ID C5KRD8_PERM5 Unreviewed; 722 AA.
AC C5KRD8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 08-NOV-2023, entry version 45.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
DE Flags: Fragment;
GN ORFNames=Pmar_PMAR015808 {ECO:0000313|EMBL:EER12959.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER12959.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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; GG675793; EER12959.1; -; Genomic_DNA.
DR RefSeq; XP_002781164.1; XM_002781118.1.
DR AlphaFoldDB; C5KRD8; -.
DR EnsemblProtists; EER12959; EER12959; Pmar_PMAR015808.
DR GeneID; 9056073; -.
DR InParanoid; C5KRD8; -.
DR OMA; GICEIWI; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
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:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; NOL1/NOP2/SUN DOMAIN FAMILY MEMBER 2-RELATED; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000007800};
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 67..383
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT NON_TER 722
FT /evidence="ECO:0000313|EMBL:EER12959.1"
SQ SEQUENCE 722 AA; 79809 MW; C7C7AD1E7774109E CRC64;
MGKNSKNYYK RKGLGVSSHH QQSKGTDEEP SGWRYDSRGD KATFQSDAFD EYYNTQGLLP
PEEWKKTLEC LRTPLPTSFR VMDLGVSSGI VKEQAKKFQE EISKIHPGEF EELPFVEDGY
QVNLPRPVLR APLSGLKSFH EFLVNQGQAG VLMRQETVSM LPALALKGEL KQDSLILDIC
SAPGSKTSQL LEMLNECPRP DVSKPPEGMV VANELVVKRA HLLIHRLRHH NSPNLLVTAH
AGQSFPSCFD GVTGQRIEFD AALCDIWINL YSTCALNPIE DEAVVGSVVA ASEGALELGE
WKEAPKGLKY EKGVSSWKVK SGGRWFSNFE DAERELGEGK NARLVKSSMF PQASEGVDLS
KCVRVYPHLQ NTGGFFIAVI RKKARVPWET TGEGDMPEVG EEKDTDEVDR EKDTAKAKEE
EDTVSERSQD ASSSQAPMEM QSDFYECPND FTELIKDQFG IPSGEVDGLL WSKSPEPKPR
KLWLMSRSVD RLLRSSSRRG LKVVSAGTPA FDRPSGAHSE PRVLVTALQW LTMTKRVYEV
TPADFAKLLI IKVPAEAVGL GQVKESAIVV RCAVGEVSLR MPVYRRRHLA EGLVSEDIRP
GLAWCVSKEL DEDIEFPGVT LSAHSKVKKA QLPPAHDEGK KDEDAPREGQ QSIQAEESIL
NDPLLAGVLT ASAINTKGLK QCFYLRRQEL VMSSLGMGGG LSKVRETPGS IGGFGICEIW
II
//