ID W2ZQA7_PHYPR Unreviewed; 4556 AA.
AC W2ZQA7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dynein heavy chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=F442_05829 {ECO:0000313|EMBL:ETP48399.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP48399.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP48399.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP48399.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:ETP48399.1}.
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DR EMBL; ANIY01001243; ETP48399.1; -; Genomic_DNA.
DR EnsemblProtists; ETP48399; ETP48399; F442_05829.
DR Proteomes; UP000018948; 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: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; 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; 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; 2.
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; 2.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 2.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 821..1270
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1404..1691
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 2015..2157
FT /note="Dynein heavy chain AAA 5 extension"
FT /evidence="ECO:0000259|Pfam:PF17852"
FT DOMAIN 2405..2508
FT /note="Dynein heavy chain 3 AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17857"
FT DOMAIN 2599..2911
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 2925..3254
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 3282..3510
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT DOMAIN 3779..3897
FT /note="Dynein heavy chain region D6 P-loop"
FT /evidence="ECO:0000259|Pfam:PF03028"
FT DOMAIN 3936..3984
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 4023..4136
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 4171..4435
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT DOMAIN 4501..4551
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT REGION 17..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1956..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3994..4015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4436..4466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3139..3187
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 19..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4436..4461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4556 AA; 510742 MW; AE807EA5E2652603 CRC64;
MTGGNVSNDG IVKAIENKVE IPKAQDRGES KQRRHNFLSE ETPRRGDLLA RRDEVRTLTE
KLVEGLTQGS NSSGADTGVS SWTPGGAVPR DSFFYLRRVD SNPYNLEMAS HSKIDPKDYY
TVSRLGITHF ASEGVEFQSL QKFERENYIY SLLVKLPFFK KYRIWKRFTI WKQVVCARKR
VDACMSLNNS LFILLPHLHE ALLQLRHACL DLQQARLFDF EHPTGPGEPA GWDTDSINTQ
QQKTYTLAEF LQRLKAQKTR VERLVDHFIS DAEMTAKHAC EKYLYSFLQH TGFNDVKPCS
TDRPRSSVVA AQRKVSTSAL GVASQQKPMT YTERATMKTQ CRRITKFLRV VEFLISDAML
RMAISSTVHL RNALATYIRD LNDDEDSGDE CPRCEEIKRS ATFPTISRST TQPLLRVEVV
LHGTSTSLRT STISGGTYSH DVPVRLDDPM KILEFIPSKE TLRSQLETMV FNGLSAITNR
DRLIRNSMFK VYVEASMEDT IQGGDGDSDG GELSSEGMDL DILIMEDSIF AETLQSVTTI
ILDAYNHAEE NCENLVVYLE RYLENGSFCK LVSDPSRYLN TDVHDFRGFL DKFLQEAQDV
DFVADNSPCG LLMLDRMKLN GYLKPSPRKC LDVLYKLIPI VLRQLNDDLT NEYTVANDRI
STIPTTVEAF SESLALLREL QIGQDAMEEK YNGVRSLYRL LEEYRVKMTD TDQMNAFVLT
QKRSQLKASI DLFESNRDQY VAKFSVELEA RLPNLVSNLT SVANALSDPI LFDLKSDINE
TIIYLTQIED NVLQLEAGVK LHHDYEKILG LPMTTAFDEM DDLKVDLALK NDLWKAFRDW
SVAVSLWEKQ QFPDEIDFGS ISEHTERLYV QITKWEQKLS EGMGPLCTYL KSSVDEYRAT
LPILMDLRCQ SFEDRHFVQL RELLGINIRH LGLSPGAPNS SVLTLGELVK MHLAPFGPQV
NRIASDATQE RQLKDMLTKI VVLWDRLEFD VKPYKKSKDY YILDAIESFY TMLEESLVNM
TAVLNSKFVA PIIDTAVMWH KRLLLFQETF DAWIECQRKW MHLETIFSAP DIQKQLPNEG
ATFIGINQFW KELMRKTRDQ RGCLKITGAI LIGASSGSKT YKDGSSSSGG GSGGVGQALL
DILTKHNASL ERIEKSLEDY LEMKRRSFPR FYFISNDELL EILAHAKEPQ IVQRHLPKCF
DALAKLDISD DSAHGSSAVS SAQDIVAMIS PEGERVAFGR IIKARGNVED WLNAVLVNMK
VTLHKHVKSC LADYQHSSRE TWLFRHPAQA VAVVSYIIWA RECEFCFRSR SQNPVQELSL
WHQTICTQLG NLTRLVRTNL TSVQRRVVVS LVTTDVHFRD IVESLVVKNV TDANDFLWQQ
QLRYQWYADR DECEIYQANC RIKYGYEYMG ACSRLVITPL TDRCWMTITG ALELRYGAAP
SGPAGTGKTE TSKDLAKALG ILCIVINCSN QMSYSMMGSI FNGVTQAGAW VCLDEFNRID
IEVLSVVGQQ MSILRSARLM NSTEVLLDGK YVPLRDHHVI ITMNPGYIGR TELPDNLKVS
FRPVAMMVPD YALIAEILLF AEGFLLAKPL SRKVTKLYKL CSEQLSQQAH YDFGMRAVRA
VLTLAGTLKR SSTIIAASGS FSMNVTDPAV TSSNDENVIL IKAMVGANTP KLTDADNRLF
QGIIRDLFPD TLSSIGAVEC NALIEGVGVF PPPSGHGGSN WMIALEEEIN EQLRQAGLQG
ARQWTKKLLQ LFATLDVRVG VVQTGSTGSG KSTALNILSA AVSALRERIA HPDVRFQRVV
SFTLNPKSIS IVELYGFFHP ITREWTDGLA SQLLRTCIME KNEEILVRQS ANQTVGVGSD
PLTWNLAFYW INFDGPIDAH WIESMNTVLD DNMTLCLANG ERIKLLPKIQ LLFEVADTSA
ASPATISRLG VVYYHPDCLG WKPFVETWVS RLSTQGFDPT PQASPPPVST PRESHLQTPL
STKMKTRVLK YFVLFVESGL TFIHSVSLSS NTSPQVPIST CDLAFVATIC HIFQALLLHR
APPELFAVAP APRSNFADIS SPESLLSLED QQNRCLDLIF IFSFAWAIGG NLNLDQVKNA
FQDFLGKLIS SNEQHLSPDI MAIDGKIPTP AGVSQATGDV QDFFIDFQYL SFSPWSNAGL
EHSLQPSEIK AGTLLVPTMD VLKYRSLVEL MTINARQPIL LTGATGSGKS AIVHNILDHH
ARIAADIYPS SSDTDSPLSV IAHGKVLPLI LNMSAQTSSA GTQLSIESKF SKKRRTLLGA
PVNKQLVVIF VDDVNIPATE KNGAQPVVEL LRQYLEYGGL YDRERFFWKD INDSVLIAAG
GLPGGGRQTL CPRFVRQFAA VFCLPSCDAS AMKAIFNSIL ASHITTSGSS VFAKNVKDTL
LQTADATCQL FQRVVQGLLP TPSKCHYTFN LRDVTKLMQG IVLGTRVSGA LVSSSKKGGA
QPTCSLTAQT VVNLWAHEGI RVFRDRLTDS TDRRWFSEQL VEVASKVFGV SWTVDTIGID
NATDRRRTHN AIDNGDPPNQ EHSTLLFSPR RVENRGIVTG ISMKYDQVGD LNRFKMFLNG
QIKEYNCSPT VQESCRQPLE LVLFEDAMIH TAAIARILIQ PRGHGLLLGM GGCGKRSLAR
LAVFLTGYYC FEIELRKGYG LVEFREDLKQ MMKLAVLGDT GEGPSTRQGI SVNAVPTVFL
LNDSQLTSDV FLEDVNTILN GGDIPKLFTT EEMERIINDV RALLERSISD AKSSQGGHNQ
GDTSSKVGDL TRKDCEDYFH MMVRNSLHFI LCMNPLGETF RARVRQFPAL INCTTIDYFD
EWPKNALEYV ADFYLSQEDT QAQPRSGPGT RRASTRDFLS SSMIRSAVTA LCVEAHVSVT
ASLPTFLTKY RCRVYITSQH YLDLISLFRR IHREKKAQLE TKLQRLMAGV VKLEETNSLV
STLQEELLVL QPVLVSKTME AEELLHQVAI DQAEAEQVAE RVRSDKAMVK QQQQEVAACQ
ADAQNDLDQA LPALNAAVAA LDSLDKKDIS EVKGFVKPPQ VVQVVMEAVC IMLGEKADWD
TSKRILSRSS FMAELKEYDK DNIQPAILKR IRKYIESPEF AVDEVRKVSH AAMSLCMWVH
AIDTYARIVK EVVPKRQRLA EMNAVLEVAN TKLEAKQQEL TKVLDKVRNL KEKCDATLAE
KQRLLDESVL TQLRLKNAEK LTKGLSGERV RWKSSITLLK QEGSSILGDS FLVAASMSYL
GPFDGEFRAQ LLSQWSGATR SSVGVSPSFT LANAYGDSRE LREWQLLGLP SDNFSTDNGI
FTLKSRQRWS LMIDPQQQAT QWIKRLEQFN HLEIVKADDQ NLMQAVEDCL VSGKHILIED
VTEALNPSLE PVVAIKPSQK SADNKRATRK YVKLEDRVVE TDTERFRLYL ATKLANPHFV
PDVYIRVNVI NFTVTRDGLE EQLLSDVVKR ERMEVEERKH TLLASIARDQ KQLQDLEIRI
LSLLSDAKGN ILDDVELIRT LETSKQTSNV VAQRLAESEA TKQEVLEIRN QYQGVAVRGA
MLFFVIADLA DIDPMYQFSL EYFNRVFIKS LNEAPVKAYL SERLESLKHH ITLAVYRNIC
RGLFKAHRQL FALVVCLKIM IDADELEQRD VVLLDRLVVD IDTTITTDAE STNMSDSCLV
EPKDNAIGDP NHIIDAVDRA FLALSRKHPL FSALSDSFYR ENSAWSNWIA SENPYLAHLP
EGLDESLPHF TRLVLVRWLR EDAFMMAVRC FIDQTLGAEY LEDASMDVEM KDVYSDIDKS
TPCLFILSPG ADPISSLERY AREKNICEDK YHVISLGQGQ GPIVEAKIVE CKTQGYWLIL
QNVHLAKSWL PELQTHLTTI NQEARNGEIH EDFRLFLASF PVEYFPVSVL QNSVKVMTES
PMGVKANVQR SMMLLKQMNA DGNNSHLTSN ASMKLRLAFG LSFFHAVVRE RSKFGSLGWN
LKYDFSDADF VSAVTLQRRL LDAVANMLAT KASASDVPQT ETSDDGMSNT QEPRSGTTFL
QFDTVPWDAL LFLAGEIYYG GRVTDEFDRK CLMAVLRRYC SEPCFKRKSN KTHRSKSTIR
RVTKAKSAST LENTIFSSTD DSFFAPEFQT EDDMVRFVDG LSDMDGPNVF GMHPNAHISY
QKKQSNHFVK LVMQLQNSGE DVSFADKLSN DCTSDAVDGN KSMEQAVVDL SKAIQEQLPS
PTTLNSIEKC LLGRTRENWQ DPLSVVLQQE VAACRKSVRH VDASLIELQH AIQGTAVMSA
TIEQTLHSIA AQQVPVDWMT NDSNLTPTTE SLSQWVKNLL NRFEFLRRWV EHGRVPGNMF
PLPFFSFPQG LFTAILQRYS RRHGIPIHFL DFEFRVLSDS KSGLLSSVDD PAVQQSLENE
VAGQADDGVY LAGLVLEGAN WNSELGCLCS SLPGIMRQNM PIIQVVAQQN STLATASSNV
QTKGPSQSDN AVISSTRNKV GGDTKAAARS TQLLKRGDTY KRSSRSLIGS DVEGTEDSLA
FNTYSCPVYR TAMRKGTLST TGTSTNLVLA MDLPCQGEPD YFVLNGTALV CSNTLE
//
