ID Q8IIH3_PLAF7 Unreviewed; 2147 AA.
AC Q8IIH3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PF3D7_1119400 {ECO:0000313|EMBL:CZT98856.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT98856.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|EMBL:CZT98856.1, ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
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; LN999945; CZT98856.1; -; Genomic_DNA.
DR RefSeq; XP_001347872.1; XM_001347836.1.
DR AlphaFoldDB; Q8IIH3; -.
DR IntAct; Q8IIH3; 1.
DR STRING; 36329.Q8IIH3; -.
DR PaxDb; 5833-PF11_0201; -.
DR EnsemblProtists; CZT98856; CZT98856; PF3D7_1119400.
DR GeneID; 810748; -.
DR KEGG; pfa:PF3D7_1119400; -.
DR VEuPathDB; PlasmoDB:PF3D7_1119400; -.
DR HOGENOM; CLU_238711_0_0_1; -.
DR InParanoid; Q8IIH3; -.
DR OMA; FNAHELK; -.
DR OrthoDB; 1386at2759; -.
DR PhylomeDB; Q8IIH3; -.
DR Reactome; R-PFA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000001450; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; 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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 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.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CZT98856.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450};
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 995..1013
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1039..1063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1593..2147
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 182..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2115
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2147 AA; 256822 MW; 8FFA5824A98B2014 CRC64;
MFDGESKNRR INLSGKKQVI VNKDFFIEKA KKEKENNLTL IKRKNAFKKI SDYIGFKKCL
ENRKKEINEV VSKRINDIIL LEKIVCPSIY RQALQLCVYE FSLQSSFLYS DLNCYNYYKS
MDFDGIYPPV KYLLNTLKFY NKIDENCVDK TNGVDKENEI VDEKVKDDEK IKDDDKIKDD
DKIKNDDKVK NDDKVKNDDK VKNDDKVKND DKVKNDDKIK NDDKIKNDDK VKNDDKIKND
DKVKNDDKVK NDDKVKNDDK IKNDDKVKND DKIKNDDKVK NDDKIKNDDN NKKNNIPVGN
NISEKHTLQF DENKNDNDNN MTEIESHFYY RHKKELDILI KHLDILLGNY YIYNYNIYSE
YYKDVKKIKN IIPTPINNNI LKHHLNDHNY TNGSFSNHNN KKHISSKGNI LNIESDINTN
LLHIYYLYNF IINNKFIDEL VKRKITNENK KLNVFLTSRC TRSSIEMTNN NKNNMSDVDN
SNRSSNVYTS VLNKKQNVKE LSACLKNISD YIILSIEGII TVIKKISIYY QNKVDVKCDN
IKLMIYLCDM IYIYFYILKI KGKDMKCNNI MDIKYKIKLL INFVKLNLEY IKEPYILFIS
FFKYNIYELF ENTINIKNEL KEWKILLIRI INNTYKDVDI MKELIYNNNY YYYYYNYNRS
YFKVPYYNMK YYLYNQKSYD EYNISGVNLF RNLLLFVHFN KNIMYDNVLN ILTDVYLFLP
LEYHPYIYNN TEDINPPQKN DNSVIKIKNE ENYFEKQNLS LDMGYYYNKE IIESLIYICK
KYRFDKLDTL LFFLLPFRNI NGKIYDTYRN YYDYMKNIEK GVYANYDKLY KSRININNNM
VTNNMDHMNN NVNNNRNINI STNFKNNNKK ASIHDNINNN NNNNNNNNNY MDNFENYQDK
KNKGIMFYSD MNDFPFLANN QVTHYNYEDN KYNNNNNNNN NNNYLYGGHN NNVHGNFFFS
LENIIGKRDK KNIGSNSYLF NDMINNDIIL RIKRILIINN IHIYLIKKIY LFWCYSCKSN
DNSFFKNVMF FPYYDNTHIS IYLSSFCFLL YYYLVVNMFN QLIDINKFKM IKRNEVHHND
IRYNMIPKYD MENDQQHNNS NNNNNNSNNN NNNNNNNNNN NNNNNNNNNN NNVVTNFLMN
KYFKRVCKLL ILSLWYILKN SINCIYNELT KKKNLNVKNQ QLHYMEDIDD EDIYNDEDEE
HENEIIKKEE NHMDVIHSKQ FTSTIYSSDY NICLLNFEKI NISIGDIMYD QNSYVVNKGH
VYLNVQEDNI CLIKRNIENE DKEQSVKCYN SMDEIKNIFD ELDKINMYNY DNYVDRHMFF
YNKNNTNMEH LKFAHNVKSF SNDESFQYST PFESSSFVND NNNNNNNNNN YSHTHINHSY
NERIMTSNHN NMSSHNRGEF FFDNLKNKNT NTKKKINDDS CYSNVINYYL YKNDNKGLSY
ILPILLKKLY KLNSYIHIFD DEFFVIKETF NLLKNRFHII GESNNINYNN NNNNNNNNNN
NSNDEETTLY LEKNDIYLNN NIKFVNVLAN YLLRYVPFTL PFDDRLLIFY HFRNKNKESI
RDDSTFNILE RKHMLIRRTN ILEDGFISLN ILDNLQIKQN VRISFIDKNG NEETGIDGGG
LFKEFIILLC REIFHENFIL FQNVENHTLF PKYYNENDNL ILYEFSGKII GKAIYERILI
ESVFNKVFLN NLIFDNMDIN DLYFIDQNVF NSLLYVQNDE NVEKLCLTFC IYEKKYPDGE
KFTKEQYDKI TNYFYELSKR NHYNMYSLHT HHNNIINNNN NNNNNNNNNL FFFNQMDNLE
NLFFSSDDNT YNFTNMNNFF HMINNLDSMI SNVNSRNYST FSHNNMNRNN FINIPNGINN
ININNIIMND DTSNYSSTDE RSAHIPPTDL EYSFSHRDFI PFHELGEQNE HMEEELPSIN
IRRKNMENND DKKNKRNNKH NIYNNKNNNI TNNNLCDDEQ NWECIDLIEN GRNIPVTDKN
KKLYIKLYIN YKYNQLIKKK TQRFSKGLSQ LIPIKWFKLF SAHELKTLIS GKDKCFDVDD
LKRNVVYGGG YNENSTTVLH LFEILKDFSS NEKSLFLMFV TSCSRSPLLG FQELYPKFCI
YRVPDHTRLP TASTCVNLLK LPDYLSKEVL YKNLITAIND TQGFDLS
//