(data stored in ACNUC9543 zone)

SWISSPROT: Q8IAW2_PLAF7

ID   Q8IAW2_PLAF7            Unreviewed;       163 AA.
AC   Q8IAW2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-DEC-2019, entry version 110.
DE   SubName: Full=Ubiquitin-conjugating enzyme E2, putative {ECO:0000313|EMBL:CAD51248.1};
DE            EC=2.3.2.23 {ECO:0000313|EMBL:CAD51248.1};
GN   ORFNames=PF3D7_0812600 {ECO:0000313|EMBL:CAD51248.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD51248.1, ECO:0000313|Proteomes:UP000001450};
RN   [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.D.,
RA   Eisen J.A., Rutherford K.M., 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.A.,
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.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA   Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA   Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109, ECO:0000256|SAAS:SAAS00805669}.
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DR   EMBL; AL844507; CAD51248.1; -; Genomic_DNA.
DR   RefSeq; XP_001349399.1; XM_001349363.1.
DR   SMR; Q8IAW2; -.
DR   IntAct; Q8IAW2; 1.
DR   EnsemblProtists; CAD51248; CAD51248; PF3D7_0812600.
DR   GeneDB; PF3D7_0812600.1:pep; -.
DR   GeneID; 2655284; -.
DR   KEGG; pfa:PF3D7_0812600; -.
DR   EuPathDB; PlasmoDB:PF3D7_0812600; -.
DR   HOGENOM; HOG000233454; -.
DR   InParanoid; Q8IAW2; -.
DR   KO; K10573; -.
DR   OMA; WEAIIFG; -.
DR   PhylomeDB; Q8IAW2; -.
DR   Reactome; R-PFA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-PFA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000001450; Chromosome 8.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:GeneDB.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:GeneDB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8IAW2.
DR   SWISS-2DPAGE; Q8IAW2.
KW   Acyltransferase {ECO:0000313|EMBL:CAD51248.1};
KW   ATP-binding {ECO:0000256|RuleBase:RU362109, ECO:0000256|SAAS:SAAS01166781};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362109,
KW   ECO:0000256|SAAS:SAAS01166768};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Transferase {ECO:0000256|SAAS:SAAS01018623, ECO:0000313|EMBL:CAD51248.1};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU362109,
KW   ECO:0000256|SAAS:SAAS00805691}.
FT   DOMAIN          7..139
FT                   /note="UBIQUITIN_CONJUGAT_2"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   163 AA;  18687 MW;  D1D2DBE377582EA9 CRC64;
     MSNLAKKRLI RDFRKLQTDS PFGVSGSPIG NDIMKWRAVI FGPADTPWEG GTFHLELLFG
     NEYPNRPPKV KFLTKMFHPN IYMDGNICID ILQKHWSPIY DISAILTSIQ SLLSDPNPNS
     PANQEAALLF VENRIEYNRR IKNCVKESFN FIEQKAEEDA EKS
//

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