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Database: UniProt
Entry: A0A0W8CQF3_PHYNI
LinkDB: A0A0W8CQF3_PHYNI
Original site: A0A0W8CQF3_PHYNI 
ID   A0A0W8CQF3_PHYNI        Unreviewed;       967 AA.
AC   A0A0W8CQF3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Ubiquitin fusion degradation protein 1 {ECO:0000313|EMBL:KUF86371.1};
GN   ORFNames=AM587_10003014 {ECO:0000313|EMBL:KUF86371.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF86371.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF86371.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KUF86371.1}.
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DR   EMBL; LNFO01002293; KUF86371.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8CQF3; -.
DR   STRING; 4790.A0A0W8CQF3; -.
DR   EnsemblProtists; KUF86371; KUF86371; AM587_10003014.
DR   OMA; EDQIMAY; -.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02568; PseudoU_synth_PUS1_PUS2; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR   Gene3D; 2.40.40.50; Ubiquitin fusion degradation protein UFD1, N-terminal domain; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR   InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR   InterPro; IPR041708; PUS1/PUS2-like.
DR   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   InterPro; IPR004854; Ufd1-like.
DR   InterPro; IPR042299; Ufd1-like_Nn.
DR   PANTHER; PTHR12555; UBIQUITIN FUSION DEGRADATON PROTEIN 1; 1.
DR   PANTHER; PTHR12555:SF29; UBIQUITIN-DEPENDENT PROTEOLYTIC PROTEIN-RELATED; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 1.
DR   Pfam; PF03152; UFD1; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT   DOMAIN          213..381
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   REGION          249..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..924
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..967
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-1"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR641708-2"
SQ   SEQUENCE   967 AA;  108394 MW;  4325FD5665F89B83 CRC64;
     MLTRFALRPA GRTALRSSFC RGLAASSGTD DGIKTGRRWT DLFTTTEPAK LVKRKVAIVT
     GYMGTGYHGL QLNDNVKTIE DDVRQAIFDA GAMRESNFVD LGKIDWARSS RTDKGVHAGC
     IVFSGKLLID EENKMDPVSG RVYGLKEALN ASLPDNIRVF SCTRVSKRFS ARKNCVLREY
     EYFMPLSFLK DSLVGSDGED FDTDEAVAEF CRALRRYEGV HDFHNFTRSR SYFYKMQAKR
     KHYRANYQRN AAEDESDDVD AEDVEDESAE VDSVVDDYSE ESSQFEDEEE LTRKLLLRHR
     RSIYSCSGTL VPDFCGEPHL RVHIVGQAFL LNQIRCMVGG ALAVATKGMS RVEFDAALLT
     NRIVRVPIAP AEGLVLLSSS FGGKSHTVSL YEDPNTELAK ERKDVVHRVL LNRKEDEEMR
     QFREEVIYKE ISRSWDMEEK MDRWRAYLER CYEANERLNQ DELSAVLYEM DQAKLATKNK
     NQAHVEQNRF ELTEYGRKSV GALLPKQFAT KLCVRYSVAP GIFTSDLRRA VTRHLKTGKI
     PLDADEEQIL EYIDNYGPAN LAKEGRKLRL SIRTQQQQDR RVDTTLLSTM VWTVTHLSTR
     SISNLWAMNC PQFGFGGDGN PFGVQFNFGD FPQRFDEHYR VYPVSFCDKA HLEDGDKTRL
     HIEYPMLFKV TNEGVERSSH CGVLEFSAPE GSCYMPYWMM QNLFVKEGGI LNIQNVSLPK
     ATFVKLRPQS QDFLDISNPR AVLEGSLRKF SCMTVGDTIC LKYNNKNYML DVREVKPEPA
     ACIIETDCEV DFEPPADYVP PVPQSAAVAP PAAPSDIPYG GVPTMKAEDV KPPRLGGTGF
     GSGLRLKKSG EKSSTDADAL RAARLRKYEA FHGTGHSLSG KTSTFSGATA GGTRLGGSSN
     GGYSLNGSSS ASNSNDTTAK AKQSVGHRLN GEAVGASDDE EMKDEEMKEN EEHKGVVPFQ
     GEGRRLR
//
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