ID   ELP1_XENLA              Reviewed;        1170 AA.
AC   Q2TAQ1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Putative elongator complex protein 1;
DE            Short=ELP1;
DE   AltName: Full=IkappaB kinase complex-associated protein;
DE            Short=IKK complex-associated protein;
GN   Name=elp1; Synonyms=ikbkap;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the elongator complex which is required for
CC       multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC       uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC       (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC       catalyzes formation of carboxymethyluridine in the wobble base at
CC       position 34 in tRNAs (By similarity). ELP1 binds to tRNA, mediating
CC       interaction of the elongator complex with tRNA (By similarity).
CC       {ECO:0000250|UniProtKB:O95163, ECO:0000250|UniProtKB:Q06706}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000250|UniProtKB:O95163}.
CC   -!- SUBUNIT: Homodimer. Component of the elongator complex.
CC       {ECO:0000250|UniProtKB:O95163}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95163}. Nucleus
CC       {ECO:0000250|UniProtKB:O95163}.
CC   -!- SIMILARITY: Belongs to the ELP1/IKA1 family. {ECO:0000305}.
CC   -!- CAUTION: The elongator complex was originally thought to play a role in
CC       transcription elongation. However, it is no longer thought to play a
CC       direct role in this process and its primary function is thought to be
CC       in tRNA modification. {ECO:0000250|UniProtKB:O95163}.
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DR   EMBL; BC110776; AAI10777.1; -; mRNA.
DR   RefSeq; NP_001089940.1; NM_001096471.1.
DR   AlphaFoldDB; Q2TAQ1; -.
DR   SMR; Q2TAQ1; -.
DR   DNASU; 735009; -.
DR   GeneID; 735009; -.
DR   KEGG; xla:735009; -.
DR   CTD; 735009; -.
DR   Xenbase; XB-GENE-5813405; elp1.S.
DR   UniPathway; UPA00988; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 735009; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   InterPro; IPR006849; Elp1.
DR   PANTHER; PTHR12747; PTHR12747; 1.
DR   Pfam; PF04762; IKI3; 1.
DR   PIRSF; PIRSF017233; IKAP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..1170
FT                   /note="Putative elongator complex protein 1"
FT                   /id="PRO_0000283998"
FT   REGION          722..1170
FT                   /note="Mediates dimerization"
FT                   /evidence="ECO:0000250|UniProtKB:O95163"
FT   REGION          1014..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1028..1046
FT                   /note="Required for binding to tRNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q06706"
FT   COMPBIAS        1014..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1170 AA;  132653 MW;  9D734528A6F6DF67 CRC64;
     MILVKANLSL LGGAKKETQF HGSEGKQAAQ QKIMVVKPAL PWDDHKPRIT WRGDGQLFAV
     SSVCKESGTR KIRVWNRELA LQSTSESIEG LEQALSWKPS GALIASSQSK PNKHSVIFFE
     KNGLVHGEFT LPFTKGQIKV KELLWNSDST ILAIWLEDNE KDESSSGCCV QLWTVGNYHW
     YLKQSLNFGT DEMKKIECLM WDPENAYRLH VFSTGWHYFC FDWFWGTDHS DGGQGDVAVI
     DGDKVLVTSF QQAVVPPPMS TYFIQLSCAV NEVTFQLEPK KNSGIAILDS TNILSIYRYG
     NSTVNDPTVK LGAVSGNGFR TSSQTPKLEK KLRLPRNACD VQLRSFRLLT WVQDDTFLAV
     SQESNSSIST VHHMNTDQMD GQDINVRDVG TITGHIISLC YSPNTKHCAL QTSNGKIWKY
     LCEYPTPAVE PWIDSMGQEV KFPQPCVQTA LASIEGEDMV IGLTERSRLF INNSEVASNI
     TSFHLYEEFL LLTTHSHTCR CVSLRDTSLK ALETQLNSAS NPNDETIRKV ERGSRIITVV
     PCDTKLILQM PRGNLETIHH RALVLAQIRK WLDRLLFKEA FECMRKLRIN LNLLYDHNPK
     AFLDNVDLFI KQIGSVNYIN LFLTEIKEED VTKTMYPTHA LSTMQSSEGA KAKKVDIVCD
     AVRAAMEKWD PQKFCLSILT SYVRRTIPQL EIALQKVHEL RESPSTTIVS ADEALKYLLF
     LVDVNELYDH SLGTYDFDLV VMVAEKSQKD PKEYLPFLNK LKKMETNYQR YTIDKHLKRY
     KKALSNLSKC GPDYFTEFLS FVKDQSLYTE ALELYPHGTV EYKAINAAYG DHLVSKQQYE
     LAGLIYARCN SIEKALDAFI ASGNWHQVMC MASQLEYSGE KIAALARTVA GKLVEQRKQA
     DAAVLLEQYA EDYEEAILLL LEGAHWEEAL RLIYKYIRLD ILETNLKPAL LDAQRNHMIL
     FDNQKTTFTR HKERLSVVRE MKEKARLGLL DEDVTGCAEA DLFSDTSSIM TASDASGKYS
     QSNSRISSRS SKNRRKAERK KHSLKEGSPL EDLALLEALA ETIQMADKLR GDVHNLLKVL
     ILFEYDARAK ELQQNFDDLL LLFETSIPEI WPPSVQQNTA APILGPHSTA NSISISYQHQ
     RNVNISMQDS ELFTAPKLNK NIQWKLSLLL