ID U6G9Q4_EIMAC Unreviewed; 1595 AA.
AC U6G9Q4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=DNA repair protein, putative {ECO:0000313|EMBL:CDI76033.1};
GN ORFNames=EAH_00000130 {ECO:0000313|EMBL:CDI76033.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI76033.1};
RN [1] {ECO:0000313|EMBL:CDI76033.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI76033.1};
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:CDI76033.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI76033.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG670307; CDI76033.1; -; Genomic_DNA.
DR RefSeq; XP_013253328.1; XM_013397874.1.
DR EnsemblProtists; CDI76033; CDI76033; EAH_00000130.
DR GeneID; 25268083; -.
DR VEuPathDB; ToxoDB:EAH_00000130; -.
DR OMA; DGWWNPQ; -.
DR OrthoDB; 11932at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 753..939
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1120..1163
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 52..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1595 AA; 175464 MW; 351B6636D406F3F2 CRC64;
MHRAHQDGSR SSDHDEGASR FAALVRCSVQ EAQEWLCKSA GSIEAALDSY LAQERSSKRH
KTNAASPRPC SPSLNSAFSP VEVDFAPRKS ATVWKRHSET SRRASPDFFG PGGQAKVQAG
RETPSGNTEL LIDLVDDSGE EDGNLTSETK VCDPRKTAGK FGCADEVPPP EPAKGPPAPA
VDDLPDDFSF FLGKCVASGT VTSGTMSKLS LTDPLTLMVE VRLPHTQRWG PQQGSRRAKV
SNSGYRILYI HLDDPVLLEH QRRLGQPNLR SRRPDESPLF SCGSSNAVGG KKAAKGSNRC
SPLAGLDFHN LLSSISEQTT FLRLLIDDRE AVRFDREVAS ALAPLLLLGA IKVDVCWLPD
KMPPRRLAIN STLSVRMTVH MTIQALRLSA LRQRGDPYLS QVHFPLLIGQ AFESLLHLLA
LQPVPAGSLL PEEERDANVL GPDEEAEVRK SLDSLSRPKG PSGSSLTGKE DTRGASERSL
QGASRAFNRE EERGEVSEGT DVFDEDEEYA ERSDALCQLV LKDRAESANL QREQQRRRRL
GSLYPPASMF ASRLRPYQAQ GLWWMLQCES EQSLRLEDED EELDPLWAKY DLPSAAAAYG
TMHGPTLVPA PSSDCKRART FVPRCFYLNT SSGLVSLEKP STTGRVRGGI LADCMGLGKT
VQVLALIAVS EYQERDPAGA AIWLAASVGG CAHDTGAASR TSSAAKPVSS PDELTGAAAR
QWDAFASSQL SASPISVSSD GDGADLNRGR GQPIPSGGRN SLLAVDPHTL QRTLKRGRDN
LLQGGTLIVV PLSLIGQWYA EVQRHLARGV ATVLQYYGPA RPRDPKVLAA YTIVLTSYQT
LASDFRHLSK HIQAEKGTLH CEPHSAHTLE LGCVPESPIA SIRFRRVILD EGHIIKNTSS
LVNRACNSVE ADSRWVLTGT PLQNDLSDAF ALVQFLRVSP MGSRRWWRAK VTQAMERGMV
RAAVETVRSI LVPLMLRRHG DQIGEDGKPL LPLPPLTIHT FTLQLTYEER LFYQTIFEHS
KAKFDQLVQS GQVLQHYTHV LQLLLRLRQA CNHPLLPSHR EQQRRQQFID LICPAQDPLK
CRSRDALGGL TSPSPPPRPA PDPILQKYIQ DAVEGKLEDC PICLEPPTDA VVLTNCWHVL
CVTCVLLLQS NSNGAAAACP TCRSKFLHQH VRLLPSGPKA SAQRWIQVVQ KKHREALAAA
DEAGSKDGKQ TGAQQAPSGE RECFSSVLNA ACPTEDSSTD LHISAAKYEG ALLAISDDTF
FFSTKMRLLL ALLEADVTAG RSCVIFSQWT SMLDLLEMAF ARVEAVRSAV QPRVSGARND
DNDDDDDVVE MGATSAERDT PHFPTGKLNN EVRRGEYLLS AQQEAPTKRL YNYRRIDGTL
GLEARQRTIQ WFSDDNLRSM SPKVGSCTSR ATEAEVEPFM GQFNLQPFAC ASDPTGDWHR
EGGPPLKQFG ATKSTMGNKG GEDRLSSQHG KILLLSLKTG NVGLNLVKAT RCYLIDGWWN
PQVEKQAMRR LWRYGQDQPV SVYRFVCART VEERMEELME WKGRLSRTTL RSADGFEQER
PADPEAGDAD KRRGRLSLQD LKKLFEGWEA GSVPT
//
