ID A0A0L1IL59_ASPNO Unreviewed; 1801 AA.
AC A0A0L1IL59;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=ANOM_011394 {ECO:0000313|EMBL:KNG80314.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG80314.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG80314.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG80314.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG80314.1}.
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DR EMBL; JNOM01000636; KNG80314.1; -; Genomic_DNA.
DR RefSeq; XP_015401237.1; XM_015556650.1.
DR STRING; 1509407.A0A0L1IL59; -.
DR GeneID; 26813198; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000037505; 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:KNG80314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1423..1801
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1145
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1768
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1801 AA; 198560 MW; 3D475B7F8D49C0F5 CRC64;
MARTRPNLHR QDPLEDSSTG APATAARITR SAARLAAEPP PPATSGPSPA IPAAGSAPSR
KRKAHPRSDR SVEAPGQPNP PSPPRRAKKQ RRAASPQPAA ASAPPRRGTR NRTVMSQSGS
SSHPTEEPSR NQPSPPASRR KSSRNGKVSQ DRFSAAQSPP PRRQQKKRSS RNNPDVTMKE
ADEDLERRER SEERESSPPS DSNDGTNHSG LDDDDGDLFH NSLFGSRSPL GLQSTLRALS
GMMTGMSSRL REILCNLRAK DDPSIQLIAL QELSDLLLVS NEDNLSGQFS PDPYVKELVS
LMQPNEFGEE NPEIMLLACR CLANLMEALR GSVANVVYGG AVPILCQKLL DIQFIDLAEQ
ALSTLAKISV DFPASIVREG GLTACLTYLD FFPTSTQRTA VTTAANCCRN LPHDSFPVVR
DVMPTLLNVL SSNDPKVMEQ GCLCVSRIVE SFKHKPEKLE ELIEPAMLKA ILRLLLPGTT
NLIGPHIHTQ FLRVLAIVSK ASPRLSVELL KMNVVDTLYQ ILTGVSPPGN LEDTTVKMDS
VLVMQALIHR PREQVLETLN VICEMLPGVP GRHVPQTDGW LNNPLDSDPS LGLKSPKAKE
VAEKRRSLLR ECKGELKRFA MILLPTLTDA YSSTVNLEVR QKVLIAQLKM LHHLDAGLVE
EALRSVPYAS FLAAILSQKD HPSLVSSALR CSELLFQRLE HVYQCQFHRE GVVSEIFKLA
EGPLSDEKQT KPSSDSSAAM DTSSDSRREA EDVDGPGDDD THDDDYDEHE DERDENDDMS
ESDSSSASGQ VLSTRIDNAM KDLVVRDART FVDLYEAGHG KDMREKAIEV LAELQNLASN
LEVCYRSDAR EDGLGLFQKL ASYFDGDALE SITSSELLNS GIIKVLLDVF GDFNSSSMRK
ARAAFLQAFM GSTISEKAQS QSTATTPFSV LIQKLQDLLS RTEHFEVLTV SHNSLENTRS
NAAHMLGKQL RLKLVADEDS DIPRTYRSIM VSIHAIATFK ALDDFLHPRI SLSDRPKPSR
SRESLFSQIA NAARLRDQLT GNGEFPGSDI PSLPRQSTNN DRSSHPEDSQ PNAQESSIEG
QERSSRSRRS GRHQQTSEDP AHDDEPLECA DERHLSEDEE EDDDGDDGEL NAIMDDLDDD
LSEDNAPDPT AVNMEVASSG KVTARKEDGT RVATPSQSTP ASKASSSASS VAQNPAGNNS
LATAGRPFSS YAAAMASIPS DWHLEFSVDG NPITGDTTIY RAVHHNRQDS DPSGRHVWSA
VHTVKFRRVP GPPPPEPTAL TTSVPESAAK NASTEMPPSL SQETTTASIL QLLRLLHEMN
ATLDDILTES KELVALKPEA LAQFINTKLT AKLNRQLEEP LIVASSCLPS WSEDLARLFP
FLFPFETRHL FLQSTAFGYS RAMMRWHNSQ NGDDGRNDHR RDDRPFLGRL QRQKVEYFEE
VGTGLGPTLE FYSTVSKEFS KKKLKIWREN DCNDAEEFAF GKRGLFPAPM SEQYASSEPG
KKQLHLFKVL GKFVARSMLD SRIIDVSFNP AFFRIADSSF SVAPSLGTVK AVDQDLANSL
LLLKRFANAK AAVENKGLSE PQKREALLNV EVDGVKVEDL SLDFTLPGYP SIELIEDGSD
VPVTIENVDL YVERVVDMTL SSGVQRQVEA FREGFSQVFP YSALRTFTPA ELVMLFGRAE
EDWSIETLMD SIKADHGFNM DSRSVRNLLQ TMSELDAQQR RDFLQFVTGS PKLPIGGFKS
LTPIFTVVCR PSEPPYTPDD YLPSVMTCVN YLKLPDYSSL DVLRTRLSVA IQEGQGAFHL
S
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