ID M7XI29_RHOT1 Unreviewed; 4649 AA.
AC M7XI29;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Dynein heavy chain, cytoplasmic {ECO:0000256|ARBA:ARBA00022197};
DE AltName: Full=Dynein heavy chain, cytosolic {ECO:0000256|ARBA:ARBA00033439};
GN ORFNames=RHTO_07288 {ECO:0000313|EMBL:EMS23554.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS23554.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS23554.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS23554.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. {ECO:0000256|ARBA:ARBA00011655}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KB722647; EMS23554.1; -; Genomic_DNA.
DR RefSeq; XP_016274673.1; XM_016420946.1.
DR GeneID; 27371301; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_7_0_1; -.
DR OrthoDB; 312195at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
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 CDD; cd00009; AAA; 1.
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; 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; PTHR10676:SF314; CYTOPLASMIC DYNEIN 1 HEAVY CHAIN 1; 1.
DR PANTHER; PTHR10676; DYNEIN HEAVY CHAIN FAMILY PROTEIN; 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; 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; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
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 1948..2086
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2613..2763
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3197..3273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3451..3478
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 4649 AA; 521845 MW; D65A77FED6FC8661 CRC64;
MQDRRPSSPA VDGAESPPTA TPGPRNQFDL AAFRKYLGQL LPLLIEAEPA DLESLFERSD
FSERATRWAN DPNAGVLYVV KQREERDADE QQDDSLPDTF TYSLTSSLSY SPLQSATLAL
IKHAPILDSS LPLASQLHFL NLFGPASSSS GSNALAAGAS AGSVVYEGLH RLVHYGVAPA
FEAYVESKAR KDAAGRAVED SKDADVKMGI PMTKKKFAEL ELSLLHLQQN VEIPDIVLAV
HPVVAAAVSQ AEAAGIRPSV DLIDSALFSD SAFLNKLQSE VNNWVKEVQK VTKISRDVAS
GTASQEVNFW LSMEKALEGI EKQLKSEPVQ LSLDILKHAK RFHATVSFIA DTGLNDAFKT
VHDYNVLMKD FPLNELLAAT DLNKIKDSIN QIFVHVNKKL KLSPYPVRRI LPLVEAISRD
LQTQLHKVLT SQRLTYLDYP LFEQAMRAAE GVFQAWDESF KEFTNVAREV TRKRGERFIP
IKIDPGHAKL QERVLYFRHF RKQHHQLQVM VGPLGSETKR STAVNGDGTK ENGDVDGELA
REWSSTLGDI DMEVEVRQAY EGIKGIDVLD VSDDGTQIWI AAETGYNERV ARVENHIISR
LRDRLGGAKN ANEMFRVFSK FNALFVRPKI RGAIAEYQSQ LIDSVKDDIR RLQDKFKSGY
QSSEAYQMSQ LRDHPPISGA IIWARQIERQ LSGYMKRVED VLGTEWSHYA DGQRLQTESQ
SFRAKLSTRP IYDAWLVDIN RRNLQISGRL FNITKSRQQA GALQLTVNFD PQIITLFKEV
RNLLWLGFQV PHTISNVAKD AKRVYPYAVS LMETVRTYSQ TIAKLEANPD IAPLVATSHK
KAQEQIAKGM SYRWDHFVNT FDNRSLPYAG ASDSSGSKHT HWVREFASIV SEFQDRTDHL
IALWADVSRT VDELSTCAYT RDAFSTLLAS LQKTIDTLNL EGYANLDSWT LALDKRVEAK
LVGRIRAVIE RWCGEFSKAP EARAADSSRP GASRRKAAVA HEDQPEDGLA LETILHEVRI
QNQVIYLDPP MEQARATWYR QLQTWLGVVC GLTRIQSSRY EIGLSIRAAQ PGALDYSTLL
ASLTDGTLER PFALVEAKLE GVGSYVDKWL QFQSLWDLEA EYVYSQLGDR LSAWQQLLLE
IRKTRSTFDN SETQRSFGVA VIDYEQVQSK VNAKYDAWQR DLLSRFGGKL GVAMKETHAA
VAKARHDLEQ HSIETSSTAA TVAFITFVQD VKRKLRQWAP EIEIFSSGQK TLERQRYQFP
SDWLYLDQVE NEWSAFNEIL KRKDASIQEQ LAGLQLKVVA EDKVLQGRIE ETVADWDANK
PIQGSLKAEA AMNAIGVFEG RVNRLKEQHD MLSRAKQSLD LEATKDDRLE PVLEEIRDLK
AVWTALLGVW AQVAELRDTA WQSVQPRKVR QQLDGLLAST REMPSKMRQY AAFEFVQESL
RGYLKSNSLV ADLKSEALRE RHWRQLYKSL RVAGHYSPST MTLGTVWDLD LKRNETAIRD
VIVQAQGEMA LEEFLKQVKE TWTGYALDLV NYQNKTRLIR GWDDLFAKCG ENVNSLNAMK
LSPYYRVFEE EASAWEDRLN RIHLLFDVWI DVQRQWVYLE GIFSDSTDIK HLLPVESQRF
SNINAEFLAV MKKVFKSPLV LDVLNIPGAQ KSLERLADLL SKIQKALGEY LERERSSFPR
FYFVGDEDLL EIIGNSKDIL RVSKFLKKMF AGLSSLKLDE ELSRIDGMVS REGEEVPFST
PIVLAEYPRI NDWLARLESE MKTSLAQLLA RSYADLVAFY ADPAGLDGTR FLAWIEGTPA
QLVVLAIQIA WTDGVESALQ AGGALDRPLS VILRSLEVLA DAVLGDLQPI QRRKCEHLIT
ELVHERDVVR RLAQDSVQSA ADFAWLYHMR FYLDVGKENV LGQLQVKMAS ASFFYGYEYL
GVPDRLVQTP LTDRCYLTLT QALDSRLGGS PFGPAGTGKT ESVKALGVAL GRLVLVFCCD
ETFDFQAMGR IFVGLCQVGA WGCFDEFNRL EERILSAVSQ QIQSIQLGLG ETVASPSHEI
ELVGRQLRIN PDTGIFITMN PGYAGRSNLP DNLKKLFRSI AMTRPDRELI AQVMLFSQGF
RTAEKLASKV VPFFNLCAEQ LSSQPHYDFG LRALKAVLVS AGHLKRARLQ AAADANGSDS
VDISEQEIVI QSVTETIVPK LVAEDVPLLT SLLADVFPGI DYVPVDLDDL KKHILDVCKE
RNLVAGDVWL QKVVQLYQIQ NIQHGLMMVG PSATGKTSAW RVLLAALERL TGIEGVSYVI
DPKAIAKDAL YGTLDPTTRE WNDGLFTHIL RKIVDDVRAE SSKRHWIIFD GDVDPEWVEN
LNSVLDDNKL LTLPNGERLN LPPNVRIMFE VESLKYATLA TVSRCGMVWF SDDAVSPDML
CRNYLDTTRS TPLDVADEDA SFSRQTQGDG DEVSAVLSTQ QLVAAKLEPF FERDGLVANA
LAFAAGVDHI MDFTPSRALT TLFSLLNKSI RTIAEYNAQH PDFPLQGDSV EAYTLKRLLL
GLVWAFTGDS KLDTRAKMGD FLRNQSGLDF PPLGPGGSLI DFDVQVSTGD WVSWQDSVPT
IEVETQAVTS PDVVIPTMDT ARHEEVLYSW LSEHRPLLLC GPPGSGKTMT LFSALRKLPD
LEVVGLNFSS ATTPDLILKT FEQHCEYRKT PNGVVLAPTQ IGRWLVLFCD EINLPATDQY
GTQKVISFLR QLVEQNGFWR TTDKAWVRLE NIQIVGACNP PTDPGRVPLT HRFLRHAPLV
MVDYPGEASL KQIYGTFTRA LLKVVPPLRG FAAPLTDAMV DFYLASQARF TTDAQAHYVY
SPRELTRWTR GIYEAIKPLD ALSVEGLVRV WAHEALRLFQ DRLVTEDERK WTDDKIDEIA
LAHFPTINRD EALARPILYS NWLSKHYVPV DREELREYAK ARLRVFYEEE LDVPLVLFND
VLDHVLRIDR VFRQVQGHLL LIGTTLSRFV AWMNGLSVFQ IKVHNKYTGD DFDDDLRAVL
RRAGCKGEKI AFIMDESNVL DSGFLERMNT LLANAEIPGL FEGDEHASLM TACKEGAQRD
GLMLDSHDEL YRWFTSQVAR NLHVVFTMNP PSGGLASRAA TSPALFNRCV LDWFGDWSDQ
AFYQVGLEFT NTLDLDAAGY TAPANFPIAY RQLSIPPVHR TAVVNALVHV HQSMYESNAR
LARRQGRVNH ATPRHYLDFV NQYVRLFNEK RDELEEQQRH LNVGLDKLRE TVVQVEDLRK
SLAVKRTQLE AKNAEANDKL KRMVADQQDA EQKKVASIEM STALEKQKHA IAERREIVMG
ELADAEPAVE DAQAAVSNIK KQQLTEVRSM ANPPEAVKLS MEAVCILLGH RIEGWKSVQA
VLRSDSFIAS IVNFDTAHMM TRQLRDKMRN DYLSRPSFNF ETVNRASKAC GPLVKWVIAQ
VNYSSILDKV GPLREEVQML EDQAETTMHQ ASALSSMISE LEARIAAYKD EYAALISETQ
AIKSEMEKVQ TRVDRSVKLL DSLSSEKSRW EAGSKTFEEQ MSTVAGDVLL SAAFLAYAGY
FDQSYRQAMW QGWANHLSDA GIEYKPELSL TEYLSTADER LEWHSRGLPT DELCVENAIM
LKRFDRYPLV IDPAGQATSF LLNEFRDRKI TVTSFLDEAF LKNLESALRF GTPILIQDVE
HLDPILNAVL NKELRRAGGR VLIRLGNQDI DFSPSFTMFL ATRDPSVEFA ADLNSRVTMV
NFSITRASLQ TQSLAQVLKV ERSEIDRKRS DLLRLQGEFR ARLHQLEKSL LAALNESQGN
ILDDDKVIET LETLKKEAAD ITRKVEETET VMAEVDEVTS EYLPLAQACS SVFFILDDLH
LLNRFYQFSL RFFLDIFDYV LLDNPSLKGV AESHERTRIL FDDLFTHVFR RTSRAVLHSD
HLTLAVLLAQ VKLRGQGEEL DEQELSFLLE GGETTAATST TASIAILDST EQQRLQAFER
LGVFRDVRSN LVEREGDWQA FLASPAPETI VPQIWSDLDP VHAALRNALI VKCFRPDRLI
PALTAFVAVV FKRDLFAETT YDLSDMVQNE VAAASPVCLC SVAGYDASYR VDNLVAATSA
RCASIAMGSQ EGFALADQAI AAAARTGNWV LLKNVHLAPT WLSQLEKRLQ SLNPNRAFRL
FLTMEMNPAI PVNILRQGRV LMNEPPPGIR ANILDSLRTL NPARLANGPA EKTRLYFLVA
WFHAVVQERL RYVPLGWSKV FEFNDSDQDA ALNTIDAWLS SAAKGRANID PAAIPWQAIR
SLVRETVYGG KIDTEFDQSL LDSFVDTLFS PRAYDVDFDL VSSGENEAGL KVPDAVHLDQ
FLEWAAQLPE QEPPSYLALP PTAERVIAAA QASSLLARLV KMRSLDDDET VGADVKRGST
SAQPAWMRVL KKTCLEWLDV LPRDLPALPA AEATTSDPLA RFFEREVSLS RSLVPSIRTD
LENLVRVCDG ELKQTNAIRS LLSDLNKGTV PGTWKRYRCR DLPASVWIAD LAKRLAQLHR
IVANGDLAKS PVAPGLLFHP HGYITASRQA VAHATKTSLE ELMMQVNLAE TGEEHSFVVE
GLALVGATWE SSKLAVNDGS AVRLEASSIS WKPKQGGSRS VQAGHKMMSI PCFLDSTRAD
VLLNVEVPVE TADSTMVIQR AVALVAVLD
//
