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Database: UniProt
Entry: A0A453K5Y4_AEGTS
LinkDB: A0A453K5Y4_AEGTS
Original site: A0A453K5Y4_AEGTS 
ID   A0A453K5Y4_AEGTS        Unreviewed;      3446 AA.
AC   A0A453K5Y4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET5Gv20304400.4, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET5Gv20304400.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR   EnsemblPlants; AET5Gv20304400.4; AET5Gv20304400.4; AET5Gv20304400.
DR   Gramene; AET5Gv20304400.4; AET5Gv20304400.4; AET5Gv20304400.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000015105; Chromosome 5D.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd14327; UBA_atUPL1_2_like; 1.
DR   Gene3D; 6.10.250.1630; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
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; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF398; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF06012; DUF908; 2.
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; 2.
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:UP000015105};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1314..1355
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          3312..3446
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          946..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1805..1825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2094..2226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2346..2612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2710..2740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2945..2988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3192..3222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1023..1040
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1807..1822
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2100..2150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2151..2184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2185..2199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2200..2226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2443..2471
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2473..2488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2498..2515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2526..2540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2549..2577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2594..2611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3196..3220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3446 AA;  381153 MW;  409BAAD5CE2D8CA7 CRC64;
     ADVLSSSVEN PEGEAQVRNP DRRWQRRRWQ RTGPASRCGC SRSCLAAAPC RRRSKSSPSR
     PAKVKAFIDR VINIPLHDIA IPLSGFHWEF NKGNFHHWKP LFMHFDTYFK TYISSRKDLL
     LSDDMSESEP LTKNTILQIL RVVQIVLENC QNKTTFAGLE HFKNLLASSD PEVVVAALET
     LASVVKINPS KLHMNGKLIS CGAINSHLLS LAQGWGSKEE GLGLYSCVVA NERNQLEGLC
     LFPADMENKY DGTQHRLGST LHFEYNLAPV QDSDQANDKS SNLCVIHMPD LHLRKEDDLS
     ILKQCIDKFN VPPEHRFALF TRIRYAHAFN SPRTCRLYSR ISLLSFIVLV QSSDAHDELT
     SFFTNEPEYI NELIRLVRSE DIVPGPIRAL AMLALGAQLA AYASSHERAR ILSGSSIISA
     GGNRMVLLSV LQKAISSLSS PNDTSSPLIV DALLQFFLLH VLSSSSSGTT VRGSGMVPPL
     LPLLQDKDPS HMHLVCLAVK TLQKLMEYSS PAVSLFKDLG GVELLSQRLH VEVQRVIGVA
     EITSVLASDT SKSEDDHLYS QKRLIKALLK ALGSATYSPA NPARSQSSND NSLPMSLSLI
     FQNVGKFGGD IYFSSVTVMS EIIHKDPTCF PALKELGLPD AFLSSVTAGV IPSCKALICV
     PNGLGAICLN NQGLESVRET SVLRFLVETF TSRKYLIPMN EGVVLLANAV EELLRHVQSL
     RSTGVDIIIE IINKLSCPRG DKITEAARAE EKTDMETDVE GRDLVSAMDS GTDGTNDEQF
     SHLSIFHVMV LVHRTMENSE TCRLFVEKGG LQTLLTLLLR PTITQSSGGM PIALHSTMVF
     KGFTQQHSTP LARAFCSSLK EHLKNALQEL DTVFRSCEVT KLEKGAIPSL FIVEFLLFLA
     ASKDNRWMNA LLSEFGDVSR DVLEDIGRVH REVLWQISLF DEKKIEPEAS SPSANEAQQV
     DAAVGDTDDN RYTSFRQYLD PLLRRRGSGW NIESQVSDLI NIYRDMGRAA TDSHRVGADR
     YPSTGLPSSS QDQPSSSSDA NAKSEEDKKR SEHSSCCDMM RSLSYHINHL FMELGKAMLL
     TSRRENSPIN LSPSVVSVAS NIASIVLEHL NFEGHTISPE REITVATKCR YLGKVVEFID
     GILLDRPESC NPIMVNSFYC RGVIQAILTT FEATSELLFA MNRPPSSPME TDSKTGKEEK
     DTDCSWIYGP LSSYGAAMDH LVTSSFILSS STRQLLEQPI FSGTVRFPQD AERFMKLLQS
     KVLKTVLPIW AHPQFPECNL ELISSVTSIM RHVYSGVEVK NNVSNIAARL AGPPPDENAI
     SLIIEMGFSR ARAEEALRQV GTNSVEIATD WLFSHPEEPP EDDELARALA MSLGNSDTPV
     QEEDDRTNDL ELEEVNVQLP PMDEVLSSCL RLLQAKETLA FPVRDMLVTI SSQNDGQNRV
     KVLTYLIDHL KQCLVASDPL KNTALSAFFH VLALILHGDT AAREVASKAG LVKVVLNLLC
     SWELEPREGQ TTKVPNWVTS CFLSVDRMLQ LEPKLPDVTE LDVLKKDNSP TQTSVVIDDS
     KKDSESSSSV GLLDLEDQEQ LLRICCKCIQ KQLPSGTMHA ILQLCATLTK VHVAAISFLE
     SGGLHALLSL PTSSLFSGFN SVVSTIIRHI LEDPHTLQQA MELEIRHSLV TAANRHANPR
     VTPRNFVQNL AFVVYRDPVI FMKAAQAVCQ IEMVGDRPYV VLLKDREKEK SKEKEKDKLV
     DKDKSSGVAT KITSGDMVMA SPVSAKGKQS DLSARNMKSH RKPPQTFVTV IEHLLDLVMS
     FVPPQRAEDQ SDGSSSMDMD IDSSSAKGKG KAVAVTHEES KQAIQDATAC LAKNAFVLKL
     LTDVLLTYAS SVQVVLRHDA ELSSTRGPTR TSGGIFNHIL QHLLPHATKQ KKERKPDGDW
     RYKLATRGNQ FLVASSIRSS EGRKRICSEI CSIFVEFTDN TGCKPPMLRM DAYVDLLNDI
     LSARSPTGSS LSAESVVTFV EVGLVQCLTK TLQVLDLDHP DSAKIVTGIV KALEVVTKEH
     VHLADFNAKG ENSSKTVLEQ NNVDSSSNRF QVLDTTSQPT AMVTDHRETF NAVHASRSSD
     SVADEMDHDR DIDGGFARDG EDDFMHEIAE DRTGNESTMD IRFDIPRNRE DDMAEDEDDS
     DEDMSGDDGE EVDEDDDDEE NNNLEEDDAH QRSHADTDQD DREIDEEEFD EDLLEEEDDD
     DEDEEGVILR LEEGINGINV FDHIEVFGGS NNVSGDTLRV MPLDIFGTRR QGRSTSIYNL
     LGRASDQGVL DHPLLEEPSM LLPQQRQPEN LVEMAFSDRN HENSSSRLDA IFRSLRSGRN
     GHRFNMWLDD GPQRNGSAAP TVPEGIEELL LSQLRRPMAE HPDEQSTPAV DAQVNDPPSN
     FHGPETDARE GSAEQNENNE NVDIPAVRSE VDGSASAGPA PPHSDELRRD ASNASEHVAD
     MQYERSDTAV RDVEAVSQAS SGSGATLGES LRSLDVEIGS VEGHDDGDRH GASDRTPLGD
     VQAATRSRRP SGNAVPVSSR DISLESVREI PPNTVQESDQ NASEGDQEPN RATGTDSIDP
     TFLEALPEDL RAEVLSSRQN QVTQTSSEQP QHDADIDPEF LAALPPDIRE EVLAQQRAQR
     LQQQSQELEG QPVEMDAVSI IATFPSEIRE EVLLTSPDTL LATLTPALVA EANMLRERFA
     HRYHSGSLFG MNSRNRRGES SRRGDIIGSG LDRNTGDSSR QTASKLIETV GTPLVDKDAL
     NALIRLLRVV QPIYKGQLQR LLLNLCAHRE SRKSLVQILL DMLMLDLQGS SKKSIDATEP
     SFRLYGCHAN ITYSRPQSSD GVPPLVSRRV LETLTYLARN HPNVAKLLLF LQFPCPPTCH
     TETLDQRRGK AVLVEDGEQQ SAFALVLLLT LLNQPLYMRS VAHLEQLLNL LEVVMLNAEN
     EVNQAKLESS AERPSGPENA TQDALEDASV AGSSGVKPNA DDSGKSSANN ISDLQAVLHS
     LPQAELRLLC SLLAHDGLSD NAYLLVAEVL KKIVALAPFI CCHFINELSR SMQNLTVCAM
     NELHLYEDSE KAILSTSSAN GMAVLRVVQA LSSLVTSLQE RKDPELLAEK DHSDALSQIS
     DINTALDALW LELSNCISKI ESSSEYTSNL SPTSANATRV STGVAPPLPA GTQNILPYIE
     SFFVTCEKLR PGQPDAVQEP STSDMEDAST SSSGQKSSAS HTSLDEKHTA FVKFSEKHRR
     LLNAFIRQNS GLLEKSFSLM LKVPRLIDFD NKRAYFRSKI KHQHDHHHSP VRISVRRAYI
     LEDSYNQLRM RSPQDLKGRL TVHFQGEEGI DAGGLTREWY QLLSRVIFDK GALLFTTVGN
     DLTFQPNPNS VYQTEHLSYF KFVGRVVGKA LFDAQLLDVH FTRSFYKHIL GAKVTYHDIE
     AIDPAYYRNL KWMLENDISD VLDLTX
//
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