ID A0A094D9E7_9PEZI Unreviewed; 1953 AA.
AC A0A094D9E7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=F-box domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V496_06798 {ECO:0000313|EMBL:KFY56110.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY56110.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY56110.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC 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:KFY56110.1}.
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; JPJY01001282; KFY56110.1; -; Genomic_DNA.
DR STRING; 1420909.A0A094D9E7; -.
DR HOGENOM; CLU_001755_0_0_1; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 66..111
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT DOMAIN 1117..1530
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..575
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1413
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1236..1242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 1360
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1953 AA; 215370 MW; D532C9C650B72C5A CRC64;
MPSLKQSRSK RTTPIAIVSN KGPWSQWHDP NDTEINSPAP TVSAAMRSAD PISAPEGGKA
KQTPRSLTFF DLPSETQNAI IKQCPTPDLI SLSLVSKHFR DLAAARIYRY FHIVFPDGDD
GSYESDMDGL AAGLDTMVTS EYDYARYLKE IDLESLSGGA KGERAYGQYT YDLSCGKFMN
TLLLLTLRKA KTLETFRWDV RVELSRPVYK SLHGIPALKH LCVRMHSGSS LYQKPPPLPS
LKCFPDDTIE MVKKFTKAIV GRSEDLPIKM SSAEARAILA SHAKDLKTDH GPPTISGFKN
LKTLAILDMD SLEYVKEIRT CIHNSSSTLK KLKLSFSEEL ARKARKPPPV DDTGDDSDQE
MDEFGNMIPP PPVGAPSSTD DSSSPGKAFR ALEAKQAQDA VLAQIFGLDS KAREIPASDA
GGKEKKASGG MGDTVNSFIK DITALSKKVM GAPSSSELTP EQREFVKAVE KRARKLLKGE
KGALAGDPGK DGLEEDSNAE SSTEKATPSS SSDTSEAGKA EEEDKAKTTE SEDKYVGLFD
NEDKKAPNAN QSTVDSPQPD DIDVCEPEMG LDPQDDDSAT SELAPETAND GIPTTAVGST
ESLSPKKLEP TLITAVESIK SLTKHFIEKP DLGKNFSRDV LELALAQRAL EGYRFHDIAV
DSYQYNVIRG AAEAHNKSLE KTDKSMSEYV RTTRGLTLKS LSIYLIPIKT SVLSRAVDLH
VLERLSLLNV GSQAPLWNYL AKENKISPLP LCKIHTDNVT AHFLKFVNQL ENLEELFILE
RSTKSSEYSF APKTTVTNDN IRHYVLKKHA SSLVRLVVKN ENDYTWDANV KFLELLCQQG
KNLTELGISF ASPALHTFNQ FLPGLVSLKA LHIINFRNED TCHWVMREIP RFIADALSSH
PSMKLEYLAL GSTVGRLAWK VKVVPKPEDK GKGKATIYTS NTNLLPEEKL SESESEEEDD
STPGLRLETV ECGRFYDVPG VGGHNPPPPP PGWSRDLVLG LVASGETIPR RSGVAQGFDE
LLCAAARRKS LMFKGSVSLR RQYYSLFQSS LSDFTMGRGG KRGGRGGGRG KGRGGGGGGR
DSRDNRVSYD KIEKTNEKFE RYYDSIIELP EEERVEFWAA LRRDLPNSFR FAGSKGHALA
VQKQLRERYI PEITKIEHYD GTAVEAPKPV PWYPDELAWW MTTPKNVVRR FPPFAAFQKY
LVSETSVGNI SRQEVVSMIP PLLMGIEPGM TVLDMCAAPG SKAAQLLEMV HKGEEARIRN
ALRLHAKEDG REISPGLEVV GDEDLNVDSE DFGRATGLLI ANDSDYKRSH MLIHQLKRLS
SPNLIVTNHD ATIFPSIKLP STKEDPAQNR YLKFDRILAD VPCSGDGTCR KNPNLWQDWS
PSNALGLYVT QVRILVRALQ MLKAGGRVVY STCSMNPVEN EAVIASAIER CGGLEKVQLV
DCSDQLVGLK RKEGLKKWTI MDKSGKVWED WPSVDAENQK GGANHATARL AEGMFTPTGE
AAKIPLERCM RVYAHQQDTG GFFITVLQKM TEFKAKPESE AKKSEPKPAV ISIVEEIEAQ
PEPAPGANVA PKIEAADLLE GSTSTDLQDQ NVPAVARENQ ASDKPDATLP AKRAFDDSDV
APSSPKKAKI ESNGTEAEAM SLDNRQVHFP PPPGAELDAT IRPGDLRPET TPAATTSLPA
PVKAKGRNQQ QFEEPFKYIS GDHPEVQSID EFYKLSQRFP RDRFMVRNAL GEPAKTIYYT
SALIRDILVE NEGKGIKFIH GGVRMFMKQD VQGEGVCRWR IQSEGMPILE GYVGEGRVVR
LYKRSTLRKL LIEMFPKVTD GCWKELGEIG ERVRDIGMGC CVLRIEPSDD EDGFKERIVL
PLWRSLHSLN LMLAKEDRTA MLLRIFNENV PLVNNHHPSQ RAAAVVDAAV AEAEVAEAKT
ANGNGEVVAE KSEDVEMDAA EAPLESEAAS DQL
//
