ID G2WWF7_VERDV Unreviewed; 1220 AA.
AC G2WWF7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=VDAG_01943 {ECO:0000313|EMBL:EGY19927.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY19927.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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DR EMBL; DS572697; EGY19927.1; -; Genomic_DNA.
DR RefSeq; XP_009656267.1; XM_009657972.1.
DR AlphaFoldDB; G2WWF7; -.
DR STRING; 498257.G2WWF7; -.
DR EnsemblFungi; EGY19927; EGY19927; VDAG_01943.
DR GeneID; 20703406; -.
DR KEGG; vda:VDAG_01943; -.
DR eggNOG; KOG0941; Eukaryota.
DR HOGENOM; CLU_002173_5_1_1; -.
DR InParanoid; G2WWF7; -.
DR OMA; AENSSWW; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000001611; Chromosome 7.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
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; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EGY19927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001611};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 873..1220
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1188
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1220 AA; 136317 MW; 793C9A7589DAFB27 CRC64;
MTSPWPPRRP PPPPPPRSPR RPAPQPSRRP SDDFVTRLHN TSLNAPPSEL ARLSRHDFAL
EDSQANADSS SSESDIHPSR PRRRPAHSRS MSVPFPSLFS SKKKQRPGPV HDDDSDDSHN
DPPVTRSAAK THTRGNMSQG NRDFATGNCM TCNSLVRWPR DLKVFKCTVC VTVNDLSPEE
HAGHRSGGVP QWLRGAKPAT SSSSSPPDQP ARSVDKSGTK EISLEHTKSL VHSCLQEYLV
QVVRQGKAAE KLRGLSSGRP HSPVDQDDHS IGHWIATNPT TPNSVSQRTQ KEEPATYMFS
EQPTLRQSHH QQSPRSYSSS YPARPLVHSI FGEESIRPAA PLQPEIDGKR LFKPLEDYLV
SCFSSLQCVN SSFLPSRPHY TARPESDDSQ PVFPTQSTGN ATRPVFAPEP KGGNVRRQTA
VPRSDPRCAE SQSQLVDLDP KLLLLGNFAE NGMWWTGNQR ESQQHAQSKG RKTSEAAHSV
VSMRCPQIEW DQVASWYATL LNAAESWTAI YDSLYQEEAF EPLSAAALQD LEDVLLAAQE
RVQRVLLKVT EMLLKRPGRA LTDPEDMRFL LILLENPLLY AIPSYYRGSK QSGTGGSRGG
KNGSDSTHAR GGPISGQHSG VIKRILGLMS NASNSCHTHL IAWFARYPES RFSIIKDLTS
GFLTFRLIRQ NEKKYEAKVD VIDGLIPNMS TGRSAASLHA ALGTSSSSKK KPKEQPKKMV
YHDDWQIRAA ARVLALLFAA NNTLGVRRAD ATMLGNSSVV LREGVQVFGQ VLPTSDFYNS
MIDYADLIAD FEAWETKRSK FAFCQYPFLL SIWAKSQILE YDARRQMTTK ARDAFFDSIM
TRKNVTQHLT LDVRRDCLVE DSLAAVSEVI GSGGEDIKKR LRIEFRGEEG YDAGGLRKEW
FLLLVREVFN PEHGLFTYDE ESQLCYFNPN SFETSDQFFL VGVVIGLAIY NSTILDVALP
PFAYRKLLAA APISSIPSSA HPRPVMTYNL EDLAEWRPRL AAGLKQLLDY DGDVEETFGL
DFVVPVEKYG TVLQVPLCPG GEWKSVTNAN RREFVDCYVR YLLDHAVTRQ FEPFKRGFYT
VCGGNALSLF RPEEIELLVR GSDTALDIDS LRAAAEYDNW GTKNPDGTEP VIGWFWDTFK
SAKPSEQRKL LSFITGSDRI PAMGAALLPI KISCLGEDEE RYPIARTCFN MLSLRRYGSQ
ERLEHMLWTA VHESEGFGLK
//
