ID A0A6A2YN00_HIBSY Unreviewed; 406 AA.
AC A0A6A2YN00;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=U-box domain-containing protein {ECO:0000256|RuleBase:RU369093, ECO:0000259|PROSITE:PS51698};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369093};
DE AltName: Full=RING-type E3 ubiquitin transferase PUB {ECO:0000256|RuleBase:RU369093};
GN ORFNames=F3Y22_tig00111372pilonHSYRG00230
GN {ECO:0000313|EMBL:KAE8680721.1};
OS Hibiscus syriacus (Rose of Sharon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8680721.1, ECO:0000313|Proteomes:UP000436088};
RN [1] {ECO:0000313|EMBL:KAE8680721.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YM2019G1 {ECO:0000313|EMBL:KAE8680721.1};
RA Kim Y.-M.;
RT "Draft genome information of white flower Hibiscus syriacus.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|RuleBase:RU369093}.
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 ECO:0000256|RuleBase:RU369093};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369093}.
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:KAE8680721.1}.
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DR EMBL; VEPZ02001321; KAE8680721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A2YN00; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000436088; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR FunFam; 3.30.40.10:FF:000442; RING-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
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; IPR058678; ARM_PUB.
DR InterPro; IPR045185; PUB22/23/24-like.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22849:SF103; U-BOX DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22849; WDSAM1 PROTEIN; 1.
DR Pfam; PF25598; ARM_PUB; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000436088};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369093};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369093}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..406
FT /note="U-box domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025415500"
FT DOMAIN 24..98
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
SQ SEQUENCE 406 AA; 45639 MW; 91657DF3F8C0F414 CRC64;
MSFIFRSFFL VLSFLPSMKE DQMGIPHLFR CPISLDLLSD PVTLSTGQTY DRSSIENWFA
YGNLTCPVTM QKLHDPSLVP NHNLRHFIQQ WRQMAQPFHP DYSTTIDPLF CMNRGLESPQ
ATSQEKLQIL QKIRVLIDEA PCKIPFLLQT GLLPLLLQLL FGKLDPGFTE ELLYCILKLM
SFDEFGCLNM LKEESKMESF VVLFENGTAM IKQSLCHLVG AISASSETTE LCEMIGKDRR
FLHRLVDLIH QNSETSKAGI EAVSALCFLE SNREELVRHG LINGLVTYIL NSETKKRSSA
AAVTAMATIE QVMGMEKAKE ALIKDPQGVK AVVKMVFRVS DHEGSESALN SLITVCCESL
QARENAIAAG VLSQLLLLLQ SQCSCRIKTK ATVLLKLLRS KWDEEQ
//
