KTI12_ORYSJ
ID KTI12_ORYSJ Reviewed; 301 AA.
AC B9GAG9; C7J842;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein KTI12 homolog {ECO:0000305};
DE Short=OsKTI12 {ECO:0000305};
DE AltName: Full=Protein DEFORMED ROOTS AND LEAVES 1 {ECO:0000303|PubMed:25518926};
DE Short=OsDRL1 {ECO:0000303|PubMed:25518926};
GN Name=KTI12 {ECO:0000305}; Synonyms=DRL1 {ECO:0000303|PubMed:25518926};
GN OrderedLocusNames=Os11g0312782 {ECO:0000312|EMBL:BAH95225.1};
GN ORFNames=OsJ_33743 {ECO:0000312|EMBL:EEE52025.1};
OS Oryza sativa subsp. japonica (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=39947 {ECO:0000312|Proteomes:UP000059680};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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 [5]
RP FUNCTION.
RX PubMed=25518926; DOI=10.14348/molcells.2015.2297;
RA Jun S.E., Cho K.-H., Hwang J.-Y., Abdel-Fattah W., Hammermeister A.,
RA Schaffrath R., Bowman J.L., Kim G.-T.;
RT "Comparative analysis of the conserved functions of Arabidopsis DRL1 and
RT yeast KTI12.";
RL Mol. Cells 38:243-250(2015).
CC -!- FUNCTION: Elongator complex-associated factor that is not a structural
CC subunit but rather transiently contacts the complex (PubMed:25518926).
CC Regulates both meristem activity and organ growth; acts as a positive
CC regulator of adaxial leaf patterning. Required for an early step in
CC synthesis of 5-carbamoylmethyl (ncm5) groups present on uridines
CC (ncm5U) at the wobble position in tRNA (By similarity).
CC {ECO:0000250|UniProtKB:Q9LMH0, ECO:0000269|PubMed:25518926}.
CC -!- SUBUNIT: Interacts with the elongator complex (By similarity). Binds to
CC calmodulin in a calcium-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P34253, ECO:0000250|UniProtKB:Q9LMH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P34253}. Nucleus
CC {ECO:0000250|UniProtKB:P34253}.
CC -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH95225.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP008217; BAH95225.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000148; EEE52025.1; -; Genomic_DNA.
DR RefSeq; XP_015615301.1; XM_015759815.1.
DR AlphaFoldDB; B9GAG9; -.
DR SMR; B9GAG9; -.
DR STRING; 4530.OS11T0312340-00; -.
DR PRIDE; B9GAG9; -.
DR GeneID; 9270154; -.
DR KEGG; osa:9270154; -.
DR eggNOG; KOG3062; Eukaryota.
DR OrthoDB; 1300128at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0080178; P:5-carbamoylmethyl uridine residue modification; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045106; Kti12.
DR InterPro; IPR013641; KTI12/PSTK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12435; PTHR12435; 1.
DR Pfam; PF08433; KTI12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; tRNA processing.
FT CHAIN 1..301
FT /note="Protein KTI12 homolog"
FT /id="PRO_0000432191"
FT REGION 262..275
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 301 AA; 33438 MW; 71EC5F004C80671E CRC64;
MALVVICGQP CSGKSAAAAC LAAALCSSTS DLTVRIIDES SLHLGRNDSY KDMVVEKNLR
GVLRSEVDRS VSRDSIIVVD SLNNIKGYRY ELWCLARASG IRYCVLFCDT EVDHCREWNT
KRQEKGEPTY DNNIFDDLVS RFEKPDRRNR WDSPLFELFP SRDGVMESSP VIAEAVSYLT
KKVDSKTRDV KVLQPTIATQ TARTTEANSL YEMDKATQEV INAIVEAQSC GLGLPVNKIS
LGPDLPTICL QRSVGLPELR SLRRTFIKLA GQYSLSGPPP PADADSATRM FVDYLNREIS
S
