ID Q38EW4_TRYB2 Unreviewed; 387 AA.
AC Q38EW4;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000256|ARBA:ARBA00016279};
GN ORFNames=Tb09.160.4430 {ECO:0000313|EMBL:EAN76656.1};
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:EAN76656.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:EAN76656.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN76656.1};
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:EAN76656.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN76656.1};
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).
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000256|ARBA:ARBA00005339}.
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DR EMBL; CM000207; EAN76656.1; -; Genomic_DNA.
DR RefSeq; XP_826986.1; XM_821893.1.
DR AlphaFoldDB; Q38EW4; -.
DR SMR; Q38EW4; -.
DR STRING; 185431.Q38EW4; -.
DR PaxDb; 5691-EAN76656; -.
DR GeneID; 3660049; -.
DR KEGG; tbr:Tb09.160.4430; -.
DR VEuPathDB; TriTrypDB:Tb927.9.6040; -.
DR eggNOG; KOG2336; Eukaryota.
DR InParanoid; Q38EW4; -.
DR OMA; MNIVKDY; -.
DR OrthoDB; 315430at2759; -.
DR Proteomes; UP000008524; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; ISM:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; ISO:GeneDB.
DR GO; GO:0032182; F:ubiquitin-like protein binding; ISO:GeneDB.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IBA:GO_Central.
DR GO; GO:0071569; P:protein ufmylation; IBA:GO_Central.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF9; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 5; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 21..271
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 387 AA; 42022 MW; 4D24C8D5D70B5EBE CRC64;
MSQDRGKRQV LDATVRDDNP YSRLMALQRM GVVENYEAIR QKSVAIIGAG GVGSVVAEML
TRCGIAKILL FDYDKVELAN MNRLFYRPEQ QGMSKVAAAK QTLEGINPDT EIVPFDFSIT
AAEHWQDFAD ALTKNGGVKP STPVDLLLCC VDNFQARLTV NYACLLFNIP WMESGVAENA
VSGHIQLLLP GVTPCYECCP PLVVATGMPE AKREGVCAAS LPTTMGIVAG FLAQNALKYL
LNFGTVSEYI GYDAVRDYFP SVTIKANPDC RNATCVEKQR EYAERKARLG DAAHPLHNAA
KHRTEREAKE REAAKARAAA SAKEWGIVVE EHGKDDLSVN TKGDTGGVEY AYGAGGKAEG
NAPREDEFVA ADSGESLEAL MAKMRAM
//
