ID   A0A0B7N8C0_9FUNG        Unreviewed;       180 AA.
AC   A0A0B7N8C0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=EKC/KEOPS complex subunit CGI121 {ECO:0000256|ARBA:ARBA00016009};
DE   AltName: Full=EKC/KEOPS complex subunit cgi121 {ECO:0000256|ARBA:ARBA00015316};
GN   Name=PARPA_05540.1 scaffold 18616 {ECO:0000313|EMBL:CEP11660.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11660.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP11660.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11660.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CGI121 acts as
CC       an allosteric effector that regulates the t(6)A activity of the
CC       complex. The EKC/KEOPS complex also promotes both telomere uncapping
CC       and telomere elongation. The complex is required for efficient
CC       recruitment of transcriptional coactivators. CGI121 is not required for
CC       tRNA modification. {ECO:0000256|ARBA:ARBA00025043}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CGI121/TPRKB family.
CC       {ECO:0000256|ARBA:ARBA00005546, ECO:0000256|RuleBase:RU004398}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LN726728; CEP11660.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7N8C0; -.
DR   STRING; 35722.A0A0B7N8C0; -.
DR   OrthoDB; 1437975at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2380.10; CGI121/TPRKB; 1.
DR   InterPro; IPR013926; CGI121/TPRKB.
DR   InterPro; IPR036504; CGI121/TPRKB_sf.
DR   PANTHER; PTHR15840; CGI-121 FAMILY MEMBER; 1.
DR   PANTHER; PTHR15840:SF10; EKC_KEOPS COMPLEX SUBUNIT TPRKB; 1.
DR   Pfam; PF08617; CGI-121; 1.
DR   SUPFAM; SSF143870; PF0523-like; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004398};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
SQ   SEQUENCE   180 AA;  19913 MW;  5C5C495028F10962 CRC64;
     MNPVTHMETC CLELYPDKKV HIALFKNVEN ASELRQRLLT QDSTLACSLI NAKLVINKIH
     ILLAVNRAVS DEFTGKLKTH NVHSEILYGF GVTNNIGKTF STFGIADDTT DVLAVKIDES
     ERDAESHLRK CVQGHLVPLD DLSTTTDLKS IENIYQLGNL EQDTNIILSL VAGAMALRGH
//