ID G3TIV4_LOXAF Unreviewed; 738 AA.
AC G3TIV4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000014603.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000014603.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014603.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000014603.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014603.4};
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 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 AlphaFoldDB; G3TIV4; -.
DR STRING; 9785.ENSLAFP00000014603; -.
DR Ensembl; ENSLAFT00000017411.4; ENSLAFP00000014603.4; ENSLAFG00000017413.4.
DR eggNOG; ENOG502RGAW; Eukaryota.
DR GeneTree; ENSGT00940000154578; -.
DR HOGENOM; CLU_024295_0_0_1; -.
DR InParanoid; G3TIV4; -.
DR OMA; IMANDCD; -.
DR TreeFam; TF325526; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007646; 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 Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
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; IPR048418; DTX3L_a/b_dom.
DR InterPro; IPR048409; DTX3L_KH-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF41; E3 UBIQUITIN-PROTEIN LIGASE DTX3L; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF21717; DTX3L_a-b; 1.
DR Pfam; PF21718; DTX3L_KH-like; 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 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:UP000007646};
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 559..598
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 193..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 82811 MW; 5AE4DC577DE81C90 CRC64;
KASAPCPPSP LVVRVSEPGP RLRRKLESYF QSRRSGGGEC TVRALGDSAP DTFRVEFRER
AAKERVLKKG EHRICVENKP VSIFLEPTEK PVEKIMSQRT SLVTPSGAGA LYDGKHPNER
HIPNTVDSCV SKIFLAVTAE LNCNLLSKEL RKHIATLCPN VKKVEGLDGI EKVCGDFRDI
EKIHRFLSEQ LLTSEQQQRR SPSVGRTHNS CSSPEQQTRK EENSHSFQVS LPFLEYFEYT
CPDKIKFIEK RFGVNIKTQE SSPNMVYLDF TSSQSGNLEV ARECFVHEFQ KGTESLKLES
MVLADRKQAN EITQALNHRF RKLLIKEKGK ELTLLGPQDD ISAAKHFLAV RNSESSVKTP
VKISAPNGMM NGIEVDTAHY ELLEAELQQE IPVIERKYNT SIRAFGKTKD AQKTCILFEP
KDKEIDLSAH ACASFIDAYQ HVSCQLKREI FSLKLLSKDR EHLHGTKFAD DFRRKHPNIH
LSLTQNSMNL TGLPNHLAKA KQYVSTREGM HLLAGEKWNE DHGTPMDIDS NDSETASPPV
KGSASSGASG VDKKEEDTCA ICLDNITNKQ VLPDCKHEFC TPCINKAMSY KPVCPMCQTQ
YGIQTGNQPD GTMVVAYSPL SLPGYAPYPT IMITYKMSGG VQTKDHPNPG KRYDGTHRTA
YLPDNVEGQE VLRLLRKAFD QKLIFTVGQS RTSGASDVIT WNDIHHKTSM YGGPKMFGYP
DPHYLQRVKE ELKAKGIK
//
