ID A0A0N5C910_STREA Unreviewed; 513 AA.
AC A0A0N5C910;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001439300.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001439300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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. {ECO:0000256|RuleBase:RU201113}.
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 ECO:0000256|RuleBase:RU201113};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000256|RuleBase:RU201113}.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC interaction with substrate proteins. It is related to the TRAF family.
CC {ECO:0000256|RuleBase:RU201113}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0N5C910; -.
DR STRING; 174720.A0A0N5C910; -.
DR WBParaSite; SPAL_0001439300.1; SPAL_0001439300.1; SPAL_0001439300.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03829; Sina; 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; IPR004162; SINA-like_animal.
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; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF2; E3 UBIQUITIN-PROTEIN LIGASE SINA-RELATED; 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|RuleBase:RU201113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU201113};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU201113};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00455}.
FT DOMAIN 272..307
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 324..384
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 36..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 57826 MW; 4CACBDD6BF56F54E CRC64;
MSNRHRSDRD NKNERTTRRV IYRNSNRANS EELINVSSNN QTLEINSSSG SSNSMQSNTP
PPQIVYTRSS SNRLFQRQNQ HGRSIGLSNN HNRNRATARI VGTTENSNVS HESSSNINNT
NHTPSESRIE TRTILRNNEE PEPKIERKNN NRSDDRMDFR SGGERSNNRN NYQTNESMDG
QGEAMNTTMD DSSIDEERMD VLNESFPVSR TNDVPEIRNN VKNVFKNDKL NFSNTIDDLR
SKQDITLTNK LLIETLNKPV PASNDVLSAF ECPVCMEYMV PPLYQCGSGH LVCGSCRPKL
NCCPSCRGPV PNVRNLAMEK IAATIYFPCK YNGNGCLDAF AASEKLSHEE GCEYRPYCCP
CPGASCRWQG AVEHVMPHLM KAHRSITTLQ GEDIVFLATD ISLPGAVDWV MLQSCYGCHF
MLVLEKQEKY GNTEQFYAIV QLIGSKKEAE QFIYRLELSN QKRRLCWEAA PKSIHEGISS
SLNCSDCLLF DSKLAKLFSE NGNLGINVTI TKV
//
