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Database: UniProt
Entry: A0A1M2VBC8_TRAPU
LinkDB: A0A1M2VBC8_TRAPU
Original site: A0A1M2VBC8_TRAPU 
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
//
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