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TRM11_DICDI
ID   TRM11_DICDI             Reviewed;         507 AA.
AC   Q54QA6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=tRNA (guanine(10)-N2)-methyltransferase homolog;
DE            EC=2.1.1.-;
DE   AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11 homolog;
GN   Name=trmt11; ORFNames=DDB_G0283969;
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: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC       tRNA methyltransferase complex that mediates the methylation of the
CC       guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM11 methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00959}.
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DR   EMBL; AAFI02000058; EAL65472.1; -; Genomic_DNA.
DR   RefSeq; XP_638838.1; XM_633746.1.
DR   AlphaFoldDB; Q54QA6; -.
DR   STRING; 44689.DDB0302468; -.
DR   PaxDb; Q54QA6; -.
DR   EnsemblProtists; EAL65472; EAL65472; DDB_G0283969.
DR   GeneID; 8624362; -.
DR   KEGG; ddi:DDB_G0283969; -.
DR   dictyBase; DDB_G0283969; trmt11.
DR   eggNOG; KOG2671; Eukaryota.
DR   HOGENOM; CLU_029646_3_0_1; -.
DR   InParanoid; Q54QA6; -.
DR   OMA; MWMPTAN; -.
DR   PhylomeDB; Q54QA6; -.
DR   PRO; PR:Q54QA6; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
DR   PROSITE; PS51627; SAM_MT_TRM11; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..507
FT                   /note="tRNA (guanine(10)-N2)-methyltransferase homolog"
FT                   /id="PRO_0000328121"
FT   REGION          459..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  58661 MW;  0471677018D4787F CRC64;
     MPKYLINFVQ QYASFRIHEL ESVARLFNID IQYNKEDLEF IESLDPEIET PFLYVTVNSE
     EDIKKICTRS VLIKSVYSIW AETQLLDEIL NELHSKFDKQ FLSNYMINKT FKIEVESYGS
     KYNQKEKLEM MQKLKDSPLW DSGKCLMHPT EEQMDKHILW YILTDFGVER QGLVKDFTLL
     PRKVYFGQRI AKGNRDDIIK YNLSDRKYLG TTSMDPELSL VSANMGLVKK GHFVLDPFVG
     TGSFILVASH FGAQTVGCDI DIKAMRKEED CNLETNFKDH GLTSQFLGTI LCDNSCPPWR
     VNSMFDSIIT DPPYGIRAGA RKIGFKENRK FVPVPEGLRR DHIPQCIDYS VPDVMADLLE
     LAAKTLIVGG RLVYWLPTTP DYKETDLPRH PCLRLITASC LQILTNRWGR RLVTMEKIIE
     YNDSIHNKSL LVQEDLGQFD PQHKDLRAVV FWKKMGTNEK TKKKEQKKKS VENHLKSKNN
     NDVINNNSND TNSNNNCNNE NNIENQK
 
 
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