ID A0A0A0AMC6_CHAVO Unreviewed; 317 AA.
AC A0A0A0AMC6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
DE Flags: Fragment;
GN ORFNames=N301_01775 {ECO:0000313|EMBL:KGL94170.1};
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:KGL94170.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL94170.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL94170.1};
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,
CC ECO:0000256|RuleBase:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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DR EMBL; KL871957; KGL94170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AMC6; -.
DR STRING; 50402.A0A0A0AMC6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd09633; Deltex_C; 1.
DR CDD; cd16671; RING-H2_DTX1_4; 1.
DR Gene3D; 3.30.390.130; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF7; E3 UBIQUITIN-PROTEIN LIGASE DTX1; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 110..171
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 73..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL94170.1"
FT NON_TER 317
FT /evidence="ECO:0000313|EMBL:KGL94170.1"
SQ SEQUENCE 317 AA; 34386 MW; 24B16BCE8AA2FF24 CRC64;
LPSPCRVPAL PVKNLNGTGP VHPALAGMTG ILMCAAGLPV CLTRAPKPIL HPPPVSKSDI
KPVPGVNGIC RKTKKKHLKK SKEPPVPRWR AESRGVTSPS HPSTRARQDC TICMERLVTS
SGYEGVLSHR GIKPELVGKL GKCGHMYHLL CLLAMYNNGN KDGSLQCPTC KAIYGEKTGT
QPPGKMEFHL IPHSLPGYTD SKTIRIVYDI PTGIQGPEHP NPGKKFTARG FPRHCYLPDN
EKGRKVSVPH GTGWGGMGWD GMGWDGMGWK CNPVVWNEIH HKTEFGSNLT GHGYPDPNYL
DNVLAELLAQ GVSEATL
//
