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Database: UniProt
Entry: C5KRD8_PERM5
LinkDB: C5KRD8_PERM5
Original site: C5KRD8_PERM5 
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
//
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