ID U6MBH6_EIMMA Unreviewed; 2914 AA.
AC U6MBH6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Dynein heavy chain family protein, related {ECO:0000313|EMBL:CDJ60413.1};
DE Flags: Fragment;
GN ORFNames=EMWEY_00030280 {ECO:0000313|EMBL:CDJ60413.1};
OS Eimeria maxima (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ60413.1};
RN [1] {ECO:0000313|EMBL:CDJ60413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ60413.1};
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:CDJ60413.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ60413.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG721846; CDJ60413.1; -; Genomic_DNA.
DR RefSeq; XP_013337063.1; XM_013481609.1.
DR EnsemblProtists; CDJ60413; CDJ60413; EMWEY_00030280.
DR GeneID; 25337014; -.
DR VEuPathDB; ToxoDB:EMWEY_00030280; -.
DR OMA; NTANIFE; -.
DR OrthoDB; 275566at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.1270.280; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 6.10.140.1060; -; 1.
DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF34; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 2.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 204..323
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 473..691
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1017..1165
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1387..1718
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 513..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1649..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2836..2856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1770..1804
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1951..2006
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2181..2243
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 514..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2914
FT /evidence="ECO:0000313|EMBL:CDJ60413.1"
SQ SEQUENCE 2914 AA; 319732 MW; 3A135AD26AB3EA53 CRC64;
MISAEGERVP FYKSFKLRGP VEKWLTDLEM TMKKTIQTLM KTTKAQVYGQ PPNEWVFQTP
AQISACLSQL FWTMDVEEAL STGGQQLEMV QQQQLLLLQQ LTATVHRDLS PLQRFAVSAL
AIQTLHNRDV LETLIQINLT NPDGFDWQKQ LRHYWDDEIE SISIVQLTAE FSYGNEYLGA
PQRLVITPLT DRCWLTITTA LKELFLNSSI AGPAGSGKTE TVKELAKVLG FLCVVLNCSE
AVDLYVLDKV FAGVLASGAW ACLDEFNRLD LEVLSVVAQQ LLRMRHLLMT AATTNPQGPT
TDKPHDGPSV CASCGIFSTL NPNYGGRAEL PQNLQCLFRP VAMVVPDFEA IAEITIFAQG
AVQLSPQIHY DFGLRAAKAA LLRAGEIRRE HPNKSEEAAL AQAIRDSNES KFTAEDKPIF
QALLQDFFPQ VLEEADKENA IEQEIREAMK FLDLVPHAES VQLGVYLRQL LESRRGTIVL
GSAGTGKSST ISAATHSLSF AWSAAASAAE DADTDADATT SSTSGATNSS SSSSGGGGGG
AAAGGTEEAA EEADEEAAGE DDSASRDRST SSSSNRLSSR MSSSSSIWGP AAAAVQCRTV
NPKAVTTAEL LGVFNETTKE WSDGISSLII REYAENQSKP KKQILIFDGP IDSLWVESLN
TVLDDNQMLC LPNGERIRLT PSIRLLFEVS DLEAASPATV SRCGMLYVSS QVLHWKHIME
AYLARLADLV PREFICSLRG LFELSIPPCQ VFLQSEKASG DSDNNNNNNN NGNDGNNTNS
SGSSSSTSTL SAEAIVQSIF RMLIALLELP VHPTAPDPRQ KGNREPTDSK SRRMSQRASS
VHADPPRCLY TPEELEFLLA PCFFFCFVWS VGGSGCMQDV FSFSRFCEDL FEEYVSLPRG
ADVLDLCLNI QLKANASLTC KRSNSGVPTL EEEPLPSLPS PREEGAGGDK PPPKETKIKL
TDPQALEKAK RHKAYFIPWE KTIPDDPIDL TADFHSLLVP SKETIRMRSM VELLIKGKIP
ILLSGPSGAG KTALMKQLLQ QKQREERVQV ISLGFSSNIK PATLQALLES KLETKRKALL
GPPANHDCIV WLDDCNLPLP DSFGSQPTAE LIRQIEEFKG FYDLKRMHWK AVERLFFILS
VADPTAGRPL LSPRLSRHFQ GILVSDMDDC STQKIFQTIL ETHFAHIGAK QELRVQAKAI
VDASIELYRQ VKMTLLPTPS RPTYLFNFRH LKNLFQGLIS ADADAIAPRN AFVRLWMHEC
KRTFGDRLMS REEGEWLEEL LRDLATRRLY YSAAAAAAAQ QQQQQQQKSG NYLNLWGDCF
SRGQLHYREA PPMEQLLLLL HQYSEEAASM LQTGTEGDTT GAAANPVVFF PEAAERIVAL
CRHLKYPQGN VILLGVGATG KQTTARIAAC IRGYALKEFE CHADGSKDSA GDSWTGSQQQ
QQSTTSSSSS GGSGMEAGSS SITGSSNTST TTTSTTSRSS AALNKFREDL KDVLMSAGLS
GGKETIFLVN DSQILDEQIL EYADAIANTG EVHGLLDSDS VEMIVSDLTS AAVAGGLISS
SATPSSSSTS SSTSTEFILS LFRDNILKRL RICLCLSPIG SSLRARLRRN AGLNKAFIYL
FFSVWGASAL SDVAAHLFAA STPQLQQPQL QQLQQQQPEE QQEQSQQQQQ QQQQQRQQQQ
QQHKKTLSQL CVDIHLSAEA EAKHFYERER RIVYVVPKAF LDFISLFNIL LGQRRSALNS
KLQLLSSGIA QLEAAAVQVK QLQGELQQLR PVLQEKHAKA EALLKQVEAD KAVAEAEEKN
VSKEGEIVAQ HRSAALALQA EAQQEFDEAL PALEAALSSL DSLDKRDITE IKSFAKPPPL
VMLTMEAVCT ILGEKTEWEQ CRKVLADTGF LNRLTSFDKE HISPTTLKKL EKILQRPDFT
PEVVGKQSVA AMSLCMWVLA INKYAKISKE VEPKRKKVEE LNARLAEADE ALKESQNRCR
QVQAKVQQME QELQQQLREK ETLEKETLLC QTRLNRANFL TQGLTKEAVR WRESLAAAAQ
HLSSLEGDSL LAAASLIYLG PLMEFYRERL QQHWQQLLQQ HQIACSPGFD LRDIMSSPVE
INEWRMQVED IEEDIPPFFS PLLRLPLQQP QQALENPPRV FLGGMDIRLS IVDFSVTREG
LEQQLLVEIV LIENPEAERQ KTQIQIQNAI DQRQLQELEE TMLRLLSTCG GSILDDAQLT
DTLEEARETA AAVAERLKEA AIVMSDLEAI SKCFKPAASR GSLLFFTAQQ LQTLNPMYTC
SLELFLKAFT EAIKEQHQEY QLQQGPAAGE AAASSDGLAA AMPATDLQLS PPTGATETPI
VTPTAAAAAA TAAAIATNED RIRALVEAAS LAVYSQTLTG LFEKDKLPFA FAVAAEVLKR
EKFPEASEAS ELLMGGMAWG SEDCSSNETD DSSRPNPVPE LLQQQQWQQL LSLSAAVSSL
QRFPVHIVAE TDKWRQWLQT AAIHKQVPPL FKEEERVFRA FETMLLLSIV KQEAVAAFAL
EVVEQVLGPS FSELSSPSLE QVVSCSDSSN PLLVLLSPGA DPTSSFFSLA EQQNPKPRFD
CISLGRGQWP KASKVLANAI REGGWVLLQN CHLAKSWMAE LQKERSSFGS LGWNESYRFG
AADLGASLTL LRCIWTFGET VGGETPSSAS STSLDPLRRL VCEVTYGGRL TTNWDSRCLR
CLAENILKDN ILQDPQALAD KGVGPIGLEE DLDVAFAMLQ SQAAASPQLL GLHASAAVLL
ERDRGRQLLQ QLHSLQPLEA AAAGGSAAEQ LLLSRVEQIQ QRIGSCLNLL LEPKTVDVSK
AVAAAKEAAA AAASAAASGA TGTAETTTAA ENDADAHKHP QDALGVFFVQ EASRFSCLLQ
TIAQTLEQLR LAIKGLVASS PETEALFDAI NKNQ
//
