GenomeNet

Database: UniProt
Entry: A0A6P8TA25_GYMAC
LinkDB: A0A6P8TA25_GYMAC
Original site: A0A6P8TA25_GYMAC 
ID   A0A6P8TA25_GYMAC        Unreviewed;       530 AA.
AC   A0A6P8TA25;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   18-JUN-2025, entry version 22.
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|RefSeq:XP_034060643.1};
OS   Gymnodraco acuticeps (Antarctic dragonfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Gymnodraco.
OX   NCBI_TaxID=8218 {ECO:0000313|Proteomes:UP000515161, ECO:0000313|RefSeq:XP_034060643.1};
RN   [1] {ECO:0000313|RefSeq:XP_034060643.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
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}.
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DR   RefSeq; XP_034060643.1; XM_034204752.1.
DR   AlphaFoldDB; A0A6P8TA25; -.
DR   FunCoup; A0A6P8TA25; 1980.
DR   GeneID; 117538839; -.
DR   KEGG; gacu:117538839; -.
DR   InParanoid; A0A6P8TA25; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000515161; Unplaced.
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; 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; PF22191; IBR_1; 1.
DR   Pfam; PF21235; UBA_ARI1; 1.
DR   SMART; SM00647; IBR; 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:UP000515161};
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          154..365
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          158..207
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  62042 MW;  DDF8B65C56B66E76 CRC64;
     MDSDEGYNYD YDDEEEECSE DSAEEEPEDD NLELGEVELV DPVVAGGERD ELGETGGGGH
     GPGDEEEEDY RFEVLTAEQI LQHMVECIRE VNEVIQNPAT ITRILLSHFN WDKEKLMERY
     FDGNLDKLFS ECHVINPSKK PRIRPAINTR SSAQDMPCQI CYLNFPNSYF TGLECGHKFC
     MQCWGDYLTT KIIEEGMGQT ISCPAHSCDI LVDDNTVMRL ITDSKVKLKY QHLITNSFVE
     CNRLLKWCPA PDCHHVVKVQ YPDAKPVRCK CGRQFCFNCG ENWHDPVKCK WLRKWIKKCD
     DDSETSNWIA ANTKECPKCH VTIEKDGGCN HMVCRNQNCK AEFCWVCLGP WEPHGSAWYN
     CNRYNEDDAK AARDAQEVRS RAALQRYLFY CNRYMNHMQS LRFEHKLYAQ VKQKMEEMQQ
     HNMSWIEVQF LKKAVDVLCQ CRSTLMFTYV FAFYLKKNNQ SIIFENNQAD LENATEVLSG
     YLERDISQDS LQDIKQKVQD KYRYCESRRR VLLQHVHEGY EKDLWEYIED
//
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