ID A0A395IAU0_ASPHC Unreviewed; 1810 AA.
AC A0A395IAU0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-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=BO97DRAFT_333503 {ECO:0000313|EMBL:RAL17332.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL17332.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL17332.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL17332.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; KZ824267; RAL17332.1; -; Genomic_DNA.
DR STRING; 1450537.A0A395IAU0; -.
DR VEuPathDB; FungiDB:BO97DRAFT_333503; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:RAL17332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1454..1810
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..770
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1777
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1810 AA; 198614 MW; DCDF9160FF18E7AD CRC64;
MSSRVTRSAA RHAAEPHPST SAGSSPTNPA AGPASIRKRK APRPDQSVGT SEQANPSSTP
RKSKRQRRAA SSTPPAPQAA STAAHRRGTR HRPATMSQPG SSSRPTEESS KAHVSPPSRR
KSNKSGRSED RTPTTQSPAP RQKKRSPKTD SDVLMREAEE DLEEQEQMEE EHESPPISDD
HEGTIPSALD EDDDDDDDDD DADLFHNSLF GARGHLGLQS TLRALTGMMS GMSSRLRDIL
NNLRMKDDPS IQLIALQELS DLLLVSNEDN LSGQFSPDPY VKELVALMQP NDFGEENPEI
MLLACRCLAN LMEALRGSVA NVVYGGAVPV LCQKLLDIQF IDLAEQALST LAKISVDFPA
SIVREGGLTA CLTYLDFFPT STQRTAVTTA ANCCRNLPHD SFPVVRDVMP ILLNVLSSND
QKVVEQGCLC VSRIVESYKH KPEKLEELIE PAMLKAVLRL LLPGTTNLIG PHIHTQFLRV
LAIVSRASPK LSVELLKMDV VDTLYQILTG VSPPANLGDT AVRMDSVLVM QALIHRPKEQ
VLETLNVICE ILPTVPSRHV PQLEGLIGVS GASKLPKAQE SAEQRRELLL GCKTELKRFA
MILLPTLTDA YSSTVNLEVR QKVLTAQLKM LHNLDVGLIE DALKTVPYAS FLAAILSQND
HPTLVSHAIR CAELLFIRLE HVYRHQFHRE GVISEIFKLA QEPLSTNKQE KQSGGASTTQ
DASKEEKPAA AVPAKDASVV GSDDEDGQDD DEGEDDYDEQ DDEDDNDDMS ETSSSASGQL
VATKIANALK DLVTHNAQGF VSQYEASQGK DMRDKALEIL KELQSLASDI EACYSGDGDD
EGLSLFKKLA TYFDGDALES ITSSELLNSG IIQVLLGVFG DFQSSSMREA RAAFLQAFMG
STISEKAQSQ STATTPFSVL IQKLQDLLSR TEHFEVTTVS HNSLENTRSN AAYMLGKQLR
LKLVADDDSD IPRTYRNIMV SIHAIATFKA LDDFLHPRIS LTDRPRLSRN HESILAQLAN
ANAARLREHL ASGDNASSDS PQLPRTSTGT SNTSRPRETL TGATESESRS RRFGRPEAAA
ESEHDNEPLE CADERQMSDD EDHEDDGDDE ELNAIVDDLD EDLSDDNAHD PTAVNMEVAS
SGKVTARKED GTRVATPSQT PASKSSTSAP GPAPNPSSGS SLATAGRPFS SYAAAMASTP
TDWHIEFSID DHPVSSDTTI YRAVHHNRQQ VDPSVKNVWS AIHTVKFRRV PGPPPPEPST
IAQGGSSAAG QAEGEEMPAS LSQGPTTARI LQLLRVLHEM NATLDDIVAE TKELVALKPE
PLAQFINTKL TAKLNRQLEE PLIVASSCLP TWSEDLARLF PFLFPFETRH LFLQSTAFGY
SRAMMRWHNS QNGDDNRNDS RRDDRPILGR LQRQKVRISR TRILESAMKV MELYGSSPSV
LEVEYFEEVG TGLGPTLEFY STVSKEFSKK KLKIWRENDC LSGEEYAFGQ RGLFPAPMSE
AQAASEAGKK QLHLFKILGK FVARSMLDSR IIDISFNPAF FRIADSSSSV APSLGTVKAV
DQDLANSLLF LKRFANAKKA IEEDRGLSAA QKSQALQAVE IGGVNVEDLS LDFTLPGYPA
IELIKDGSNI PVLIDNVDQY VDRVVDMTLG SGVQRQVEAF RAGFSQVFPY SALRTFTPKE
LVMLFGRAEE DWTIETLMDS IKADHGFNMD SRSVRNLLQT MSELNPQQRR DFLQFVTGSP
KLPIGGFKSL TPIFTVVCRP SEPPYTPDDY LPSVMTCVNY LKLPDYSSLD RLRERLSVAI
KEGQGAFHLS
//
