ID G0RD99_HYPJQ Unreviewed; 3995 AA.
AC G0RD99;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=TRIREDRAFT_2956 {ECO:0000313|EMBL:EGR50706.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR50706.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR50706.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
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}.
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DR EMBL; GL985059; EGR50706.1; -; Genomic_DNA.
DR RefSeq; XP_006963056.1; XM_006962994.1.
DR STRING; 431241.G0RD99; -.
DR EnsemblFungi; EGR50706; EGR50706; TRIREDRAFT_2956.
DR GeneID; 18484436; -.
DR KEGG; tre:TRIREDRAFT_2956; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_2956; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008984; 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; IPR016024; ARM-type_fold.
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; 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:UP000008984};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3659..3995
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 224..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1944..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2022..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2309..2505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2630..2649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2654..2674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2799..2877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2976..3002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3146..3172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3284..3363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1944..1975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..2000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2053..2067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2309..2327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2418..2492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2799..2847
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2976..2995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3146..3163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3296..3356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3962
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3995 AA; 444917 MW; D6FEB79EE23C9EC0 CRC64;
MGKITKTMQP KHRETLSSWL KQYVESASTA PLPLLPQQLA DFPTRWPFGR GDLYHWIPLL
NRFDSVLEHF CKVYNLNEGP QQRDFGCDVL LNHAKDSAFE GEKQWQMDEL TQLGFPSDGD
RVLIEAILKF TRMLLEHCGN RSIYASSAHL NDLLNCIPPS ILIATLEVGS ELAQRYQASV
KRIGSASRHI SAALLANHYN IDLDRVQQIA LPFVKTPIFN MSESAPTSTH ASGSKGKDKA
ATGSGSRNVA TSHANDLVAI AASDDSRWSA WGDVKVSYYP QEAAPSQYDA PAEAGRSTLP
LTPTPLRRSS TMNPQHTPRA RNAASDDSSP LVPRTSASVE DHSSSGQKTF ELPQHVVASR
PIYELVKRCP DDMPPAAKYE AFHRLRVAKA LISSQESRQQ ILATRLLAVT NLAYIHSESN
FVEKVLRQDI DETRRFQLVY QLAELIHPSA DGTIEIPLRL QTIALALLEA VSSFHARRQD
VLSALNANVN HGILLYVIRK AVAGMTETHD GDDGDKANEI DEWRNNLFSL TLHLSMATRV
GSEMVSAGLM DILVEILNIR SVIAQRHHSM VLAFLDGLVW TYPNAFTAFF NANGLDAVAR
LIVDTIGEAR SLLRASKGIK PEQQSSAVDY EIPYYQQQTL KWILKFVHHI MSNSYSYSGN
TDRLLRNLAE KSDLLANLRD IINDKKSFGS VVWTNSVTIL SDFINNDPTS FAAISESGMI
KTYLEAITGR PIPDDYTTRP RYRESEGDEP GTVDVSAITS ITDLDSRPHP PSDDSIRQSL
GRPVATGILA SSDAINVVPQ VLNSISLNNA GMQLVVASRA FESFLEVFES PAHVKCMEVD
TELASNVGAS FDELARHHPP LRKSISNAVI DMVARVRMLG IEKARVAGWG VKLLPIGSLQ
AAAESTSVAE APKPPQEAAD MDMADVAAPQ ALEADKRTET ERDSPYESFT PYIYALSNFL
TTYLSNGVLK NNFVERGGIE LLLDMCQSPS LTAGYGDSMA SRVLNQVISQ LIEHGAAQGL
TSLLNRAQRA IDVLEPLSTK TEAVPPYFAP FLTDLGIEYS SSEAAEILAT GTNIVKALLN
AQTYMKIISD CFVSSRGNTL QFYPVNVYDY YIKLVKSIGP LLRGVLAEEA GELTAIPQHW
SLRRHSPPTA GGSRGTGADV EGDDGSLTDV LGGTDSWRPN DGADASSTSR LTEQEQASPR
FQNYETLRVL LHPMIPTSFP LFQTIGKALL PRREANHGDP YHRPRHLQIA RALADTVLDH
LRPSVATPEP TSKDFHYWII MLHTIHEMVI EHPASSRPTD RANVQIIMPV LLAFKERDGI
VVLNDMLRVF ADTVKSSTAA TAEDSSKVKV AAFGLKKILD LYFILVNGKH IGDTHTYYNL
QRQTDRSQFV QNIHSQITVE FRALILPVIM ELWDSTFVER VPDQTVKRLV DILKIVALGE
GELQSMPKDK VPFVLLKYTE VPFNWRAVRS LVRQLADDFD ESLAQEAAYR TFGNPNTASA
YCSAHEAEIA GARNPVPPED APDASSLAEG TTPTSASRDA SGSRAPEPEA MSLDISPDTS
AENLDDLISQ LPESNDLANE TESGADTGSK AAEPTPASAE AGSTAEYTAD SFNALKQGLD
DHRSKLRENL IDQCLDVIRA HPDTAIEVSE LITTVVLRHQ NADAHEEVGS TLTSALTSLA
LDEDERKRNG KCIAAYAHLL ALLLQDEMFF SRNMDTLRDK IGEYVALLKV PPSTPSEELP
PWIPFVLLVL ETLLSHDEKP VAVQWRAPKS LDEPVAEPVI QLRTPLLDDQ QRSDVLESLL
DLLPRIGKEE MLATAILRVL IILTRRRSLA KQVGEKKNLQ RLFLMAKQMS GSGSERLRQI
RLTAHLITIL RHIVEDEEII KQVMRAEIKS DIPNLQRTQR GHLDVPTYLR AMAPIALRAP
DLFVEVTNEL LRFSRWNAPT AEGTRSQTLV WKEEDSSSTN VAQPESENVQ SEDVKPSTES
GDKEMPDALK PHHDSKRPVV ENPDGVIHFL LCELINYREV EDKEVPPPSR DAKTETESAA
SGDAQDSASA EGVAADGKDK KPSKPTFKSE EHPIFVYRCF LLSCLAELLQ SYTRTKMEFI
NFKRSAPPLS TNTPVKPRSS ILNYLIYDLL CQSSLSGTSD NIAAKKKAAT SAQTQKVLVA
LVSKTNEKVF DRKQEKYAYD DEPDLLFVRK FVLDTILKAY EKAPLTDEPL EVRYARMQCL
AELMNNMIGE KDKEQTSGSR NVDSVQTRSQ AQLRRLMYEK GYLDKLTSSI AEINLNFPGV
KRAIKYILRV LRVLTDTAKE LSHSNILVSD SQAEQSDEEF ASTSSLSDLD EGREETPDLY
RNSALGMLEP RGEDDESESE EADDDDEDMY GDEYDDDEMD YGDEEISDDE DDISDDDEEL
SQMGEIEGLH GDPGVVEVIM DDEDDDDDDE DDEDDDEVDS ADMEDLEDRV EIVDEDGNPL
EDDGESGWES ETSAEEDEEP EVDDIDYEAE GQDEDEAHLH GMGPGDLLDN MARAIMGGDE
DGYEPELMEA LDEHYMDDGH DDGDEDDEED MEDEEYIYDD DYPLNDPLPP MPALGWDGFT
PEVDDRHRQV FLLDNNRRPV LARMDNRNPF PPRFIPGTHR DLSDFRSYFS RSHRNNGQQP
NADDGMNPLL RRSDQAQENQ PRPGHPHSIG LRFPEGFLGP GRHLMEGPMG FLGELMEFLP
IMGRGNQHAF HVHISGPGGT RSTDLGPIRG LRSEQRRDAA SQEPHQAVAF TPETTLDRYQ
EEARMIFGNP VAEAARLGTA IIAQLTPAAM ELERKLKAEE EENQKRLEEA RKKREEEERV
AREAKEAEEK AERERKEAEE REAAARLAAE AAEAAALAAS QTTEPQPGTG QGGGAMEGVE
STEAGVAHDD QANTSRANVP RVTTIIRGEE VDVTELGIDP DYLAALPEEF REEVIAQTVS
ERRSQAREEA ASGEATEVFQ EFLDALPEEL RMEIAQQERQ DQRRRHREDG RRQATAADGQ
DAIPAEMDPA SILLTFPPEL REQALIDQGE DIMGQLPPDM AAQVRALTQH RPPVAHQRGG
MRPIGESKTQ RKTVVQMLDK AGVATLLRLM FIAQQGSIRN YLFSVFADVC ENRQTRLEVI
STVLQILQDG STDMNAVERS FGQLSLKARK QKDKEKDGDQ KNPQGLKRTL TTVGSLTASG
QTNSETSPLL IVQQCLDLLV DLCTKNPHIP WLFLTEHESI GSSSLKRSLS RRGKGKDSKA
HKYAINSLLT LLDRELVTES SLVMTHLADL LNRVTLPLQN LERRRKEAQD EDASGSKGTG
AETQAVTTNA NEAEQRDNNE QTVDGSSASA QATSSEQKAA GTEESAEQSK SAPQKRARQL
QPPVIPPQNL TLVVRVFVAR ECSSKTFQNT ISTIKNLSAI PGAKTIFGQE LVSQARLLSS
NIVSDLDDLL PHIEAATSGT EIQGVALAKF SPGASEQNKL LRVLTALDHL FDGKKKSDDA
DDGSSEKNEK QDLVTSLYHN STFATMWEKL SACLSAIRQR ENMLNVATIL LPLIESLMVV
CKNTTTNDDL SSSMVGKDML SSPQPESRTA NLFFTFTEEH RRILNELVRH NPKLMSGTFS
LLVKNPKVLE FDNKRNYFNR SVHSRSGQNQ SRPSYPPLQI SVRREHVFHD SFKWLCFKSA
DEMKYGKLNI RFNGEEGVDA GGVTREWFQV LARQMFDPNY ALFIPVSSDR TTFHPNKLSG
VNDEHLRFFK FIGRIIGKAL YEGRLLDCFF SRAVYKRILG KSVSVKDMES FDPDYYKSLC
WMLENDITDI ITETFSVEDD EFGVTKIVDL IPNGREIAVT EENKHEYVRV VVEHKLLSSV
KDQMENFLSG FHDIIPAELI SIFNEQELEL LISGLPDIDI DDWKANTEYQ NYSPSSPQIQ
WFWRAVRSFD KEELAKLLQF VTGTSKVPLN GFKELEGMNG INRFNIHRDY GNKDRLPSTH
TCFNQLDLPE YDSYDILRSQ ILKAITQGSD YFGFA
//
