GenomeNet

Database: UniProt
Entry: A4CAK7_9GAMM
LinkDB: A4CAK7_9GAMM
Original site: A4CAK7_9GAMM 
ID   A4CAK7_9GAMM            Unreviewed;       527 AA.
AC   A4CAK7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=PTD2_21407 {ECO:0000313|EMBL:EAR28415.1};
OS   Pseudoalteromonas tunicata D2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR28415.1, ECO:0000313|Proteomes:UP000006201};
RN   [1] {ECO:0000313|EMBL:EAR28415.1, ECO:0000313|Proteomes:UP000006201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D2 {ECO:0000313|EMBL:EAR28415.1,
RC   ECO:0000313|Proteomes:UP000006201};
RA   Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA   Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA   Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR28415.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAOH01000004; EAR28415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4CAK7; -.
DR   STRING; 87626.PTD2_21407; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   HOGENOM; CLU_005316_6_2_6; -.
DR   Proteomes; UP000006201; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.10.450.720; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR048457; YebU_pre-PUA_dom.
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   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF21150; YebU_pre-PUA_dom; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
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          76..360
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        296
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         174..180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         225
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   527 AA;  59289 MW;  3196206632FF6B06 CRC64;
     MSFYYFLSLN CFILAAKSHN KWLFIGFYLI PPRFADIITL SQKSKATTLD KHTYIPAEFI
     ADVQRYLPSH LSLDDYLTSC QSPLRPALRV NTLKMSVADF KTYAANHDWQ ITPVPWCEEG
     FWYQRPQAQQ NLSIGNTDIH LSGAIYIQEA SSMLPVFALQ HQNDLTDCIL LDMAAAPGSK
     TSQIAAQMKN TGVLVANEFS SSRLKSLSAN MQRLGIANVA LSHFDAAVFG PYMEQSFSHI
     LLDAPCSGEG TVRKDPDALK NWSIESNQQI AQVQKQLIES AFYALKTGGT LVYSTCTLTP
     LENQEVCQYL LDTFAGQIEV VKLDDLFFDA KRAATSEGYL HIWPQLYDTE GFFVAKFKKS
     SHSSHPKPQT KKGQFPFTLY GKKDAQTLLN ELKKQFGIDS LPGQLHLRDK EVWLFPSEFA
     LINEKIKYSR MGILVGQTHR TGVRLCHEFA TCFGHLALKN TYELSSVQAN DYFQGKDISL
     PTSTNDTGEV LLRLCGSVIG LGKWQKSKIK NSLPRDLVRN NQLITWV
//
DBGET integrated database retrieval system