ID W9LFB1_FUSOX Unreviewed; 3991 AA.
AC W9LFB1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=FOZG_01711 {ECO:0000313|EMBL:EWZ51743.1};
OS Fusarium oxysporum Fo47.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660027 {ECO:0000313|EMBL:EWZ51743.1};
RN [1] {ECO:0000313|EMBL:EWZ51743.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo47 {ECO:0000313|EMBL:EWZ51743.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum Fo47.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EWZ51743.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fo47 {ECO:0000313|EMBL:EWZ51743.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum Fo47.";
RL Submitted (JUN-2012) 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; JH717896; EWZ51743.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOZG_01711; -.
DR HOGENOM; CLU_000215_0_1_1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030766; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3655..3991
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 222..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1581..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2028..2068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2308..2501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2514..2559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2628..2666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2805..2903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2969..2997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3037..3075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3146..3171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3291..3346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..2005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2028..2042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2354..2404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2419..2461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2470..2487
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2530..2557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2633..2649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2805..2848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2870..2885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2969..2985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3040..3065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3149..3167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3291..3316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3317..3336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3958
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3991 AA; 445446 MW; 318BF61D6B8ECC60 CRC64;
MGKITKPMQP KHKDTLSPWL KSYVETTSTT PLPLLPQKLE SFPSRWPFGR GDLYHWIPLL
NRFDSILEHF CATYKLNEGP QTRDFGCDVL LNQDQESTFG SERRWSTEEL AGLGFSSNGD
RQLVEVVLRY TRMLLEHCGN RSIYASSAHL NDLLNTTSLS VLIATLEVGS ELAQRYQASV
KRITNPSRQI SAALLANHYN IDLDRVQQLA LPFVKTPIVS LSDPVTTHTP GSTKGKERAQ
GGSPKSANSI HANDLVALAA SDDKRWHGWG DVKVAYYPQN TQQDSAGTEA ERASLPSTPT
PLRRSSTMTS QHHTPKGRGN FDDSSPIAPR TPGVSDETTS AGPKFYEIPQ SVIASTSVYQ
LVSRTPADLP PASKYEVFHR IRASKALMDS GESRQKLLAV RLLAINNLAY IHNEANFLEK
VLRQDADETR RFQLVYQLAE LIHPTAHGNV DVPLWLQAVA LALLEAVSNF QAKCQDVLSA
LNANVNHGIL LYVIRKAVAG MKEDDDSDKG NQVTQMDEWR NNLFSLTLHL SMTTRVGSEM
VSAGLMDILV EILNIRSSVA QRNHSMVLAF LDGLIWSYQN AFTAFFNAKG LDAVSQLVVD
TVKEAQALHK AGQGITKDQQ SGQVDYEIPY YQQQTLKWLL KFVHHIMSNS YSYGGNTDRL
LRNLADKTDL LGSLRDIIGD KKSFGSVVWT NSVTILSDFI NNDPTSFAAI SESGMIKTYL
EAVTARPLPG DVLAEPKPSD KDEDDDESNS ANETVTAIVA NDSRPHPPTE DSIRELSRET
LAAGILPSSD VITVVPQVLN SISLNNAGMK LVAASRALDS FLEIFESAAH VRCMELDGDL
ATNVGGSFDE LARHHPALRL AISNAVIDMV ARVRYLGIEK ARTAGWGARM LLIDDEGKTV
SVDENGNFIR PIASPEQSQG PETSGDTDVN MSDVPSNDTD SEGQKDDSPD SPTRSITPYI
YALGYFLSSY ISNQGLRTSF VEAGGLELLL DICESPSLPT NFGDTVASRI LNQVVSQVVE
SFPIRGLPSL IRRAQVAIDT LKPLSDKTEA LPPYFAPFLA SDLKTTHDEA VKNGTKMIKA
LSNAQTFIKI ISDCFATSRS NALQFYPVNV YDYYLKLVNS IGPLLRGVLT EEAGELNVVP
QHWSFRRQTS VEGLTSAHLP ETDVDDSTSL PDMLSSTAQF QAKDALDDSK PSRPTDEEQA
SPRFQNYETL RHLLHPMIPT TFPLFQTLGK CLLPRRERDP RDLYHRPRHL EIARALANAV
LGQLRPSVAN PTPTSKDFHF WIIMLHTINE MLIDQPSPRP SDRSSAQIIM PVLLAFKEEG
GMDVLNSMLK IFARAVREGP DAATDETSRS KVAAFGLKKV LDLDLMLVNS KQLTDAQNAF
TLQPRSGDRS SNSTYICQQL VVEFRAAILP EIIELWDSSF VERVPHQTVT RLIDILKAIS
VADGEPSSST RDKPPFHLFR YTDVRFDWRS HRGTIEELLA KGYDADLVHE AVYRANGNPN
LADHYCSAHK AGLAGARNPI PSADSDTSVL QQTPQEPSGV GETEGVNTGG AVEADRMSLD
GPPEIDTPDL AERFIGETLG GIIDPSQDVD EIHEGPSLPA ETPGCAAEES KRNESSPLAT
KEEVDKFRAK LRGNMIDRCL DVVRAHPETA IEVSELIRTV VLKQQPSDTE DEIGQTLTLA
LSSLAQDEEE EKQRTGKCIA AYAHLLALLL QDERFFDNNV ENLREHINEY IGFLKVSPTS
STEGMPPWIP YVLLVVETLL RHDERPVAAQ WKAPKSLDEA VSDPVIQMRT PIVGDHERTQ
ILESLLEILP RIGKEETLAI AALRVLVILT RSRRLARLVG DKKNLQRLFL MAKQLSGSGS
ERFKQTKLTA HIMTVLRHIV EDEETIKQIM RAEIKIGLPN LQRTQRGHPD VNNYLRAMTP
IALRAPDLFV EISNEMLRFT RWTPPSSDNP RSQSLELKQE ASQSTSDTGV DDTDNLVDDI
KQSTEPADKE MIDAPKSHES KRPVVENPDG VIHFLLCELL NYREVEDKEV QTTEKDSKID
PASGSEDAAS ASKDNNAADV KDKKPPKPVF KTDEHPIFVY RCFLLNCLAE LLQSYNRTKM
EFINFKRNAP LTTSTPIKPR SSVLNYLIYD LLCQGNLSGT ADTIAAKKKA ATSAQTQKVL
VALVAKTSEK AIDRGKDKFA YDEEPDLLFA RKFVLDTMLK AYERAPLSDE PLETRYSRMQ
CLAELMNYMV GERDKDPGAA SRGSDNVQAR SHAQLRRLMY EKGYLDKLTS SIAEINLNYP
GVKRAIKYIL RVLRVLTETA KELSHSNILP SDSLSDTADD DLGSTSSLSD LGDDREETPD
LYRNSTLGML EPRGEDDDSD EDEEEDDDED MYGDEYDDEM DYGDDDISDE EDNISDDDEE
LGEMGEIEGL HGEPGVVEVI MDEDEEDESD DDDDDVESAD MEDVEDQVEI VDEDGNPLDD
DGNSEWESAS HDGEDDEDQE EDDLEFDADV HGEHMPMEPG DILNGMARAI IGDGDVYDPD
LMDGLEDHYL DDGHDEDEDE DDEDEMEDDE YLYDDDYPLD DQPQPMPALG WDGLGAEDED
RHRQMFMVDN PGRRRFIPSR TTDSRSPFPP GFIVGSHRDA VGGDFRSFFS RSHRPGAGQS
NTDDGTNPLL RRGDQNREPS QRPTINHTIG LRVPEAIFGS GGRHIEGTMG FLGELMEFLP
IMGRNGQPAF HLQITGPHGH RESRELGAVR ASRIEQRRDG SAQDPLQAVS FAIEGTMDRY
QEEARMVFGT SNVTETAKLQ NIIVAKLTPA AMELEKKLKA EEAEQQKREE EERKKREEEQ
RLAREAKEAK EKAEREKREA EAREAAERAA SEAAANQDVS AEGQGNGGAM EGVESTNQSQ
AERSEATDQT ADDGPRVMTT IRGEEVDVTE LGIDPDYIAA LPEEFREEVI AQAISTRRSE
AREETNGNPT EAFQEFLDAL PEELRHEIAQ QERQEQRRRA REETNRQATA STGQAVMPEM
DTASILLTFP PDLRQQVLMD QGEELMDRLT PEMAAQARAL SQHNGHSVIT GRSPQASTSR
QPGPPNPQEG AKAQRRTVVQ MLDKAGVATL LRLMFITQQG SIRNHLFNVF ADVCENKQTR
LEVISTLLQI LQDGSTDMGA VERSFGQLSL KARRPKDKEK DSEQKTPQTL KRSLTGLAAA
NTTQTNSETS PLLIVQQCLD LLVELSSKNP HIPWLFLTEH EAVGSTLKRS LSRKGKGKDS
KSHKYAINSL LSLLDRDLVM ESSVVMTHLA DLLNRVTLPL QNLERRRKEA EDELKAIDSR
PLGEMSKTED PVEQASKAEP TETSNVTQSN TDAKEDTVTD VNAKKQEKKD AVQKKLRQLQ
PPVVPAQNLT LAVRIFVARE CSSKTFQNTI STIKNLSAIP GAKATFGQEL VHQARLLSEN
IVADLDDLLP HIEKASSGTE IQGVALAKFS PGASEQNKLL RVLTALDHLF DNKKKGDEAE
SSKNKDERHD LVTSLYHNST FSAMWEKLSA CLSAIRQREN MLNVATILLP LIESLMVVCK
NTTTNDDPSQ QKEMVLSSPP PESRTASLFF SFTEDHRRIL NELVRSNPKL MSGTFALLVK
NPKVLEFDNK RNYFNRSVHS RSGSNQSRPS YPTLQLSVRR EQVFHDSFKS LYFKSGDEMK
FGKLNIRFHG EEGVDAGGVT REWFQVLSRQ MFDPNYVLFT PVSSDRTTFH PNKLSGINDE
HLMFFKFIGR IIGKALYEGR VLDCYFSRAV YKRILGKSVS VKDMESFDPD YYKSLCWMLD
NDITDIITET FSVENDEFGA TTVVDLIPNG REIAVTEENK HDYVRLVVEH KLLSSVKEQM
AHFLQGFHDI IPAELISIFN EQELELLISG LPDIDIDDWK SNTEYHNYTP SSQQIQWFWR
ALRSFDKEER AKLLQFVTGT SKVPLNGFKE LEGMNGVNRF NIHRDYGNKD RLPSSHTCFN
QLDLPEYESY DHLRSQIMKA ITAGSEYFGF A
//
