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Database: UniProt
Entry: A0A2P5AW94_PARAD
LinkDB: A0A2P5AW94_PARAD
Original site: A0A2P5AW94_PARAD 
ID   A0A2P5AW94_PARAD        Unreviewed;      1029 AA.
AC   A0A2P5AW94;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Ubiquitin conjugation factor E4, core {ECO:0000313|EMBL:PON40797.1};
GN   ORFNames=PanWU01x14_294880 {ECO:0000313|EMBL:PON40797.1};
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476 {ECO:0000313|EMBL:PON40797.1, ECO:0000313|Proteomes:UP000237105};
RN   [1] {ECO:0000313|Proteomes:UP000237105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
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:PON40797.1}.
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DR   EMBL; JXTB01000432; PON40797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5AW94; -.
DR   STRING; 3476.A0A2P5AW94; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000237105; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16657; RING-Ubox_UBE4A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT   DOMAIN          931..1005
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          435..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          510..537
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1029 AA;  116376 MW;  F959D422081DE3CD CRC64;
     MATPKPQRSP EEVEDIILRK IFLVSLTETA AESDSRVVYL ELTAAEILSE GKELRLSRDL
     MERVLIDRLS GNFASAEPPF QYLIGCYRRA CDEGKKIASI KDNNLRSEME SAARQAKKLS
     VSYCRIHLAN PELFSAANSS PNRPNGSPLL PLIFSKVGSS LDGFGGVVGG SGGVESPPGF
     LEEFFRDSDF DSLDPILRGL YEDLRLGVLK VSALGNFQQH LRALHFLVSL PVGAKSLVNH
     PWWIPKGVYL TGRAIEVTSV LGPFFHVSAL PDHTIYKSQP DVGQQCFSDA STRRPADLLS
     SFTTIKTVMN NLYDGLSEVL LLLLKNQDTR QGVLEFFAEV INKNSSRAHI QVDPMSCASS
     GMFVNLSAVM LRLCEPFLDA NLTKRDKIDP KYVFYGDRLD LGGLTALHAS SEEVAEWTNK
     RQSDGENRLL QSQEATSSGI NTFGPPITKS SSSGEKTKYT FICECFFMTA RVLNLGLLKA
     FSDFKHLVQD ISRREDALTT LKDMQGQTPS PQLQLEITRL EKEIELFSQE KLCYEAQILR
     DGTIIQCALS FYRLMVVWLV GMVGGFKMPL PSTCPTEFAC MPEHFVEDAM ELLIFASRIP
     KALDGVLLDD FMNFIIMFMA SPNYIRNPYL RAKMVEVLNC WMPRRSGSSA TASLFEGHQL
     SLEYLVRNLL KLYVDIEFTG SHTQFYDKFN IRHNIAELLE YLWQVPSHRN AWRRIAKEEE
     KGVYLNFLNF LINDSIYLLD ESLNKILELK ELEAEMANTA EWERRPAQER QERTRLFHSQ
     ENIIRIDMKL ANEDVSMLAF TSEQITAPFL LPEMVERVAS MLNYFLLQLV GPQSKSLSLK
     DPEKYEFRPK QLLKQIVCIY VHLARGDSEN IFPSAISKDG RSYNEQLFTD AADVLRRIGE
     NGKVIQEFDE LSAKAKVAAS EARDAEATLG EIPDEFLDPI QYTLMRDPVI LPSSRITIDR
     AVIQRHLLSD STDPFNRSHL TADMLIPDTE LKERIEEFIR SQEMKRREGL STQSIKATIQ
     TTDGQMLID
//
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