ID A0A094FYY2_9PEZI Unreviewed; 2168 AA.
AC A0A094FYY2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=TRUD domain-containing protein {ECO:0000259|PROSITE:PS50984};
DE Flags: Fragment;
GN ORFNames=V498_02905 {ECO:0000313|EMBL:KFY96084.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY96084.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY96084.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000256|ARBA:ARBA00001166};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000256|ARBA:ARBA00007953}.
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:KFY96084.1}.
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DR EMBL; JPKA01000482; KFY96084.1; -; Genomic_DNA.
DR HOGENOM; CLU_001386_0_0_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02576; PseudoU_synth_ScPUS7; 1.
DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.30.2350.20; TruD, catalytic domain; 2.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR NCBIfam; TIGR00094; tRNA_TruD_broad; 1.
DR PANTHER; PTHR13326:SF21; PSEUDOURIDYLATE SYNTHASE PUS7L; 1.
DR PANTHER; PTHR13326; TRNA PSEUDOURIDINE SYNTHASE D; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR Pfam; PF01142; TruD; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 955..1224
FT /note="TRUD"
FT /evidence="ECO:0000259|PROSITE:PS50984"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFY96084.1"
SQ SEQUENCE 2168 AA; 238663 MW; 39DB5EAE9751F923 CRC64;
GSKVGSASGS KIGSQVGSQV GSQVGSQVGS QVGSKAGSVG GAVEGGTERR SRNSSPSGSP
GGSPADSDDG GVKRGWSERM KGRRRRTQRW LERKEDKNAI TAGMVSRAQG GRNRPWGRRA
ILGGTEPDID GGEGDEKKKR VGGFVTMVDA SPAPIRLPSY EKAAKKGEEK GEEDKGKGEG
EEEEEEEWEE GDEEDEWDED SLVRLSDWWR QMLGKGKDPT WQELDMMSAF LTDLYEEETP
SLEMILTTRL HKLLEALIKS VNEQGQRYEG KRYRKVARKA TEIRDKWMHD LGDELYNMRA
ERRKMLKSEK GRLARIHMRQ VGEHSSRWVV EGPCVEEGVE FEPGMWWLND ACAERDGGSR
GDSGFRRRDA NAETDDYALY AQWSHRFDDA ISYAGAGQTS TGATAVYAEI TTGARGGFAR
SMDTVLAVPT PSMLDDWEIY MEVKDDSVRR SIGEAWYRES LTKEREEEKD RLSWHQVRAY
EDARRVEEDK RRKQEEKRRA EEDARRALED EKRGVKMKKA ERELRRRNMG HGAGAANGGG
EEHARKRVRR EDGVSTTATP TIDPSVAHPS VKEDMEKRKT AELTSNASHS REREVGILRW
VNEENVGFEG VLKQRYTDFL VNEITPDGKV IHLTNIYPPK QSKQQQAKPA QPSAPKEPAQ
PVESVPVPTT TVAATEEVVQ TPASTAAEPP KKSTAPETPG NAAATADSFA LAAEDEVLLD
NYFGADVREQ IVKMYKKILA KPNEKAATYG SVTSDPILDR ELRTKLHQDM RRIFDSRLET
NTDKDGLIRI SAAPKAGPNR GARGATNQQT PRNQQKGKLG WAELGGEHLH FSLLKENKDT
MEVISFISSR LGMKPRSFAF AGTKDRRGVT VQRVSVFRKN AEQIAHLNRD MWGSKIGDYT
YEKHALELGD LTGNEFHITL RDCQFPGADN LDDEGKLALA NKVVGGAVES IQSHGFLNYY
GLQRFGTYLI GTDEIGKLIL KNDYKGAVDA ILSFSPECLS AGQDPDFVTS DGKPLSRDDI
ARAKAIDIFR TTGRAKEALD KLPRKFSAES TIIRHLERGD RKTDYMGAIL QINRNLRLMY
VHAYQSLVWN HAVSERWRQS GDKVVEGDLV LVEANADKPA VEELDQNGEV VILPAADDTA
VSTDDMFQRA RPLSADEAAS GKFSIFDIVL PTPGYDIEYP MNAIGGFYKA FMGSERGGGL
DPANMRRAQK DFSLSGSYRK MMGTVGNDVR YEVKAYTEDN EQMVETDLDR INKARGQPSR
NAEPKHRYAG KEVFGITDAV AGRNAWTDSA NTIAEGDKAI ESAAVAGAGD KSSAPAVHET
FIQKDARSGE QTGVKETVLL PGSATAAAND TTNTEAPAAT TIAESTEDKK RGADDMSAND
NEAVEIRRKI AVIVKFQLGS SQREDLHAKA PAVPISDPKL IPKLPLHLLG LPHVLGPPPT
SRAPSKLLKV PHGAFTPDAA SSHSRLVLGG SALLLMDLDM IAQLMADSHT SAHSMEKVQI
RLWRLPTLAK FSGPSIRLQD FKPLIPLEVD EYHGLNSPSL LVTRLAFDQN NGGLLITSIQ
QLSAASVAPS FSLVAVSALC ASFGFARGAN VPTPTAPGAL KFNDHPEQST KVYNVSAAKT
TLSYKYTNEE LAMLWNQVGK IEVGPITTTV SPTPEPTAYA RPGLFHPEVP TYEPALNASK
LPDDFMWGVS ASSYQIEGAA RDEGKGPSIW DLISHRGYGS VADNTTGDIV AQHYYLYKQD
LARIANLGIP YFSPSFSWPR FFPFGAAGSP VNQEGVAHYD DVITSMVNLG IKPVITLFHW
DTPLALFNSY GAWTSPEIVD DFFNYAKFVI SRYDEYVPVW FTFNEPQYCN WQYASYPAGS
EKGNYPAYHG IEGGLEARIA CSHYTLLAHA KVAKWYHEEF KGKGRITFKN SGNYYAPLNE
ASEGDIDAVA RQYAFSLGWF GGPWSDGDYP DMLKETLGPL LPTFTKKEKD MIKGSCDFYA
IDGYTAFFGS ELEGGSAACA ANSSNPSFPE CAGSSQLDPS GFPIGPQADS GVSWLSSTPK
AMRAFLNVLT KELFPSAPDI VVSEFGFAEP DEGLSSNLGS ILWDLRRADY MQSTLDNILA
AKVQDGVNVT GAFGWSIVDN FEWFAGSSVK FGLQYLNYDT LERVPKASAF QFIDWFKRYG
GATLPDKA
//
