ID A0A0C9XV58_9AGAR Unreviewed; 1935 AA.
AC A0A0C9XV58;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-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=K443DRAFT_496518 {ECO:0000313|EMBL:KIK08916.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK08916.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK08916.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK08916.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-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}.
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DR EMBL; KN838540; KIK08916.1; -; Genomic_DNA.
DR STRING; 1095629.A0A0C9XV58; -.
DR HOGENOM; CLU_000366_0_1_1; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000054477; 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:UP000054477};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1592..1935
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1397..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1902
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1935 AA; 209614 MW; BECFA9739A35034F CRC64;
MDLQPIHQQE ATSSSSASTA PQDSLPTESK ALRSSARVKA AKQKSKSKGK GKEREVNDID
QQPSASSSAP STETTATATA TRSRATTGSA KQKRSREAVT GKGKAKEISE ELPPRSVKRI
RRNTSATTAP LSINEPVKDH KGKKRAAPDL DDEDNVGPSF KRSRTTAYSL RSSTSSPQVL
EMPKKSRQPT SKGKAAFKSK MAIAGPSRLE DEDIDMIDAA ETELHKQEDI GAEDRTGLIA
KVEGTKEGGE VEPEGHGISG VDDDGEDDDD DEGGDGDDVP GDDEGMVPSS DGPPIPGGLD
ETAAMAIFGD YRQFGSYMMS LSSRLKTMLT NIKSTADPTT RLVTLQELSE LLSISTEDTL
AGSFQVEQFV RELVKILGGR GADEDEDDEG DEENAEQDED AALAAALAMS TGGSFQGDDN
LEAQVLACRC LANLMEALPG VAHTVVYHGA IPVLCSKLIE ISYIDLAEQT LSTMEKISEE
FPSSIVREGG LAALLNYLDF FSIAVQRTAL QAASNCCRNV SPEHFPMIHG VWPIIRNCLS
YSDQRLVEFA CLCVIRVVDS YHRASVENLE ALVDTALIRA VNQLLLPAGG SPLIASNTYT
LLLRAMATSA RASPKITVAL LEADIVDTLY QILTGVLPSA SEAAEGRGGT AGGQGSGGGL
ADMTIMDNLA HRPKDQVEET LSLISELLPP LPKDGVFDHK AYTEKSLARM VKAKAKAERA
AARQAPQPTP SPTVMSSLDT VSAPLAENEA SPAPGPASEV AGPESEDAAV ISGVKDVAPD
RTEILRSTHA VGRFMQLLVP ILIDVYAASV ITPVRIKTLT GLLKAVSFMD ADGLKSVLMF
VPVASFASSI LSSKDHPSLV IGALQLVDLL LAKLPSLYKP TFRREGVFHE IETMSERSVT
STKSKDKDKE SNESPEPVVQ PISTSSIPGF KKLSSLSLDP EDAITLRARV IQFKYLNGDE
DANEDSAFES LRRLVDRISD QNATEKELSE GLWELAELFS SPHTSVSSFE LLQSGVVDGL
LQFAVDEHRA VNSKRRKEMF LDAFAGRKVK SMGNNQSPFA ILVKKLQESL TRMESFDVIT
VAQNSDDSKR SSPSLLARQL RLRLITGDES DVPRNLHNIV VSIHAIATFQ ALHDYLRPRV
AGLLGPSSRL SGMFAALAAS GFTGSTSRAL NEESSQASRT VSGALETNPP PPVAPSTVTR
RRSQRLSAKA NPSAANESPS GTDQIVADAS ASAGPSLQGE ATFAEPAPSD TVVDSELQAD
FSDDEDIDAE VYDEEVDPDI SVSDKTISLS VIEDGSKIEA QTPDGTRVAT PSASVQDGPT
PPTLRASLSN KTSYAAALKA KPTDWHLEFS MDDQVLPLDL TVYGAIHQHE MRKKTGSLPL
NMIWQGVYTI KFKKVAGPLP SSESRGDDIG TKNRSPSPSL SSLPDDAPHA KILRLLRVLN
QLNTLEAERS VFVGEKRNLP DSAFINNKLT AKLSRQLEEP MIVASSCLPD WALDLPQHFP
FLFPFATRYN FIQSTSFGYA RLILKWQSQQ TRGQDSSRRD DGIGFLGRLQ RQKVRISRKH
ILESAVKVFE LYGSSSSVLE VEYFEEVGTG LGPTLEFYSL VSKEFARKDL KIWRDSDAAG
SGVYVDHPTG LYPAPISRED IANDGGQKRT HILRVVGQFV AKAMLDSRII DLSFNKVFLK
HVLGEEVPLT LASLKLVDMD LANSLAKLQS IAQDSGNIGT DPLSLKVARI EKVTIEDLEL
DFTIPGYDIE LRENGRNMPV TSANVDEYVH EILDAILGKG IQIQAKAFRD GFSKVFPMAD
LRAFTADELV MLFGNGDEDW SIEKALKADH GFNVESRAIR DLLEIMAQYD RPTRRAYLQF
ITGSPKLPIG GFRGLNPALT VVRKPHEAPL IADDYLPSVM TCVNYLKLPE YSTKAVMREK
LRIAIQEGVG SFHLS
//
