ID   KTI12_ORYSI             Reviewed;         301 AA.
AC   B8BK80;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein KTI12 homolog {ECO:0000305};
DE            Short=OsKTI12 {ECO:0000305};
GN   ORFNames=OsI_35919 {ECO:0000312|EMBL:EEC68066.1};
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 {ECO:0000312|Proteomes:UP000007015};
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).
CC   -!- FUNCTION: Elongator complex-associated factor that is not a structural
CC       subunit but rather transiently contacts the complex (By similarity).
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:P34253, ECO:0000250|UniProtKB:Q9LMH0}.
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=EEC68066.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CM000136; EEC68066.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B8BK80; -.
DR   SMR; B8BK80; -.
DR   STRING; 39946.B8BK80; -.
DR   HOGENOM; CLU_027147_1_0_1; -.
DR   Proteomes; UP000007015; Chromosome 11.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033588; C:elongator holoenzyme complex; ISS: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; ISS:UniProtKB.
DR   GO; GO:0006400; P:tRNA modification; ISS: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_0000432192"
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