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Database: UniProt
Entry: Q57XM0_TRYB2
LinkDB: Q57XM0_TRYB2
Original site: Q57XM0_TRYB2 
ID   Q57XM0_TRYB2            Unreviewed;       226 AA.
AC   Q57XM0; D6XKH1;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE            EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
GN   Name=Tb07.22O10.640 {ECO:0000313|EMBL:AAZ12318.1};
GN   ORFNames=Tb927.7.2540 {ECO:0000313|EMBL:AAX69649.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:AAX69649.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:AAZ12318.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ12318.1};
RX   PubMed=16020724; DOI=10.1126/science.1112181;
RA   El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA   Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA   Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA   Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA   Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA   Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA   Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA   Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA   Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT   "Comparative genomics of trypanosomatid parasitic protozoa.";
RL   Science 309:404-409(2005).
RN   [2] {ECO:0000313|EMBL:AAZ12318.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ12318.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [3] {ECO:0000313|EMBL:AAX69649.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX69649.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA   Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA   Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA   Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT   ".";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AAZ12318.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ12318.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA   Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA   Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA   Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT   "Sequencing, closure, and annotation of Trypanosoma brucei chromosomes 2
RT   through 8.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000256|RuleBase:RU362109}.
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DR   EMBL; AC159413; AAX69649.1; -; Genomic_DNA.
DR   EMBL; CP000070; AAZ12318.1; -; Genomic_DNA.
DR   RefSeq; XP_845877.1; XM_840784.1.
DR   AlphaFoldDB; Q57XM0; -.
DR   STRING; 185431.Q57XM0; -.
DR   PaxDb; 5691-AAZ12318; -.
DR   GeneID; 3658462; -.
DR   KEGG; tbr:Tb927.7.2540; -.
DR   VEuPathDB; TriTrypDB:Tb927.7.2540; -.
DR   eggNOG; KOG0419; Eukaryota.
DR   InParanoid; Q57XM0; -.
DR   OMA; SMCTRNS; -.
DR   OrthoDB; 130166at2759; -.
DR   Proteomes; UP000008524; Chromosome 7.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
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   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF254; UBIQUITIN-CONJUGATING ENZYME E2-17 KDA; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362109};
KW   Ligase {ECO:0000313|EMBL:AAX69649.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU362109}.
FT   DOMAIN          64..210
FT                   /note="UBC core"
FT                   /evidence="ECO:0000259|PROSITE:PS50127"
FT   REGION          207..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        148
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   226 AA;  25088 MW;  BE73093A1878D76C CRC64;
     MDNESTNEAA INISRQTARV AIDGEETAPH GIEVTAEAEA EAEAVVRSIP QPQATVENSH
     NFASAQRRLM NDLQVIHMNK CEQFWTRPLE GDLFQWKAVV LGPDGTAWEG GVFKLLLQFP
     PEYPFSPPSV RFTTKIFHPN VYGNGDICLD TLKDKWCPSL SVESVLLMII SLLSDPNPNS
     AANAEAASMY VQSRDKYEER VRRVVEESLE QSFSDADDDD ATEGAE
//
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