ID A0A1M2VBC8_TRAPU Unreviewed; 3717 AA.
AC A0A1M2VBC8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JUN-2023, entry version 24.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=TRAPUB_4364 {ECO:0000313|EMBL:OJT04892.1};
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT04892.1, ECO:0000313|Proteomes:UP000184267};
RN [1] {ECO:0000313|EMBL:OJT04892.1, ECO:0000313|Proteomes:UP000184267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC735 {ECO:0000313|EMBL:OJT04892.1,
RC ECO:0000313|Proteomes:UP000184267};
RA Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA Hilden K.;
RT "Genome sequence of the basidiomycete white-rot fungus Trametes
RT pubescens.";
RL Submitted (OCT-2016) 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:OJT04892.1}.
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DR EMBL; MNAD01001510; OJT04892.1; -; Genomic_DNA.
DR STRING; 154538.A0A1M2VBC8; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000184267; 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:UP000184267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1290..1330
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3382..3717
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 209..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1836..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2086..2266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2524..2626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2768..2797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3011..3053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3273..3292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2097..2125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2245..2262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2524..2565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3018..3053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3275..3292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3684
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3717 AA; 405713 MW; 545146334F991FE0 CRC64;
MRITHKSKRA VAPLPQVVEF INKLADTPNE DLPEVLSQID SWKWPRSDLN AWIKVLNKFD
EILEEAIRDY DIDNLQVNVF TPLTKKTICE ILRFERLLLE NSTNRKTFNS YDRLNNLMFS
SDLDVLILAL NLLLRPAQQY SSQPAVSHAL SISTPRLTSL AKRWPNLRDY DINLVDLVSE
KGKTQIEALP TEAREVNFVF YRQAPSGAAA AKEKEKEKEK PAEGDVFDSV AQTPSRKPAG
TVGGANTAST SSGAVTIHID STTIESKSAM DILADAIEAH NVPDSEKFEL LMRIRGAQVM
TNEHAADREK LVIVRLLATA IFGHTHSDSQ AQSSLFLYEP DLIAHIAELL QLDRGVDGQV
QTASVAALDA MSRYRSKIQD VLTAVNAGVN HGILMALLRK TVSDVAQPTS TLPQAFVEAL
FSFITFLATH SSGGNMIVGA GLVPVLIQAI ENRLPNRLYL VSKTMQLLDN VLYGYNNAFQ
LFCNAHGVDI LVDRIQYEVD LGIEEWANDG LPNDVVASYG KLSVARTAVL KHTMRSMHRM
MQSSGTSEGL RGLLDSSLLK SVKKVLQNRA IFGPSVLGLA INIMSIFVHN EPTCLPVIQE
TGLPEAFYGI VEKGLEPVIE IIQSVPNAIG ALCLNQAGQD QLAARPNIIP SIFYIFTSEE
HQRVLQEKEN AVLIGTSLEE LIRHHPSLKD KVFIAVKATM AKIEELGNLY TPPNDIKHLY
RLQPTAPAPV VTSTGETGAP MEVDATTAAS GAEAQAPAEP SLPPPTNDLY NRPNDNIIIS
YIDVFGKFLE GFFQHVPHCR DFVADPEGLD HLARLTALPC LPYDFANSVG SDSLVQVIRT
MAEAATTETL AFLLKLVQDS LEECKDFWET MEERPKLLSL VEFAAGEDEQ KANDRFRKLV
TLHIRTSLLS DIYATAGYSH GRASATLLQA LLGHKPSTLA DIGSLHRACI WENIVLKAAL
SARDASATPP PAPTPSVSAA QEPSASTAAG LPAAASSSAV VSANGAATAD LPAPVSFVKK
EEKPKDKNAA GLKHLVSQMP SALSPFFQSV VRLFQTRRSS DIAQKQKIKE AAGILADVLV
KHLGPQTLND KLSLFAYYTT MLSTATVLLV DERPSQRVLH TVLLAAFARV GGLDSLFSLC
GEFVTTVDAI TRLHADQRTE IMKQELTHAY GGLKVSLVLL QPLVSSRPLF DSTQTPMAIT
TDKKDTDAEY FEPHNFLVRM RLTALPLVRT IWESSWLTAA PISVSKTVVQ VVMEILNAEN
EEAKDVQSAA SLLGGGGGGN IPMPRMAAPN PDENRIQQLV DMGFPRSAAE RALVRTRNNV
AAATELLLVH PYPLPPDPVP AHLPPLPVAE PAPAVADGDV EPASVEGQDD APAEVPTDPL
AELVANAPAD AEAPGVAEAS TGSATPEGSS EATAQGSAEQ SSEAAEGTGE GSSAAAEQEP
AVPGKSTEEW LKELNVAREP FKAELGRRVL SLVDEHPSLV FDVQKVFVGP ASEYRTQAVK
ALIDDIHAFS PKAYDVQEQP LFVRCHLLAL VLGDTSSPAA QMTDKEAESL MNVLLSLLLT
NPGEGGHPVI PKWLPAQLLV IECLLVIGEA PRAITLPKED EPIVREPIAQ GTRHAEARNA
LFEFCMRLLA VPTLPKDELI STLRILVLLT RDSSVAESFV KRGGVAMLFQ YMKISSGTQS
GAGIQSYIAI IMRHIVENPT ILQHVMRQQL RQFFSHPRTR VVDVGTFVSG CNSAALRDPE
AFVKVTEDLC QMSNPYATSK TISLKPAATL AAPSQQAITG EKTDKADDKS NEMQVDETPA
QPAQYALSDS TETLIHYLIG ELTRTVKTDL YPEHAAVDTS KPADGPTATD THTESAQQST
EPKPPQDPVD YTYPCFIMQV VTELLFSYDA CKIAFLSYSP KKRNQTPAKE GSAKHRTAAI
QFLLSDLLTF GTINPQPPAD ARKQITLCNW AMSVIVALCV DTTVTQDIKD VPTELVSIRK
FVLEAISRAL KDLPTSENTE NRYSRLLALS DLCHRLLTVR FNSGKKAGDE APTHIAKVML
EKNFVSTLTN VLAEVDLNYP NIRNVVSSVL RPLEYLTKVA MKMSRVSDKV KELPEEEVES
SESDISEEED DEEEEDDDET ESPENDAATD LYRNSSLGLF GGEMEDVHYD DEDMDDDGED
DEDDDVEMDF GDETGSEDTS ATDDDVEGAL GDEGESEDGW HDEEEEEEEG LVENEGEPID
DDAEDEEEED EGDEVMWQDI AVGDGDGEDP GDEGDEEEDA GDMPIAPMGM VDEADVLSEG
DDEFADELGL VDEAHPGPNL FDLAAGVANA LATGPFNAGL GGGVEGHPVM WTGSVRSSRR
RVADDDLEIF GRPRNLPAAS AENVTHPLLL DPATSAARSS QARSSRRGQR TLLSGGLDAQ
IFDDTWGEGA TQLLQHILSH GHAIGNEALH INVPAGVLGS LNRNGRAGAI SASIRLERAP
RPGDARTEGR SLEPLLTTQR WGEEAKMLHG RFEQTRLSKL QNHVIIALLP AAIDAYKKAK
EAEEREQARQ REEETRAADA AAKKEQEERE AAEKAKQEEE AKAAAEAEAA ALQAAADAAS
SAATDPDVEM ADATEENPEA GAETPVEENG PDAAESSTRQ EEAAVPERIM VTIHGNPVDI
TDTGIDPTFL EALPDDMREE VLNQHVRDRR AAQVERPADS QISAEFLEAL PPDIRAEIIQ
QEAVERAQRV RAEQAMPQPA GAGVDIDPAT FIASLDPQLR QVVLMDSDDV FIQSLPSHMI
AEANIHREHG RPSRPRHVAP DQAARAAQPQ AAPPAKALPS RDAIQLLDKS ALAALLRLLF
YPHVLKKNLL YKVLVNLCEN AKSRTDLFNL LLSILQDGSG DLASIDKSFA QMSVRHSKST
APQTPKAIGK QRVPTDYFGS LSLPQNDVVP ELIVQRCLEA LTYVVSSNEL SSLFFLTEHE
LPFGLRRSAS KKGKGKEKPA PQTHFPIVLL LSLLDRPSIL RTPSIVESVV ALLATVTRPL
AGLKSKKDEA AESSKAAAPS ATVVQPAQGA SEQAVVPPSA SASGSAAPSN LPATSAATTA
TAAAATPAVP AADAPKQPTT VEEKVLLANP PHIPHHVLRL IVNVLTAGEC SGRTFAQSLS
LIQHLSFIPD AREVIASELR ARAQEFGQSL HSALAELSVA LRDADADPDA LSTIIASKFS
TASSDQAKLL RVLKTIDYMY SPKTPGNTSD ADIEKVQGIY ESFRFSSLWQ RLGDCLSIIE
EKPEMEHIAT VLLPLIESLM VVCKYVGPKT PSGATTRALR GSASPRSPTT ARESMEDLFV
SFTDAHRKVL NLMVRNNPSL MSGSFSLLVH NPRVLDFDNK RNYFNQQLHR RPHNREHHGT
LQLNVRRQRV FEDSFQYLQR KTGDQIKYGK LSVRFYDEEG VDAGGVTREW FQILARQMFD
PNYALFQPCA VDKLTYQPNR ASWVNPEHLS FFKFVGRVIG KAIYDGRLLD AYFARSIYKQ
LLGKPVDYKD VEWVDPEYYN SLVWILENDP SPLDLTFSVE ADEFGVTKLV ELKEGGATIP
VTQENKKEFV QLSANYRLYS SIKEQIEALL TGFYEIIPKD LGSIFNEREL ELLISGTPDI
DVDEWRSATE YNGYTGSDPV IVWWWRALKS FTREERAKVL SFATGTSRVP LGGFVDLQGV
QGTQRFSIHK AYGDTDRLPQ AHTCFNQIDL PQYSSYEMLR QQVLLAINEG GEGFGFA
//