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Database: UniProt
Entry: A0A0S4IND8_BODSA
LinkDB: A0A0S4IND8_BODSA
Original site: A0A0S4IND8_BODSA 
ID   A0A0S4IND8_BODSA        Unreviewed;       934 AA.
AC   A0A0S4IND8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=FtsJ cell division protein, putative {ECO:0000313|EMBL:CUE74298.1};
GN   ORFNames=BSAL_55700 {ECO:0000313|EMBL:CUE74298.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUE74298.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CYKH01000162; CUE74298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4IND8; -.
DR   VEuPathDB; TriTrypDB:BSAL_55700; -.
DR   OMA; DITTEDC; -.
DR   OrthoDB; 119516at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR   InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10920:SF13; PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3; 1.
DR   PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR   Pfam; PF11861; DUF3381; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF07780; Spb1_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:CUE74298.1};
KW   Cell division {ECO:0000313|EMBL:CUE74298.1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..201
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   DOMAIN          236..401
FT                   /note="DUF3381"
FT                   /evidence="ECO:0000259|Pfam:PF11861"
FT   DOMAIN          737..910
FT                   /note="Ribosomal RNA methyltransferase SPB1-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07780"
FT   REGION          326..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..515
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..638
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..669
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        730..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..919
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..934
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   934 AA;  105333 MW;  5A4B5D44B6D4AE3C CRC64;
     MGTKSKKKAK TRLDAYYRLA KDQGYRARSA FKLIQLNRKY DFLAKSKVLV DLCAAPGGWC
     QVAAKHMPIG SKIVGVDLVP IAPIRGCKTF VGDITDDKTR KMVVTWLKKE PVDCVIHDGA
     PNVGGVWSRD LFEQNALVLC AAKMATALLR PGGWFVTKVF RSQDFQKLMW VMKQLFDKVE
     ATKPLASRME SAEIFVVCAG YKAPKHLDPK MFHAQSVFAD VAEEKIVNAA GILVTPKNNV
     PQGYDEFATI THNVATLSDF LHCREPREFL KTHHEIRFPE EDRHMLKSKH SRKELVYLCH
     DLLQVGEGDR RRLIRWREQL LREQQRAAQD EAAGDDNSEI GSDAGAAAGS DNEGEDTQQL
     LGDGEGDVTE MARQLLEIRK HQAKELKKKQ KKLVDRKLKQ VKGLINYDPT ASADHLTDTT
     GFDYKGAAAL DADGIVDTEE GAENANDWTI ANVGAIDEER LSKLMDKHFE DPEADRHLND
     PLAPVMGATL GDEDDVDLGS GDDKDDDDEA GSDEDDDVIR PLPIGQSLQV IEGREESYDV
     DYYGNYIVAE KSNRVRLFEE GFGNNNEDEE GEEDDDNMSP QEKKVAARKA KDTADLDEAG
     KQSKWQRRHL NIDKVLNRTF PKPRDPKKRN KRLEEDQIEL DNGSDDDAAA AGKKAKADKG
     PRMKFGAEAD DDTDDSEDDY VASDISSLGG NASDDNDDFE VRKGRQDTRK KRAIIPDIGK
     LTAMELVKQQ RKQTTKDNKT LRRENKKNKA SGKKKDKKED TTFEEIPIAL TDPDIRARTH
     AIATKMLDKR SRRDILDASI NRFMNNDDDD LPDWFVKDEQ RNCKVILPVT AADVENERNR
     FRELNARPGK KVMEAQGRKR RKAQRMLRGL IEKGKSDPRA RQKANGTSVR TLMRSTAIKG
     ENINKKKNKP LDPKSMGEKK RTRQRLKRQG KGKR
//
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