ID E3QHF5_COLGM Unreviewed; 1308 AA.
AC E3QHF5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=HECT-domain-containing protein {ECO:0000313|EMBL:EFQ30317.1};
GN ORFNames=GLRG_05461 {ECO:0000313|EMBL:EFQ30317.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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DR EMBL; GG697348; EFQ30317.1; -; Genomic_DNA.
DR RefSeq; XP_008094337.1; XM_008096146.1.
DR STRING; 645133.E3QHF5; -.
DR EnsemblFungi; EFQ30317; EFQ30317; GLRG_05461.
DR GeneID; 24410826; -.
DR VEuPathDB; FungiDB:GLRG_05461; -.
DR eggNOG; KOG0941; Eukaryota.
DR HOGENOM; CLU_001858_0_0_1; -.
DR OrthoDB; 1820836at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
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 Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF16558; AZUL; 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 Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 953..1308
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 156..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1276
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1308 AA; 146317 MW; E74618741A95E1CD CRC64;
MTRDIRCPEE GPQHETSLDA DLLAALWEDA PFARLPPDAP PELKDMVQTI ENPKRVYAIH
RASRRHNFQI LVEIYILQLR YGCDSKACTT PTCFSCRKRL AGKAPIRRYN TTSARTLAVY
LASQDNPETG LCPYLKPPKE TPAALNSLIL SPKSAAPAFN DPFPKRSATP KGPRRRKSVT
SARLNGEDGG SQKATPGAEE TGRRPPSLSK ERSHFDSTTG AAKVAFKVAE RPISKDYRSF
AANVFGTVAF KMLEWLTPAG LDAMSEKVAA LEADATHSPS REETQRSQKP SGQSTPTQSM
PSVIYADKTS SDVAQLTTDH GPDTVLDQAS QKLHSSTSAL SNSRPSKPKR SSSARVRANS
KPTRKLSIEP YPTSSLSEDV TSGLASPRTS HEKPLRPSKP SHVNPYAIPE IPSTPSFFDS
VPPQNHSVTI VQEPESPLTT SFRNARPPAE SSNPREVAMQ TRTHHAQSSH SIDDTKHSEQ
SEEPVDVPIA DNMLPQSLTY LNVEVVDLLC DILQDDGTSE SHLFDPPKIT STYSGLKGRA
PKMQRKRNPR STYPKRLRRQ WKLFIEQSLF NILSDPAALV SSFVKDDELL DSHTIWYCML
RLTRVAPSLV FHSLWMAAGS LFGAPKSLQS LRSPTTKVFR RTEWSLANLE AGHLLSICLH
ALVAAAPLIT DSRILFDMSR VRSNGLTLAG SGALARQPAW LCLLYDDAFS NELALRLARR
LFAAISARKC FADMATQDDG VEDEGSDALL PLLSQLDLLN SYSSSNPELV HLERAGHESR
VSTLLLDWAK TVMLQEWDGQ PEILCDGSFG GALSLIAAMY EKRQDLLLGD VQFRVDYFAE
RLDSINMPVA WLAHISSKQK KHLLDYPFIF DPSTLVSYFR SINFSKMSRS YEESSSLQTR
MKAIVAPGGL ITNPHHKLVL QDLLKTASSK YLILEISRKN VIRDAFDQLW RREDRELHRP
LKIHLGEDAG EEGFDSGGVQ QEFFRLAVAE CLNPDYGAFT VDDRTRMAWF VPGSIVPSWK
FEILGLLVSL AVYNGLTLPI TFPRALYRKL LGEPVDELHH IADGWPDLAM GLTTLLEWDE
RQGLVEDVFA RTYEFSVSMF GQPISREMND QTRSWPQFEV AAGKSLADEN PKDAPLVTNE
NRNAYVSDYI KYLTDVSVRP QYEAFERGFR ACLHHKALQL LTPPLLQSLV EGVQEIDISE
LRRYTRYVGW DASHRGVRDF WSIVKRYDEK MKRRLLEFVT ASDRVPVGGM KNLQFVVQRN
GEEEGERGHL PTAYTCYGTL LLPEYKDKDV LRERLAMALE NAQGFGFA
//
