ID A0A3B6GNZ6_WHEAT Unreviewed; 459 AA.
AC A0A3B6GNZ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CFC21_045437 {ECO:0000313|EMBL:KAF7034417.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS3D02G029400.1};
RN [1] {ECO:0000313|EMBL:KAF7034417.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7034417.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS3D02G029400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3D02G029400.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS3D02G029400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7034417.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7034417.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119}.
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DR EMBL; CM022219; KAF7034417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6GNZ6; -.
DR STRING; 4565.A0A3B6GNZ6; -.
DR EnsemblPlants; TraesCS3D02G029400.1; TraesCS3D02G029400.1; TraesCS3D02G029400.
DR Gramene; TraesCAD_scaffold_075129_01G000300.1; TraesCAD_scaffold_075129_01G000300.1; TraesCAD_scaffold_075129_01G000300.
DR Gramene; TraesCLE_scaffold_059989_01G000300.1; TraesCLE_scaffold_059989_01G000300.1; TraesCLE_scaffold_059989_01G000300.
DR Gramene; TraesCS3D02G029400.1; TraesCS3D02G029400.1; TraesCS3D02G029400.
DR Gramene; TraesCS3D03G0053000.2; TraesCS3D03G0053000.2.CDS; TraesCS3D03G0053000.
DR Gramene; TraesPAR_scaffold_059604_01G000300.1; TraesPAR_scaffold_059604_01G000300.1; TraesPAR_scaffold_059604_01G000300.
DR Gramene; TraesRN3D0100058200.2; TraesRN3D0100058200.2; TraesRN3D0100058200.
DR Gramene; TraesROB_scaffold_054801_01G000300.1; TraesROB_scaffold_054801_01G000300.1; TraesROB_scaffold_054801_01G000300.
DR Gramene; TraesWEE_scaffold_117924_01G000100.1; TraesWEE_scaffold_117924_01G000100.1; TraesWEE_scaffold_117924_01G000100.
DR OMA; QVDSKCH; -.
DR OrthoDB; 875020at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019116; Chromosome 3D.
DR Proteomes; UP000815260; Chromosome 3D.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049548; Sina-like_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR10315; E3 UBIQUITIN PROTEIN LIGASE SIAH; 1.
DR PANTHER; PTHR10315:SF173; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF21362; Sina_RING; 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 Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT DOMAIN 89..147
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..332
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 51336 MW; B468C0BC6FC7D916 CRC64;
MDGSSSSKRK AEAQREGESS AKRLNVTVGM EHLDCPICLK PLRPPILQCS VGHFICSYCC
TYQVDSKCHL CSEETTFERC FGMEHVVESV TVACSNEMYG CAETVTYYKK EEHKEACPYA
PCFCPESGCG FAGPTKVLLE HFTTQHKCPS TTLPDSGTVS LCLQPGLHVL QCTRNSYFFL
LSMASEPFGH VISVVCVEPN RRKSKFTCNL SYDCITTGCC GSTSCHIRSS SLSDGLPAVY
DLILPKGKVS DDANGIMLRA TINQQALSHS RSCFRGKGPT SALQQRPDTC DDEEDDDDIP
KSHRRSHPAK EEEEVEEEDE DDEDNEEEEE EDERPLSVRR SHLAEEEEEE EDERPLSLRR
SHPAVQLRPN AYHDDGQGEE DEEDARPVSV SRPRVRGTAP ARVVLQSDTD DEDDFPIAFR
SARLRGMRPA PAVQERHYFD TSDEDDLPIA FRPFIRGTA
//
