ID A0A183QGF6_9TREM Unreviewed; 1834 AA.
AC A0A183QGF6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000271901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000271901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR STRING; 6188.A0A183QGF6; -.
DR WBParaSite; SROB_0000271901-mRNA-1; SROB_0000271901-mRNA-1; SROB_0000271901.
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: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; 1.10.472.130; -; 1.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 6.10.140.1060; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
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; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF1; DYNEIN HEAVY CHAIN; 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; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF12777; MT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE 3: Inferred from homology;
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 1..255
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 422..560
FT /note="Dynein heavy chain AAA 5 extension"
FT /evidence="ECO:0000259|Pfam:PF17852"
FT DOMAIN 782..875
FT /note="Dynein heavy chain 3 AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17857"
FT DOMAIN 941..1083
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 1091..1162
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 1176..1521
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 1550..1771
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT COILED 1406..1468
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1834 AA; 209160 MW; F79FCA73C191CD92 CRC64;
MGKFFKGLAS SGAWACFDEF NRIELEVLSV VAQQNDKLKF EVIYKNIVLR NVKYDTSPNN
NHEVTNNQSN RISSLNGKLA RTVLFRPVAM MVPDYAMIGE ISLYSYGFMD ARSLSVKIVT
TYRLCSEQLS SQAHYDYGMR AVKAVLQAAG NLKLKYPDEN ENIILLRSII DVNLPKFLAH
DIPLFRGIIS DLFPGVMLPE ADYSIFLAEV HKNKTSELFT QKFLCYRYDF IIYFYAPAIS
LLSFMLVGEP FGSKTTVLHT LATVMTRLNE NGHDEYEKVV YKTINPKAIT MGQLFGEFDP
VSHEWTDGVT ANTFREFAST DTPDRKWVVF DGPIDTLWIE SMNTVLDDNK KLCLMSGEII
QMSRVMSLIF ETMDLSQASP ATVSRCGMIY MEPLSLGWRP LVRSWINRLP TSLTTGDTKD
MINSFFEWSL DPCMEFIQTN CRTLVATRQG NLVTSCLGFI DMLIEDVANE EDANENRYLR
LWLQTSIVFG IVWGIGGCLD YNSRQKFDHF LRNLLSGTNE KHPLPKELGQ KLDFPFPESG
LVYDYYYKFK SRGSWRHWNE KNKTDDQVSD RKIREIIVPT MDTARYKFIV DLCMKKHRPL
LYVGPTGTGK SVYVQEKLMR EIDKDKYVAY FVNFSAQTSA NQTQFIVMSK IDRRRKGVYG
PPIGKTAVLF VDDLNMPTKE IYGAQPPIEL LRMFLDHGYW YDLKDTSKLT LQDIHLIGAM
GPPGGGRNDV TQRFMRHFHV ISMTPFNDET MTKIFSTLMN IYIRSQEFSS EYITVGQIIV
SSTLEVYKAA IENLLPTPAK SHYLFNLRDF SRVILGVCLI QKDRIESKHT FSRLWAHEVM
RVFYDRLTDD ADRTWLYEFI KRCLQNNFKE KFDQLFAHLT SKEGEEIDET HMRSYLMFGD
FMNPESMPED RVYEEIKDIQ AMYPVVERCL EDYNNANKKK MSLVIFRYVL EHLSRICRIL
RVPGGHALLV GVGGSGRQSL TRLASAMAGY TVFQPEISKN YGKNEWREDI KTLLRRAGAE
GKSTVFLMTD SQIKEETFLE DVDSLLNSGE VPNLYSSEEK AELMDIIQSS LAASGGNKSV
DLSPLALYAL FSWPEDGLVR VANKAIQNLD IEDHVRESTV HLFKYFHTSI TPLAEKFLMN
LGRKTYVTPT SYLELIDSFQ RLLTQKQNET MKAKMRYVNG LDKLAFAAEQ VADMQIKLEE
LQPQLVLASR ENEKLLTVIA TESVTVEEQR VKVKAEEEVV NQKADASKAL SDECRADLAE
AQPALEAALS ALDTLKPSDI TIVKSMQNPP PGVKLVMEGV CVMRDIKPDK INDPSGTGKK
INDYWGPSKK LLGDLNFLNL LKEYDKDNIN PTIMQRIRKD FMTNPEFDPT KVARASSAAE
GLCKWILAME QYDRVAKIVA PKRIKLAEAE EELAENMACL KKTQDALAEV EAKLENLQNQ
LGSTQNEKKR LEDEVSNCAT KLERATKLIG GLGGEKDRWH QAAEYLEKLY DNLIGDVLIS
AGIIAYLGPF TSTYREECIS NWIIQCKQQN ITCSEPFSLT QCLGDPVKIQ QWNIDGLPRD
AFSIDNSVIV ANARRWPLMI DPQGQANKWI KNMEKDTGIT VVKLTDSDFI RNLENGIQFG
TPILLENVGE DLDPSLEPLL LKQTFRQGGV DMIRLGENII EYSKDFRLYI TTKLRNPHYL
PEIAVKVSLL NFMITLEGLE DQLLGIVVAK EKPELEEARQ ELIVTTANNK RMLKETEDKI
LATLSESEGN ILENEAAIEI LDSSKLISDD ILKKQKVAEE TQKKIDNARM DYSPIAKHSA
VLFFSLTDLP NIDPMYQYSL AWFVNLYVNS IHDR
//
