ID A0A2Z7BD40_9LAMI Unreviewed; 620 AA.
AC A0A2Z7BD40;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=25S rRNA (Cytosine-C(5))-methyltransferase nop2-like {ECO:0000313|EMBL:KZV31329.1};
GN ORFNames=F511_40798 {ECO:0000313|EMBL:KZV31329.1};
OS Dorcoceras hygrometricum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Gesneriaceae; Didymocarpoideae; Trichosporeae;
OC Loxocarpinae; Dorcoceras.
OX NCBI_TaxID=472368 {ECO:0000313|EMBL:KZV31329.1, ECO:0000313|Proteomes:UP000250235};
RN [1] {ECO:0000313|EMBL:KZV31329.1, ECO:0000313|Proteomes:UP000250235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. XS01 {ECO:0000313|Proteomes:UP000250235};
RX PubMed=25902549; DOI=10.1073/pnas.1505811112;
RA Xiao L., Yang G., Zhang L., Yang X., Zhao S., Ji Z., Zhou Q., Hu M.,
RA Wang Y., Chen M., Xu Y., Jin H., Xiao X., Hu G., Bao F., Hu Y., Wan P.,
RA Li L., Deng X., Kuang T., Xiang C., Zhu J.K., Oliver M.J., He Y.;
RT "The resurrection genome of Boea hygrometrica: A blueprint for survival of
RT dehydration.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5833-5837(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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}.
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DR EMBL; KV007516; KZV31329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z7BD40; -.
DR OrthoDB; 1268at2759; -.
DR Proteomes; UP000250235; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000250235};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
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}.
FT DOMAIN 217..506
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 309..315
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 360
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 620 AA; 69770 MW; BF8B746FD5BD5FF9 CRC64;
MGAPKLNKKK KGETAPSHPP GKKLKVELPL AKQPRKEDFL SDSDGIGEEP ETHQEFGDEE
QEVETDSDMS SQGDDPFADD ILQGSDEEED GSDEDSDSDA DIEKRARAID EEKAQEEEDA
EAELQLNIKE EADEFRLPTE GELEEESHRP PDLSNLQRRI KEIVRVLSNF KSLRQEGATR
KDYIDQLKMD LCSYYGYNDF LIEALIEMFP VVELMELIEA FEKPRPICLR TNTLKTRRRD
LAGVLLNRGV NLDPLSKWSK VGLVVYDSQV PIGATPEYMA GYYMLQSASS FLPVMALAPQ
EKEKVVDMAA APGGKTTYIA ALMKNSGIIY ANEMKESRLK SLTANLHRMG VTNTIVSNYD
GREMPKVLGV SSVDRVLLDA PCSGTGVISK DESVKTSKSE LDIQNCVYLQ KQLILAAIDM
VDAGSKSGGY IVYSTCSIMV AENEAVIDYA LKKRDVKLVP CGLDFGRPGF IRFRGHRFHT
SLEKTRRFYP HVHNMDGFFV AKLKKMSNTK PTQQPSEPSG EVEEEPELND GNGVEGDVQP
EPENEQKQKK KRKNSTEMNK KVINGSPKKS QEERKSANER EKKKHRSREE ISKTREEKRV
ALREAKRKAK IKSRAAANRR
//