ID U6KL34_EIMTE Unreviewed; 1045 AA.
AC U6KL34;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=DNA excision repair protein, putative {ECO:0000313|EMBL:CDJ38822.1};
DE Flags: Fragment;
GN ORFNames=ETH_00029815 {ECO:0000313|EMBL:CDJ38822.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ38822.1};
RN [1] {ECO:0000313|EMBL:CDJ38822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ38822.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ38822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ38822.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG674071; CDJ38822.1; -; Genomic_DNA.
DR RefSeq; XP_013229578.1; XM_013374124.1.
DR AlphaFoldDB; U6KL34; -.
DR EnsemblProtists; CDJ38822; CDJ38822; ETH_00029815.
DR GeneID; 25255042; -.
DR VEuPathDB; ToxoDB:ETH2_0934300; -.
DR VEuPathDB; ToxoDB:ETH_00029815; -.
DR OrthoDB; 218108at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd22254; CSB_WHD; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 244..439
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 652..863
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDJ38822.1"
SQ SEQUENCE 1045 AA; 115735 MW; 81D610B69CD9F70F CRC64;
SILEEVEKSL SSKSATEKLP QQQQQQQQQQ QQQQQPGQIE AGADAAAAAA ATAATTATAA
TAAAAPSASS SRAQPPETAA AATAAAAAAA ELPELDLLSS EETSGSDSSW EAPEGKRKPA
AAAAAAGGAA AAAGAEAEEA ADAEAADTDP KSEEDEEDSS AEESDFAVAA AAASQQQQQQ
QQVDYSELDD SCSQQYSRRL QQQQQQLQQQ QEEEPVLLCG CFKVPAAVYR QLLPHQQQGL
EWLLLLLQQQ TGGLLGDDMG LGKTIQIAAF VAALHNSGFL SARWPFQDRR RQLLSSSSSS
SSGSSSSSSS SEGGVLLVCP ATVLPQWLRE LHKWCPAVRV CVFHDKDLKG LRAAAVAASK
SNGVLLTTYE TFRRHLNLLL SFTWKMAVLD EGQKIKNPHA AITLAVKRLG TPHRYLLSAT
PIQNSLIELW SVVDFVSPGR LATLPVFQQQ IADPIREGSF ASVSSAAAAA AARCALLLQQ
LVAPLLLRRR KEECMQHLKL PPKKEEVLFC ALTPIQYEVY RDVLHAFWGQ QQQQQQQQQQ
LGKRQLRSKA FAALAVLRKI CNHPDLVLQQ QQQQQQQQQQ QHRQRLKQLQ QQQEMMHMLP
PNVEVKRRRL QRQQQQQQQQ QTESTEEATT TAAAAAVPGD FGSPSRSGKL RVLMAMLRVW
QQQQQKVIVF CQTQQTLNCI AAALEASGVQ TPQQQQQQQQ QKRERSRKGS KEQHMSKEET
IREVEIKKEI NKKDLNENSK KLFLKLDGST PVEKRQKVIN CFQNLPSVFI LLATTRVGGV
GLSLTAANRI VIFEPDWNPM TDSQARERSW RLGQQRPVFV YRLLAANTLE VKIYQRQLFK
GFLSSRILDK CKQPNKFKYR NKIRCSYMNA VAAAEIDELK ALAGSSSSSS SSSMSSSKRE
DWLGTAEAAT GDAQLLQSLF ENEGVQHSLD HEQMEMPQQP KGLKESKEIG ANLDWKKGYS
WEAAGAPLSK EDAEMAEGLL EFLLSKKKDN YAASTGEILE AFAFRVPEHR KQVFRAILKQ
LCILRRSEDP EKEPSLWQLR EEFRA
//
