ID A0A1V9YIC0_9STRA Unreviewed; 596 AA.
AC A0A1V9YIC0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Ubiquitin fusion degradation protein {ECO:0000313|EMBL:OQR85461.1};
GN ORFNames=ACHHYP_11807 {ECO:0000313|EMBL:OQR85461.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR85461.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR85461.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR85461.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SIMILARITY: Belongs to the UFD1 family.
CC {ECO:0000256|ARBA:ARBA00006043}.
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:OQR85461.1}.
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DR EMBL; JNBR01001675; OQR85461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YIC0; -.
DR STRING; 1202772.A0A1V9YIC0; -.
DR OrthoDB; 77320at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 2.40.40.50; Ubiquitin fusion degradation protein UFD1, N-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004854; Ufd1-like.
DR InterPro; IPR042299; Ufd1-like_Nn.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001293; Znf_TRAF.
DR PANTHER; PTHR12555; UBIQUITIN FUSION DEGRADATON PROTEIN 1; 1.
DR PANTHER; PTHR12555:SF13; UBIQUITIN RECOGNITION FACTOR IN ER-ASSOCIATED DEGRADATION PROTEIN 1; 1.
DR Pfam; PF03152; UFD1; 1.
DR PROSITE; PS50145; ZF_TRAF; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00207}; Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00207};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00207}.
FT DOMAIN 403..445
FT /note="TRAF-type"
FT /evidence="ECO:0000259|PROSITE:PS50145"
FT ZN_FING 403..445
FT /note="TRAF-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT REGION 183..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 64753 MW; FDA7E31E11857341 CRC64;
MGPKAGFRGS FTCYSVACID MPDLEFGDKV ILPPKVLLEM QCLKIALPIV FKVTSSQTAA
LPCQYCSVLE FSAPDGQMYA PYWMMQNLLV DEGGPLHLET AFGIPRGIYC RFQPHESVFL
DLAAALGPKV LLEAAMRKYS VLSIGETIAI EYGAEKHLVT VVEVKPGAVV HLFGDVDLEV
DFKAPENTDP RRPKSAAPRD EHGDLKEALV AVAPPVTDPT PSAATPATFG RRLGDGGYVQ
VDVAATSAKA AHKLSFQEAQ RKTKSDHGPN PLTTRSLKAF ETTGYVLETR GEPGPEMAEP
VTVSVPVTAV SEAVPCGYCL GDIPRANFEL HELRCKARTA YHRVLCSTCG EKTLKCQLAD
HVHCPECPFL GTAEALAQHH QDVHANVRCP CGATVPSNLL RQHQDTTCPR TLTVCSVCTL
SFPRVKHAQH LAACSSRTLQ CERCKQYINV LAFNQHEATC IEEGRVEKDA VKAARHAGRF
ACPYCTAATF DTMTALDKHT EHECTIARSF NGSSAPLKES PPILRGKLRR KTDLVKPRST
LQQAGGRVVE KPVTSSLGEI QLLKGASLGV AKPTATRQRK ADAILNRTSR KPPTKR
//
