ID F4PB66_BATDJ Unreviewed; 499 AA.
AC F4PB66;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=BATDEDRAFT_17756 {ECO:0000313|EMBL:EGF77803.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF77803.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF77803.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) 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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
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DR EMBL; GL882891; EGF77803.1; -; Genomic_DNA.
DR RefSeq; XP_006681619.1; XM_006681556.1.
DR AlphaFoldDB; F4PB66; -.
DR STRING; 684364.F4PB66; -.
DR GeneID; 18237230; -.
DR HOGENOM; CLU_002173_9_4_1; -.
DR InParanoid; F4PB66; -.
DR OMA; RTTYQPN; -.
DR OrthoDB; 164548at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; 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 InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW Signal {ECO:0000256|SAM:SignalP};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..499
FT /note="HECT-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003319925"
FT DOMAIN 163..499
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 466
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 499 AA; 56560 MW; 65572E6F932B35D9 CRC64;
MHVATVLLPL IESFMVVSRP VVMAKKPTPT TGSNLVTSSS AGSLLLNLHT QSSTGALPAG
GRLSVRQQSD VALIDRESFS VFTESHKKIL NTMVRNNPSL MNGSFSLLVH NPKVLEFDNK
RTFFTQQLHK KTNTHRDHYG SLPINVRRQY VFEDSFHQLS GRSGDELKYS KLAVRFHEEE
GIDAGGVARE WFSVLARQMF NPDYALFRPS AADKVTYQPN RASGVNPDHL HYFKFVGCII
GKAIYDGRLL DAYFTRSFYK CILGIQVDYK DMEAIDPGFH KSLEWILQND IEDVLDLTFS
TEVDDFGRQR IIDLKPNGRN ITVTDENKVE YVKLITEQRL VVAIKDQIHA FLAGFNQVIP
ADLVRIFNEQ ELELLISGMP DIDIDDWKNN TEYQNYTASS PQVQWFWRAV RSFSQEERAK
LIQFATGTSK VPLEGFKALE GSTGVQKFQI HKEFSDVSRL PSAHTCFNQI DLPQYDSYEQ
LRSMLLTAIS ECGTGFGFA
//
