ID A0A8X7C6E5_9ARAC Unreviewed; 501 AA.
AC A0A8X7C6E5;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=ARIH1 {ECO:0000313|EMBL:GFY59131.1};
GN ORFNames=TNIN_3251 {ECO:0000313|EMBL:GFY59131.1};
OS Trichonephila inaurata madagascariensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Araneoidea; Nephilidae; Trichonephila;
OC Trichonephila inaurata.
OX NCBI_TaxID=2747483 {ECO:0000313|EMBL:GFY59131.1, ECO:0000313|Proteomes:UP000886998};
RN [1] {ECO:0000313|EMBL:GFY59131.1}
RP NUCLEOTIDE SEQUENCE.
RA Kono N., Nakamura H., Mori M., Yoshida Y., Ohtoshi R., Malay A.D.,
RA Moran D.A.P., Tomita M., Numata K., Arakawa K.;
RT "Multicomponent nature underlies the extraordinary mechanical properties of
RT spider dragline silk.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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:GFY59131.1}.
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DR EMBL; BMAV01012439; GFY59131.1; -; Genomic_DNA.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000886998; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR CDD; cd16626; RING-HC_RBR_HHARI; 1.
DR FunFam; 1.20.120.1750:FF:000002; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR054694; Parkin-like_IBR.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22605; IBR_2; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000886998};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00175}.
FT DOMAIN 127..338
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 131..171
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 59056 MW; 9037A413FE44D738 CRC64;
MDTGDDELYD ADSGNESSAE DEDELSISLE PESTSREKLE TEEFHYEVLS TEQIVQHMVD
CIREVNTVVQ IPPTITRILL NHFKWDKEKL YERYYDDDQE ALFKEAHIIN PYKNPPSTSK
DSRFGPRTEE CEICLMTIPK NMMTGIACGH RFCTECWKEY LTSKIMDQGM CQIIACAAHG
CDILVDDQTV MSLITDPKVK LKYQHLITNS FVECNRLLRW CPQPECNYVI AVQYVDAQPV
TCRCRHTFCF ACGENWHDPV KCNLLRKWQK KCDDDSETSN WIAANTKECP KCNATIEKDG
GCNHMVCKNQ NCKSDFCWVC LGPWEPHGSS WYNCNRYDER EAKSARDAQE KSRAALQRYL
FYCNRYLNHM QSLKFEHKLY ASVKDKMEEM QQQNMSWIEV QFLKIAVDIL CQCRQTLMYT
YVFAYYLKRN NQSAIFEHNQ RDLESATETL SEYLERDITQ ENLLDIKQKV QDKYRYCESR
CKALLEHVHE GYEKDWWEYI D
//
