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Database: UniProt
Entry: A0A0L0S7H0_ALLM3
LinkDB: A0A0L0S7H0_ALLM3
Original site: A0A0L0S7H0_ALLM3 
ID   A0A0L0S7H0_ALLM3        Unreviewed;       701 AA.
AC   A0A0L0S7H0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=AMAG_03956 {ECO:0000313|EMBL:KNE58376.1};
OS   Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS   macrogynus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE58376.1, ECO:0000313|Proteomes:UP000054350};
RN   [1] {ECO:0000313|EMBL:KNE58376.1, ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE58376.1,
RC   ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Allomyces macrogynus ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA   Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA   Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA   Lander E., Nusbaum C.;
RT   "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL   Submitted (NOV-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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; GG745333; KNE58376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0S7H0; -.
DR   STRING; 578462.A0A0L0S7H0; -.
DR   EnsemblFungi; KNE58376; KNE58376; AMAG_03956.
DR   VEuPathDB; FungiDB:AMAG_03956; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000054350; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 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; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 2.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 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:UP000054350};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..126
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          220..253
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          272..305
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          361..679
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          245..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        659
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   701 AA;  78764 MW;  ABDC494E94C5D84C CRC64;
     MLGSSRRQVN PWPSNWRRFI NFTVIAADGL YKRDAAKLPY PFATVTVDGI QQSTTAIIRR
     TLNPYWNESF EIEVTPSSVI TVQISDQRLR KSGDAQPSLG IANVHLGQTD FNLDAVGADR
     MLTLELSRPK PNASVRGKVI VNLSTKVSNM SRAASLANAS AVNAAGAVES SASSVSSMAA
     TSVVNPSTIT RGLLGEERSQ SPAQSPLVAA VNNLNLADLG PLPAGWEMRT MPSGRPYFVD
     HNTRTTTWGD PRDQQSVSAA PPSAPSVSMT LDQLPDGWEM RTTQFGRVYF VEHNTQKTSW
     NDPRLGETVP KYRRDFQEKL DHFSRQPEML RQPGWCQFSV SRKLLFETSI AALMRLPVHE
     LKKRPSITMD GEEGVDVGGV SREFFLLLSQ EMFNPDYGLF EYAESDKRTL KINPKSAVNP
     EHLTYFRFIG RVVGLAIFHG FFLDALFVGS FYKTILKQKI TVSDMESFDA AHYRSLKWML
     ENDITDVLDE TMSTEDHRFG EVVTINLVPG GRDIAVTEKN KKEYVDKITE WHIVKSVEKQ
     LNAFRQGLFE LVPANVISVF DERELELLIN GLAEFDVDDW VTHSVYLGYT ASEPVIIWFW
     QCVRSWDNEK RARLLQFATG TSRIPSSGFR YLQGTDGPCK FTIERARGDV QALPKAHTCF
     NRIDLPPYQS YAMLERKTLD GRRGDHGLWA RVGRVADLEL A
//
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