ID U6MI41_EIMMA Unreviewed; 1769 AA.
AC U6MI41;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=SNF2 family N-terminal domain containing protein, putative {ECO:0000313|EMBL:CDJ61320.1};
DE Flags: Fragment;
GN ORFNames=EMWEY_00009820 {ECO:0000313|EMBL:CDJ61320.1};
OS Eimeria maxima (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ61320.1};
RN [1] {ECO:0000313|EMBL:CDJ61320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ61320.1};
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:CDJ61320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ61320.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG722056; CDJ61320.1; -; Genomic_DNA.
DR RefSeq; XP_013337970.1; XM_013482516.1.
DR EnsemblProtists; CDJ61320; CDJ61320; EMWEY_00009820.
DR GeneID; 25334968; -.
DR VEuPathDB; ToxoDB:EMWEY_00009820; -.
DR OrthoDB; 231695at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..151
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 667..823
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 435..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1098..1154
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 443..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDJ61320.1"
SQ SEQUENCE 1769 AA; 191877 MW; 0516CCE59141F2A0 CRC64;
LGKTIQTLCF LSYLSAMKVD GPHLIVVPLS TVGNWLHEIH RFTPSLTHIK ICGSRNERQH
AMQDRLAAKG LYDLYVTTYE TVKSEEEFFV EQIPHWQCIV LDEAHRIKNA SGAIRHSLDR
VQGNMRLLLT GTPLQNNAQE LFTLINFLMP DVFRDSLVIE QAFAQNAKSA AGKSGGKQPR
GRSKAAALAE MDVDTMFKQE DLNKIRQLLD RVMLRRLKEQ AIALPRKVFH DIWLPISDLS
AKWYRRLLEI KSLQEEARSN SARVNFRKML GLVIKMRILC AHPKGVCARE SQLQRLQAFF
SQEDPALQEE VTKAARELQA VEGAAHLAGS SKLLFLDKLM CHLHFLNCKY VPAYERDYMA
HKNDAATYEF YKRHEEAVLT ALAEGRKPPR RPKRSELIGI PEYRALLERG MPNRDLTTAR
DESFLKEGLF AAEPVMPTKD SCNPELQERK RGQGEDDDVS DNEGVGKRKQ EPADADVSDA
DAVAAQTSAE DQPRSRTERR ARRNLIVDDD DLVPVDSGAS AAAGQSQEGA AGGATDVAPS
TPTAPAGQEA GGETETAAMA VKSPEEKREG DDKSNLPTAC CTGSPASHKD HKEGVDSLEG
QPVKAEPIVA AASQAQADDT KREVLVATTP AAAGATAPVQ GTEGQTKAES SPDSDRSDLK
SNGGDKAAKS EAANTPRVQR LLIFTQFQLV LDELEAYCKY RGWRYLRLDG STNKFVRELD
IRDFNNDNTC YFVYLISTRA GGLGINLTAA NHVVIYDHDW NPFIDLQAVD RAHRIGQQRE
VHVWSLVSEW TVEERMAFRR EQKLRLDKLL VQQQVEEEAD ALDGEEGEDI KEHRSEKIST
DEVRRLMLHG KKAIVQMAST GTEDIANLCL EDLVSRARQP LPVLGEDEEP LVLEGSASFE
EDMDEKNLVD INEVMDEEAE ERRNQQQLAE GTEEPAAPEG PCEGGVGKPS TEGEEAKPSG
STSPGGGAEE EVEVCEAPTT AGSGTKGGLE AELQSAGVLW RSGRERKKPV ALYVPQEFTQ
REERRKLRHE TRCFVCGNGK DHVQSSVDRE GKPVEVAYDY CRYNVGEDYY MQLRQRGMNV
TPHNWILLLC SKCKAVEEQQ TRRRLTKEEK DHEKLMQQEL RQQQRQLHLD GARLRLEKDE
MKHLQRQRAE EERRLFDRKQ AVDRLDEAAE ISLRQAYQRL FPEAFLAEIE KRSAAAKAAQ
RASREAAVAE AMNAAAAAGA DGQAALASAA AAAIKKASKK PTNQLANMKL PSQSLSVCDN
CRFPCHGVKE YPGPCCFPDE VIQKFVARAR PASQSEPNSG GGGAGAAGGA DGVIELDASP
GEGGTAKEGS DASASPGIPQ SALRALASSA ALLQGGFPDA GGSASATAAA AAAAAGCDQR
VKYMQRQVCA ACHEWRIGKR SHTRKHCLTL TAEQRQEYDE RRAKMLLVAE LLRTKDPIPD
ANPGAYPSAS PQRLKAFFQQ YQEAADRILE ECMVAAGLQH AIASRFTSSK KVVPSPIGQA
PVAAGQGSQN NVPSLNSVAA SKDRISMILN RSKEMLLMKR HMELQVLATL SAANGRGPGP
NLANLNNDQK KLLGSSGEGE KPLMTPPSDT NSEVEVIGVS RVGAPTADVS SVAPGANCAP
TVAEAVPTAA GAVAAPEGAV KAAVGKRQSA DAPNSGARGA TVAALPAASK RQRRTVPIKT
ADAVAAYVQA AEMGGGSIAA SAVAAAVKQK PIIEFFKSRN KAAASAIGGL TKQPLLAGAG
GQGASRPGGM AGATLASWGP KPASDTESD
//
