ID A0A2H5NVF4_CITUN Unreviewed; 225 AA.
AC A0A2H5NVF4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CUMW_077310 {ECO:0000313|EMBL:GAY43795.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY43795.1};
RN [1] {ECO:0000313|EMBL:GAY43795.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC form of a thioester and then directly transfers the ubiquitin to
CC targeted substrates. It probably triggers the ubiquitin-mediated
CC degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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 -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119}.
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:GAY43795.1}.
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DR EMBL; BDQV01000021; GAY43795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5NVF4; -.
DR STRING; 55188.A0A2H5NVF4; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044286; SINL_plant.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR46632:SF16; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 10; 1.
DR PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 37..95
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
SQ SEQUENCE 225 AA; 25509 MW; 31C277DAF619728D CRC64;
MVCTTCRSKI KNDSCPFDRS PIAYTRNRVI EKLLESVKSV SCKNAEYGCN ETLGYLEKND
HEKACKHSPC SCPLSGCDFL GSSSQLYQHF RAQHQNSSVL FRYDQDFSIR LDAKNDKFLV
LLEGRDDNIL FVLHNATSNQ QQNGLSISCI SSSREARNEY KISVSFGSNN VSTLTFRSAI
SSSKKQLDNL PKLGFPLVPW LLDATDGRLN LKICIFKDRL PHWLR
//