ID A0A024U5K9_9STRA Unreviewed; 662 AA.
AC A0A024U5K9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=H310_06167 {ECO:0000313|EMBL:ETW01495.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW01495.1};
RN [1] {ECO:0000313|EMBL:ETW01495.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW01495.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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; KI913962; ETW01495.1; -; Genomic_DNA.
DR RefSeq; XP_008869343.1; XM_008871121.1.
DR AlphaFoldDB; A0A024U5K9; -.
DR STRING; 157072.A0A024U5K9; -.
DR EnsemblFungi; H310_06167-t26_5; H310_06167-t26_5-p1; H310_06167.
DR EnsemblProtists; ETW01495; ETW01495; H310_06167.
DR GeneID; 20083217; -.
DR VEuPathDB; FungiDB:H310_06167; -.
DR eggNOG; KOG0940; Eukaryota.
DR OrthoDB; 5478214at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR001876; Znf_RanBP2.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF446; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 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.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..96
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 328..662
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 205..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 629
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 662 AA; 73891 MW; 643C0DAD828B1CD6 CRC64;
MAAIDLSSFK YVAIAVGVAI ALLAFANWAY YKYCFVPPPP PDPLRNGQFL SFMPGLKRQD
LDGFQHDVEL WSCSVCEFQN AITKPDCLLC GTRRDIRFID IHAVAQPKPA TFARSFSSNY
IQVTSTRASS SFHATASRMY SMAFENVVLP EDLNSQQRSA RMRKQWIRQL DIHGVVRWAR
RFLESAQVPD AHVIQLNTVP MPSALGSLSP VAESPHTTPP SPAACPSPED QKDAPAQTCQ
VTWQPLDSIP ANATVLGTMV PSATATSLLE ISKLPFYMKY SWFLHQIDDL VVPYDELHIK
VRVDRRTVVA EAVENLSSYP GRALCAIVRY EFAGESAQDA GAVQREWYML VSEGLLVESN
GLFVVLNRED NSYFINPNSS HAWTHPNRMD HLQAFHAVGR FLGRSLLDGQ VIPMHLNPVL
LKAILGVPLT LDDVESLDRT VYKGLVYLLE HDNAHELALT FSATETRGDD VVEVDLVENG
HLRPVTDANK ADYVRLMVRY LMFGRIEAQL LALIQGVYDI VPPELVMPFD HKEFELILCG
LSQVDVSDWK ANTVTSSNLV NSKPLEWFWE VVEGMSPPDR SKLLQFATGS SRVPVQGFKG
LTSYDGEICH FTLKGVPYEC GVYPATHACY NRIDLPLYPA KEMMVEALTM LLMSDPTGFT
IA
//
