ID A0A0R3T347_RODNA Unreviewed; 423 AA.
AC A0A0R3T347;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 10-JUN-2026, entry version 58.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN ORFNames=HNAJ_LOCUS1407 {ECO:0000313|EMBL:VDN97266.1};
OS Rodentolepis nana (Dwarf tapeworm) (Hymenolepis nana).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Rodentolepis.
OX NCBI_TaxID=102285 {ECO:0000313|EMBL:VDN97266.1, ECO:0000313|Proteomes:UP000278807};
RN [1] {ECO:0000313|EMBL:VDN97266.1, ECO:0000313|Proteomes:UP000278807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; UZAE01000541; VDN97266.1; -; Genomic_DNA.
DR STRING; 102285.A0A0R3T347; -.
DR OrthoDB; 941555at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000278807; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:TreeGrafter.
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:0030154; P:cell differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd03829; Sina; 1.
DR FunFam; 2.60.210.10:FF:000002; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.40.10:FF:000041; E3 ubiquitin-protein ligase SINAT3; 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; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU201113};
KW Reference proteome {ECO:0000313|Proteomes:UP000278807};
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 149..184
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 201..261
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 44113 MW; 6CB1A4B4F98AA140 CRC64;
MNSSFSHAGS DRPTSIVAAE PSARPTSSHR NVSVTAASVE RHFVGGTSTS AIPHQQQRPA
ASAALFDFDA AAGSGNGGGS DNGCKSGGNN NAVCCNGVVN HPASVSVTPI TAATAALPPN
GPERPQPTGA GQDPPGANNS MDLVSLFECP VCMDFALPPI LQCQSGHIVC ASCRSKLSSC
PTCRGNLENI RNLAMEKLAA TILFPCKYAV TGCTETFHYT AKAEHEAICE HRPYSCPCPG
TSCKWLGQLD QVMPHLLQSH KSITTLQGED IVFLATDITL PGAVDWVMMQ SCFGHYFMLV
LEKQERVSSF FALVLLIGTK KQADQFVYKL DLTASKRRLT WEATPRSIHD GVQAAIDASD
CLVFDSKMAQ LFADNGSLGI NVTISRARGG GSSGNNIVGG SSCSGGGTAA SGPGGSGNST
VWA
//
