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Database: UniProt
Entry: N1Q5A8_DOTSN
LinkDB: N1Q5A8_DOTSN
Original site: N1Q5A8_DOTSN 
ID   N1Q5A8_DOTSN            Unreviewed;       841 AA.
AC   N1Q5A8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=DOTSEDRAFT_41268 {ECO:0000313|EMBL:EME50119.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME50119.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME50119.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446535; EME50119.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1Q5A8; -.
DR   STRING; 675120.N1Q5A8; -.
DR   EnsemblFungi; EME50119; EME50119; DOTSEDRAFT_41268.
DR   eggNOG; KOG0939; Eukaryota.
DR   HOGENOM; CLU_001858_0_0_1; -.
DR   OMA; APWIMIN; -.
DR   OrthoDB; 1820836at2759; -.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; 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; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 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:UP000016933};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          459..841
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        808
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   841 AA;  94776 MW;  25A00B2EC8DE70D8 CRC64;
     MESTIGSTVV GSLADLVTRY NYQVLHGCGN DACTEVTCHT GNTNTSRRPV RRPKPRTARA
     TALCQALSPR PRAHLCKHLI DLDDGSNSGR DEGPRDPSSL IQLLCDTRSV RQLTARPSNV
     GLEPELEELH QRHASLSDLL RSAGSAPPLP ADDFVDNADL VDRLMQTSFT WLIDRLPSLT
     RAAPWIMINR DIISKGLAYP QRNENMPSDD SYNPWAAILD MLDHGPYLRL IGKTMAVIGR
     RSHLENVLHR QDPQRKLYPD PGRQSIALML ASALGKINHA GDVDGSELVT FAVVIWLKKA
     FARTWNTNPV FKSGGAIHGI LELLQHLEED MSRRRQTSSL PSDVYEMPLI NAQIDPLTMA
     TSYLDWTPTN SNQQHVMQYP IIFSMKQLSL HFRVLCHLLM RRSHSLADAA VMLRGRSGVH
     FEEAELFQQL RFSEEHYLLI SVSRDEILED TWTQLWQRRK AELRRPLRVR LGERSELEIG
     HDLGGVQIEY FNLVCREVFA AQAQMLTTNS HSGISYFRPG SLQPLYMFEM FGLIVALALY
     NGITLPVRLP EVFYTILSRL NKSDSSLHLV GEFQLQDLND TWADEVRSLQ SILNDEVEDL
     EYSFPLEANG LRFSVQYPVA RSEPARYELH ISDIMLIDGG RPDASHCNPT YLEWPGWRLS
     GPSGEAEVVT AENKTRYVQD YIYHLCYGSV APQLDAFLKG FHGCGLIPRK VLAIFQDHQL
     KSHLEGSDHL DIDELKAAAR YDGYEAKSKY IQMFWRVVSS WPEKKQKLLL KFVTAAERIP
     ITGASQLTFV IKKAATENLE SLPASSTCFG TLILPRYPTA EILQAKLSLA LMYGSEGFGT
     G
//
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