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Database: UniProt
Entry: W6UMB8_ECHGR
LinkDB: W6UMB8_ECHGR
Original site: W6UMB8_ECHGR 
ID   W6UMB8_ECHGR            Unreviewed;      4796 AA.
AC   W6UMB8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   SubName: Full=Dynein heavy chain 5, axonemal {ECO:0000313|EMBL:EUB62286.1};
GN   ORFNames=EGR_02739 {ECO:0000313|EMBL:EUB62286.1};
OS   Echinococcus granulosus (Hydatid tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC   Echinococcus granulosus group.
OX   NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB62286.1, ECO:0000313|Proteomes:UP000019149};
RN   [1] {ECO:0000313|EMBL:EUB62286.1, ECO:0000313|Proteomes:UP000019149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24013640; DOI=10.1038/ng.2757;
RA   Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA   Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA   Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA   Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT   "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL   Nat. Genet. 45:1168-1175(2013).
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00008887}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EUB62286.1}.
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DR   EMBL; APAU02000013; EUB62286.1; -; Genomic_DNA.
DR   STRING; 6210.W6UMB8; -.
DR   EnsemblMetazoa; XM_024491988.1; XP_024353482.1; GeneID_36338454.
DR   OrthoDB; 166463at2759; -.
DR   Proteomes; UP000019149; Unassembled WGS sequence.
DR   GO; GO:0005930; C:axoneme; IEA:UniProt.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProt.
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; 1.10.287.2620; -; 1.
DR   Gene3D; 1.10.472.130; -; 1.
DR   Gene3D; 1.10.8.1220; -; 1.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.20.1270.280; -; 1.
DR   Gene3D; 1.20.58.1120; -; 1.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 1.20.920.30; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 6.10.140.1060; -; 1.
DR   Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 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   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035699; AAA_6.
DR   InterPro; IPR035706; AAA_9.
DR   InterPro; IPR041658; AAA_lid_11.
DR   InterPro; IPR042219; AAA_lid_11_sf.
DR   InterPro; IPR026983; DHC_fam.
DR   InterPro; IPR041589; DNAH3_AAA_lid_1.
DR   InterPro; IPR042222; Dynein_2_N.
DR   InterPro; IPR043157; Dynein_AAA1S.
DR   InterPro; IPR041466; Dynein_AAA5_ext.
DR   InterPro; IPR041228; Dynein_C.
DR   InterPro; IPR043160; Dynein_C_barrel.
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; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46532:SF4; DYNEIN HEAVY CHAIN 8, AXONEMAL-LIKE PROTEIN; 1.
DR   PANTHER; PTHR46532; MALE FERTILITY FACTOR KL5; 1.
DR   Pfam; PF12774; AAA_6; 1.
DR   Pfam; PF12775; AAA_7; 1.
DR   Pfam; PF12780; AAA_8; 1.
DR   Pfam; PF12781; AAA_9; 1.
DR   Pfam; PF17857; AAA_lid_1; 1.
DR   Pfam; PF18198; AAA_lid_11; 1.
DR   Pfam; PF08385; DHC_N1; 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; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT   DOMAIN          2122..2259
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2402..2557
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2730..2878
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          887..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4493..4517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          3342..3383
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3577..3632
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        892..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4796 AA;  545957 MW;  E3D974618668B4CD CRC64;
     MPGGFPSQRG ERIRGARENR RALIDDRHLN ILMRLERAFG VETQTASEWL LDFGQLEALN
     IFFEANGAKV LMVTYADQNF NVHSTAKEAF KIQKKNLRGT KRYFFHNGQL PLKTETYETF
     TCKLDPAAGF VIPMFDYLRN FILPGVQVQA ANMHQLTPRQ HDDYCDYLAN YINSLETVIA
     CSQEHVILPP YMLHEQVHFN DMEGLIALSK TPEGLSLLEE NASAWMKKIY EEAKAVELIH
     VEINQTGPDG EFRFWKCQMT RMNSLVQELS RPDIKNVISV LEQAKSTIIP TWVQLDKKVK
     YANAEAAGNV KYLSAVEKLC APLVVTDIKT IISWMPNLMK SLKLLFQCSP FYNTYSHMTV
     LLVKITNQII YICKRYLTYN GTKSIWEQDN DEMVARMTDC IEVNLAYQTA YRVTRQGMID
     AKEKRIFNFS EVQIFGNMNL FTQRLDYLTR VLKTLKQYSV LHEFVLEGKE PMIAKFDRLK
     SMIASRPYDY LDHRNSMFEA DYDEFKERIS EIHDMLLSTI SANFTKPSSL MNAVRLQERL
     ETINIPGLEH GTRYRQLCDR LMQEINNIMD QFQTNFASPP LGRNMPPFGG RIAWARNFYR
     RLEEPMNAIC TKAPKALISP DGQDLVSAYN EVTGKIVGYE IAVYQTWTKL ILKKLNGLSA
     SLIVYSHQPA PFGRPFVNLD PDIIGLLREI FVMDKLQCPI PSFAKETLLK AKYIKYHYEQ
     LKYMCGRYVQ ITSSVPEKYH VLVIPSMMRV NRALEPGMHL HNWNSITTMN YVNNVLSTLT
     EFERLLKQID DISVNRIDFV LSELSQTTIL SLPGPDDPAL EIFDLVRLAK GQILAAADTM
     NALTITVLKA TVEMLNILLE DYDKFVDENN LEKIIADEVQ IRYAHMENQE PNGGGPNRTK
     AANSEAATSG KAAVVTKGNN GGVESQTATQ TKEDLKLPPE VHASLKTAVQ VALAADDMMM
     NLGTRATEAV CQSVRTALDS IWSRLAVKEA AGILKDIPAG MKVKAESTRP QPLVRCYARL
     VGTQVDIWPR PAEIQAALRS IVGGIEGSCK GVLAWGMDGR KREINEKVLT AGPFDNELAH
     DGTSVTAGSN SQTSADEKHV SMFVPSSNSS THTEAGETEN SLSPPGPPGP SASTWGAEVE
     GGSNADTQGL PGSGGGTNSD SNSRKMRGSR NTLFAKQITG MLETDITLRF NTYKEVHGDR
     EIYRLRNFIS SGLQQMKKIV FQNDGFIYET ESLTSYLEQF SHIYKCDVDA ELEAFLGAEP
     CMHEFQMKFS YLQSFEEQIE REPDHYVVGA LYVGLDDFKR KIRITLNALK KASCTSPLKS
     HSNFLRDIIG LSFLRLLKNY VQAFISEFIS PLDEIQNQIE EWDRNLAKKI TNLDDIAFVM
     DTLADIREKD IKQDMTLLRC EDATNLISKY NMPFPKELSD RVESCRYAYF RIKEKALQKL
     DHLLSIQAGY RDGLLESIKA LKELVEEFET DYDEKGPMVP GLPPQIALDR QIQFKNRHDN
     LTRKMLTARK GEELFGLPIT DYSRLGGIGK ELDLLQRLYG LYNEVSKTVS GYYDIVWRDV
     NMEKIAADLE EFQRKCKRLP KALKSWPAYT DLEKTINDFN EKVPLLEMMT NKAMKPRHWQ
     RLAALTNYNF DVESESFMLK TMLDAPLLES KDDVEDICIS AVREKDIEAK LSGVIVDWTH
     QELKLASFKA RGELLLKGDR VSEIVPMLED SLMILGSLMS NRYNVPFRKP IQEWVQKLSV
     TSEVLENWMR VQNLWVYLEA VFVGGDIAKQ LPQEAKRFQT VDKAWVKVMD RARDNPNVVA
     CCAGDGSLTE ILPRLLNQLE VCQKSLSGYL EKKRLKFPRF FFVSDPVLLE ILGQASDPTA
     IQPHLLAIFD NTKSVLFSEK APDILAAFSS EGERLDMFAP VKCEGQVESW LNTLLITSRL
     SLHLSIQKAS FLIMDPSCEL IEFFTAQLAQ IGIIGLQIIW TMDATEALKE AKVEPKAMTK
     TNKHFLDVLN LLINETTKDL NSLQRTKFET LITIMVHQRD IFDDLASGQI HIIFTYSYVL
     PNYLQQFYEY LVKQGIKSPD DFEWTKQTRT YFNEEVDACV VSITDVDFAY QNEFLGCTER
     LVITPLTDRC YITLSQALSM HLGGAPAGPA GTGKTETTKD MGRCLGKYVV VFNCSDQMDF
     RGLGRIYKGL AQSGSWGCFD EFNRIELPVL SVAAQQIAIV LSAKRDGMSS FIFTDGDEVS
     LDPEFGIFLT MNPGYAGRQE LPENLKINFR SVAMMVPDRQ IIIRVKLAAC GFVDNIILAR
     KFFVLYKLCE EQLTKQVHYD FGLRNILSVL RTLGSARRKN PKDSEDRTVM RGLRDMNLSK
     LVDQDEPLFN SLIDDLFPGT ILEKATYPEL QRAIENATSQ FNLINHPAWN LKVVQLYETQ
     NVRHGMMALG PSGAGKTACI RTLMAAMTEF WEPHREMRMN PKAITAPEMF GRLDVSTNDW
     TDGIFSTLWR RTLKKKPNEH IWLILDGPVD AIWIENLNSV LDDNKTLTLA NGDRIPMAPN
     TKILFEVHNI DNASPATVSR NGMVFMSSSV LEWDPISKAR LNYRPDNERR KFHELFQNSF
     PQSYRFVSQT LAIKMPYLEA FFVHQLCTLL DGLLVLENQQ GNTDKYLERI YIFALMWSIG
     ALIELDDRAR LEKFWRTELS VKLDLPSVDD SKSETIFEYF VGPNGEWVHW SSRIDEYIYP
     TDKDPEFSSI LVPNVDNIRT DYLIRLVGKQ EKAVLLTGEQ GTAKTVMLSK YMASFPIDAY
     TFKSLNFSSA TTPGLFQRTM ESFVEKRVGT TFGPPAGKKM ILFVDDISMP MINDWGDQVA
     NEIVRQTMEM RGFYSLDKPG EFTNIVDVQF LAAMIHPGGG RNDIPERLKR QFACFNCTLP
     SNNSIDKIFS TIGLGHYCQA RGFTEEVINM VRDLVPFVRR VWQQTKTKML PTPAKFHYIF
     NLRDLSRIWQ GIIYGTSEVF TTPDLLIKLC KHEMTRVIAD RFIDPADLIW FDRNFNRTLE
     DMMGEEVASS AQDEVFFVDF MRDPPEATGE EGEDFDFSAP KVYEPIFELG VLVDRLNNFL
     RERNESVRGA PLDIVFFRDA VIHLVKVSRV IRTPRGNCLL VGVGGSGKRS VTRLATYIAD
     YADFSIVLTR SYNVNDFLDD LRTLYRKAGQ EGKGATFVFT DSDVKEEAFL EYMNNMLTSG
     MVSGLFSRDD IDDILNALIP VMKREFPRRP PDIETLNEYF LQRIRKNLHI CLCFSPIGKR
     FRTWALYFPG LISGCTIDWL HKWPKDALLA VAKQYMGNFN IESSASVKER VIDLVATVHD
     GVAIKCEQYF ERYRRTAHVT PKSYISFLSG YSKVYGQQLA NIQSLINRLS SGLQKLDEAQ
     ESIAKLSVEL VEKKKELQIA NAEAEVVLSD VMQQTQAAEQ VKNKVLVVKN KCETIVSSIA
     AEKLVAEGKL EAAKPALEEA EAALNTIKPG DIATVRKLAK PPHLIMRIMD CVLLLFQRPL
     LPFQEDPDRR GCMKPSWNDS LKLMANTNFL QNLLNFPRDY ITEETVDLME PYFMAEDYNL
     ETAKKVCGNV AGLCAWTTAM EKFYWINKEV IPLKDNLAKQ EIKLNAAKID LAKAEAVLEE
     KERQLSIVRA LFEKAMLRKK ELAEDAEACQ KRIATATTLI DGLSGEKVRW TEETRTLGDQ
     VIRLVGDVLM ATAFLSYCGC FNQDFRNRII NSWVKSLMKM KIPHTHNLDL INMLTEGPTI
     AEWNLEGLPS DDLSVQNAII VTQASRYPLL IDPQSQGKNW IIKHEAAHNM LVTTLEHRYF
     RTHLEDSLSQ GRPLLIENIG VDLDPVLDNI FDKNFLKSGT GLKVKVGDKE VEISPGFTLY
     ITTKLPNPAY SPEIFARTSL IDFTVTSKGL EDQLLARVIQ TEKEELEQMR INLIAQMTAN
     KRRILDLEDN LLMRLASTEG SLVDDQGLVD VLQTTKSTSI EVAEQIALAQ ETETEITAAR
     EEYRPVAARG SLLYFLLSEV SAVNPMYQTG LGRFLKLFDE SMELSEKCVV TARRIINIIE
     YMTYSVWSFA VRGMFKLDKT MATLMLALRI DLQRKAVRHE EFMVFIQGGS ALDLKTCPAK
     PGKWISDLTW LNLVALSKLT EFSSIVQQVT STEKQWRLWF DKEAPEEETI PCGYEHTLDV
     FRRLLLIRSW CPDRALQQAK KYIVHSLGQA YIEDVPVNII DLSNEADART PLCGLLSMGA
     DPTPFIEHAA RKVRINLGVV SMGQGQEIYA RRLLKTAIVE GNWVLLQNCH LCIEYVQELF
     EMLTTFVHDQ FRLWITTEEH KMFPINLLQI AIKFTNEPPE GIKANLTRTY LGITQDFLEI
     CVTNHWRIIL YSLAYLHCTV QERRKYGPLG WCIPYEFNQS DFNASVQFLQ NHLDSLQFKK
     GQRISGIDWK CTCYMISEIQ YGGRVTDDFD LRLLKCLTRN SFQEAMFSPE YTMVEHYPIP
     LFGTVAEYLN YIKNDLPPRD SPEAFGLHTN ADINYSTQTT RRILATIVSI QPKDDSGDLG
     DGKDEDDSDT GGTHKPAVET REMIVHRICT ELLKKLPPPY IPFQVAEQLK ALGALKPLNI
     FLRQEVQRMN KVIKLVLATL TDLRLAIDGT VVMNEDLRDA LDCIYDARVP AFWIKSSWDS
     STLGFWFSEL LERNTQFSTW LEKGRPLYFW MTGFFNPQGF LTAMRQEISR SHEGWSLDSA
     VLSSHVTKLN VDEVREPPPE GVFVYGLFIE GAAWERRSGR LIEARPKILY EPMPVIHLFA
     VQEGKKTVVG RLPYTCPIYR KPKRTDLMYV TSLDLACSKN PDHWIKRSVA LLCDIK
//
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