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
//