ID A0A1B8GVZ1_9PEZI Unreviewed; 1887 AA.
AC A0A1B8GVZ1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=UFD4 {ECO:0000313|EMBL:OBT99993.2};
GN ORFNames=VE01_01948 {ECO:0000313|EMBL:OBT99993.2};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBT99993.2, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBT99993.2, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBT99993.2,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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DR EMBL; KV460210; OBT99993.2; -; Genomic_DNA.
DR STRING; 342668.A0A1B8GVZ1; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000091956; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1531..1887
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..235
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..795
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1854
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1887 AA; 205836 MW; 71320A9022877225 CRC64;
MAQERTHSQR TRSVAPSVFD ENEPTSDAFH SGTPSSLNST LRNTRASARQ AATASDLAPP
SAATPSQPPP TTRPSRKRKA AEREASPLPE PEPAKPAKSK RRQKRQRTTE QETTAAPAAP
PTRQRKGKST AVMSSPGASA GPANEGGSAA SSATRKSNRN KKSNPDLAAA AAATPTAPRK
SKKQHKNAEA ETDPNEGNDV EPADEDDDDE DDSDDNDNDD LPRGFNEEDE DDDPFGGFGG
PGGPPHGLSN TLRALSGMMS GVSSRLREIL SNLKQKEDPS MQLIALQELS EILLVSTEDN
LSGHFSPDAF VKELVTLMQP SDFGEENPEM MLLACRCIAN LMEALPASTA NVVYGGAVPI
LCQKLLEIHY IDLAEQALST LEKISVEYPA SIVREGGLTA CLTYLDFFAT STQRTAVTTA
ANCCRNIPED SFPVIRDVMP ILLNVLSSND QKVVEQGSLC VSRVVESFRY QPAKLEELVS
SDLLKAILRL LLPGTTNLIG PSIHTQFLRV LAFTAKASPT LSAELFKMNV VETLYQILTG
VSPPNGVHDV ASKLDSVVIM QALIHRPREQ VIETLNVICE LLPGVPQDLP SFMDDAFEIA
IASEPSGTSS RKKSLNEKRI ELLEGCKEEL KRFAVILFPT LTDAFSSTVN LSVRQKVLTA
QLKMLSTLDR DIIMEALRTL PYASFLAAIL SQQDHPTLVN SALQAAELLL TRLDDVYRYQ
FYREGVITEI TKLAQSAEPV EGEDKKPESG ETTENAEAEA TSAVADNAPA EPAVANDRDE
DDNSSDGDND VDMDDPQDDR SASNGSSRTS SVSLDGQRPS LPEGVTTMQQ LIAQRAKKFL
EVHENEKNSK IMKKKAMKIL SNLQDLAVKI EDFYLRQQFG NGVELFDQLA AYFDGDVLES
VTSAELLNSE VVRVLLEVFN NPDEELANDA RSAFLEVFMG RTVNRKPKTA TADSPATPFS
VLIHKLQDLL SRTEHFEVVT VHQNTFDGNR SSAASMLAKQ IRLKLVADDD SDIPRAYRNI
MVSIHAIATF KALDDYLRPR ISISERSRSS RHRDGLSGAL AALAAAGMAN PYGPPSAASR
LAERQFAAAM AGHAAPPPPP AASRSSRRHK SKTAPTATPA SAAESATGTP QEKSARRSSR
RRQSQTDQPP PPPPPPQQDD DSLQGALECA DERMLSEDDE IDDSAALDAI VGELNEEMEE
DNGEDPGAVN LEVAVGGKIT ARKEDGTKVA TPAQAPSASA AAHGPSSAQP ATSAPPAAAT
PTQSNRPMSY AAAIQATPQD WHIEFSLDDK PISNEITIYR AVHSTTGHID EQTSRNVWSG
VHAIKFKRVA GPPPAEPSSF IQANEAAETT ASGIPASLDK HPATSSILRL LNILHALNAN
IDDVLAENKD TLKLNVEPLS QFVNTKLTAK LNRQLEEPLI VASNCLPSWS EDLAHLYPFL
FPFETRHLFL QSTSFGYARS MTRWQNAQSA DESRRDRHRD ERPFLGRLQR QKVRISRSKI
LESALKVMEL YGASQSMLEV EYFDEVGTGL GPTLEFYSTV SKEFSKKKLK LWRETEGNDS
DEYAFGLRGL FPAPMSEEQA QHENGKKILH LFKMLGKFVA RSMIDSRIID VSFNPTFFRI
GDESTTVTPS LGAVKTVDAQ LAASLKLIKK FVHAKKAVDE NGSLTAAEKV AAAENILVAG
VRIDELGLDF TMPGYSTIEL IHNGSHTAVT IDNVDLYLEK VIDMTLGSGV QRQVDAFRTG
FTQVFPYSAL SAFTPNELVM LFGRVDEDWS LETLMDSIKA DHGFNMDSKS VKNLLQTMSE
LSDTQRRDFL QFTTGSPKLP IGGFKNLTPL FTVVCKPSEP PYTSDDYLPS VMTCVNYLKL
PDYTDLEVMK RRMDTAIKEG QGAFHLS
//