(data stored in SCRATCH zone)

SWISSPROT: A1AZL2_PARDP

ID   A1AZL2_PARDP            Unreviewed;       383 AA.
AC   A1AZL2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ABL68706.1};
GN   OrderedLocusNames=Pden_0594 {ECO:0000313|EMBL:ABL68706.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68706.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP000489; ABL68706.1; -; Genomic_DNA.
DR   RefSeq; WP_011746939.1; NC_008686.1.
DR   STRING; 318586.Pden_0594; -.
DR   PRIDE; A1AZL2; -.
DR   EnsemblBacteria; ABL68706; ABL68706; Pden_0594.
DR   KEGG; pde:Pden_0594; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037301; -.
DR   KO; K03500; -.
DR   OMA; IVRWKRL; -.
DR   BioCyc; PDEN318586:G1GW1-602-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZL2.
DR   SWISS-2DPAGE; A1AZL2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   DOMAIN      135    383       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   ACT_SITE    337    337       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     246    246       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     284    284       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   383 AA;  40670 MW;  33097875BA614AA9 CRC64;
     MTPAARAAAA IDILDRILDG QAAEAALIRW ARASRFAGSG DRAAVRDLVF DALRRLRSRA
     ALGGALSGRG LLLGMCREEG IDPATLFTGE GHAPSVLSEG EGQAGRAPTP DEALDLPDWL
     LPLWRKALGG DAEPVALAMR DRAPVWLRVN LRRADPARAA AAMAEQGIAT APHPDLPTAL
     RITEGARRLA GCHAYREGLV ELQDLSPQMA CALLPAQGSL LDFCAGGGGK ALALAAQGAG
     PVTAHDIDAG RMADLPARAE RAGVRIRLAA PGKVAGRFDT VVADVPCSGS GTWRRGPDAK
     WRLTRDDLEQ LAARQCRILD QAAGFVADGG HLAYMTCSVL DAENDDQVQG FLARNRRFEQ
     VLARRFTPLT ASDGFYLALM RRR
//

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