TRM6_DICDI
ID TRM6_DICDI Reviewed; 521 AA.
AC Q54UB1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit trm6;
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit trm6;
DE Short=tRNA(m1A58)MTase subunit trm6;
GN Name=trmt6; ORFNames=DDB_G0281175;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC methyltransferase, which catalyzes the formation of N(1)-methyladenine
CC at position 58 (m1A58) in initiator methionyl-tRNA.
CC {ECO:0000250|UniProtKB:P41814}.
CC -!- SUBUNIT: Heterotetramer; composed of two copies of trmt6 and two copies
CC of trmt61a. {ECO:0000250|UniProtKB:Q9UJA5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}.
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}.
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DR EMBL; AAFI02000040; EAL66884.1; -; Genomic_DNA.
DR RefSeq; XP_640865.1; XM_635773.1.
DR AlphaFoldDB; Q54UB1; -.
DR SMR; Q54UB1; -.
DR STRING; 44689.DDB0238374; -.
DR PaxDb; Q54UB1; -.
DR EnsemblProtists; EAL66884; EAL66884; DDB_G0281175.
DR GeneID; 8622921; -.
DR KEGG; ddi:DDB_G0281175; -.
DR dictyBase; DDB_G0281175; trmt6.
DR eggNOG; KOG1416; Eukaryota.
DR HOGENOM; CLU_010916_0_3_1; -.
DR InParanoid; Q54UB1; -.
DR OMA; TFHNRTE; -.
DR PhylomeDB; Q54UB1; -.
DR PRO; PR:Q54UB1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; ISS:dictyBase.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; ISS:dictyBase.
DR GO; GO:0030488; P:tRNA methylation; ISS:dictyBase.
DR InterPro; IPR017423; TRM6.
DR PANTHER; PTHR12945; PTHR12945; 1.
DR Pfam; PF04189; Gcd10p; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..521
FT /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT catalytic subunit trm6"
FT /id="PRO_0000328539"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 58147 MW; 3F305EF8FC4E2FCC CRC64;
METETPMDVE TKSTTSNTND NNNNTTIVKT TSNIIKEGDH VILDINNGEK FSVIKVKLGS
KVKIGKKQIL INSIIGESYY SSFQVSNEKN TLERITQKEI DDRLNNLVEL NQNDADNRNL
DQNNTAQKLT QEDINEMKQK GTDSNTIIKT IVENSESFKT KTSFSQIKYL KKKIKKYSTI
VKIIKPTLKS LTEAYYKKDS RKICGLRFDS FGQLLTLGNI RANSQVLVVE TCMGLVTGSI
AERMNGQGTI LSAYIGKGPS LSIVNNFGFN TDVLNTIYPF NLNITSVLNK GEDISKLPPT
ASSGIYDKQV KEKEKEKEKD ENVKDEKESG EEAKTIINQR NDTSNENIVK LLKDGGVWSL
VIVTKYSPLN ILLSCWPYLN SSGSFVIYSQ FPQPLMEVHQ FLHKNQMAVN QQISEIWMRE
HQVLPKRTHP MMGMDGASGF ILYGTKVTKP IQKSTTTTTT TTTTTTNNSI NPTKTTASLD
IENKVIDATT SSSSSSTAAA TTTEEDKEDS ESALKKRKID E