ID Q2UJP0_ASPOR Unreviewed; 1367 AA.
AC Q2UJP0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=AO090003001134 {ECO:0000313|EMBL:BAE58225.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE58225.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE58225.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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};
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DR EMBL; AP007155; BAE58225.1; -; Genomic_DNA.
DR STRING; 510516.Q2UJP0; -.
DR EnsemblFungi; BAE58225; BAE58225; AO090003001134.
DR VEuPathDB; FungiDB:AO090003001134; -.
DR HOGENOM; CLU_004270_1_0_1; -.
DR OMA; GSSHRIN; -.
DR OrthoDB; 164548at2759; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; 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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
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:UP000006564};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1053..1358
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 21..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1356
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1367 AA; 154097 MW; E4706CB5FE7BCB73 CRC64;
MPSSGRHGIV PIQPYRFHRT QVPARGNDDG TNPLLVRTDR GPEAGQSRGP GNEAFTDWVH
GMEPVSTGRL LPMDSPAIGG QGAPGFGVIT RPDGIHVHVD RRAILPNRNQ DIFGLGRPQA
PPSRTRDDPS QAVSFALATT RSRWQEEARI LFSSTYVEKT QRVVNSLLKI LVPPAIEEEK
EREKKMAEEL KRREEELAER ERQERIAKEE EEREQQRKEE EENARRQQER EQQEAEMQAS
GVTSEPMDDV QPTDAPAEAA TPPVQAETGP SEPQPRVHTT IRGRELDITG MEIDPEYLEA
LPEELREEVI MQQLAEQRSQ AAAAGEEPSE INPEFLEALP PEIREELLQQ EAADRRRRER
ESARRQGASG GAPPRAEDMD AASFLATLDP SLRQAVLADQ PEEILATLGP EFVTEARALP
GRRLTQFGDI ARVDHRQRNE PTDEQEPKKQ QRRQIVQMLD KAGVATLLRL MFMPLQGNAR
HQLNDILHNV CENRQNRVEV ISLLLSVLQD GSSDVSAIER SFAQLSLRAK SPSVQKTPQS
VKRNLAFQTS SSVSNEVTPI MVVQQCLGTL SFLSQYNPHI AWFFLTEHDP SSTLKLKAFR
KGKGKENKAN KFALNALLTL LDRKLIMESP NCMEQLSSLL SSITQPLTLL SRREKEKQEE
EDKGKKPEPA QDDRSTEEQQ QQQQQQQQQE QPSEAAEPTT SAADTTMTDA PLPSVENTEA
QSTTAQPEEG TSAEPSKSET GKGSAEDEKH KKKSIEPPVV PDHNLQLVVH ILAARECNGK
TFRETLSTIN NLSAIPKARD VIGNELVHQA QDLSTTILTD LDELLSHINQ ARTGTDMQGL
ALAKFSPASS DQAKLLRVLT ALDYLFDPSR SDKAKGGDSE QVAKEDVLQT LYESSTFGPL
WTRLSECLTL IRQKENMLNV ATILLPLIEA LMVVCKNTSL KETPLSRNAR ELSVSSTSVG
AGLNMESLFF KFTEEHRKIL NELVRQNPRL MSGTFSLLVK NPKVLEFDNK RNYFTRRIHS
RGAEPRHPHP PLQLSVRRDQ VFLDSFKSLY FKSADELKYG KLNVRFHGEE GVDAGGVTRE
WFQVLARGMF NPNYALFIPV AADRTTFHPN RLSGVNSEHL MFFKFIGRII GKALYEGRVL
DCHFSRAVYK CILGRSVSIK DMETLDLDYY KSLLWMLEND ITDIITETFA VETDDFGEKQ
VIDLVENGSN IPVTQENKEE YVQRVVDYRL VRSVKEQLDN FLKGFHEIIP ADLISIFNEQ
ELELLISGLP EIDVDDWKAN TEYHNYSASS PQIQWFWRAV RSFDKEERAK LLQFVTGTSK
VPLNGFKELE GMNGVSRFNI HRDYGNKDRL PSAHTCFNPG SEYFGFA
//
