PETS_ORYSI
ID PETS_ORYSI Reviewed; 1123 AA.
AC A2ZLC1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Polyprotein of EF-Ts, chloroplastic {ECO:0000303|PubMed:15548736};
DE Contains:
DE RecName: Full=Plastid-specific ribosomal protein-7, chloroplastic {ECO:0000303|PubMed:15548736};
DE Contains:
DE RecName: Full=Elongation factor Ts, chloroplastic {ECO:0000303|PubMed:15548736};
DE Short=EF-Ts {ECO:0000303|PubMed:15548736};
DE Flags: Precursor;
GN Name=PETs {ECO:0000303|PubMed:15548736};
GN Synonyms=EFTS {ECO:0000303|PubMed:15548736},
GN PSRP-7 {ECO:0000303|PubMed:15548736};
GN ORFNames=OsI_38621 {ECO:0000312|EMBL:EAY83405.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2]
RP GENE FAMILY.
RX PubMed=15548736; DOI=10.1105/tpc.104.026708;
RA Beligni M.V., Yamaguchi K., Mayfield S.P.;
RT "Chloroplast elongation factor ts pro-protein is an evolutionarily
RT conserved fusion with the s1 domain-containing plastid-specific ribosomal
RT protein-7.";
RL Plant Cell 16:3357-3369(2004).
CC -!- FUNCTION: [Elongation factor Ts, chloroplastic]: Associates with the
CC EF-Tu.GDP complex and induces the exchange of GDP to GTP (By
CC similarity). It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex
CC up to the GTP hydrolysis stage on the ribosome (By similarity).
CC {ECO:0000250|UniProtKB:A8J637}.
CC -!- FUNCTION: [Plastid-specific ribosomal protein-7, chloroplastic]: Binds
CC to psbD and psbA 5'-untranslated regions (UTRs) in vitro.
CC {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBUNIT: [Plastid-specific ribosomal protein-7, chloroplastic]:
CC Component of the chloroplast ribosome 30S and 70S subunits, as well as
CC polysomes. {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBUNIT: [Polyprotein of EF-Ts, chloroplastic]: Component of the
CC chloroplast ribosome 70S subunit, and at low levels, present in
CC polysomes. {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBUNIT: [Elongation factor Ts, chloroplastic]: Associates transiently
CC with chloroplast polysomes. {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:A8J637}.
CC -!- SIMILARITY: [Elongation factor Ts, chloroplastic]: Belongs to the EF-Ts
CC family. {ECO:0000305}.
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DR EMBL; CM000137; EAY83405.1; -; Genomic_DNA.
DR AlphaFoldDB; A2ZLC1; -.
DR SMR; A2ZLC1; -.
DR STRING; 39946.A2ZLC1; -.
DR PRIDE; A2ZLC1; -.
DR EnsemblPlants; BGIOSGA037533-TA; BGIOSGA037533-PA; BGIOSGA037533.
DR Gramene; BGIOSGA037533-TA; BGIOSGA037533-PA; BGIOSGA037533.
DR HOGENOM; CLU_012395_0_0_1; -.
DR OMA; MQVAAYP; -.
DR Proteomes; UP000007015; Chromosome 12.
DR GO; GO:0009507; C:chloroplast; ISS:UniProtKB.
DR GO; GO:0043253; C:chloroplast ribosome; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0061770; F:translation elongation factor binding; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 2.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 2.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 2.
DR Pfam; PF00889; EF_TS; 2.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF50249; SSF50249; 2.
DR SUPFAM; SSF54713; SSF54713; 2.
DR TIGRFAMs; TIGR00116; tsf; 3.
DR PROSITE; PS01126; EF_TS_1; 2.
DR PROSITE; PS01127; EF_TS_2; 2.
DR PROSITE; PS50126; S1; 2.
PE 3: Inferred from homology;
KW Chloroplast; Elongation factor; Plastid; Protein biosynthesis;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..73
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 74..1123
FT /note="Polyprotein of EF-Ts, chloroplastic"
FT /id="PRO_0000449228"
FT CHAIN 74..686
FT /note="Plastid-specific ribosomal protein-7, chloroplastic"
FT /id="PRO_0000449229"
FT CHAIN 687..1123
FT /note="Elongation factor Ts, chloroplastic"
FT /id="PRO_0000449230"
FT DOMAIN 143..212
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 263..331
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 68..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 121088 MW; AF72A787E9CB458B CRC64;
MTPVVHCSVG NISLFHIGSF RPSHEIQIRR FRSTERYSRV PSRRLLQPQR AFNLISIYKR
SSWSSARRPR TLSAATVGTD VTVEDPNPPP SGETSEESSE DTAPDTAEAS EQAEASTSSI
PKAGRNIRKS EMPPLNDEDL VPGASFTGKV RSIKPFGVFV DIGAFTEGLV HISRVSDGFV
KDISSLFTVG QEVSVRLVEA NKETGRISLT MRTGGDYVKP KTETPKAASG GRNTTATTSR
GSPRQTRERD EAKSMGETNY VQGQFLDGVV KNSTRAGSFV TLPDGSEGFL PREEEAVALF
TLIGHSALEV GQQVRVKVLN VVRGQVTLTM KEGEDDEEDL ASLNTQLKQG WSRGTNAFEL
AFRRNKEISA FLDQREKIIV PDVQEAAVAS VGTELDAEVG IEQSPGKEPE TGNAESVAID
SSITEVKETD SIAAVEKDSE ISKTESVETA SSVVISEDDS TVDGKLVEPT ASVSATETEI
KEDSSEGSVT TEPTEAASTE FVTAVVEESA PTASSVETSE DDSTVDDKLV EPTASVSATE
AESKEDSSEG SVASTESVTA VVEESAPVSS VAIEVPAPEA SEASAQEIIE DSTTVEGAAD
DQTVESDSPP PEGVELSSNG APDSSIAEDK PDEPEESLIV EEVPVTASSE SEDKEPAAVP
EEVAASSEKT ADVAVAGAEA STATATISPA LVKQLREATG AGMMDCKKAL AESGGDIEKA
QEFLRKKGLA AADKRAGRAT AEGRIGSYIH DSRIGVLIEV NCETDFVSRG DIFKELVDDL
AMQVAACPQV QYISLDDVPE EVMKKETELE MQREDLLSKP EQIRSKIVEG RVKKRLGEYA
LLEQPFIKND KVTISEWVKQ TIATIGENMK VNRFVRYNLG EGLEKRSQDF AAEVAAQTAA
KAPPAAPPKD DKPEETAETE EKKPAVAISA ALVKQLRDET GAGMMDCKKA LAETGGDIQQ
AQEFLRKKGL SSADKKSSRL TAEGLIGAYI HDNRIGCMIE INSETDFVAR NEKFKELVND
LAMQVVACPQ VEYVSIEDIP ESVVIKEKEI EMQREDLQSK PENIREKIVE GRISKRLGVL
ALLEQPFIKD DSKTVKDLVK ETIATLGENI KVRRFTRYTL GEN
