ID A0A2H5MZ57_CITUN Unreviewed; 336 AA.
AC A0A2H5MZ57;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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_004270 {ECO:0000313|EMBL:GAY32821.1};
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:GAY32821.1};
RN [1] {ECO:0000313|EMBL:GAY32821.1}
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 -!- 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:GAY32821.1}.
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DR EMBL; BDQV01000001; GAY32821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5MZ57; -.
DR STRING; 55188.A0A2H5MZ57; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd23127; RING-HC_BAH1-like; 1.
DR CDD; cd14482; SPX_BAH1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033326; BAH1.
DR InterPro; IPR004331; SPX_dom.
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; PTHR46764; E3 UBIQUITIN-PROTEIN LIGASE BAH1; 1.
DR PANTHER; PTHR46764:SF2; E3 UBIQUITIN-PROTEIN LIGASE BAH1-LIKE-RELATED; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51382; SPX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 1..165
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT DOMAIN 232..281
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 336 AA; 38521 MW; FEDFE586353ACE0F CRC64;
MKFGETFTEY LHGERFLDKC SHVEYKRLKK VLKSCRTCKG LHDSACKTEQ QWDEGKDISE
SQLCQCQSSC QLCDHMFFSE LMKEASDIAG CFSSRARHLL HLHVASGMQR YVLRIRQCFK
NDQQAMIEEG RVLIEYIIMN AIAIRKILKK YDKVHKSVNG KNFKSKMRAE HIELLQSPWL
IELGGFYLNF NGLNCGASSE FSGHFSFDFN ASRPVMTLAL PSSIKLEYDL TCAVCLDLVF
NPYALSCGHL FCKLCACSAA SVMVFEGLKS ASPDSKCPIC REAGVYAKAV HMLELDLLVK
RRFKEYWKER LIAERAEMVK QSKEYWDLQT IHAVGY
//
