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Database: UniProt
Entry: G3U5A3_LOXAF
LinkDB: G3U5A3_LOXAF
Original site: G3U5A3_LOXAF 
ID   G3U5A3_LOXAF            Unreviewed;      1243 AA.
AC   G3U5A3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=HECW2 {ECO:0000313|Ensembl:ENSLAFP00000023011.1};
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:ENSLAFP00000023011.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000023011.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023011.1,
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:ENSLAFP00000023011.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023011.1};
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR   AlphaFoldDB; G3U5A3; -.
DR   Ensembl; ENSLAFT00000036108.1; ENSLAFP00000023011.1; ENSLAFG00000011976.3.
DR   GeneTree; ENSGT00940000155466; -.
DR   HOGENOM; CLU_002173_14_3_1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd08691; C2_NEDL1-like; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.60.40.2840; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037795; C2_HECW.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR040524; HECW1_helix.
DR   InterPro; IPR032348; HECW_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF127; E3 UBIQUITIN-PROTEIN LIGASE HECW2; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF18436; HECW1_helix; 1.
DR   Pfam; PF16562; HECW_N; 1.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          65..196
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          699..732
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          877..910
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1132..1243
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          237..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1076
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1243 AA;  137871 MW;  B5B2A0E3767F52BD CRC64;
     DSKNRGVTGT QKGQIVWRIE PGPYFMEPEI KICFKYYHGI SGALRATTPC ITVKNPAVMM
     GAEGMEGGVS GSSHSRKLVS FTLSEDLRAV GLKKGMFFNP DPYLKMSIQP GKKSSFPTCA
     HHGQERRSTI ISNTTNPIWH REKYSFFALL TDVLEIEIKD KFAKSRPIIK RFLGKLTIPV
     QRLLERQAIG DQMLSYNLGR RLPADHVSGY LQFRVEVTSS VHEDASPEAV GTILGVSTVN
     GDLGSPSDDE DMPGGHHDSQ VCSNGPTSEE SAADGTPKHS LRTSSTLEID TEELISTSSR
     TSPPRGRQDS LNDYLDAIEH NGHSRPGAAT CSERSMGASP KLRSSFPTDT RLNAMLHIDS
     DEEDHEFQQD LGYPSSLEEE GGLIMFSRAS RADDDGSLAS QTKPEDNPVE NEEAFANEAT
     SFEDKPENHA ELADSTLPSG PSPDENENGP ESQQSADQGS GELCGSQEMD QPTSGADTGT
     SDTSGGSRRA VSETESLDQG SEPSQVSSET EPSDPARTES VSEASTRPEG ESDLEGADSS
     CNESVTTQLS SVETRCSSLE SARFPETPAF SSQEEEDGVC AAEPTSSGPA EGPQESVSTP
     GSLPVVQVPS GEEEGPESAT LPDQEEMGAV WQRRGSLEGA TAENQPQEEG DAGDAQGTCE
     GATAQDEGAT GGSQANGHQP LRSLPSVRQD VSRYQRVDEA LPPNWEARID SHGRIFYVDH
     VNRTTTWQRP TAPPAPQMLQ RSNSIQQMEQ LNRRYQSIRR TMTNERPEEN TSALDGAGEE
     ADFHQASADF RRENVLPHST SRSRLTLLLQ SPPVKFLISP EFFTVLHSNP SAYRMFTNNT
     CLKHMITKVR RDTHHFERYQ HNRDLVGFLN MFANKQLELP RGWEMKHDHQ GKAFFVDHNS
     RTTTFIDPRL PLQSSRPTSA LVHRQHLTRQ RSHSAGEVGE DSRHAGPPVL PRPSSTFNTV
     SRPQYQDMVP VAYNDKIVAF LRQPNIFEIL QERQPDLTRN HSLSLNREKI QFIRTEGTPG
     LVRLSSDADL VMLLSLFEEE IMSYVPPHAL LHPSYCQSPR GSPVSSPQNS PGTQRANARA
     PAPYKRDFEA KLRNFYRKLE TKGYGQGPGK LKLIIRRDHL LEDAFNQIMG YSRKDLQRNK
     LYVTFVGEEG LDYSGPSREF FFLVSRELFN PYYGLFEYSA NDTYTVQISP MSAFVDNHHE
     WFRFSGRILG LALIHQYLLD AFFTRPFYKA LLRIVIICSL SQI
//
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