ID A0A1Z5JC32_FISSO Unreviewed; 1133 AA.
AC A0A1Z5JC32;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FisN_22Lh256 {ECO:0000313|EMBL:GAX11563.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX11563.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX11563.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX11563.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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:GAX11563.1}.
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DR EMBL; BDSP01000041; GAX11563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5JC32; -.
DR InParanoid; A0A1Z5JC32; -.
DR OrthoDB; 3084186at2759; -.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 291..324
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 519..790
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 523..575
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 129..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 937..971
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 137..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 127940 MW; 554CF3254D19AEAC CRC64;
MRCSLIRPRA KLADDISETP HAIVIRSLRR RLCQAFCEGN AIKALCIYKA QRSDWERWAE
SEKEAAQKSA SNDLSRQTSN LTMQLTNDSQ DEIGLLQSEM NPSEFFCADD YFKPNDPYND
EIKEAVVPTP LPKPKRREPF SMFRFGDKGK KEDDNTSGND DNKLHMTTPL HEAARLGCGE
LVRLMLAHDS VDCQKRNGQY RTPLHMVAGG IAKEDHVGIG PLISPKGDSK PVGTSGSKLR
TFFRRKSKSD VVKFKSLAVA CSMDSRVDAL RAIISWSEQR EVLSTNSVDS DGRTALHYAA
ELGREKICHE LLSSFGANLT IVDSMGMNPC EKAAEQNYHD LAAFLEAKAV LYIDPFGMDN
ELYESNLGLQ HLNGFSRQTL TTPFSWFETL VDVQKERERR RDIMENKMKK ILSLRIEKEE
FKARILARGT MDDEVEWSAT KTVEKSSDTP SGKPESLLDA LRWFLGRVRS CHADKLLSLN
EWNLKRCVER FYIDPIQMLK DAGLHFQPDS SDEGNKTQDF QTCLICCEEF NAQSAKRERL
SNCLHRFCRD CLSDYVSNCA KSGMSCFKVT CPHHECNSPL LQSELADFAS DSDYALLVDT
SNADFVVGAY DVRYCPHPGC AGVVQFNASV FRESIEDHLT IHKTVGAVCT YDSGGDHHGP
LTYEGVCDTA YYGTLKQPKL AHRFCFNCGE SMHWPVSCRQ LEEWNEVVKE HVQEVSGVED
SDDYKDVAQK LWMRANTRPC PKCQAPIQKS DGCNHMTCRG CRYEYCWICS GDWKHHTTET
GGFFRCNRWI DQKDHEAYGG LKPDAADIAA AKYITDEQLA DPTKMEVTYG TAMHEARVSR
SRTREMGRFL HHYRRWNAHC ESAVLERNMR DSAIERLAPV VKIASQFVPP YSGDFNFGGQ
GLSFIHAAFT ELLECRATLQ HSYAYLYVQF DTKPGVRGKL SKQLRTEKRA VERIQAELET
MTEQLSDVVA RSHLRATQMQ ILFLTSATAE KRKEFSSCMI TILAKQLKRS SKDGTQAKSA
SRDGREGNFI RNDSANGDKA KLHRRSSNGS DDLVVGDGSS REDIEADIRA SLARFMKNTG
ELDVLRIESD NCEDAFDDKE TQGDWPCLTC TYVNCQGFHC AICGTSRREL SGV
//
