ID A0A2H3SP11_FUSOX Unreviewed; 810 AA.
AC A0A2H3SP11;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=BFJ68_g1658 {ECO:0000313|EMBL:RKL22411.1}, BFJ69_g5774
GN {ECO:0000313|EMBL:RKK78032.1}, FOXYS1_1488
GN {ECO:0000313|EMBL:KAF5267636.1}, FRV6_02093
GN {ECO:0000313|EMBL:SCO77881.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO77881.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|EMBL:SCO77881.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|EMBL:SCO77881.1};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000285084, ECO:0000313|Proteomes:UP000285860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK78032.1,
RC ECO:0000313|Proteomes:UP000285084}, and Fo_A28
RC {ECO:0000313|EMBL:RKL22411.1, ECO:0000313|Proteomes:UP000285860};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
RN [4] {ECO:0000313|EMBL:KAF5267636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 39464 {ECO:0000313|EMBL:KAF5267636.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (FEB-2020) 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 ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
CC -!- SIMILARITY: Belongs to the RSP5/NEDD4 family.
CC {ECO:0000256|ARBA:ARBA00010334}.
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DR EMBL; JAAFOW010000225; KAF5267636.1; -; Genomic_DNA.
DR EMBL; MRCX01000041; RKK78032.1; -; Genomic_DNA.
DR EMBL; MRCY01000005; RKL22411.1; -; Genomic_DNA.
DR EMBL; FMJY01000001; SCO77881.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10012619; -.
DR VEuPathDB; FungiDB:FOC4_g10013612; -.
DR VEuPathDB; FungiDB:FOIG_07348; -.
DR VEuPathDB; FungiDB:FOMG_06554; -.
DR VEuPathDB; FungiDB:FOXG_05190; -.
DR VEuPathDB; FungiDB:FOZG_10945; -.
DR VEuPathDB; FungiDB:HZS61_003777; -.
DR OMA; DNYTIQI; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR Proteomes; UP000285084; Unassembled WGS sequence.
DR Proteomes; UP000285860; Unassembled WGS sequence.
DR Proteomes; UP000558688; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000558688};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..113
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 228..261
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 328..361
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 387..420
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 476..810
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 141..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 778
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 810 AA; 91457 MW; CB9A5B82F2E4B29E CRC64;
MTSRTDSNRP NLRVTIIAAD GLYKRDVFRF PDPFAVATIN GEQTKTTTVS KRTLNPYWNE
SFDFRTNEDG ILAVQVFDQK KFKKKDQGFL GVINIRVGDV IPELSPDADD QMLTRDLKKS
TDNLVVHGKL IINLSCNLSA PARGGQASTA RPSLGTGPSN ASNLSAPPPE NRPGSSLSGP
NGAGGSQVNL AHRPSSINSV GGASAPGPNA SGQTRQSNQL SPFEDAQGRL PAGWERREDN
LGRTYYVDHN TRTTSWNRPT ASGAQEQRND REAATQVERQ RHQNRTLPEE RTGSNSPTLH
AQQPQPSASP ATNGGAVMHT GATSPGTGEL PPGWEQRWTP EGRPYFVDHN TRTTTWVDPR
RQQYIRMYGG QNNANGQIQQ QPVSQLGPLP SGWEMRLTNT ARVYFVDHNT KTTTWDDPRL
PSSLDQNVPQ YKRDFRRKLI YFRSQPAMRI LSGQCHIKVR RSHIFEDSFA EITRQSATDL
KKRLMIKFDG EDGLDYGGLS REFFFLLSHE MFNPFYCLFE YSAHDNYTLQ INPHSGINPE
HLNYFKFIGR VVGLAIFHRR FLDAFFIGAL YKMMLGKAVA LADMEGVDAD FHRSLQWMLD
NDISGGILEQ TFSTEDERFG VMTTEDLIPD GRNIDVTNEN KKEYVDLMVK WRIEKRIAEQ
FQAFKEGFQE LIPQDLINVF DERELELLIG GIAEIDVDDW KKHTDYRGYT ESDEVVQNFW
ATVRSWDGEQ KSRLLQFTTG TSRIPVNGFK DLQGSDGPRR FTIEKAGEIT NLPKAHTCFN
RLDLPPYKSL EMLQQKLTIA VEETMGFGQE
//
