ID A0A2B7WPB5_9EURO Unreviewed; 4136 AA.
AC A0A2B7WPB5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=GX51_06700 {ECO:0000313|EMBL:PGG98615.1};
OS Blastomyces parvus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGG98615.1, ECO:0000313|Proteomes:UP000224080};
RN [1] {ECO:0000313|EMBL:PGG98615.1, ECO:0000313|Proteomes:UP000224080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH130 {ECO:0000313|EMBL:PGG98615.1,
RC ECO:0000313|Proteomes:UP000224080};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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:PGG98615.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDNC01000116; PGG98615.1; -; Genomic_DNA.
DR STRING; 2060905.A0A2B7WPB5; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000224080; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 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:UP000224080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3800..4136
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 212..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2036..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2122..2176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2409..2597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2741..2782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2923..3033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3098..3128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3174..3198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3398..3508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2049..2064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2073..2099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2143..2170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2409..2424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2428..2442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2458..2503
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2519..2558
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2575..2597
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2923..2980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3177..3195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3398..3426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3427..3464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3477..3506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4103
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4136 AA; 460035 MW; 48358D8DA5E1A73C CRC64;
MGRIKKVAAL KHEATISPAL ATFVQQTITV DIPELPSHLS TFPRRWPFPR GDLYHWIVVL
NRFDTILQQV VEKYDLHLGP QTKPFGRLVL HDACVSAGTA ATTQESDAHL DKLGFGSEGD
RELVEALLGF SRLLLEKCGN RSLYSSSDRL NDFLNTTSLP LLQSTLRLGV SLAQRYFSRQ
RQSNSTHFHQ SLLATHYNIE LERVQKLAAP FAKPAPAKPA DNSSVSIKGK EKATQVQVGR
RGPVTKCNAN DLIALTKEPS DALEPNGVPA QAWEEWANIS MSYYSPSSDA GEATSSAGVE
STPNAPHPPA TPTPLRRAST HPSSRLSRSS VADESPTVPL TSSPIYKYDE TNRGVKVLEI
PSSTIVSTSI EQVLQTHLEE LPNDPSKYEL LQRLRVAYAL STSTETRRQI LAIRVLAVTN
LAYIYPETLF QQKVLNHDSD IPKRLQLAYQ LAEFVHLGVT SDIAASTLNQ AFALNCLDAL
AKHKSRSADV CAALSVNVNH GILMFLTRKA VADLAIEEKE DDPPEADDWR EALFALLRTL
PNAGTRTPET LVAAGLIPLF VDILNLRTDK ARKIYPRVME FLDTFVHSVR DALATLAGAK
GFHAISDLIS FETKTSFDSV AKDEGIPAHF KTPSIDYQIP YFQQQSLRWL FKFVNHVMQH
NSGGYERLLR NLIDSPPLLS ALRLVVENAR IYGSHVWSGA VNILSHFIHN EPTSYAVIAE
AGLSKSLLEA VTGRPMPSDT TDINNATTDT EDGDHAPAEP RPLFIPARAE AGDHETLRSK
IARKPDRKLA EGILPSTEAI LCLPQAFGAI CLNQGGLELF RKSDALESFF DMFESPEHVK
CMKTDSNLVR VLGGAFDEFV RHHPPLKSAV MSAVLLMVAR VAQHCKSKAS ERGLGAKLWT
EGEDGKLSVA GGPSSLLGDI GSAFTHALGN QQPPSEAAAT EPTEPADSEM RSAMTTPRDG
DALTPPKKPE NGDLKDLDGD GLSVSNYIFP VVKFLNAFFE NHSICASFIE SGGVEYVLDF
ATLQSLPFDF HNTEASQQLA QVIHYMVEVK PHLVLPSLLK RTQDAVDCLA PFWRQPSQTG
FFAPLTNPSK QIENTTETPD SEDVKAQGTY FTKHLVAVHT LTDILREAYT PPIYPTRPSQ
QTSPFIQVNL ADKYVALVKR LGSLHSACVW EEILLQKDMP ESWNEATRVP GYGFDGDEEI
ELPSTVPADD VSEPGDVAAE DATGTAAAGT GLPNGETTRR SAVTQTSVGS EKGATFRNVK
TLRYLLSSLP SSITGFFQLL GHGLISKRRI DSYQRQKASA VADAIASMIL EQLTLDAPKK
ATCVKDQFSY LIVILSSFSQ LLFDTTAERP HSHCLTIILS AFKKFNGIQT MKDLCGLFLN
EIKTLGPQAQ EDSTPKDVPA RLASAYGGIK IILNFFSEMT SAQYIIDSTQ TQAMATAGGD
RDRPDYFLPA QFLVELRMEV IPMVREMWSS GFVEEASSSI LKSLIDILRS VLEGEYESGA
FRRGETFPAV SAMTPKTFTF NRERLATLKE NGHDENLARE ALYRCNNSAS AAEEYCSSQK
GLRPPPRSPV SSHELDQTTS STPSLRDTIF ANLNTSQPPS DSTQILSATP FDIASLFPHL
TQPGTSVEES GTNQAESAAN QGAQSDDTSN SSGLLAMSID NILNDREESR TEETNMPAQR
PETAAQPAST SQPAPSPKRR EVVTVEDLDS ERDKVRNNLI ERCLDVLNGH HDITFELADL
IGSATAKLPD PVNFRREVGE TLMHFLISLQ MEENFQSAGK KIAAYAGLLA LVLQDKDVYE
ATLEELKENF STLLGFIKIP SAPPEKPTEE SCPWIPQVLL ILERVLSDDV TPPLIRWNPP
SPDGSAGSEE SAQLEEPVIP FSDKMELFET MVDILPRIGK DETLALSVAR ILVILTRERD
IAVRLGEKRN LQRLFVMIKQ LASGSDDRLQ NTFMLILRHI IEDNDTIRQI MRSEIVAGFE
SRSPRQTDTT GYVRQFAHLI LRNPTLFVEV TNEKLKLQRY DAHQRPQLLV LKSEANDAAS
QRDQAHPSQV DNESSEKPEA AEPHTEPQDG QSAEGNEPRE DKEGKEGKDT KEKCKSTELK
PPVVENPDGV IHYLLSELLS YRDVDDKEPP TESTDKSLPR TESQSDVEMA SGPASPTSSA
SGTQTTKSPK KTEKPQFKAD EHPIYIYRCF LLQCLTELLS SYTRTKVEFI NFSRKADPFS
TTPSKPRSGV LNYLLNSLVP IGTLEHGESI TFKKRVNTSN WAMRVIVALC TKTGEFGGPS
RRRTVVNDDN EPELLFVRKF VLEHALKSYK DANASNEPLD AKYARLLSLA DLFDKMLSGG
TSGDGTTHFP SSTRQVAKTM FEKNFISAFT ASISDIDLNF PPAKRAVKYI LRPLNKLTQT
AVLLSETSSI ATTPGQTDED EISSATSVSD MEDEREETPD LFRHSTLGMF EPNHEEGTTS
EEDSEDDEEM YDDEYDEEMD YEEDMPENDG EVVSDEDDED LDGRGPIEGL PGDSGMDIEV
LIEGDDDDDD DDDDDDDDDD DEDDEDDDED EEGSSAMDDD LIAGEITGDN DNDSLRDGDE
GEWESEDISD NDEEEDGMNQ LETELGDFAQ GDHGSNLQNV LRILGEQNRN RLDIHRLELD
MGIGDELHDD LMDDEMQDDQ DEDDEIDELE GLDEMDDDED DLVQTFDFDH ADQFMLHDTD
AAMDHRHAGH GRFRGIPPPP WSMFSGGGLG NRHGIVPIPG YRTHRNQIPS RGNDDGSNPL
LRRSDRPTDV APGSRGPPEA LSDWVHAIDP NHQGRLLTMD SPVTFMNAIM QALGQGGGGF
GVVSRPDGVH VRLDQGHVFS NRIQNFFGLS RPPATTRRPR DDPYQAVTFV LSTTSTRWQE
EARLLFNNTY LEKAQRVVNS LLKVLVPPAI EEEKVRQKQL EEELKRREEE RIERERQEQL
AKEEAEKERK RKEEEEEALR RQEEAERAER AAEESAQQAA EHPEGEPMDG VQPTEPTQEQ
TAAPSEAEAA AAGPSEPAPR IHTTIRGRQL DITGMDIDPE YLEALPEDIR EEVIMQQLTE
QRSQAAASGE EPSEINPEFL EALPPDIRDE LLQQEVADRR RRERDAARRN AAASGGPAAP
DDMDPASFIA TLDPSLRQTV LADQPEEILA SLGPEFVSEA RALTGRRLAQ FADVGRLDQR
SRPDASQRDQ GTKKPQRRQI VQMLDKAGVA TLLRLMFMPL QGNARHHIND ILHNVCQNRQ
NRSEVLSLLL LILQDGSADV SAVERSFAHL SLRAKTPAAA QRTPQLKRTL SLPMPGANND
VTPLVVIQQC LGALSFLTQY NPHIAWFFLT EHDTAASLKM KALRKGKAKE NRASKFALNS
LLSLLDRKSI MDSPSCMEQL SSLLSSITQP LTLLLRKDKE RQEKEAKEKE AKEKETKGKE
AERTEATSES TQPAQPTEAP TQATEVTADE TTPHSDTTMA DAGPTGQGQD RAEGQEEATG
SSAEEKAEPS KLAEEDKQKK PRIPEPPVVP EHNLQLVVRI LAARECNGKT FRETLSTINN
LSAIPGAKEV FGKELIAQTQ ALSNSILGDL DDLLPHINQA ETGIEVQGMA LSKFSPASSD
QAKLLRALTA LDYLFDPNRL DKEKYSEPES SNNEDVLKIL YEGTTFGPLW AKLSECLHAI
RQKENMLNVA TILLPLIESL MVVCKNTTLK DAPLSRHGRE YSVSSPPPES GMEGLFFNFT
EEHRKILNEL VRQNPKLMSG TFSLLVKNPK VLEFDNKRNY FTRRIHSRGS EIRHPHPPLQ
LSVRRDQVFL DSFKSLYFKT ANEMKYGKLN IRFHGEEGVD AGGVTREWFQ VLARGMFNPN
YALFIPVASD RTTFHPNRLS GVNQEHLMFF KFIGRIIGKA LYEGRVLDCH FSRAVYKRIL
GKSVSIKDME TLDLDYYKSL LWMLENDITD ILTENFSVES DDFGEKQTID LVENGRNIPV
TQENKEEYVQ RVVEYRLVGS VKDQLDNFLK GFHDIIPADL IAIFNEQELE LLISGLPEID
VDDWKNNSEY HNYSASSPQI QWFWRAVRSF DKEERAKLLQ FVTGTSKVPL NGFKELEGMN
GFSKFNIHRD YGNKDRLPSS HTCFNQLDLP EYDSYETLRQ RLYTAMTAGS EYFGFA
//
