(data stored in SCRATCH zone)

SWISSPROT: Q9LDL2_ARATH

ID   Q9LDL2_ARATH            Unreviewed;       626 AA.
AC   Q9LDL2;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   11-DEC-2019, entry version 96.
DE   SubName: Full=Uncharacterized protein AT4g26600 {ECO:0000313|EMBL:CAB79515.1};
GN   OrderedLocusNames=At4g26600 {ECO:0000313|EMBL:CAB79515.1};
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 {ECO:0000313|EMBL:CAB79515.1};
RN   [1] {ECO:0000313|EMBL:CAB77061.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bevan M., Zimmermann W., Grueneisen A., Wambutt R., Kalicki J.,
RA   Wohldmann P., Smith A., Bancroft I., Mewes H.W., Lemcke K., Mayer K.F.X.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAB79515.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zimmermann W., Grueneisen A., Wambutt R., Kalicki J., Wohldmann P.,
RA   Smith A., Mewes H.W., Lemcke K., Mayer K.F.X.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAB79515.1}
RP   NUCLEOTIDE SEQUENCE.
RA   EU Arabidopsis sequencing project;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; AL078465; CAB77061.1; -; Genomic_DNA.
DR   EMBL; AL161565; CAB79515.1; -; Genomic_DNA.
DR   PIR; T08926; T08926.
DR   eggNOG; KOG1122; Eukaryota.
DR   eggNOG; COG0144; LUCA.
DR   ExpressionAtlas; Q9LDL2; baseline and differential.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023273; RCMT_NOP2.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02012; RCMTNOP2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9LDL2.
DR   SWISS-2DPAGE; Q9LDL2.
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   DOMAIN          258..521
FT                   /note="SAM_MT_RSMB_NOP"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..356
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   REGION          524..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..29
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..58
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..129
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..188
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..542
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..584
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..620
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        454
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         374
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   626 AA;  70615 MW;  88B63C4118780138 CRC64;
     MAALTRNKKK GSNSQTPPLN KQTKASPLKK AAKTQKPPLK KQRKCISEKK PLKKPEVSTD
     EEEEEEENEQ SDEGSESGSD LFSDGDEEGN NDSDDDDDDD DDDDDDDEDA EPLAEDFLDG
     SDNEEVTMGS DLDSDSGGSK LERKSRAIDR KRKKEVQDAD DEFKMNIKEK PDEFQLPTQK
     ELEEEARRPP DLPSLQMRIR EIVRILSNFK DLKPKGDKHE RNDYVGQLKA DLSSYYGYNE
     FLIGTLIEMF PVVELMELIE AFEKKRPTSI RTNTLKTRRR DLADILLNRG VNLDPLSKWS
     KVGLIVYDSQ VPIGATPEYL AGFYMLQSAS SFLPVMALAP REKERVVDMA AAPGGKTTYV
     AALMKNTGII YANEMKVPRL KSLSANLHRM GVTNTIVCNY DGREVISKDE SVKTSKSADD
     IKKFAHLQKQ LILGAIDLVD ANSKTGGYIV YSTCSVMIPE NEAVIDYALK NRDVKLVPCG
     LDFGRPGFRE HRFHPSLEKT RRFYPHVHNM DGFFVAKLKK MSNAMQPSGN DEPAVTMEQA
     QVSSSDDDDE KAEAIEELEK PPVASGQPKR ESNTKEDTNK RKNPRSKEIH KGKRNKNTKT
     ESGNVEEPRK QKKKRSQWKN EIAQAR
//

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