ID   A0A0A0ASH9_CHAVO        Unreviewed;       271 AA.
AC   A0A0A0ASH9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   Flags: Fragment;
GN   ORFNames=N301_02539 {ECO:0000313|EMBL:KGL96463.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL96463.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL96463.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL96463.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KL872627; KGL96463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0ASH9; -.
DR   STRING; 50402.A0A0A0ASH9; -.
DR   Proteomes; UP000053858; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; 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; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF16; E3 UBIQUITIN-PROTEIN LIGASE RNF115; 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:UP000053858};
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          195..236
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          61..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL96463.1"
FT   NON_TER         271
FT                   /evidence="ECO:0000313|EMBL:KGL96463.1"
SQ   SEQUENCE   271 AA;  30306 MW;  2DE5429082DDCCFC CRC64;
     LQEYTCPRCE SGFIEEVTDD SSFLDGSGID DGPSTQFAEL WDHLDHTMFF PDFRPFLSSS
     SLDQDSRDNE RGHQAHADLW GPSRPPRLPM TRRYRSRGSS RPDRSPAIEG IIQQIFAGFF
     ANSAIPGSQH PFSWSGMLHS NPGDYAWGQS GLDAIVTQLL GQLENTGPPP ADKEKISSLP
     TVTVTQEQVD TGLECPVCKE DYTVAEQVRQ LPCNHFFHSN CIVPWLELHD TCPVCRKSLK
     GEDSTRQTQN PEASASNSFS SESQLHDRWT F
//