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Database: UniProt/TrEMBL
Entry: Q4UHS2_THEAN
LinkDB: Q4UHS2_THEAN
Original site: Q4UHS2_THEAN 
ID   Q4UHS2_THEAN            Unreviewed;       197 AA.
AC   Q4UHS2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   26-NOV-2014, entry version 56.
DE   SubName: Full=Ubiquitin conjugating enzyme, putative {ECO:0000313|EMBL:CAI73367.1};
GN   ORFNames=TA06755 {ECO:0000313|EMBL:CAI73367.1};
OS   Theileria annulata.
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874 {ECO:0000313|Proteomes:UP000001950};
RN   [1] {ECO:0000313|Proteomes:UP000001950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M.,
RA   Coulson R.M.R., Cronin A., de Villiers E.P., Fraser A., Fosker N.,
RA   Gardner M., Goble A., Griffiths-Jones S., Harris D.E., Katzer F.,
RA   Larke N., Lord A., Maser P., McKellar S., Mooney P., Morton F.,
RA   Nene V., O'Neil S., Price C., Quail M.A., Rabbinowitsch E.,
RA   Rawlings N.D., Rutter S., Saunders D., Seeger K., Shah T., Squares R.,
RA   Squares S., Tivey A., Walker A.R., Woodward J., Dobbelaere D.A.E.,
RA   Langsley G., Rajandream M.A., McKeever D., Shiels B., Tait A.,
RA   Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata
RT   compared with T. parva.";
RL   Science 309:131-133(2005).
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU004027}.
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DR   EMBL; CR940347; CAI73367.1; -; Genomic_DNA.
DR   RefSeq; XP_954044.1; XM_948951.1.
DR   ProteinModelPortal; Q4UHS2; -.
DR   SMR; Q4UHS2; 2-152.
DR   STRING; 5874.Q4UHS2; -.
DR   GeneID; 3864004; -.
DR   KEGG; tan:TA06755; -.
DR   EuPathDB; PiroplasmaDB:TA06755; -.
DR   eggNOG; COG5078; -.
DR   HOGENOM; HOG000233455; -.
DR   InParanoid; Q4UHS2; -.
DR   KO; K04649; -.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
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   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001950};
KW   Ligase {ECO:0000256|SAAS:SAAS00039334};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001950};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS00039337}.
SQ   SEQUENCE   197 AA;  22429 MW;  B46129E2DB2C11BC CRC64;
     MYMESREHLR LKRELKDIEN ENDSTVEAYV VDDNIFKWKG HILGPPGTPY EGGHFTLDIS
     IPEDYPYSPP AIKFETKIWH PNISSETGAI CLDILKSEWS PALTIRTALI SIQALLSAPE
     PDDPQDAQVA NMYKRNYQEF ENTAKLWTST FARSRDESRE GKISLLLEIG IDRESAVRAL
     EENGWDTTVA INRLMDG
//
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