ID Q4UD38_THEAN Unreviewed; 468 AA.
AC Q4UD38;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAI75263.1};
GN ORFNames=TA02675 {ECO:0000313|EMBL:CAI75263.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI75263.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI75263.1, 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 archaeal Rpo12/eukaryotic RPC10 RNA
CC polymerase subunit family. {ECO:0000256|ARBA:ARBA00025770}.
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DR EMBL; CR940352; CAI75263.1; -; Genomic_DNA.
DR RefSeq; XP_954739.1; XM_949646.1.
DR AlphaFoldDB; Q4UD38; -.
DR STRING; 5874.Q4UD38; -.
DR GeneID; 3865136; -.
DR KEGG; tan:TA02675; -.
DR VEuPathDB; PiroplasmaDB:TA02675; -.
DR eggNOG; ENOG502RSUQ; Eukaryota.
DR InParanoid; Q4UD38; -.
DR OMA; VDCLYLV; -.
DR OrthoDB; 231247at2759; -.
DR Proteomes; UP000001950; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.20.58.2190; -; 1.
DR Gene3D; 2.20.28.30; RNA polymerase ii, chain L; 1.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR006591; RNAP_P/RPABC4.
DR InterPro; IPR039747; RPABC4.
DR InterPro; IPR029040; RPABC4/Spt4.
DR PANTHER; PTHR12056; DNA-DIRECTED RNA POLYMERASES I, II, AND III; 1.
DR PANTHER; PTHR12056:SF2; GEO11084P1; 1.
DR Pfam; PF03604; DNA_RNApol_7kD; 1.
DR SMART; SM00659; RPOLCX; 1.
DR SUPFAM; SSF143503; PUG domain-like; 1.
DR SUPFAM; SSF63393; RNA polymerase subunits; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 146..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 54729 MW; B0A9AA0BAD02434F CRC64;
MESGFNDTED LIEPITYICG ECGHDVALQP TSAVRCRNCG SRILYKKRSY RELKTLAEVL
YSTPESKLLD VYSKFEHFKT KLNSLLSSIA RYRIQLQASE DNAIFGPKTL KIVQSVVSDY
DKLYEIYQEN LFEVFSPLEH IWNEGLNGSK DESDNTEKDD VKSINQETKS QLNQIEEYKK
KLKDNIKEFE QVDFERIRNE ETELSGLLNK VLKIYREDPC DNLETILCDI CEAHPDEFLK
IVENVANLVK EISRRPDELS LRVLRLNNEK LREDFLSHHN SVKLLKFAGF KIATTSDIQQ
TLSNCLNTNI LLVNMKFDEE YFLYLHEPDM FTIYNKWRAW LDNLNYISDS LTNFNTAMSK
KNSKTAVKKR INIIKTEFMI NNKKKELRRE LKKLQNHVKS QFLKLTINSD TDNVKDGIPE
IDITKTKPKN RGTNFSRSFD SSRPLRARDK KIIQASLKRK RKLTMQLN
//
