ID R7SXJ3_DICSQ Unreviewed; 3738 AA.
AC R7SXJ3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 28-JUN-2023, entry version 56.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=DICSQDRAFT_181365 {ECO:0000313|EMBL:EJF60455.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF60455.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF60455.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF60455.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH719416; EJF60455.1; -; Genomic_DNA.
DR RefSeq; XP_007366873.1; XM_007366811.1.
DR GeneID; 18841001; -.
DR KEGG; dsq:DICSQDRAFT_181365; -.
DR HOGENOM; CLU_000215_0_0_1; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053319; 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 CDD; cd14297; UBA2_spUBP14_like; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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 InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
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; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1324..1364
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3403..3738
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 211..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2117..2297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2366..2390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2547..2567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2602..2648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2786..2823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3024..3101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2270..2297
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2626..2640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2805..2822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3036..3070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3705
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3738 AA; 408731 MW; 265E74859B44839A CRC64;
MRILHKSKRV VAPLPQVAEL IDRLINTPND DLHEVLSQID SWKWPRSDLN AWMKVLNKFD
AILEEAIRDY DIDNLQVNVF TPLTKKTVCE ILRFERLLLE NSTNRKTFNS YDRLNSLMFS
SDLDVLILAL NLLLRPAQQY SSQPAVSHAL SISTPRLTSL AKRWPNLRDY DLNLVDLVTN
KGRAQVEALP TEAREVNFVF YRQASSSSTA GKEEKKESIV EGDVSSSAAV QTPRKPTSSA
AATSANASTS SGAVTIHIDS KTIESKPAMD ILADAIEAYH VPDSEKFELL MRIRGAQAMT
HAWAADREKL VVVRLLATAI FGHTHSDSQA QSSLFLYEPD LITHIAELLQ LDRGVDIQVQ
TAAVAALDAM SRYRSKIQDV LTAVNAGVNH GILMALLRKT VADVAQSTST LPQAFVEALF
SFITFLATHA SGGSMIVGAG LIPVLIQAIE NRLPNRLYVV SKTMQLLDNV LYGYTNAFTL
FCNARGVDIL VDRIEYEVDL DIEECANDGA PNDAVAPYGK LSVARTAVLK HTLRSIHRMM
QSSGTAEGLR GLLDSSLLKS VKKIMQHRAI FGPSALALAI NIMAIFVHNE PTCLPVIQEA
GLPEVFYSVI EKGLEPVIEV IQSVPNALGA LCLNQAGQDQ LTARPNTIPS LFSIFTSEDH
QRVLQEKENA VLIGTSVEEL IRHHPTLKEK VFVAIKSTMA RIEELGTSYS VPDDIKHWYR
LQPQNPAPAP AGAESTGENV AMEVDHSTPA TEQATLPASL PPSGEQPSHR DDFWGRSHDN
LIISYIDVFG KFLEGFFQHV PHCRDFVADT DGLNGLAKLT TLPCLPYDFA NSVASDSFVQ
VVRTMAEAAT NETLAFLVRL VQESLAECKD FWGSLDEQPK LLGLVEFSAG AEEEKANTQF
RNLITLHTRV SLLSDIYATA GYSHGRATQT LLQSLLGKTP NPLQELGALH RACVWENIIL
KSILSAQGID ASPQHDLLAL FGSASTPTQG VLSSTLSATT TATANTSSTS AANGASASAS
TAAANGATPT NATNANGATP AEPSASTSTP SANAKKEEQP RDKNAKGVKH LVGQIPSALA
PFFQSIVRLF QTRRGSDLAQ KQKIKEAAGI IADVLVKHLE QKSFSDKLSL FSYYTSMLNA
ATILLVDEKP SQKSLHTMLL VAFVRVGGLD ALFGLCREFI NTIEMVSKVK VDERTEVTKQ
ELSHAFSGLK VALQLIQPTI SAKPLFDATQ TALALTVDKK DTDADYFEPH NFLVRMRAAA
LPVVRSIWEA EWLPSAPISV SKLVVHIVME LLNAENEEVK DVQTSASIIG GGPIGMPRIP
PMQSPDENRI RQLTDMGFPR SAAERALTRT RNNVNAATEL LLSHPYPFPP DPDPAPEPAP
AAAEGEAVAV PAGDQDQIQA DTPDAAPAEA GDAPAEAPAS EDNVESGDAA ETAQGDATEE
TMEETSSTAS DSEAPAAPAP EEVSAPPGKT SEEWVMELTT AREPLKEGIG RRVLSLVDEH
PSLVFDVQKV FIGPTSEYRT QAVKALIDDI QAFLPSAYDV QEQPLSVRCH LLALVLGEPS
SPAAQMPEKE AETLLNVLLS LLLSNPGEGG QPTLPKWLSA QLLVIESLLV LGDSPRSVTL
PKENEPINRE PIAQGPRYAE ARNTLFDFSM RLLGVPTLPK DELISVLRLI VLLTRDHNIA
EAFMERNGVA ALFQYLRISS GTQSGTGIQS YIALIVRHIV ENQITLQHVM RQEVKRYFSH
PRSRNVDIGS FVSGCSSTAL RDPEAFVKVA EEMCTLSQPF SPMKTVSLKP EVEPNATSQH
AIPGGNKSNE MQIDEAPVQQ ASGAPVESTE TLIHYLIGEL MKTVKTDMAP ENLSAATSVD
TGKLTSTHTP ASSENRTDAA QPSSTELRSP QDPVDYTYPC FIMQVLTELL FSYESCKIAF
LSYTPKKRNQ TPAKEGGLKH RTAAIQFLLS DLMTFGTINP QPPSEARKQI TLCNWAMSVI
VALCVDTVTN QDLKDVPTDL VSVRKFVLEA ISRALKDLPS SDSPELRYSR LLALSDLCHR
LLTVRFNVNG KKAGDEVPTH IAKVMLEKNF VATLTNVLSE VDLNYPNIRN VVSSVLRPLE
YLTKIAMKMS RISDKNKEVL EEKQAMSESD ISEEDEDEDD ETESPETEEA SQLYRNSSLG
LFGGEMEDVH YGDEDDMDEE DDEDEDGDVE MDFGDETGSE DTSATDEEDV EEDLEDETGE
SEEGWQEEDE EDEEGLVENE GQAAEEDADE DDEDEGEEVM WQDIAVGDGG ADEGADEGEE
EEDVGDMPMA PMDMDDEGDV ISEGEEFADE LGLVDEARLG HGPNLFDLAA GFANVLGGSL
AAGIHGAPDG EPVVWTGAVR STRRRGAGDD DLDIFGRSRN PPAPSAENVT HPLLLDPATA
AARASQARSS RRGHRGLLAG SGVDIDQALG EGATQFLQQM LTHGRAGGHE ALHINLPAGL
LANFPRNGRG GAISASIRLE RAPRPTDGRT EGRSLEPLLT IQRWSEEVKM LHGKFEQARL
SRLHNHVVLA LLPAAAEAYK KAKEAEEREQ ERIREEQVRA AEEAAKKEQE AIEAAERAKA
EEEARAVEAA AQAAVEAEAA AAAQESAAAA DTDVEMADDS PSAETPAAEN GPQTAESSNR
PEEAAAPAQE RVTVMIHGAP VDITDTGIDP TFLEALPDEM REEVLNQHVR DQRAAQLERP
ADSAISAEFL DALPPDIRAE IIQQEAAERA QRTRAEQATQ QGGPLDIDPA DFIASLDPQL
RQVVLMDSDD VFIQSLPSHM IAEANIHREP GRPPRPRQVP PRQGGAQGAP QQASQPTKAP
QSREAIQLLD KSALAALVRL LFYPHILKKN LLYKVLVNLC ENAKSRTDLF NLLLSILQDG
SGDLASIDKS FAQMSVRHSR PTAPQTPKAI GKQRVSTDYF GSLSLPQNDV VPELIVQRCL
EALTYIVSSN ELSSLFFLTE HELPIGLRRS SSKKGKGKEK QAPQTHYPIV LLLGLLDRPS
ILRTPSIVES VVGLLATVTR PLASLKDKDS KKSENAESST AGASTASPGE QPSSGAQPVD
NTQSVIVPDT ASSDPAPAPT PASAAVPATA QGESPQKPPA SVEEKVLLAN SPHIPHHVLR
LIVNVLTAGE CSGRTFMQSL ALIQHLSYIP DAREVIASEL RSRAQEFGQS LFAALDELAV
ALRDADVQPD VLATTIAAMF SSASSDQAKL LRVLKTIDYM YSPKTSGNST EADIEKVQSI
YETFRFSPLW KRLGDCLSII EEKPEMEHIA TVLLPLIESL MVVCKYVGPK TTSGATARAL
RASTSPRSPT SARESMEDLF VTFTDAHRKV LNLMVRNNPS LMSGSFSLLV HNPRVLDFDN
KRNYFNQQLH RRPHSREHHS TLQLNVRRQR VFEDSFQYLQ RKTGEQIKYG KLSVRFYDEE
GVDAGGVTRE WFQILARQMF DPNYALFQPC AADKLTYQPN RASWVNPEHL SFFKFVGRVI
GKAIYDGRLL DAYFARSLYR QLLGKQVDYK DVEWVDPEYY NSLCWILEND PSPLDLTFSV
EADEFGVTKL VELKEGGASI PVTQENRKEF VQLSANYRLY SSIKDQIESL LAGFYEIIPK
DLVSIFNEQE LELLISGTPD IDVDEWRSAT EYNGYTSSDP VIVWFWRALK SFNREERAKV
LSFATGTSRV PLGGFVELQG VQGTQRFSIH KAYGDTDRLP QAHTCFNQID LPQYSSYEML
RQQLLLAINE GGEGFGFA
//
