ID A0A0K9PII9_ZOSMR Unreviewed; 824 AA.
AC A0A0K9PII9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase {ECO:0000313|EMBL:KMZ68060.1};
GN ORFNames=ZOSMA_24G00830 {ECO:0000313|EMBL:KMZ68060.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ68060.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ68060.1}.
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DR EMBL; LFYR01000864; KMZ68060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PII9; -.
DR STRING; 29655.A0A0K9PII9; -.
DR OMA; RGWRTMS; -.
DR OrthoDB; 120922at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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 CDD; cd00590; RRM_SF; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_met.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR45904; TRNA (URACIL-5-)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR45904:SF2; TRNA (URACIL-5-)-METHYLTRANSFERASE HOMOLOG A; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 54..83
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 130..197
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 54..83
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 680..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 745
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 745
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 520
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 570
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 717
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 824 AA; 90992 MW; 691A15B4A96BFE0E CRC64;
MAAEEGSLKI TMDDEDVVAM VGSAGVDDKE MENGDKLVTS ATLKHARDDE NIPYWKTSLC
SYFRSNSSKC NHGDNCRYAH GEEELRPRPD NTWDPTSERV KKVAKIECDD SDQPLGNLGL
SDQTEKCLIG IPVNWDTDKL KDFLDQHGIL YKIAKKKKGM SVGFLTFSDV HQLHTALQDL
KGKQIGGKYI KVADSIPRSS TNKQMPKSSI ECDDLGKVSG DITDDNAVNA EGLVIKCRNA
REAVAPLAYM LYNEQLEYKK KSLLHILKKL TRNARKACPS SVPYPDWIQN AREIGGLSCE
LEGIIESPLS TGYRNKCEFS VGYSVDGKRT VGFNLGNFRE GIVAVEEPTD CPNVSNISCQ
YALIFQDFLH LSKLPLWDRF NNSGFWRQFT VREGRNPVQC DGGERDDVKI SEVMLIIQIC
SSGTDDDVMK VEFERLTSTL VEKASASSPP LPLSALVIQD HKGISNAASA DCPLFPLPVQ
KIGNNSDISG SPKNQVVTEE RIHDSICNLR FCISPTAFFQ VNTLAAEKLY SLAGDWARLS
PDTLLFDVCC GTGTIGLTLA HRVGMVVGIE MNSSAVSDAF RNADINGITN CKFVCSKAED
VIESLLKEYI VNVQQPEIPG SDMKNPVTNG ILDSFGNSNT IIVSEATKVG NATHVSETIN
TESSRQQEVS VVCDNRIIND SASPSVENHD KPSQDEKDME ENNTSMPRFK DVVAIVDPPR
VGLHPKVIKA LRTNPRLQRF VYISCNPESL MANAIELCTP TVDNPQKGGR NSRGWTNRNI
SSAGLARQRS KSMPMSKPFR PIKAMGVDLF PHTVHCEMVM LFER
//
