ID U3FYT8_MICFL Unreviewed; 878 AA.
AC U3FYT8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin-protein ligase E3A {ECO:0000256|PIRNR:PIRNR037201};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR037201};
OS Micrurus fulvius (Eastern coral snake) (Coluber fulvius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=8637 {ECO:0000313|EMBL:JAB53010.1};
RN [1] {ECO:0000313|EMBL:JAB53010.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAB53010.1};
RX PubMed=23915248; DOI=10.1186/1471-2164-14-531;
RA Margres M.J., Aronow K., Loyacano J., Rokyta D.R.;
RT "The venom-gland transcriptome of the eastern coral snake (Micrurus
RT fulvius) reveals high venom complexity in the intragenomic evolution of
RT venoms.";
RL BMC Genomics 14:531-531(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC transfers it to its substrates. {ECO:0000256|PIRNR:PIRNR037201}.
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=2.3.2.26; Evidence={ECO:0000256|PIRNR:PIRNR037201};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|PIRNR:PIRNR037201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037201}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR037201}.
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DR EMBL; GAEP01001811; JAB53010.1; -; mRNA.
DR AlphaFoldDB; U3FYT8; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR017134; UBE3A.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF16558; AZUL; 1.
DR Pfam; PF00632; HECT; 1.
DR PIRSF; PIRSF037201; Ubiquitin-protein_ligase_E6-AP; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037201};
KW Ligase {ECO:0000313|EMBL:JAB53010.1};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037201};
KW Proteasome {ECO:0000256|PIRNR:PIRNR037201};
KW Transferase {ECO:0000256|PIRNR:PIRNR037201};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR037201}.
FT DOMAIN 550..878
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 846
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 878 AA; 100840 MW; D372A1862588E114 CRC64;
MATACKRSPG EPHSENFETS RMKRAAAKHL IERYYHQLTE GCGNEACTNE FCASCPTFLR
MDNNAAAIKA LDLYKINAKL CDPHPSKKGT SSAYLENNSK GAHNNACTDR KMNKKEMQGP
RDDFKDVTFL TEEKVYEILE LCREKEDYSP LIRVIGRVFS SADALVQSFR KAKQHTKEEL
KSLQGKDEDK DEDEKEKAAC SSAMEEDLVA PSSSSRMGDS AQGDNNLQKL GPDEVSVDID
AIRRVYNRLL SNEKIETAFL NALVYLSPNV ECDLTYHNVY SRDPNYLNLF IIVMENGNLH
SPEYLEMALP LFCKAMSKLP LAAQAKLVRL WSKYSADQIR RMMETFQQLI TYKVISNEFN
SRNLVNDDDA IVAASKCLKM VYYANVVGGD IDTDHNEEED EEPIPESSEL TLQELLGEER
RNKKGPRVDP LETELGVKTI DCRKPLIPFE EFINEPLNDV LEMDKDYTFF KVETENKFSF
MTCPFILNAV TKNLGLYYDN RIRMYSERRI TVLYSLVQGQ QLNPYLRLKV RRDHIIDDAL
VRLEMIAMEN PADLKKQLYV EFEGEQGVDE GGVSKEFFQL VVEEIFNPDI GMFTYDESTK
LFWFNPSSFE TEGQFTLIGI VLGLAIYNNC ILDVHFPMVV YRKLMGKKGT FRDLADSHPV
LYQSLRDLLQ YEGSVEDDMM ITFQISHTDL FGNPMMHDLK ENGDKIPITN ENRKEFVNLY
SDYILNKSVE KQFKAFRRGF HMVTNESPLK YLFRPEEIEL LICGSRNLDF QALEETTEYD
GGYTRDSLII REFWEIVHSF TDEQKRLFLQ FTTGTDRAPV GGLGKLKMII AKNGPDTERL
PTSHTCFNVL LLPEYSSEEK LKERLLKAIT YAKGFGML
//
