ID   A0A2K6BA16_MACNE        Unreviewed;       861 AA.
AC   A0A2K6BA16;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Ubiquitin-protein ligase E3A {ECO:0000256|PIRNR:PIRNR037201};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR037201};
GN   Name=UBE3A {ECO:0000313|Ensembl:ENSMNEP00000008266.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000008266.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000008266.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A2K6BA16; -.
DR   Ensembl; ENSMNET00000032431.1; ENSMNEP00000008266.1; ENSMNEG00000028458.1.
DR   GeneTree; ENSGT00940000155050; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000028458; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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: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   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037201};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR037201};
KW   Proteasome {ECO:0000256|PIRNR:PIRNR037201};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Transferase {ECO:0000256|PIRNR:PIRNR037201};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR037201}.
FT   DOMAIN          533..861
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          161..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        829
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   861 AA;  98899 MW;  45C5A88388175695 CRC64;
     FGNESPSAKQ KRAAAKHLIE RYYHQLTEGC GNEACTNEFC ASCPTFLRMD NNAAAIKALE
     LYKINAKLCD PHPSKKGASS AYLENSKGAP NNSCSEIKMN KKGTRIDFKD VTYLTEEKVY
     EILELCRERE DYSPLIRVIG RVFSSAEALV QSFRKVKQHT KEELKSLQAK DEDKDEDEKE
     KAACSAAAME EDSEASSSRI GDSSQGDNNL QKVGPDDVSV DIDAIRRVYT RLLSNEKIET
     AFLNALVYLS PNVECDLTYH NVYSRDPNYL NLFIIVMENR NLHSPEYLEM ALPLFCKAMS
     KLPLAAQGKL IRLWSKYNAD QIRRMMETFQ QLITYKVISN EFNSRNLVND DDAIVAASKC
     LKMVYYANVV GGEVDTNHNE EDDEEPIPES SELTLQELLG EERRNKKGPR VDPLETELGV
     KTLDCRKPLI PFEEFINEPL NEVLEMDKDY TFFKVETENK FSFMTCPFIL NAVTKNLGLY
     YDNRIRMYSE RRITVLYSLV QGQQLNPYLR LKVRRDHIID DALVRLEMIA MENPADLKKQ
     LYVEFEGEQG VDEGGVSKEF FQLVVEEIFN PDIGMFTYDE STKLFWFNPS SFETEGQFTL
     IGIVLGLAIY NNCILDVHFP MVVYRKLMGK KGTFRDLGDS HPVLYQSLKD LLEYEGNVED
     DMMITFQISQ TDLFGNPMMY DLKENGDKIP ITNENRKEFV NLYSDYILNK SVEKQFKAFR
     RGFHMVTNES PLKYLFRPEE IELLICGSRN LDFQALEETT EYDGGYTRDS VLIREFWEIV
     HSFTDEQKRL FLQFTTGTDR APVGGLGKLK MIIAKNGPDT ERLPTSHTCF NVLLLPEYSS
     KEKLKERLLK AITYAKGFGM L
//