ID A0A2P5DFD7_PARAD Unreviewed; 1010 AA.
AC A0A2P5DFD7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=PanWU01x14_068540 {ECO:0000313|EMBL:PON72012.1};
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:PON72012.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:PON72012.1}.
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DR EMBL; JXTB01000041; PON72012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5DFD7; -.
DR STRING; 3476.A0A2P5DFD7; -.
DR OrthoDB; 467211at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd21037; MLKL_NTD; 1.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045766; MCAfunc.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45958; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR45958:SF8; U-BOX DOMAIN-CONTAINING PROTEIN 44-LIKE; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF19584; MCAfunc; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 7.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 260..334
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT COILED 67..94
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 195..234
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1010 AA; 112137 MW; 8E7ACCBEBDD5D500 CRC64;
MAKDVIISVS VIPTSELLSH VVLGLFETAQ AAKKVLFQEA NFKTFSAHLE KTSAILKELS
KQNIDHFESL KNTLEILNRE VKAAKQLVVD CSQRNKVYLL LNCRKIVKRL DSCTEEISRA
LSLIPLASLD LSLSINDQIC KLCKNMLEAE YRAAVAEEEI LAKIEFGIQE RNGARSYAND
LLFQIAGVLG LSTEHSALKE EYEAFKREIE DANLRKEQEE SLQMEQILSL LEKADAVTSS
EEKEKKYLER RNSLGNQPLA PLKGFYCSLT HEVMVDPVET PSGHTFEKSA IEKWLAEGSK
LCPLTNAPLD TSDLRPNKTL RQSIEEWRDR NAIITISNIK PKLQSSEEEE VLQALSKLQE
LCMERDLHRE WAAMEDCISV LVGLLGAKNR EIRKDALVIL SILAKDGEDK KEKITRMDNA
LQSIVSSLAR QYEESRSALH LLLELSKSNA AWELIGNVQG CLLLIVTMLS SEDNQVATDA
VQLLEILSFH NHNVKQMAKA NYFKPLLRLL SSGPEDIRIS MAKTLAEIEL TDHSKLALVQ
DGALGPLIQM LSQGDLETKK VAVKCLLQLS NLPKNGLQMI REGAVEPLFE VLYRHSLQLP
ALREQVAATI MYLSISTNNQ ESDGEQVSLL KSEEDIFKLF SLISLTGPDI QRSILKTFHA
LCQSPSGLDI RMRLRQLSAV RVLVQLCEAD QHTVRVSAVK LFCCLTKDGD DGTFLEHVSQ
RCIETLLRII QTSNDVEEIA AALGIIAYLP KNSEMTQWLL NAEALRIIYI CLNDGNRDVS
YKRQVIENAV GALCRFTVST NQEWQKRVAE AGFIQVLVRL LASGTSFTKQ NSAIALKQLS
ESSKNLSKPG KKHGIFQCCI SAPKTGCPAH LGSCGVESSF CMLEANAVDP LVRMLGEPDL
ETAEASLDAL LTLIDAQKPQ DGSKVLDNAN AIAAVIKLLS SNSVRLQEKC LKGLEMIFQS
DELKRKYGSS VQVPLVDIAQ KKASDMKEIK SLAAKILGQL GVLGVQSSFF
//
