ID A0A2N6NJK5_BEABA Unreviewed; 1272 AA.
AC A0A2N6NJK5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=BM221_007135 {ECO:0000313|EMBL:PMB67467.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB67467.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB67467.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB67467.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMB67467.1}.
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DR EMBL; MRVG01000007; PMB67467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NJK5; -.
DR OMA; GSSHRIN; -.
DR Proteomes; UP000235728; 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 InterPro; IPR025527; HUWE1/Rev1_UBM.
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 Pfam; PF14377; UBM; 3.
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:UP000235728};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 927..1272
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1239
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1272 AA; 142904 MW; 68FA1B42298B048F CRC64;
MENRGGPPSR FVGTQRDGGD FRSYFSRMHR PAGQQNHAED GSNPLLRRND PETENSSRPG
NSNSFGLRLP ETMFASGGRH MIDGPMSFLG ELMEFLPMMG RNNNGQAFHV QITRPGGPRA
EFAPIRPGRH DQRREVSQEP FQAVAFTTES TVSRYSEEAR MIFGSNYVLE ASRLSNAISA
ALTPAAVEHQ KKVMAVDEEN RKKAEEIRRK LEEEQKEKEA KEAEERAEQE RGRQAALERA
AAAFEAAGSF FTEDDERLAM EAVESLSSGE PASQPEASSA SRVTTTIRGE EVDITELGID
PDYLAALPEE FREEVIAQTV SERRSQALQT APAGESTEVF QEFLDALPEE LRLEIAQQER
QEQRRRVGNR RHAGNAGTVR PADMDTASIL QTFPPELRDE VLLQQGQSLM DQLTPELAAQ
SRALHQHHGP SGLQRGQHHG PPPTGNNSHA EASKAADSKP PRKTVVQMLD KAGVATLLRL
MFITHQGSFR NYLFAVFADV CENRQSRLEV ISTLLQILQD GSTDVNAVER SFGQLSIKAK
RLKDKERDAE PRTPQTLKRT LTSLSVSNTA QTSSETSPLL IVQQCLDLLV DLCARNPHVP
WLFLTEHETV GASLRKSFGR KGKTKDSKAN KYAINALLTL LDRELITESS LVMTHLADLL
NRVTMPLQNL ERRRRESLDT VLVETEKQNE GQTSGEAQAD APAAGNEDSA QKAPKQGNVP
QKRSRQLQPP VIPEENLSLV VRIFVARECS SKTFQNTIAT IKNLCAIPGT KTIFGQELIR
QARALSQNIV TDLNELLPHI LAASSGTEIQ GVALAKFSPG ASDQNKLLRV LTALDHLFEP
KKKPSQASPD NLDDSKQDLL TSLYHNETFL SMNPKVLEFD NKRNYFNRTV HSRAAHGQSR
PSYPPLQLSV RRESVYRDSF ANLYYKSGDE IKYGKLNIRF GGEEGVDAGG VTREWFQVLA
RQMFDPNNAL FIPVSSDRTT FHPNKLSKFH LNEDSNAGES TDSIHFKFIG RIIGKALYEG
RLLDCFFSRA VYKRILGKSV SVKDMESFDP DYYKSLCWML ENDITDIITE TFSEEEDEFG
VTKIVDLVPN GREIPVTEEN KQEYVRLVVE HRLLTSVKDQ MESFLKGFHE IIPAELISIF
NEQELELLIS GLPDIDIDDW RSNAEYHNYT PSSQQVQWFW RAVRSFDKEE LAKLLQFVTG
TSKVPLNGFK ELEGMNGISR FNIHRDYGDK DRLPTSHTCF NQLDLPEYDS YDTLRAQLYK
AITAGNEYFG FA
//
