NSUN5_ARATH
ID NSUN5_ARATH Reviewed; 567 AA.
AC Q8GYE8;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=25S rRNA (cytosine-C(5))-methyltransferase NSUN5 {ECO:0000303|PubMed:26268215};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:26268215};
DE AltName: Full=tRNA methyltransferase 4h {ECO:0000303|PubMed:29268705};
DE Short=AtTRM4h {ECO:0000303|PubMed:29268705};
GN Name=NSUN5 {ECO:0000303|PubMed:26268215};
GN Synonyms=TRM4h {ECO:0000303|PubMed:29268705};
GN OrderedLocusNames=At5g26180 {ECO:0000312|Araport:AT5G26180};
GN ORFNames=T19G15.30 {ECO:0000312|EMBL:AC005965};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=26268215; DOI=10.1186/s12870-015-0580-8;
RA Burgess A.L., David R., Searle I.R.;
RT "Conservation of tRNA and rRNA 5-methylcytosine in the kingdom Plantae.";
RL BMC Plant Biol. 15:199-199(2015).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=29268705; DOI=10.1186/s12870-017-1206-0;
RA Wang Y., Pang C., Li X., Hu Z., Lv Z., Zheng B., Chen P.;
RT "Identification of tRNA nucleoside modification genes critical for stress
RT response and development in rice and Arabidopsis.";
RL BMC Plant Biol. 17:261-261(2017).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C(5) position of cytosine 2268 (m5C2268) in
CC 25S rRNA. {ECO:0000269|PubMed:26268215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47780, Rhea:RHEA-COMP:11911, Rhea:RHEA-COMP:11912,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:26268215};
CC -!- DISRUPTION PHENOTYPE: Reduced methylation of the C(5) position of
CC cytosine 2268 (m5C2268) in 25S rRNA. {ECO:0000269|PubMed:26268215}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; AC005965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93533.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93534.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70298.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70299.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70300.1; -; Genomic_DNA.
DR EMBL; AK117681; BAC42333.1; -; mRNA.
DR EMBL; BT008590; AAP40417.1; -; mRNA.
DR RefSeq; NP_001331920.1; NM_001343965.1.
DR RefSeq; NP_001331921.1; NM_001343967.1.
DR RefSeq; NP_001331922.1; NM_001343966.1.
DR RefSeq; NP_197990.2; NM_122519.3.
DR RefSeq; NP_851079.1; NM_180748.2.
DR AlphaFoldDB; Q8GYE8; -.
DR SMR; Q8GYE8; -.
DR STRING; 3702.AT5G26180.2; -.
DR PaxDb; Q8GYE8; -.
DR PRIDE; Q8GYE8; -.
DR ProteomicsDB; 183490; -.
DR EnsemblPlants; AT5G26180.1; AT5G26180.1; AT5G26180.
DR EnsemblPlants; AT5G26180.2; AT5G26180.2; AT5G26180.
DR EnsemblPlants; AT5G26180.3; AT5G26180.3; AT5G26180.
DR EnsemblPlants; AT5G26180.4; AT5G26180.4; AT5G26180.
DR EnsemblPlants; AT5G26180.5; AT5G26180.5; AT5G26180.
DR GeneID; 832687; -.
DR Gramene; AT5G26180.1; AT5G26180.1; AT5G26180.
DR Gramene; AT5G26180.2; AT5G26180.2; AT5G26180.
DR Gramene; AT5G26180.3; AT5G26180.3; AT5G26180.
DR Gramene; AT5G26180.4; AT5G26180.4; AT5G26180.
DR Gramene; AT5G26180.5; AT5G26180.5; AT5G26180.
DR KEGG; ath:AT5G26180; -.
DR Araport; AT5G26180; -.
DR TAIR; locus:2179749; AT5G26180.
DR eggNOG; KOG2360; Eukaryota.
DR HOGENOM; CLU_005316_7_4_1; -.
DR InParanoid; Q8GYE8; -.
DR OMA; IQMGKHP; -.
DR OrthoDB; 1128973at2759; -.
DR PhylomeDB; Q8GYE8; -.
DR PRO; PR:Q8GYE8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GYE8; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..567
FT /note="25S rRNA (cytosine-C(5))-methyltransferase NSUN5"
FT /id="PRO_0000448894"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 444
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 312..318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 363
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 383
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 567 AA; 63174 MW; D9FBE0D07F4AF639 CRC64;
MVARRNKPKA PLVKHRFSGG DSHKPKPPPA TKQPFSGVES HKPKTSPATK QKFSGVESHK
PKTPPGKQRF SGAESRKPKT PPATKQKFSS LERSALYARR EAANILRTVL RGDAERRAVA
SIKSLVLSPS VRNKRGTFAL VCETLKYLTV IKDVLDIANV LNSKWKRQEP LVFIVCYDIL
FGKDTPSIGD AEKFLMRHKE ALLSGLATLL VRKKVDSVDQ LLGSKLTGHL KPRYVRVNTL
KMDVDSAVQE LEKHYTVQKD ETVPDLLVLP PGSDLHAHRL VANGRIFLQG KASSMVAAAL
QPQAGWEVLD ACSAPGNKTI HLAALMEGQG KIIACELNEE RVKRLEHTIK LSGASNIEVC
HGDFLGLNPK DPSFAKIRAI LLDPSCSGSG TITDRLDHLL PSHSEDNNMN YDSMRLHKLA
VFQKKALAHA LSFPKVERVV YSTCSIYQIE NEDVVSSVLP LASSLGFKLA TPFPQWQRRG
LPVFAGSEHL LRMDPVEDKE GFFIALFVRA NKLDNPKSSE LPDRVCRRRP KERTMQLHPY
LCPKMFRAWS GTLHRLKTRF LLSRNGC
