ID A0A0F4ZHB7_9PEZI Unreviewed; 1710 AA.
AC A0A0F4ZHB7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=TD95_004292 {ECO:0000313|EMBL:KKA29263.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA29263.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA29263.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA29263.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) 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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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:KKA29263.1}.
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DR EMBL; LAEV01000930; KKA29263.1; -; Genomic_DNA.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000033483; 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; 3.30.2410.10; 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:UP000033483};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1353..1710
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..623
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1011
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1677
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1710 AA; 188894 MW; 78D922C85798FC9B CRC64;
MSDDSQDLAA GPSSSSQQHK ESDLSSDQDA AMTGTEDLAL EHQDSQHSSD DDEADDEHDH
DHGHRYDDED EDPFSEYGTS HISDTLRAFH GMMHGMPSRM RSILESLRSG DVNIQYTALQ
DLSEILLVST EDNLQGQIST DLLVKELLNL MQPENTPEIM LVACRCLANL MEALPTSVGN
VVYLGAVPIL CSKLLEISFI DVAEQSLSTL EKISREFPAA IVREGGLTAC LSYLDFFATS
TQRTAVTIAA NCCRNIPEDS FPVVRDCMPK LLDVLSSSDQ RVVEQASLCV CGIVESLKYH
PSKLEDFVNV DLLRAVLRLL VPGTTNLISS SIHTQFLRVL AHTARASPQL SADLFRLNVV
ETLYQMLTGV APPSGTDDIA SKLDSVIIMQ ALIHRPREQV METLNVICEL LPSESTNNFE
ISQNQFFITD RSVLKANNEK RIKLLKDCVP EVRRFAMILF PTLTDAFSST VNLDVRRRVM
TAHLKMLSNL DKPILLEALS VVSYASFLAA IFSQKDHHVL ISMALQCSEL LLSRLGDVYR
YQLYREGVIA EITKLAHDDA VEVEELNEKP AADSEIASDD ESDEPETHDE DVTSDQDDDA
VIADAMYSDN ESLEEEGLDY EDRDGHDDEN VEHNESEDDE ESGSESSGSH DSDSDDGPCH
VARNVVSAQS QIKAAAKKFL ENHETEKQSK QMKKKALKIL TTLSELSESL EAYFLHRNAP
DMSPEAGKAL FTRLAGYFDA DVLDSVTSAE ILASGLIKVL LDIFGNPDEN LARAAQATFL
ESFMGTSSKL KGKAGIADSP QTAFSSMIHK LQDVLSRSEH FDVTTIQQSP YEGSRGNSAS
FLAKQIKLKL VADEDSNVPR AYRSLMVSIH AIASFQSLAD YLRPRISITP VSELDGISHT
GRFAALSQAL AAINNTGALS PADAQRLAAQ LGAFNSHRAG STSESYSRRH KWPEPEAPTT
PGSNSGTRKS HNRNDATGTP SAKSSSEDES MNESAECEND KQDSDEEEDD PAPNALEALL
NEFEGRHHSS SGHTSGSNDS DKNASDTKVS TPTKSPKAQS KASASKASSG SPAPSSKRAR
KTSLQTAAKG KSKSPKSDDS PTSNEWHIEF LIDGKVIPSD HTVFRTIYNF QNNDENNGRH
VWTNVHQIKY RKVLGSATPR ASSQPPSADS PEGSSSDGIP SSLTQHPITA SVLRLLRILH
DLNANIEDVM AENSEIVRLN VEPLTQFVNT KLTAKLNRQL EEPLVVASNC LPNWVEDLAR
CYPFLFPFET RHLFLQSTSF GYARSMTRWQ SGQGNDDRRA RDERQFLGRL QRQKVRIGRS
KMFESALKVM NLYGSGQSIL EVEYFEEVGT GLGPTLEFYA TISREFAKKK LKLWRDIDTS
EDELYVTGPT GLFPRPMTKA QLSSSNGTRI LHLFTMLGKF VARSMLDSRL IDIHLNPIFF
RIGDGSMSGI RPSLGAIKSV DPALARSLKM IKKFVVAKKE IDDDSSLTPE EKTAMYDSVM
VDGCSIDDLC LDFTLPGYPN IDLLHRGAQK RVTMANVDKY LDLVIDMTLG SGVRRQIDAF
RAGFTTVFPY TALNAFTPDE LVSLFGRVDE DWSLETLMDS IKADHGFNMD SRSVKNLLQV
MSTLSDTERR DFLQFTTGSP KLPIGGFRSL KPMFTVVCRP SEAPNTPDDY LPSVMTCVNY
LKLPDYSDLE TMRKRLMTAI KEGQGAFHLS
//
