ID E3RG13_PYRTT Unreviewed; 3967 AA.
AC E3RG13;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PTT_06702 {ECO:0000313|EMBL:EFQ95339.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ95339.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ95339.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL532841; EFQ95339.1; -; Genomic_DNA.
DR RefSeq; XP_003296568.1; XM_003296520.1.
DR STRING; 861557.E3RG13; -.
DR EnsemblFungi; EFQ95339; EFQ95339; PTT_06702.
DR KEGG; pte:PTT_06702; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001067; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3631..3967
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 215..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2259..2317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2352..2465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2761..2853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2887..2935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2952..2981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3029..3053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3259..3287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3304..3335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1284..1311
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 717..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1927..1946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2367..2451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2761..2795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2901..2920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2952..2968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3312..3333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3934
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3967 AA; 442519 MW; B40FA6ADF80320A0 CRC64;
MKIKKQATSR HESTLSSMIA DFVKATESIP LFQLPAHLAS FPRHWPFPRG DAYHWIPALN
RFDHILELFN KEYGLVDGPQ TQAFQRRLLL KGDVEEGNTS SNQTTTDAVL DTLHVSKDGD
RELIEQILNF TRMLLENCGN RSLYSSSERL DKLLNTTSIS LLKATLRLGH RLAQRYAAAR
MRLAPATLHP SLLSSHYNIN LDKIQKLASP FAKGPTTAAP LFGTPSAKGK ERTGSTDRLS
PSDLVGMYSL SDSSMKQEFG GLLISYYEST PTAEEGSSSK PASTEAPVPT TPTPVRRTSS
MGPSRTPRQV QPAPASDSPS TPAITPGQPS SRTNGPKTFE LSADKVAKSD IHDLVKEGLA
NLPETVHYEF FHKLRVAYMF NNGRTGRDDA VAIRLLAIAN MGYVHVEKEF MAKLGQQDAE
EPRRLQLAYQ LSELVHPPGN GETGISLELQ TFTMNALEAL AKHKSKAPDV CTALSVNVNH
GVLFYVVRKL VAGLGEETGN PDDLDEYEWR DALFSLLNTL PTSQTRTGEQ MVAAGLLEIL
VDVLKLRTAK AERNHPKILN FLDTFVYNLR DAFSALVAAK GLEIIADLMQ YEVDTSKKLA
EEDKGMPRDY KTQLTDYQIP FYHQQSLRWL FKFLNHMMSH TGGNFDRLMR NLIDSPQLLS
SLNTVLSNAK IFGSTVWSMA VTILTSFIHS EPTSYQVISE AGLSQAFLET VAGEPVSEST
TAANDSESAS TPTSYPPREA GKPLAEGILP VAEAISTLPP AFDAICLAEA GMKLFQSSTA
LKRFFEIFES PAHIKALDAD MEMPTLIGNS FDELVRHHPP LKARVLACLS ELIARVVQLC
AEKAEKEGVG AKLWTEDAAG QLAVAGGRQA LCGSRQQQST SQASDKAGTD IEMKDADEPA
NEVVLIEQVT ETEDNTKGPT TSQYIRVLCR FLSGFFSNHA MCAAYIELDG VDSILDISSL
ACLDPKPSEN RSMFEHFGHV VQVLVEQKPH IAVPSLIRRT QQALERLQPL LDHTGKQAFF
APFTSAGTPQ DNEHLQRGTQ YVKALVSAHT LVGAMTLTFQ SQMYSTRSTH NVSSQINLAD
MYARLVDSLG KLHRSCVWEE LLLQRNMPTE WEKETRVASS GFGNDEADNV FRIGNSATEP
STGTETAGAS GTASETAAVS QNSARFKNTQ TLRNLLSKIP TEIAPFFQSL GKLLLFRRSL
EPYQRQCATI VADQLAQAVI DQLEYEGPKD SEVIEDRYAY WIVILTSLSQ LIIEPHVDRP
QALTLLLVSF RNLGGFDVLA NILNQFYESA LEITQKQAEE NNEESKRLLN LSLGGIKIIL
AFFSHIINFK VIGESPQTAS MQSRSDRDKE RSDFFLTAQF LVELRYAVIR PVEKIWNSEL
IDKATTSIVK TSINILKSVL ECEGEHGAFK SIDKIPKRSK PIIKPWTPRN QEHLPRLREM
QHEESLAEEA LYRCADNFNM ASEYCRNQAR PHVSRNPIPQ YEIQTRGPPS ASPSRAEVVV
PEHTDDASMT SSEVTRDEDE SRHPETQSVQ MEDADASGAT QPELPTSVTP VPADQSNLPV
TAPHDALAYQ KRMAVGNSTE LVALDQLDEE RFKLRQTLVD RSLDVLNSHE DVTFELADLI
SAAVSKAPEP ASMRSDIGST LVQSLISLQS EDDFRTQSKK ITASAHLLAL VLQEREFYDV
IVEELKDNFT MLLGFIKIFP DQSAEDSSPW IGQVLLIIER LLAEDQLPQQ IAWTPPTEDS
QEETSVDQLP EPIVSVEEKD KLFSAIIEIL PRIGKDESLA LSVTRVLVML TRTRKLAMRL
AEKRNVQRLF LMVKQLSGIT NEGLRSAFMI VLRHMIEDDE MIRQIMRTEI QQMFESRDRR
QTDTTGYTRQ MYALAIRAPE IFVEVTNEKL QLARFDPNQR PQTLILKKAE PSPAELTDTI
GSSEVVSEAD KPKESSEAPK QPFLERTKTS DLKVPVVENP DGVIHYLLCE LLAYKEAEDK
PEPPKPTESA PEGQASNQLG SETTPTPAAT SSEPTKSEKP VFKADAHPIY IYRCFILKCL
AELLQSYNRT KIEFINFSRK ADPYTVTPSK PRSGVLNYLL NNLVPIGSLN HEGDLAFKKK
LATSNCAIDV IVSLCNKTGE HTVPKTGVPL SPYAETEPDL LFVRKFVLEH ALKAFKDANA
SDEPLDMKYS RLLSIADIFS KMVSQRPNGE MLTQNADLTP NLKQMAKIMY EKNFVTILTT
AISDIDLNFP NAKRVVKYIL KPLKWLCYVA MDLSMHYDTS SAPDSADEYE ISTASDDDLV
DNTREETPDL FRNSTLGMFE PPHESESDED SEGEEGEEMM YDDAYADDME YDEADIGDDD
VVSDDDEEIL EMDIDGMGPI EGLPGDVDVE IELDDDDNGM GSGSDDESDD EDEDDGDEDD
MDDDEGDDDM DEMDEMDEMD EAMDAMEEIT GDDENASLGE DQEDDWSDDQ DDFPGGINGD
GGMSAGALGF VIDQPGHTGQ LIEQMRQQGG PDLDDFLEDG IGEEDMDDEE EEYEEELHYD
PGMDEDEEGL PDLGWGGNWE DPPPPTVRHT HRLSPWMFPA GPGDRILVPA YRSHRPGAGP
RVTDDGINPL LQRGGRSVER DGFVRNEGNS DWVHAIEGRG PRMFSHADSP VSFISNLLNA
MSSGTGPTLQ QHGGALHLSF NNPMGLPPFD TGMRRDIARM RESYTSRSAR EDPHSAVAFV
KAYTASRWQE EARILYGPAA IEKSQRVINS ILKVMVPPAM EAARKRQEER EAEVARKIKE
EQEKKEQKER EEREKREAQE KEERERQERE AAEAASRAQE QPATEEATVA TETSPEARPM
EGVEIGQSST ASASEEPTPA APAAPTEPRI MTTIRGREFD ITDLGIDIEY LDALPEELRE
EVLMQQVAER RAEQRAEQRA QSRQQRQPQS QPQGQEAAEQ EADPSGSLPT DINEEFLAAL
PEEIRRELLA QEAQDRRRRE REENRRRNQT SAAAPQAEEM DTASFFASLD PHLRAAVLMD
TDEDTLRQLP PELSAEARAM GGDRRLHQFN DFGYRRGDRR GQPEDPSQKK KARPCVQMLD
KAGVATLLRL MFIPQQGSAK ASLSAILRYV CENRQNRAEV ISILLSILQD GSADVNAVER
SFAQLSIRAK QPQQPADKTP KISRKNGALS INADVSPLMV VQQCLNTLTQ LTEKNPAVWS
FFLTEHETGV GFKNRANRKG KAKESKASKY PVNALLTLLD RKLIVESSTI MEQLTTLLKV
ITAPLQVLKK EKEKAAEEAK NEAEVSARGQ NAGAVEEAPA QAGAQVQGTE MITAPQATGQ
TEIAAAEGEG STSKPDESKS EDDKAKKHRS LTPPEVPEAN LRLVAKILAA RECNSKVFQE
TLSVISNLSP IPGAKEIFGQ ELLGIAKDLA RSSLQDLASL TVQVSKASSP TDVQGIALAK
FSPASSDQTK LLRALTALDY LFDPSRDSKD KPEAAAEALE PAQKEDILLT LYEDSAFAPL
WEKLSECLTV IRQRGNMLNI ATTLLPLIES LMVVCKNTSL KELPLSKMLP KEFALSSPPP
ENKMENLFFN FTEEHRKILN DLVRQNPKLM SGTFSLLVKN SKVLEFDNKR NYFNRKLHSR
GGDRQAHPPL QLSVRRDQVF LDSFKSLYFK SADEMKYGKL SIRFHGEEGV DAGGVTREWF
QSISRQMFNA DYALFVPVAS DRTTFHPNRL SSINPEHLMF FKFIGRIIGK ALYEGRVLDC
HFSRAVYKQI MGKQVSLKDM ETLDLEYYKS LEWMIHNDIT DIITETFSVE VEAFGEMQTV
DLIENGRNIP VTEDNKHEYV RLITEHRLVG AVQEQLENFL KGFHDIVPAE LVSIFSEQEL
ELLISGLPDI NVDDWKNNTE YHNYTAASPQ IQWFWRAVRT FEKEEQAKLL QFVTGTSKVP
LNGFKELEGM NGFSKFNIHR DYGSKDRLPS SHTCFNQLDL PEYETYEDLR KALYTAMTAG
GEYFGFA
//
