ID Q4UDU6_THEAN Unreviewed; 219 AA.
AC Q4UDU6;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Sco1/2-like protein, putative {ECO:0000313|EMBL:CAI74743.1};
GN ORFNames=TA12095 {ECO:0000313|EMBL:CAI74743.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI74743.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI74743.1, 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., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CR940348; CAI74743.1; -; Genomic_DNA.
DR RefSeq; XP_952475.1; XM_947382.1.
DR AlphaFoldDB; Q4UDU6; -.
DR STRING; 5874.Q4UDU6; -.
DR GeneID; 3862043; -.
DR KEGG; tan:TA12095; -.
DR VEuPathDB; PiroplasmaDB:TA12095; -.
DR eggNOG; KOG2792; Eukaryota.
DR InParanoid; Q4UDU6; -.
DR OMA; PMIFFGF; -.
DR OrthoDB; 169656at2759; -.
DR Proteomes; UP000001950; Chromosome 2.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12151:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950}.
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 93..97
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 219 AA; 25250 MW; DF881257A5794984 CRC64;
MFLGEQEPSQ LVKTLESKLV GILGILNIDN IQRSIDKYRS LWGCRSRTIV TEERYGTPQL
GGSFKLIDQD GVTRSSEEFK GKYMLIYFGF CNCPDICPEE MDKQTQVVNT LDKQFGPIIQ
PVFISVDPKR DVPRVLKNYV KDYHPRLVAL TGTPEMIKDV TRKFRVYYNE GIKATEQDYL
IDHSIIHYLM DKDGNFLEFY GKNTNSQEMA KAISNVIKK
//
