ID A0A0D2X1Q5_CAPO3 Unreviewed; 927 AA.
AC A0A0D2X1Q5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
GN ORFNames=CAOG_008599 {ECO:0000313|EMBL:KJE91219.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91219.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03055};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03055}.
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DR EMBL; KE346362; KJE91219.1; -; Genomic_DNA.
DR RefSeq; XP_011270199.1; XM_011271897.1.
DR AlphaFoldDB; A0A0D2X1Q5; -.
DR STRING; 595528.A0A0D2X1Q5; -.
DR EnsemblProtists; KJE91219; KJE91219; CAOG_008599.
DR GeneID; 23301996; -.
DR eggNOG; KOG3115; Eukaryota.
DR InParanoid; A0A0D2X1Q5; -.
DR OrthoDB; 116813at2759; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03055}.
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 174..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 272..274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 927 AA; 102000 MW; 7EB551C7D141B506 CRC64;
MADTRTKRSA EELATSDAGT EAGEAKAQLH AATATAAKAT AQATEEDEVD SDDPDAEDAV
PGSRQLPRKG DYRQRAHVNP MSMHTFDYPI TPDAMDWNQH YPNMNGREVE FADIGCGYGG
LLTVAGHGNP AQGLRVCQGQ NHSATGSEYV KDKITALRER HPGRYNNVAC IRGNAMKYLP
CFFRKGQLSK VFFLFPDPHF KRTKHKWRII SNTLLAEYAY AIRVGGIIYT VTDVHDLHEW
MRTHLEQHPL FRRLTEEELA ADPVVPKLFD SSEEGKKHTP RPMLSSKILP QCVRSARTYR
GRVAPVAGRV CTLVARGQST IAAAPAVPRI PRTEVLADLT GYALGTLQLP NTTALVLTGG
KGSGKSALLM ELLGVATGSQ AASVTAATEG GSGSVTLPRI LATLPSGTIA AYTSRHATRA
TARQSQTIAQ TASTNRAEAR VTVAFDFSWP MPSVGEFIDT LEAMLLISLA PALKLAGIRP
DAVLGLAERC VGIQSTLDGL YRDLNNTGSI RPLQPAEQLI ACSKLLKSEQ ALSADRLARM
SPSSRDVCEL WRQKTSGASS LFAAAAADHP AHALIHLLVT HEDAAARRRH GLAGTSGIPA
LRFLLSAVQA VHTAPTSSQR ILMVLLNMHQ MPQWLTSRPD EEKKLFQDYH DALLLTLKRA
ALRNELPPVL MECDDPIYSR DIFDLFDSPA TEWLDQVEVE PFEMLEGDRT FVQAGLCTSL
EYSEAYSVLG GHVGDWQQFL SAYWLPASRR QEWEALVQPG TQLSPFSIAL RSFVSDRINQ
FLSTTAPKIE SSFLAENAVF ERALQERLGK TLTYRVRRLL TPTSSRLLLF QLLDVVERFV
FQGQVRVEDP AASAFYNHPA TTAMLQHGLL IVRNRGTLIV PASRLASTLL VAYCRHWLDN
LSWYELPRRF FIRYITGVLS LAPLPPG
//
