KQPITEASYV NIPVIAFCNT DSPLRYVDIA IPCNTKSAHS IGLMWWLLAR
     EVLRLRGSIP RDGKWDVVVD LFFYRDPEEV EKEDQAAKEA AAAVPTPKQE PLEYGVTGAS
     EWTEAITEQG GIQPSWADES LPGQPTVFPA SNIDEWNTTA QPAAAVKPSE EWNAGRSGNW
     GTSATGNW
 
 
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