ID A0A139H8F5_9PEZI Unreviewed; 2251 AA.
AC A0A139H8F5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=AC578_10501 {ECO:0000313|EMBL:KXS98743.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS98743.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS98743.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS98743.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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}.
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:KXS98743.1}.
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DR EMBL; LFZN01000107; KXS98743.1; -; Genomic_DNA.
DR STRING; 321146.A0A139H8F5; -.
DR OrthoDB; 37525at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
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:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022155; DUF3684.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR049561; NSUN5_7_fdxn-like.
DR InterPro; IPR048889; NSUN5_RCM1_N.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR47839; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G04830)-RELATED; 1.
DR PANTHER; PTHR47839:SF1; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G04830)-RELATED; 1.
DR Pfam; PF12449; DUF3684; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF21148; NSUN5_fdxn-like; 1.
DR Pfam; PF21153; NSUN5_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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:UP000070133};
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 1843..2221
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1412..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2227..2251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2052..2068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2232..2251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2124
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1975
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 2024
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 2251 AA; 249162 MW; AC33752F3CFC9B30 CRC64;
MVASTNLSAL RAQTMQGEDE EAVTVNTRAL IDKVLARYSG EWTTLRELIQ NAADAQARKV
KIQFETFPSA TVPLPQENDP SELLKHTLLH HTVKTLIVSN DGEHFKETDW QRLKRIAEGN
PDETKIGAFG VGFYSVFADC ESPFVTSGKE TMAFYWKKDS LFTRRGKLPD SEVQGTSFLL
DYRSQTTPVP QLLSLCHFLA TSLTFVGLES VELHLDQWNI LTLTKKMAPA AAVKIPSDVN
PKTKDGLMKI SDVEYQNAQI DARWMNVVGW NRKTTSASLA SQQQQQQQNE SGASSLRSFF
GRFTSAATNT TVRKAQREEE VFQQTILDDL AGFSSATVFL RVSTVNILTN VSRQLSQELE
RATKKPPPKE TRLSILTSSY DESTASMSTS AGSSSKRATE IFASVLPSKS GKIFIGFPTA
QTTGLLAHIS APSVIPTVER ESIDLNARYV RDWNIEMLRV AGIACRIAYT GDMTELKARI
ERTRTADGRK KVTMEDVTSA MPAAVHTYRQ YNYAESTPSS KVGQYIEEAF WTCNTQASID
VLSTRGVLPS QQVRVATEDL SFVDGIPVVP DELMEKGHEF IGKLREYGLL SDITTSDIKK
ELEVQALTEK QVQELVKWSC TKVWRQEMDA DAVQLLFDGT VASIDEQFVS TSSSPVLQLG
QISTFVNTIR IPADMPTPPQ TIPFRLTKGL SPTHLQSIGW DELQIVPWVR WIIESDGQGF
GQGQSLTSSP TVASQVLPVV SKSWDALSQS SKQTIQELFI PRTVIPTKLG MRRPPQAYFG
NVKLFDDLPT ITGLQGVKEK FLGSLGVRKT VELNVVFDRL MAKSAAGSTL EEGKWSHVDL
IKYLLSVKDD IPAEDIKRLQ QTPICPAETL SADQVDKGKL FRLSDLLEPN EAIRKLGLPV
LQWPVQYRAT SPEGRFLRLL GLKPFPSVPD LVGILAKAPA GSELQESTLN YWVAHEYQHG
YNKYPVAEID VAFLPVHPYA GEGSNLVAKP KQCYANPKCA VLRFRTLKDY LQAHHTTFGV
ALDPPMEACV ERLIKGPPTN FASAQTLFGY FANRLGEIGP DGNLAERLGN ALIVPVVNRK
PGDKAGQTRF VAPRAVFLGG SDTYGDIFDF VDFGHEANTF LLRIGSKVEP SASELAAMLV
QQPARLLETL GAEKYLMLLR KIAERAANLK KDKTLWSRLK TSPCLLAVKR VRAGEKHVDG
KPEHDDEEVT IDEYSLARAA DMIVIDDIVL YRLFQAHLLA APEEESLETF YQSLETPRVS
QLVDNDQRMG SLLRDQSSAG TLKKLLVERC RLFLDDHRAD DIRHDAAWLE KNVSIQVVEF
LQITRKLKGY RLHYTEKKTA LLHRESRLDA ILYVTARFDL YEVSRAIMGL LLRRSKQQDF
LALEMILESD LRRLKTKGYN VDRILRQKAA ESRIAESERQ KRVEEQRRLA EAEAEAASMP
QQAPAAKAIA APPSDPTAAS PERALSMPGA FDSPEQRPGS SGRGKKSTGL HVFDSIRSQL
GWNTGGRPSI DTPPPYQAND PVGGRSVTPG TERVTSPRDT QANLDSAIKA CREYNSSSVF
SQPEARQIKE TPLYCDSKPG QDLKYIAELS NGVKLYLSRN NPDPNAFLQN YREALAMFVF
TLSEVANIFE LPPQTINVFH DGAGSSIAFN SSGSIFCNLR YFMQLHMGGM TTAEGKIDAL
AYWWMTLCHE LAHNLVKFVA LNMSLYHEAA EILNTANKSG GSLKSLVFGK KSWKSDAKAL
FALATETAKW SDILSDVLEK SGVLKVEKTV TPTLALLLVH DLFLSKKGIA LPASHGLNSA
ISRHKVRLSA ELTKARLRRG FRTLDDLRQY VDAQASSGPQ NGSDGGTPAR HPRWIRINAL
KTTLDDELEY GTFSNYTQVA TLQEIMQAPA EMRAVHVDKH IPNLLAVASP DDPTTFKSYR
NGKLILQEKA SCFPAYLLDP RPGESKAIDG FAAPGNKTTH VAAILGESSQ VIACEKDAER
SKTLVKMVKL AGADSIVDVK QKQNFTRLDP KSAECADVTD VLLDPSCSGS GIFGRDEASI
TVHLPSVAND EAVPKGKKRK RGGEQKAEAK TQQQDALVEE TADEEDGDAA KLKQRLRNLS
GFQLRIVEHA MSFPAARRIT YSTCSVHAEE NEHVVVKALL SDMASERGWN VLKREEQVEG
LKKWHKRGGE EAVKVAVQAS DAELGRKRAI DAKTVAEACI RCKKGGEDGT MGFFVVAFCR
DPEAMSDIDT NGEGVVEEDD EEWRGFSDDE T
//
