ID A0A2P5AA38_PARAD Unreviewed; 878 AA.
AC A0A2P5AA38;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN ORFNames=PanWU01x14_353010 {ECO:0000313|EMBL:PON33407.1};
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:PON33407.1, 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|RuleBase:RU365038};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365038}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC ECO:0000256|RuleBase:RU365038}.
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:PON33407.1}.
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DR EMBL; JXTB01000732; PON33407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5AA38; -.
DR STRING; 3476.A0A2P5AA38; -.
DR OrthoDB; 53681at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16499; RING-HC_Bre1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|RuleBase:RU365038};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW Kinase {ECO:0000313|EMBL:PON33407.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Transferase {ECO:0000256|RuleBase:RU365038};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 826..865
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..74
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 242..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 587..625
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 769..803
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 100877 MW; C9F43D6F156B81E3 CRC64;
MGSTGEADRK RRHVSSLSPT AASAKKHHSV PISEDKKLDI TVLQYQNQRL IQKLEAQKIE
YLALENKFSQ LEEKHEPYDS TLKVVDKSWE ELARDLESFS IHTRDTSCKQ DVDYKSVVEA
GAQSTFHEAF LSRLTETGAT ESSSLCNFPK QMDGDQLKAY EKTKNILSNL VAVVDNLWYL
KDGIHAAVLK RLSEDGSCTQ MTPSELEREV KNLRLAFTDL FLKHKLLSTE LQCHRDIDAK
NKAELRNLRG ELQSRVAELE ESNCKLATLK AQRDAAKGAG FPFLNLGSKH VSSDKVRDKV
KDLQDMESTL KELMDQASCR LMEIKGLHEE RIKILQQLSN LQNKLKNVAC ISSSQAYLSV
RDQIENSKSE VIEYQASYEK LQAEKDNLVW KERELNVKSD VIDVLRRSAA IIDSKMTDLR
IEIQRQNDER KMIETKVEEA SREPGRKEII AEFKALVSSF PEEMGNMQGQ LRKYKETASD
VNSLRADVQS LSSILDRKVK ECETLFARST GQAAEIQKLQ TMVQDLKEGD SELKLILEMF
RRESTDSRDV LEARDLEYKA WAYVQSLKSS LDEHSLELRV KTANEAEAVS QQRLAAAEAE
IADMRQKLEA SKRDLLRLAD VLKSKNEENE AYLSEIETIG QAYDDMQTQN QHLLLQITER
DDYNIKLALE GLRTRQLQDE LFMDKRTLER EIQQANSCLN FYDLKAARIE DQFKICSDQI
QKLVEDKFQS SVMMDSTQKK LLDVKRSSEQ ARGSVDESQS KVDKSRVAMV DLQMELEKER
FEKRRIEEEL EVLRRKALRL RAQTEGSSII EKLQQELGEY REILKCTICL DRTKQVVITK
CYHLFCNPCV QQIIDTRHRK CPTCSTTFGP NDVKSVYI
//
