ID A0A3Q3AI91_KRYMA Unreviewed; 299 AA.
AC A0A3Q3AI91;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000015885.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000015885.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_017275567.1; XM_017420078.1.
DR AlphaFoldDB; A0A3Q3AI91; -.
DR STRING; 37003.ENSKMAP00000015885; -.
DR Ensembl; ENSKMAT00000016113.1; ENSKMAP00000015885.1; ENSKMAG00000011862.1.
DR GeneID; 108238169; -.
DR KEGG; kmr:108238169; -.
DR CTD; 563879; -.
DR GeneTree; ENSGT00940000157203; -.
DR OMA; EYENPIP; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45931:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF6; 1.
DR PANTHER; PTHR45931; SI:CH211-59O9.10; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 223..264
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 77..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..104
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 32173 MW; 5E9F7E6602F31A12 CRC64;
MAEAADTPQP QRRFYCHCCK CETKPGLSDL VCPACESGFV EEVTDDSSLL QNSTPSSAGL
PSSSLFSELL FLEHSALLSD PPSSESDSES EDGGDEEEEE EESAGQSVPS PASQVATEGG
EQDSALSSES ERSPWSGSLE EFLTDLLPDD GNPGATTTGL SSLLQLYSNP GDYAWGQGSL
DTFITELFGQ LENTGPPPAK TEMISSLPTV HVSQEQIDSR LECPICMEGY SLRESVRKLP
CLHHFHGGCI VPWLELHDSC PVCRKSLDGV VNGVPLLPAP PEEIAALREE QEQQERQAI
//