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Database: UniProt
Entry: A0A061E838_THECC
LinkDB: A0A061E838_THECC
Original site: A0A061E838_THECC 
ID   A0A061E838_THECC        Unreviewed;       156 AA.
AC   A0A061E838;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Ribosomal protein S27a / Ubiquitin family protein {ECO:0000313|EMBL:EOY00532.1};
GN   ORFNames=TCM_010413 {ECO:0000313|EMBL:EOY00532.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY00532.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY00532.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(2013).
CC   -!- FUNCTION: Component of the 40S subunit of the ribosome.
CC       {ECO:0000256|ARBA:ARBA00002225}.
CC   -!- SUBUNIT: Part of the 40S ribosomal subunit.
CC       {ECO:0000256|ARBA:ARBA00035123}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000256|ARBA:ARBA00008373}.
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DR   EMBL; CM001880; EOY00532.1; -; Genomic_DNA.
DR   RefSeq; XP_017969957.1; XM_018114468.1.
DR   AlphaFoldDB; A0A061E838; -.
DR   SMR; A0A061E838; -.
DR   STRING; 3641.A0A061E838; -.
DR   EnsemblPlants; EOY00532; EOY00532; TCM_010413.
DR   EnsemblPlants; Tc02v2_t022140.1; Tc02v2_p022140.1; Tc02v2_g022140.
DR   GeneID; 18609501; -.
DR   Gramene; EOY00532; EOY00532; TCM_010413.
DR   Gramene; Tc02v2_t022140.1; Tc02v2_p022140.1; Tc02v2_g022140.
DR   KEGG; tcc:18609501; -.
DR   eggNOG; KOG0004; Eukaryota.
DR   HOGENOM; CLU_010412_2_0_1; -.
DR   InParanoid; A0A061E838; -.
DR   OMA; GVFMAFH; -.
DR   OrthoDB; 312211at2759; -.
DR   Proteomes; UP000026915; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR   GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   Gene3D; 6.20.50.150; -; 1.
DR   InterPro; IPR002906; Ribosomal_eS31.
DR   InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR10666:SF468; POLYUBIQUITIN-LIKE; 1.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   Pfam; PF01599; Ribosomal_S27; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01402; Ribosomal_S27; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000313|EMBL:EOY00532.1}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
SQ   SEQUENCE   156 AA;  17702 MW;  1FD5C770FFD64DAD CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKKKKVKL AVLQFYKVDD SGKVQRLRKE
     CPNAECGAGT FMANHFDRHY CGKCGLTYVY QKAGGD
//
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