ID Q4UIH2_THEAN Unreviewed; 336 AA.
AC Q4UIH2;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Replication factor C subunit (RPC2 homologue), putative {ECO:0000313|EMBL:CAI73117.1};
GN ORFNames=TA16350 {ECO:0000313|EMBL:CAI73117.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI73117.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI73117.1, 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 activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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DR EMBL; CR940347; CAI73117.1; -; Genomic_DNA.
DR RefSeq; XP_953795.1; XM_948702.1.
DR AlphaFoldDB; Q4UIH2; -.
DR STRING; 5874.Q4UIH2; -.
DR GeneID; 3863400; -.
DR KEGG; tan:TA16350; -.
DR VEuPathDB; PiroplasmaDB:TA16350; -.
DR eggNOG; KOG0989; Eukaryota.
DR InParanoid; Q4UIH2; -.
DR OMA; IGPIYSR; -.
DR OrthoDB; 275853at2759; -.
DR Proteomes; UP000001950; Chromosome 1 part 1.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF20; REPLICATION FACTOR C SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950}.
FT DOMAIN 39..175
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 336 AA; 37938 MW; D305DA3279027542 CRC64;
MGVTKDVPWV EKYRPKKISD VIFQTQAVSI MEQIIETFNM PHMIFHGPPG TGKTSAALAM
ARQIYGLEGM RERVLELNAS DERGIDVVRD RIKTYTRINI SNNRVNPETN RVMPNYKMII
LDEADMITAD AQAALRRVIE NYSSISRFIL ICNYLHKIIG PIYSRCSVFH FKPIETNSQI
DRLKYICNQE GITFDPKFLT TISSGDMRKS ITILQVILGS TACLYNEITE NAIYSVSGKP
PKRVVESIFE VCRRPEGDVE SVCKQIVHDG WDISSIFQQI CEYVVESDSI GDIEKSKISL
ELANRDFALL QGGSQYFQLA SACFHIKNTI TGGTPS
//
