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Database: UniProt
Entry: K1XGQ5_MARBU
LinkDB: K1XGQ5_MARBU
Original site: K1XGQ5_MARBU 
ID   K1XGQ5_MARBU            Unreviewed;       827 AA.
AC   K1XGQ5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Spb1 domain-containing protein {ECO:0000313|EMBL:EKD19973.1};
GN   ORFNames=MBM_01925 {ECO:0000313|EMBL:EKD19973.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19973.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD19973.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19973.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC       Rule:MF_03163}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03163}.
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DR   EMBL; JH921430; EKD19973.1; -; Genomic_DNA.
DR   RefSeq; XP_007289814.1; XM_007289752.1.
DR   AlphaFoldDB; K1XGQ5; -.
DR   STRING; 1072389.K1XGQ5; -.
DR   GeneID; 18757860; -.
DR   KEGG; mbe:MBM_01925; -.
DR   eggNOG; KOG1098; Eukaryota.
DR   HOGENOM; CLU_009422_8_1_1; -.
DR   InParanoid; K1XGQ5; -.
DR   OMA; DITTEDC; -.
DR   OrthoDB; 119516at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   HAMAP; MF_03163; RNA_methyltr_E_SPB1; 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   InterPro; IPR028589; SPB1-like.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03163};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_03163}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_03163};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03163}.
FT   DOMAIN          24..200
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   DOMAIN          234..389
FT                   /note="DUF3381"
FT                   /evidence="ECO:0000259|Pfam:PF11861"
FT   DOMAIN          614..824
FT                   /note="Ribosomal RNA methyltransferase SPB1-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07780"
FT   REGION          361..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..466
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..523
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..616
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
SQ   SEQUENCE   827 AA;  93231 MW;  0058841790503C11 CRC64;
     MGIQKKHGKG RLDKWYKLAK EKGYRARAAF KLIQLNKKYG FLEKSKVLLD LCAAPGSWCQ
     VAAECMPVGS LIVGVDLSPI KAIPRVISFQ SDITTDKCRA TIRSHFKTWK ADTVLHDGAP
     NVGTAWVQDS FNQAELVLQA MKLATEFLVE GGTFVTKVFR SKDYNSLLWV FNQLFAKVEA
     TKPPSSRNVS AEIFVVCRGY KAPKRIDPKF LDPKSVFAEL SDPTPNNEAK VFNPEIKKRK
     RDGYEEGNYT QFKEVTASEF IQTTDPIAIL GGMSRLSFQQ PPNGDVALAA IDKLPETTED
     IRVACADIRV LGRKEFRMLL KWRLKVRELF GLATKKSKAP ADEEVVEVEP MDEELKIQEE
     LQALSEKESG RKKRERRREN EKKQREIIRM QLHMTVPTEI GMEQAGPNGE GSMFGLKAVD
     KLGAVDKITK GKMAILTEAD RRKDIDGIGS DDDDSESDEE EDNLDRELDS LYSQYQERKS
     DSDAKFKARK ARKEHEDGDW EGFSAGEEAS DNDQLEEDSS DESSDDERPA KRPLLTDLKG
     KDMKAGGLSR RAAQFFDQDI FKDIGELLPE EPESEAEGEE EISAALEELE TIRPMAEEEE
     PEEEIPMADS IDGSDDEDGF EVVKKTAAEK EWEEQEPRKD GKLDIDIITA EAMSLAQKIA
     SGEVTTRELI DEGFNKYAFK DREGLPEWFL DDEQRHDKPH RPITAAGAAA IKEKLRALNA
     RPIKKVREAK DRKKFKAAQR LEKLRKKSAL LQDEEGMTEK EKATSIAKLM SKAAKKKPKQ
     QIKVVVARGN NKAIAGRPRG VKGKYKIVDA RLKKDVRGEK RAAKKRK
//
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