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Database: UniProt
Entry: A0A5A7QN51_STRAF
LinkDB: A0A5A7QN51_STRAF
Original site: A0A5A7QN51_STRAF 
ID   A0A5A7QN51_STRAF        Unreviewed;       305 AA.
AC   A0A5A7QN51;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   08-OCT-2025, 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=STAS_23373 {ECO:0000313|EMBL:GER46338.1};
OS   Striga asiatica (Asiatic witchweed) (Buchnera asiatica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga.
OX   NCBI_TaxID=4170 {ECO:0000313|EMBL:GER46338.1, ECO:0000313|Proteomes:UP000325081};
RN   [1] {ECO:0000313|Proteomes:UP000325081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081};
RX   PubMed=31522940; DOI=10.1016/j.cub.2019.07.086;
RA   Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L.,
RA   Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P.,
RA   Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S.,
RA   Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C.,
RA   Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T.,
RA   Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I.,
RA   Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D.,
RA   Shirasu K.;
RT   "Genome Sequence of Striga asiatica Provides Insight into the Evolution of
RT   Plant Parasitism.";
RL   Curr. Biol. 29:3041-3052.e4(2019).
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. Mediates the proteasomal-dependent
CC       degradation of ATG6, a component of the autophagosome complex. Requires
CC       TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for ubiquitination and
CC       subsequent regulation of autophagosome assembly. Modulates directly the
CC       ubiquitination and proteasomal-dependent degradation of FREE1, a
CC       component of the ESCRT-I complex. Modulates directly the ubiquitination
CC       and proteasomal-dependent degradation of ELC/VPS23A, a component of the
CC       ESCRT-I complex. {ECO:0000256|ARBA:ARBA00054480}.
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   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC       {ECO:0000256|ARBA:ARBA00004419}. Endosome, multivesicular body
CC       {ECO:0000256|ARBA:ARBA00004559}.
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:GER46338.1}.
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DR   EMBL; BKCP01007515; GER46338.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A7QN51; -.
DR   OrthoDB; 941555at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000325081; Unassembled WGS sequence.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:2000785; P:regulation of autophagosome assembly; IEA:UniProtKB-ARBA.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd16571; RING-HC_SIAHs; 1.
DR   CDD; cd03829; Sina; 1.
DR   FunFam; 3.30.40.10:FF:000041; E3 ubiquitin-protein ligase SINAT3; 1.
DR   FunFam; 2.60.210.10:FF:000004; E3 ubiquitin-protein ligase SINAT5-like; 1.
DR   FunFam; 3.30.40.10:FF:000311; E3 ubiquitin-protein ligase SINAT5-like; 1.
DR   Gene3D; 2.60.210.10; Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2, Chain A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR   InterPro; IPR052088; E3_ubiquitin-ligase_SINA.
DR   InterPro; IPR049548; Sina-like_RING.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR001841; Znf_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:SF111; E3 UBIQUITIN-PROTEIN LIGASE DIS1; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF03145; Sina_TRAF; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325081};
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:PRU00455}.
FT   DOMAIN          57..93
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          110..170
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  34647 MW;  FD81E99F285CAC39 CRC64;
     MTSGNPYFDD LRMKPEVINP PENEDTLDVG EHVDSPSESA VKPNVAISSN VRDLLECPVC
     LNAMYPPIHQ CSNGHTLCSG CKPRVHNRCP TCRHELGNIR CLALEKVAAS LELPCKYQDF
     GCIGIFPYYS KLKHESQCTF RPYNCPYAGS ECSVVGDIPF LVSHLKDDHK VDMHSGSTFN
     HRYVKSNPHE VENATWMLTV FSCFGQYFCL HFEAFQLGMA PVYIAFLRFM GNDNEAKNYS
     YSLEVGSNGR KMTWQGVPRS IRDSHRKVRD SFDGLIIQRN MALFFSGGDR KELKLRVTGR
     IWKEQ
//
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