ID Q4WK02_ASPFU Unreviewed; 1225 AA.
AC Q4WK02;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=AFUA_1G04210 {ECO:0000313|EMBL:EAL88130.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL88130.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL88130.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL88130.1}.
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DR EMBL; AAHF01000007; EAL88130.1; -; Genomic_DNA.
DR RefSeq; XP_750168.1; XM_745075.1.
DR AlphaFoldDB; Q4WK02; -.
DR STRING; 330879.Q4WK02; -.
DR EnsemblFungi; EAL88130; EAL88130; AFUA_1G04210.
DR GeneID; 3507451; -.
DR KEGG; afm:AFUA_1G04210; -.
DR VEuPathDB; FungiDB:Afu1g04210; -.
DR eggNOG; KOG0942; Eukaryota.
DR HOGENOM; CLU_002173_2_4_1; -.
DR InParanoid; Q4WK02; -.
DR OMA; HWLMTNR; -.
DR OrthoDB; 1386at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 InterPro; IPR000048; IQ_motif_EF-hand-BS.
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.
DR PROSITE; PS50096; IQ; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 849..1225
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1193
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1225 AA; 139599 MW; 0D644201E21662A9 CRC64;
MFQSFTGNSR RPRQVNLGGR NTNPFAAYPS GRHLPQGPSA QNTLAIAQQE RLLRQQERER
LGATRKIQRT WRGYRSRKLT HSTWRTEWDT AERQRTGSSL PFEHKTRTPD DFLEPSLRYA
TAAECLSQLR LLMQFVEPWN TSDIVRLVYY ANAFQITLHE VPTIATEGEW TTPLCRLAKT
TLRVLRSALS PIVPDFAVPH LVGLLVFLTN LIPKQMARLA EDYYSVMATI TRNIESLSQR
CHVSQENLAQ SVLALLRPIT SETLTAYEWF ARSYLTIPDL SAYLGTLDQL AGNINYKLLL
SALGPLQSRF RERPQSVTDL DARLWLLAYI IYFHQYANGT QAGQQAVEPD FVKIVSELLN
STAVHLSRRL EADDMIDDDV TEETPLHPFV KEQISSLVNQ SKITGLLSQL QSTRLSQGDL
ANSESDASKE AKILATYALT LLRVFPRRGD DIRMWLYLGS ATSGDQKAGH PGSRIPAIKY
FWHASRSSRI FDKISQDSTK VLPLLKPADE SRESGLSMTQ AERDEEWTII LLFLELYTFV
LKVMDDEEFF SSQSSFTASS NSRVSWTKES ALPLKDIKDM TVFLKNLAFT LYWNSADLNE
REAPQTAGGI QSYFTGAVSS SDAITSVKDL EMRNKEKGLP GVTGIPLDYF KGLVTGLLRM
IHERDSRRKF LPDGHWLMTN RFDMEGFIPA VVAEEENRHQ LQDEDEEESQ DDWMRDDEYE
PLNLIGTGRA QQTRRIEALR RRQQQAARRK QLEAVAPRLE ILRNMPFFIP FATRVQIFRE
FIYRDQMRRR QGYIDPDAWR MSVAQASMGR MIDGRPAAQD ILSRHHANIR RESVFEDAFD
QFYELGEGLK EPIQISFIDK FNTVEAGIDG GGVTKEFLTS VTNEAFKSGS EPKLFEENDQ
HLLYPNPAAV EQRREVLRQL GFVENSPEWN EQVRDLLRRY EFLGRIIGKC LYEGILVDVN
FAPFFLLKWA LTGGAGSAQR ETAYRANLND LKDLDQGLYQ GLLQLKNYTG DVEDFALNFT
VTDTIPLPNG GTRTVTQDLK SNGSDIPVTN QNRLVYISYI ARYRLQVQPA LQTNAFLQGL
GHIIQPSWLS MFNQSELQTL VSGESGDIDV ADLRRNTLYG GVYTIGDDKE EHPTVKLFWQ
VMEEMSNEER QKVLRFVTST PRAPLLGFSH LNPRFSIRDS SEDQDRLPST STCVNLLKLP
RYTNAKVLRE KLLYAINSGA GFDLS
//
