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Database: UniProt
Entry: A0A453HKQ4_AEGTS
LinkDB: A0A453HKQ4_AEGTS
Original site: A0A453HKQ4_AEGTS 
ID   A0A453HKQ4_AEGTS        Unreviewed;       267 AA.
AC   A0A453HKQ4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=SIAH-type domain-containing protein {ECO:0000259|PROSITE:PS51081};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET4Gv20221900.3, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET4Gv20221900.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A453HKQ4; -.
DR   EnsemblPlants; AET4Gv20221900.3; AET4Gv20221900.3; AET4Gv20221900.
DR   Gramene; AET4Gv20221900.3; AET4Gv20221900.3; AET4Gv20221900.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015105; Chromosome 4D.
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; IPR044286; SINL_plant.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632:SF40; E3 UBIQUITIN-PROTEIN LIGASE; 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   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          73..129
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   267 AA;  29019 MW;  8620B0B521B0BD54 CRC64;
     HSRTNRNVRK KARLIHRHAW ICGLQCGNGH VVCCACGGGG NGNGDGGANK HCDLCGRATA
     YTHIPYMDGL VDAYQVPCPY RNFGCARSIA YHSAAEHLDK CAHAPCYCFE CAFQGSPASL
     LRHLTEESGR HCWPMEKIKY QICRPLVVPA SEHRLLLVAE EDGRVFLLAV GAGRGAAGVR
     PVNVVCVRGN VDADARPVYT GVLWVDGPPA AAGHLRSSFQ LKGDVANCGV PGEVDMEHGR
     LHAHVNPEML HGESKEIHLR ICITKFW
//
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