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Database: UniProt
Entry: A0A2K3NYY8_TRIPR
LinkDB: A0A2K3NYY8_TRIPR
Original site: A0A2K3NYY8_TRIPR 
ID   A0A2K3NYY8_TRIPR        Unreviewed;       357 AA.
AC   A0A2K3NYY8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=L195_g004768 {ECO:0000313|EMBL:PNY08252.1};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY08252.1, ECO:0000313|Proteomes:UP000236291};
RN   [1] {ECO:0000313|EMBL:PNY08252.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY08252.1};
RX   PubMed=24500806; DOI=10.3732/ajb.1300340;
RA   Istvanek J., Jaros M., Krenek A., Repkova J.;
RT   "Genome assembly and annotation for red clover (Trifolium pratense;
RT   Fabaceae).";
RL   Am. J. Bot. 101:327-337(2014).
RN   [2] {ECO:0000313|EMBL:PNY08252.1, ECO:0000313|Proteomes:UP000236291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:PNY08252.1};
RX   PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA   Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT   "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT   (Trifolium pratense) Breeding.";
RL   Front. Plant Sci. 8:367-367(2017).
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   -!- 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:PNY08252.1}.
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DR   EMBL; ASHM01002389; PNY08252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3NYY8; -.
DR   STRING; 57577.A0A2K3NYY8; -.
DR   OrthoDB; 48141at2759; -.
DR   Proteomes; UP000236291; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   CDD; cd16667; RING-H2_RNF126-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF22; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236291};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          238..279
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          131..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  39888 MW;  443C14A5FC453061 CRC64;
     MDETMAARYW CHACSQIVSP IMGMEMKCPV CQGGFVEEMS SATGISDLPN IPEPDFGPDR
     SPSLWAPILL GMMGNPRLRR RMRRIELEED YDSGNRDDEN SGVGHYDREL ESILRRRRRS
     SATIQQLLQG IRAGLTSEPQ ENTTDSDDHV REREREHVIL INPFNQTIIV QGSYDSNRDQ
     NDNPNPIGSL GDYFVGPGLD LLLQHLSEND PNRYGTPPAP KEAVEALPTV KINENLQCSV
     CLDDFEVGSE AKEMPCKHRF HSACILPWLE LHSSCPVCRS QLRVDEPKQD SDVSRNRRNQ
     RDDANIGHAN ADAEGDSEGR SPNGGRRFSF PWPFNGLFSS SASSSSSNGN GTQSERN
//
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