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Database: UniProt
Entry: A0A2G9HV59_9LAMI
LinkDB: A0A2G9HV59_9LAMI
Original site: A0A2G9HV59_9LAMI 
ID   A0A2G9HV59_9LAMI        Unreviewed;       999 AA.
AC   A0A2G9HV59;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=CDL12_05880 {ECO:0000313|EMBL:PIN21407.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN21407.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN21407.1}.
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DR   EMBL; NKXS01000945; PIN21407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9HV59; -.
DR   STRING; 429701.A0A2G9HV59; -.
DR   OrthoDB; 467211at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000231279; 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:SF8; U-BOX DOMAIN-CONTAINING PROTEIN 44-LIKE; 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; 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:UP000231279};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          247..321
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   COILED          59..86
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   999 AA;  111852 MW;  AA3F1BDC159CE701 CRC64;
     MENHMASESL LDTSNSISEV VDIARDVPIQ TDNFKKFSSF LDRIASFVQE LSKFEVKNFE
     IINKALENLK VEIEFAKQLV LDCKNRNKIY LFVSCKRIVE DLDNCTKNIS RVLSIFASGS
     LDVPAERNEW LMNLCKNMPD VKYHVSEVEE EILQKIETGL VDRNNDRSFA SDLLVRIAES
     VGIELSERKT EFENFKDEME RIESRTDASR MEQIVLLLSN ADILTTPKEK EMKYFTKRNS
     LGRKLLEPLP SFYCPITADV MVDPVETSSG HTFERAAIEK WLSDGNNLCP LTKTPLSRSS
     LRPNKTLGQS IEEWKNRNTM ISITSMKPEI QSSDEEEVLC SIEKLRGLCE RSELHREWIV
     MEEYIPIITG LLSAKKREVR VHSLAILYSL AKDSEDNKER IAKVNDSSIT YIVRSLARRV
     DESMLSLQLL LELSRSNGVR EMIGRAQGCI LLLVTLASSD DAEASEYARE VLDNLAAIDE
     NVIQMARAKF FKPLLQRLCE GPVDVQTIMA ETLADIELTD HNKLCLSSEG ALKPLLQMLH
     NSDIEVKGVA VKAIEHLLGV APNGLQLIKE GAKDPLFELL FCHTLSSRKL REHAAKSIMH
     LAVSTTSPEA SEGQISLLET QEDIFKLFSL ISYVAVDMQE ILLLAFHAMC KSPSGLNIRS
     YLRQISAVKV LIQLCELDEL VVRANAVKLF YYLTEDGDHA TFSEHVNKKC ITCLLKIIKT
     SDNEDETAAA FGIISHLPQN PQISENLLEC GTLEVIFDCL TSRNVHSSQE NTIVESASKA
     LCRFTLPSHI EIQKRVAEAG MIPILVKLLE SGSPLTKRNA AISLKQFSES SRELSVPVRR
     SHILGCCMRS PEPKCPVHSG ICTIESSFCL LEAKAVRPLV VVLEEPDDEA CKASLDAILT
     LIDGLQLQSG CKILEEAGAV PPIIKFLNSS CVDLQEKALR ALQRIFRMIE YKTKHGKSAQ
     TLLVDITQRG SRDTKSLAAK ILAQLNVLNE QSSFFSGAV
//
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