ID A0A2I0I7N0_PUNGR Unreviewed; 813 AA.
AC A0A2I0I7N0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Multisite-specific tRNA:(Cytosine-C(5))-methyltransferase-like {ECO:0000313|RefSeq:XP_031396681.1};
GN Name=LOC116207736 {ECO:0000313|RefSeq:XP_031396681.1};
GN ORFNames=CRG98_040174 {ECO:0000313|EMBL:PKI39416.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI39416.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI39416.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG2017 {ECO:0000313|EMBL:PKI39416.1}, and cv. AG2017
RC {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI39416.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:XP_031396681.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_031396681.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC 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; PGOL01003812; PKI39416.1; -; Genomic_DNA.
DR RefSeq; XP_031396681.1; XM_031540821.1.
DR STRING; 22663.A0A2I0I7N0; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000233551; Unassembled WGS sequence.
DR Proteomes; UP000515151; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233551};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 110..525
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 23..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 228..234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 813 AA; 91548 MW; 305A6A905CCAD580 CRC64;
MQIANSNKCS ILPLLPPSAT NSVTGLISHS QRMSTPAGRG GRARAPAQKV QFRRSREKAA
LPSLSDSSDS DTDDRDREGH NKFDPVITNP AFDEYYKEQE IVSPEEWDTF IEVLRTPLPA
AFRVSPSSQF CVEILSQLEN DFRKSIRPEH SDDNDTEAIT PLPWYPDNLA WQFNYSRRQL
RKDHSLERFH EFLKLENEIG NITRQEAVSM VPPLLLDVHP EHLVLDMCAA PGSKTYQLLE
IMHHSNREGS LPDGLIVAND LVAQRCDHLI HKMKRMNTAN LVVTNHEAQC FPGGFLSETN
ASQIAAETEM HPHQLLFDRI LCDVPCSGDG NLRKAPNLWR RWNAGMGNGL HSVQLQIAMR
GITLLNIGGR MVYSTCSMNP VENEAVVSEI LRRCEDSVEL VDVSTELPKL IRHPGLRKWK
IRHKNCWFST FNEVPDYCRG GIVRSMFPPD RSHRNSVGDH TSEFGEKFNS NDSIDPQTAV
QRVHLTVNYN DSVNRISNFP LERCIRILPH DQNGGAFFIA VFNKLAPLPA IRKRTISEQD
SLPSLQDQLG NLVEYMEVLE VSSSNVQNNA GGNAHTKHKW KGIDPVVFLK DESIIDNIKS
FYGISDSFPL RGHLVTRNSD SNCGKRVYYI SKQVKDLLEL NIRAGQQLKI PYVGLMMFER
KRSKEGTLTC PFRISSEGLP LILPYITKQI LYASDVDFRL LLQHKSIRFA NFLDREFGEK
AWKLIPGGCV VVLSKGDEAV KACTRAGDST IAIGCWKGKT CVNVMVSPLD CQELLHRLFP
GEENLYPPVQ GSKPSISSDD LRDGDSIRTT VGC
//
