ID A0A1L9TSK2_9EURO Unreviewed; 1161 AA.
AC A0A1L9TSK2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN ORFNames=ASPSYDRAFT_55287 {ECO:0000313|EMBL:OJJ62419.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ62419.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR EMBL; KV878583; OJJ62419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9TSK2; -.
DR STRING; 1036612.A0A1L9TSK2; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_55287; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000184356; Unassembled WGS sequence.
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 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:UP000184356};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 815..1161
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1129
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1161 AA; 130464 MW; 2AA3709C3EF698AD CRC64;
MPSRAAHNPS VHQSTSLAGV QPTASPIRVP VVGGRSPNRA RHVEASTNPR LTGAPYSSPP
SSPPYRGRHS RSISQPFASA FGATGKRRNK SIVAVDTDDD DDDDDDIYLP NPNPLSTSPR
KGLPRVPPKD DLTTGKCMAC NNTVRWPRNL KVFRCTECLT VNDLEPYQET RDPVNPGTKP
AIPRKAIPLT TERTAAIIDR CIFTHLQQCL GAPPVPPKDT LRKGLPQASP RSPEHLPLPQ
HQRPSRGRSA SSSDTREKAD GGDRAFESSS YPFRNPFAPV PPPKDAPDPR NAPRHVVPRE
HGRPHDSGRK EKHPYIFREL EDYIISGFRG CDILNASFSS AHHAPRPAPE NTRPEPEPGQ
SPRQPYVDPV VELDAKTLLV GDLAENSSWW MADEESGRGP SHAQSKPRAT KTVNSRSPRI
NWTDVDQWYQ LILRAGTSWV EKWSAMRPPL NEEDPAKAAA WDMADLSVIE KEMTESRAHL
HRTLLKATEG LLKRPRRPLK KPDDIRFLLI LLSNPLIYPP TSELASLTVQ HGERRPSRPG
ESNTGPPMGN RPHVTRNPSG GSSHHPGIIK RIVGLLSDLP VDCHHYLVSW FSRFPVRQFE
KLVELVGRFV TYRLTRQHVR RRSESANDES YLIPSFSSAA MNTPAELHAA INGINQNKPT
KKKKEEPMTY GDDWQVRAAG RVMALLFTAN NADVARRPTG ALGRESSHRG HMIPISSFYN
TRLDYSNLVV PDFEAWESKT SKFSFCQYPF FLSIGAKIQI LEHDARRQME VKAREAFFNS
ILNRKAVSQY FVLKVRRDCL VEDSLQRVGE VLGSTPEEMK KGLRIGFIGE EGVDAGGLRK
EWFLLLVREV FDPHHGLFIY DEDSQYCYFN PYCFESSEQF FLVGVVLGLA IYNSIILDIA
LPPFAFKKLL AAAPQTSAPQ PLTTRPTYKC SLDDLAEYRP VLARGLRRLL EFEGDVAETF
CHNFVADVDR YGEVKSIPLC PGGEKKPVTN ANRREFVDLY VHYHLDTAVT RQFEPFRRGF
FSVCGGNALS LFRPEEIELL VRGSDEPLDV KSLRAVATYL NWQTPKPESV PVVQWFWEYF
ERTKPDAQRK LLSFITSTDR IPAVGATSLN IQLACLGDDS SRFPIAHTCF NRLGLYRYAT
REKLERLLSE AVLNSEGFGL K
//