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Database: UniProt
Entry: Q8IIH3_PLAF7
LinkDB: Q8IIH3_PLAF7
Original site: Q8IIH3_PLAF7 
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
//
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