ID A0A2P5E2N3_PARAD Unreviewed; 1074 AA.
AC A0A2P5E2N3;
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_010380 {ECO:0000313|EMBL:PON79806.1};
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:PON79806.1, 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:PON79806.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXTB01000003; PON79806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5E2N3; -.
DR STRING; 3476.A0A2P5E2N3; -.
DR OrthoDB; 471094at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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:SF4; U-BOX DOMAIN-CONTAINING PROTEIN 42-RELATED; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
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 285..363
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT COILED 346..373
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1074 AA; 119755 MW; A41F7B9F660F8A62 CRC64;
MKTGSPLTSF ELSQSQTIYA FKNKSKLILC SCKIGWLLIP ERLPFPAASF GCRSCGGLVK
EDATLIMSLA DSLLASISEI TVSVAYIEVE QENFTEIGCY FYRASIAIME LQTTETSPPN
AMEILQSLSE SINLAKDLVQ GLQKGGKPVS GSELRSIISQ LEELIKTMGE HLSSIPSSAF
KDQEYAQVAV HSLSKEMQNS HFTVQSSQYS DVDTQITSPE QQPRQESIPI ETDLYSISVE
VSMENPYFLE PPSLPKAKSS SSIVKEERIS GSLTMLPQVA QYMEPLYDTF YCPLTKKIMD
DPVTIESGVT YERKAITEWF EKFEGSVEVQ CPTTGKKLVS RVYNLNIALK STIEEWKERN
EAARIKVARA ALSLASSENM VFEAIKDIHG ICERNPYNKV QVRSAGMLPL LVKTLGYKNQ
DVRCAVLELL RLMAEDESDI KEVIAEELDF SALIRMLSSS YQPVRHASLL LLLELSRSES
LCDKIGLVTG AILILITIKY KPSIDAFASE KAGETLKNLE RSPNNIRRMA ENGLLEPLLY
NLAEGCEEMK TEMASYLGEI VLGHDSRTYV AERASITLVK MVRNGNVLSR RAAFKALAQI
SLYQPNAKVL TEAGIVQIMV EEMFTRRIHD ELVNSKIEAA AILANIFESG LELENLRVNS
HGHTMTSDYF VYNIIYMLKN STPDELNINL IRIILCLTKT PKSMTAIISV VKETDASYIL
IELINNPHEE LGIAAMKLLI TLSPHIGHTL AERLCKTRGL PESLIQSPRE VTRISEKQAI
SAKFLAKLPH QNLTLNLALL FKNTVPTILQ TVGQIQKSGT RSSRHSISCF EGLVGILVRF
TTTLYDPQIL FLARAHNFTA VFTELLVKTS SDEVQRLAAT GLENLSSESI NLSKPPEIKK
PKLMRLFSTP KFLSSSSSRR EKIPVCPVHR GTCSAENTFC LVDAKAVERL LACLDHENAE
VVEAALSAIC TLLDDKVDVD MSMSILNRSN ALQQVLNVVK EHRQEGLWQK SFWLIEKFLM
KGGDKSLSDI SQDRLLPSTL VSAFHHGNGN TREMAEKILR HLNRMPNSTT YYTM
//
