ID F1A2E9_DICPU Unreviewed; 1220 AA.
AC F1A2E9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=DICPUDRAFT_99774 {ECO:0000313|EMBL:EGC29639.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29639.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL871408; EGC29639.1; -; Genomic_DNA.
DR RefSeq; XP_003293843.1; XM_003293795.1.
DR AlphaFoldDB; F1A2E9; -.
DR STRING; 5786.F1A2E9; -.
DR EnsemblProtists; EGC29639; EGC29639; DICPUDRAFT_99774.
DR GeneID; 10505158; -.
DR KEGG; dpp:DICPUDRAFT_99774; -.
DR eggNOG; KOG0940; Eukaryota.
DR InParanoid; F1A2E9; -.
DR OMA; GGISKEW; -.
DR OrthoDB; 7954at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; 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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF426; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 120..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 237..334
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DOMAIN 856..1220
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 566..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1190
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1220 AA; 139712 MW; E341037D56D169E3 CRC64;
MFNSTYRFYN LFKISNLMGE KGTSISCNNN NNIYHNIENN NNINFLWSFE NIFISNKIKN
YSDIVSISTY SNHNNSSSLN PNNPNINNYN NNNQIKNNND IIKNNSSINL YNITLINQNI
IFFLFIFLIL ITIIKLLKNM FNLNVFGLNN NNKNNIYHNN NNNISNSINS NNQMNLIINN
LNSSSLLSQS ININNNTPIL PSLNNYNGNE GYLISRVKDN IKNLSNDKIG CGLNSIVSGN
GISGEIGDVG DDFSFQVTSF HKNGLRKKQG GDVISVFIQG CDYNNMDEQV KVRIVDRLNG
CHLVYYNVSK SGSYLISVFV NQVPVVNSPF KVSILPIPYS VHIKNESFNF INKYLSNSNS
DNINSKDELN INNKSNIDNN SNNYNNSGVL EVGKQIVCEV SPTRVASHLI NDKVDFQIFI
KENGILKRTN INIQSEIITS NNSYQSHTSN GSSLQDFEST ILCKFKLLKS GDYILEGSIA
GIQVFSKNLT VSPGPVSNKF THLFWDGKEL ISENKLFILK ENDPENELPE FKFLIESKDS
YGNKTTPNLN DFKYYLKKSL SPLILKNNNS NNANNNIKKP NNNSEESSNI PEESSSNSPQ
TIRRFNKKNI DSIKLKHKQI KSQQLQKQLE QTQQPPNDPQ HQNYNINNDK DLIEIFPQTS
ISNDGKIVVK FNDLNEVGWY YFCVKVNDEP ITNCPFVLAT IKEKDFQALS NYYINFKASF
NCQLERNGKP INVSLVLTQN KIEIFENYYF MNIKLYEFII NPTVQILLSN NENELIIQDN
KSVVYLKSSI IDQVFLILLT SYYFFGYQCE PNFDSKVKWL KNTLSKIQKK MITLKINIST
RKQILKESIQ ILGQIDPSDL NMSRLFVKFH DEEGIDIGGI SKEWFSNFSE ELARTPINGY
YLFSEYEGTR KFHPSPFSNL IPDYKSIFRV LGRITGKSII DSVTKADRHF SLRFTPVFYK
LILGEKLSID DLELIDPDLY NNKVKLILNT PMDQVNEILG EPLTFIREIY NQNEFNNISN
KFKNNNNNNI HTIQLMKTIN LKPFGNLISV NDENKVEYLE LWVNSLLYSS IKSQVDEFRE
GLFQMIPQSI LSVLNWKELE MLICGREQIN LDDLKEHSSF TGFYTQSFIN DFWSIVNEFN
EEEKKSLIKF VTGSSSVPLG GFYQLCPHFT INLTPPIDNG TNRLPISHTC FNRLDIPLNC
LSSKNLKLAI NEGGDGFSLV
//
