ID A0A1Q9E0Z5_SYMMI Unreviewed; 1409 AA.
AC A0A1Q9E0Z5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=tRNA (Uracil-5-)-methyltransferase-like A {ECO:0000313|EMBL:OLQ01083.1};
GN Name=TRMT2A {ECO:0000313|EMBL:OLQ01083.1};
GN ORFNames=AK812_SmicGene16247 {ECO:0000313|EMBL:OLQ01083.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ01083.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ01083.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ01083.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLQ01083.1}.
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DR EMBL; LSRX01000306; OLQ01083.1; -; Genomic_DNA.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_met.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR45904:SF2; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG A; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT REGION 145..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..69
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 152..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 1327
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 1299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 1409 AA; 154693 MW; 41DED81D1E0BDF4C CRC64;
MEGGSSREDV SKCFDAMKEA FAPMLDRQKE QHALLLAMKQ EVLSQDEKLS ALQKQLQDLK
AVVEKKKKRA ARRAPTHLPK ASDSRLAPIP EEAADVAETK QVYTNAGVTF SRQLLLSCLD
APHGSMDIRM LPCLEELARE LGRPPVRKES ATAAQKSASQ KHQPWHVHQQ GGYGNSVWNS
KSSWHGWGDW QGWNGSKGPG KAVFFMRAVM YTVSMSNLSS RLRVALSEEG YGLLRRLGKR
CRGHGGICDG VFDVDREDDV DDPEKEDAEC EEMDYHQDEE EQAGAGEHQW QESLEAEAAL
ELLAEALDVD EADMGRKSRN GLWKGYDELL HGFLAEEHPQ HDELHQSLCA VFTLLADNDD
RPRELQVDVP GVGLRLLEPF LQSQDAALLR NGLAGLACLL ASRAKDAALI LQMSAVPLSA
VLNALARPVP GTAVFVWVRR TAQAKVPLLM QATGIDVILN ALSNTERGIR RELVDAKLVA
VLAIMAAHNK DVRDEIFDRV DFMMELRFAV DVAGERARAA QTHEQQRQAR RLCAGLYESF
AVLAIHGEFK ERLIASKKTL GALQALAKEE VSFVEGAGDA LQPTSTSTAS AFRANYAWAI
SRGLLWVEGV GKPGAKKCRR LCGKGDARQF VNGSISAVFN FLMAAVYGTA QYVLEDLGED
PAVGFHFASL VHNLCRSRED RVRIKTGNPM IDELSGEDFK ALEEFYERMP AEARPTRSGE
VDPGAPELAQ RFRTWCLERG EAGGAAPLVA KLCRCVSGSM QTKALIADSL KLLCSDQQER
KIVAASGGVR TLLGLSNLDQ ALGGQQEDVK FMKLLTQALA QILIVMNPQL LQYQEQLDAV
RPMLALLEHR HELLQFEGCL ALTNLLSSSE ELRSFALQSG AWSKCKDLLF SENEVQRAGL
EAMCNLTMAE EDRGYDEALV VTDQSSTTYA SCVMDVKYRI GYSTVAERFA LGKAENELKI
FGAFCASEIE RQQIAATGAL AILSGLDEEI PAVELRAVSA LLSLRRAEGV NQEVRLAIFA
VLQERLRRGF ESPDAQGHSL KVFWDVGETS GLGREAYSRA FARVAPRPLV PVAMKKLCKA
LRDCVRASAF SIFERGKGWQ QGYWRMVMVR QSTAEELLVM VQTAKLEDAQ REALAAEVIA
ALTKAELQIN VVSIYLQFND EISDAARPGA PLMHIHGDAQ LRMQLLGLSF NIGPLSFYQA
NSSTCALLYE RALEWLRPQN DVAVLDVCCG VGTIGLCASR RCRRVIGIEL IPEAVEAAKA
NAALNKVENT EWIVGKAEDV LPQVLRGLDP SLEVCAVVDP PRPGLHSSVL RALRGCPQLS
RIVYVSCNPD SLVEDVVKLT MPSESDEDPF IPLRAVAVDM FPHTVHCEMI LLLERSSKVE
DPRKEAPSAA GPAAESEGAA PSDAAKVSE
//
