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Database: UniProt
Entry: A0A3Q3AI91_KRYMA
LinkDB: A0A3Q3AI91_KRYMA
Original site: A0A3Q3AI91_KRYMA 
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
//
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