ID A0A0D1YDC8_9EURO Unreviewed; 4008 AA.
AC A0A0D1YDC8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PV11_08424 {ECO:0000313|EMBL:KIV80967.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV80967.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV80967.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV80967.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846953; KIV80967.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1YDC8; -.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053599; 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; cd22249; UDM1_RNF168_RNF169-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3673..4008
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 194..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1550..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1760..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2314..2526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2543..2590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2650..2688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2825..2927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2999..3030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3291..3386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2025..2043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2347..2375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2385..2399
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2424..2467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2475..2509
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2563..2589
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2825..2893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2999..3014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3291..3308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3309..3326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3338..3372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3975
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4008 AA; 445826 MW; 22C5EAA1328974AA CRC64;
MGKVTKKPQE KHKVSLSPAV SDLVQKVSTA HLADLPALFT AWSQRWPYPR GDLNNWIEPL
DRFDTILEKF NTKYGLDKGP QTIPFGTSLL LEGSPGTDEK RLKELGFGPE GDRELVEAIL
VFSKLLVEKC ANRAVYNSTD RLNDLLNTTS LSLLHTTLRI TFYLAQRYAE RTHTSHQLAV
KFYDFDHERL QKLAAPFGQP LSPTKRGTTS PVKTTKSKDK LPTPGKPRRG STAVNPNDFR
SLCKETTSHG DRGKSAALPD RDWQAWAHVK VTWSPQPPEQ KPATGEPPQS SDVPSTPTPV
RQHSSGLSRM DTNGTSSSSP SRLDTTQHEA QPELKHVELS PSDIANNSIE SILRDQPEDM
PPKVRYELLH QLRVAHGLMT SSKTRKELLA IRLLSIASLA NVFNESELSQ KLFPVDQGGP
KPHDLISQLV SLIHDSKKGQ PPVSLYLQTI AMETMSVLAR FKMFAADING ALGGGSSQGL
LSQLILKGLS DIGKDNDSTD TPVGDDWREA VFSMPRTLIQ ASGHHGRSSE ATMASSFITT
YLAGFNVTTG KALRVHLRML DFIKTFFHHF KDGLTTLLAS NAFESISGLL AKLVNSAWTM
LQDGEGIPAQ YKTRATDYDI PYMHQQIIRS IIDMINDIST HQGTQADRVL RSFVDSPNLL
RSFRLITDHL AAFGAHTWSE VVKAICGFLH NEPTSYTVIS EAGLIQSLLE TVNAGQNSTA
GSQQPKSLSS EPEGRPQGIP PVIDAIVNIS QVFGAICLTT AGFDYFKASG ALEKFFEIFE
SPAHAKVLSD PNVLALLGST FDELIRHHPN LRTSVLSAVI VMISRVRHIT RSLAVDYGAG
PKLWIGSEDA FSPCGGVGAL SLEIVPPPTI APESPVPART IDLPNGDKLI LKDSVLPPSK
PSGDPCDQDS HGLKANDYAR PAIGFLVTFF ENQTLCNSFL DHGGCDLVLD FVTMPSLPAD
SQPLSRNSGL IAELAAAVHM MAECKPHVVL PTLADRTRFA CAELKHFSQA QPKDWSCYFL
PLVRPGKEAG TSSDVAGSEQ AEVGLNGTKV AKALMAVLCL GHVLAEVFNA PMYSTRTTQN
LLFNQVNLAD IFADICKMMG TISAACFRED IAIQRVIPQG WAWETRARDF TSGDEEVDKI
WMSVRDDTAR LTDDITPSQP ENPPNESTKL ETDKQTPYFK NVQTLRFLFV ETPAAITEFF
CRLGRGITGR RRSDGFSRQK AALVANALAS AYLTQLQPYF LETETTTSAT SEDVESRFTY
FVIALDNVRR SFDDDSHPPA GPGPMMHPGR QSFVIEAFRK VGGVKSLTAI GTEFFDKLKS
CKVEHSMFSA NTGLKICLTI LDEFTNSKFM MDSAQSGVMK VTDPMKQIWF VPAQVLLSLR
TEALPLTRLV WESDYADQAS KDVVQKLVSI LKHVLTGDHE NEAVQSSSSY PALAPYSPRK
LFIDSQKVSI LKDKGYDEEL AREALYRASN QSSNSLTPAE EYCKAFSSNP WRRRLPIPYE
QSDLSATTRD TPSITSPPPN SIRHSVTAAL LGVPSAGSVE AALAEFANNA ADPDEMEDVV
QTPDPSSSVA PRSGGTVSSA MDLNNILNNE GESREDRPQS SQQEPTTTYS VETITEQRAE
IREDLADRCN NILNNHQNLT FELSDLIISA TKKLPDDLAK DYWRTTSDLL VSSLLSMQVE
EDINEAHGKR IAAAAHLVAL LIQDGDVFDE TLSIFKESFA GLLSYLRLPA SDGRSAEDSF
PWIAPVLLIV EKMLSRDSEP AEVKWNPPND LDSSGKAELT PNNVLDKEEK LELFDILVNM
LTRVGKDKTM AVAITRILVI LTRSRDIASR LAERRNLQRL FLMVKQLANG VGHRLQSSFM
IVLRHIVEDD ETIKQLMRSE IKAHFIARGS KQVDTTSYVR DLYHLVLRSP ELFAQVTNEM
VKLSSWQSSG GGSIGVVLRE TSDSKSTDEK MTEQAQTSTE QNEVSMEPAA SVEAPEESIE
DRNKGKALEI RPPVVENPDG VIHFILSELL NYKDVEDKEV SAETTPKADQ NPKTEQSPAP
ETSEDVLDQP PPPKPEKPKF KPEDHPIFSY RCFLMYTLTE LLHSYNRTKV ELINFSRKAD
PLTMTPSKPR AGILNYFLNG LIPSCHVEKE ESLQFKKKLL TSDWAIRVIV ALCSKTGESR
HTPAQRFSAQ AQVDDADNEP DLTFVRRFVL EHAIKSYKDA MSSNEALQMK YSRLLCLADM
FHRLISKPVV PEGSAGSQNT SYKVLARMMF EKNLIAVLTN SLADIDLGYP GSKRVIKFIL
RPLQELTTLA SQLSITDPDL ANSVAGNTAD DVISSASSVS DVDEEREETP DLFRNSALGM
LDPNRDSESD SEEDDDDEDE EMYDEEYDDE MEYDDGLVAG GPNDDEAVSD DEVDDGMGPE
GEIEGLPGDV PMDIEFVVND PHMEVDTDDD DEDDDEDDDE DDEEDDDGDD EIIVEEDDDD
DHPGEFNGDE ENDSLNGGQG DEGEWEDEEE GDEEDASEHQ DDIEEITFDG DDMPMPMTGG
GNLTQPGVLS SLLRVLNDHD IDGTAGMPHH VPPELIVPGA DHVEPDDEDE EDEEDEDGDE
MDENDEMDYG DFDHFLAGGG DGDFADHADP LLWNGLPNMR RARHFRGPGG HMASMIGRRL
THRDEFIPMG RSRLPQHGRS GLDDGTNPLL RRPQQEAPRP SRLDADGPPL DMEILREGGG
FPPFPATFQT IIRNGDTVEA GGHGAMLDAI LQALHRGERV GDGRIQFSMT APLAEIGDVL
RPPISVVSHR PHTREESSRA GNFIPALTMT RWQEEARILF GNTFVEKVQR VQYVIMSLLV
PLAQQEEKER KRKRDEEQKA EREEMERLRV ESERRKQEAE EREAVAKAEE DRLRAEAEAE
AATRGRDEVA TEHDDGDTEP MEDVQGTDTQ EQAESEGEAD DSQPRIFTTI RGRQLDITGL
DIDTEYLEAL PEELREEVIM AQYATRREQA RETGNDSTGI DPDFLNALPE DIREEIRQQE
AHAQRRRERE AARRQAATAG APAQAEEMDN DTFLATLDPA FRRVILAEQP PEILRHLDPR
HAAEGRAHAR RFFHYGNAGD RDARANDESA QRDNKRQIVQ MVDKSGVATI LRLMFLPQQG
SLRTNLWHIL RNICGNRQTR FEVINLLLVV LKEGSTDVSA VERSLASLSL RAKATIGQKT
PQPLKRTLSM QPSGGISEDV TPLVVVQQCL SALKQLCQNS VHTRTIFLRE VDVNPAAKKG
KGKAKEAKII KYPINDLIGL LDRKLIVESS SCLQSLAELL SAVTQPLSLL LRKDKEKPSE
EEKPNEGGEN AESSTSATQV PTEQQQSGEE RDIELRDAPT TTSQADQPLG SSVAGEQTEA
AEPATTSETE PVNGDEAKSK KAFEPPEISE HNLELVVSIF VAPECNSDTF HSALETVSSL
SNIPGTSVTF RIELIKHVKS LSQSICADLD ELIPQLREAQ SITDLHALSS SKFSHGGSDQ
VKLLRVLQAL DYLSASKSDT EETEDKTTSY DSLALRPLWD KLSECLTTVR EKDNITSFAT
ILLPLIESLM VVCKNATLKD SALARQVKEQ MQGSPAPEVM DDIQELFFNF TTEHRKILND
IIRQTPKLMQ GNGSFSLLVK NPKVLDFDNK RTYFTKQIHS RLHQQRHIQP PLQLNVRRDQ
IFLDSYKALY YKTADEMKYG KLNIRFNGEE GVDAGGVTRE WFQVLARGMF NPDWALWQPV
AADRTTFHPN PLSWINGEHL LYFKFIGRII GKAVHEGRVL DCHFSRAVYK RLLGKEPNLK
DLESMDLDYY KSLVWILEND ITDVISEDFS VIEEQFGEEK VVDLIPNGRN IPVTEENKKE
YVNAQVRYRL TTSVQEQLEN FTRGFHDIIP AELIAIFDEQ ELELLISGLP EIDVDDWKAH
SEYHNYSANS PQITWFWRIV RGMSNEERAK LLQFVTGTSK VPLNGFKDLE GMQGNTLFSI
HKDPSQTRLP TSHTCFNQLD LPAYDDYETL KSSLMTAINL GADYFGFA
//
