ID A0A3Q1EF95_9TELE Unreviewed; 387 AA.
AC A0A3Q1EF95;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RING1 {ECO:0000313|Ensembl:ENSAPOP00000001617.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000001617.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000001617.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR STRING; 80966.ENSAPOP00000001617; -.
DR Ensembl; ENSAPOT00000014846.1; ENSAPOP00000001611.1; ENSAPOG00000002929.1.
DR Ensembl; ENSAPOT00000014854.1; ENSAPOP00000001617.1; ENSAPOG00000002929.1.
DR GeneTree; ENSGT00940000161022; -.
DR OrthoDB; 460116at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16739; RING-HC_RING1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR042741; RING1_RING-HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076:SF2; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR Pfam; PF16207; RAWUL; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 48..88
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 151..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 43406 MW; EE7E11566ECC027F CRC64;
MAAPVNIQTP SKTWELSLYE LHRSPQEAIM DGTEVAVSPR SLHSELMCPI CLDMLKNTMT
TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSRRSLRRD SNFDALISKI YPSRDEYEAH
QRRVLERLNR LHNKEALSSS IEEGLRQQAR YRNHRVKKPT QESDNTTFSG GEDNGDSRSH
LSHDSAPSHA PHPQDQTPPE AGPSRKRPRG SEDGSGPEGD SESPTPPLRL HKEGPGSEIE
LVFRPHPQLV QDQDYNQTRY VKTTANATVD HLSKYLALRI ALEEQRSNGE VEDRGGEDGG
GETGGGGSSL SSISEKQYTI YILTRGGQFS TLNGSLTLEL VNEKYWKVRK PLELYYAPTK
DQQQPQQPPP PPPPQQQQRS PPQQRDG
//
