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Database: UniProt
Entry: A0A1Y2E2B9_9FUNG
LinkDB: A0A1Y2E2B9_9FUNG
Original site: A0A1Y2E2B9_9FUNG 
ID   A0A1Y2E2B9_9FUNG        Unreviewed;      3957 AA.
AC   A0A1Y2E2B9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Dynein heavy chain, cytosolic {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LY90DRAFT_700676 {ECO:0000313|EMBL:ORY65698.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY65698.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY65698.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY65698.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) 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:ORY65698.1}.
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DR   EMBL; MCOG01000051; ORY65698.1; -; Genomic_DNA.
DR   STRING; 1754190.A0A1Y2E2B9; -.
DR   OrthoDB; 166463at2759; -.
DR   Proteomes; UP000193920; 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; 1.10.8.1220; -; 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; -; 2.
DR   Gene3D; 3.10.490.20; -; 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; 4.
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; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR45703:SF8; DYNEINS HEAVY CHAIN; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193920}.
FT   DOMAIN          196..762
FT                   /note="Dynein heavy chain tail"
FT                   /evidence="ECO:0000259|Pfam:PF08385"
FT   DOMAIN          1344..1738
FT                   /note="Dynein heavy chain linker"
FT                   /evidence="ECO:0000259|Pfam:PF08393"
FT   DOMAIN          1872..2198
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          2355..2458
FT                   /note="Dynein heavy chain AAA 5 extension"
FT                   /evidence="ECO:0000259|Pfam:PF17852"
FT   DOMAIN          2576..2663
FT                   /note="Dynein heavy chain 3 AAA+ lid"
FT                   /evidence="ECO:0000259|Pfam:PF17857"
FT   DOMAIN          2687..2934
FT                   /note="Dynein heavy chain AAA module D4"
FT                   /evidence="ECO:0000259|Pfam:PF12780"
FT   DOMAIN          2947..3073
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          3106..3174
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          3205..3261
FT                   /note="Dynein heavy chain ATP-binding dynein motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12781"
FT   DOMAIN          3499..3619
FT                   /note="Dynein heavy chain region D6 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF03028"
FT   DOMAIN          3651..3748
FT                   /note="Dynein heavy chain AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF18198"
FT   DOMAIN          3751..3954
FT                   /note="Dynein heavy chain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18199"
FT   REGION          958..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1087..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          585..633
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2932..3025
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        967..1026
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3957 AA;  454917 MW;  EDF11224021FADE3 CRC64;
     MASKKGAPAT PTKDAEEKVV KLDPRAEWLG EQIVAQLKLK SEKWDKLVSL QENCDIIQQF
     LDTSEVNTLL FILNARDDLI VTVNFPSSLK KKGAFVLKNT LNEPIAETLE NNVTIGDLAS
     NPLDYLNCIL EEVYLPLLTN SRNMDAWPEV VAMDVLRHFY KVNGAVYVIS GKTKGKTLLP
     LPHGNNDFSE NDKALLHTLE SAVIDWTYQI KEVIKSNSAT PLEEGLYPTP QVEIDFWEAK
     EANLKCIYQQ LSDDKFQAIA DLLQSSKSTY YPAFQQIFDE VKNALEEATD INLHLTPLRP
     LIETLSSTSD FNEMMQQFPP LLHVIMLIWN HSKYYNVPGR VIVILQEICN EIIDQAQNFI
     QPNEIFGIES DEALEKINLV YHACTKFKSI YYEYKAKIAE TERPWNFDTK LAFSRFDQFI
     LRIKQLSEFF DTIIEFNRLE KIEIGGTKGK ILSSEVVDIF NEFTSTYQDW TKIDYDVLDL
     NNYQFREDLA KFQDKISDLD RRIGTIICQA FDDCSSIHSR FRLIEGFSGL LARPIIGEIF
     EKKYYDLLKE YDGDLDEVNL IFLKLKNNPS IHYNMAPITG ALQWTHELKE RINSVMEKFK
     ELNHKILLES EEAKLVKVKY DEIYKKLDEY EQELFKDWSD NIINDSEANL DKPLLTRSIK
     DSLSLFEVNF DPKVIALLKE VKYLGSLGIQ APEKAQSVYD KDEVFRNNIF ELDHVVSQYN
     NIKLTVLDVE RPLIQERVDK IDKQFEQALS VINWRSDIID DFIKSIQESV GSLLKIIQTG
     KNNVVQMQNL MKKWYSSPLI ERKDSKKPLN LDDKDTKLKA IYELIQNDGK TIFNYLEDTR
     KAYDVDKNDP NWRNYADYVD TVVADGFFNT IKCSLTYFLD NMDIEYLKKC ELSPILDSRI
     EFIQNKLTFT PSIEEDASNS FMNIFLGILR DIYQVSVLVK RVNSQNIESE LINETAEYNE
     VKSGSNNEND NKNDNETPSE ENTEGNKESS EETKATEEAT EGNTENEAKK EDSENGSRTA
     ESTLDSKENE SDEDEGYLSE MLKNPELEEL KNQLISRVRD IIDDCKKYLH NRDEWMVTFL
     ETPYERSIPQ EIEEENKEEK KQTDKNETEN NQNDDNEEQN ENDIVNNSSN DEEDESSMLK
     LEKFEVEIHP EVIFRGWLKV DAKPLKQSLN IIVKKWSYTL TKYLSDETTK TLNEMNEFIT
     NTKGGLQKEV MEGDYDALRN DIGKSFEPLR KTINLLRQFG VEMPEDIHKL LNDLPEVWDD
     TKKLSQSVKE VVAPLQAKEF EMRNYNFKEE FRQKAPFMYS IGCSNAYELI NECHFEVLQM
     EQECEQLRES CELFELNCPQ YKQLSECRKD INMLKTIWDY VGLVNKIDPD AMEQTCREFT
     KDLRKMDKEI KAWNVYSGVD QHVKDMITSL RAVGELRSSA IRERHWKQLM KTTGVTFVMT
     DDMKFKDLLS LQLHRYEDDV RNIVDRATKE LSMEKVLNDL SKTWGTMEFE YKERDRKGTY
     ILISSEELVE TLEDNQVMLQ NLMTSKYVSH FEEQITGWQE KLSTVDTVMS LWLEVQKTWS
     HLENIFLESE DIRQQLPEDS KRFDGIDSDY NELMKNAINT PNAIEACSKE GLNAKLEYLQ
     QKLALCEKSL AEYLETKRLA FPRFYFVSAS DLLDILAKGN IPHAVAIHLQ KLFDSISKLE
     FTKDENGNYT KTAIGMYSKE DEYVPFKEPL ECVGPVEVWL NHLVDTMRMT LRHLIGEAVS
     TYEEKPRDQW IFDHPAQVTL TGSQIWWATE VNASFARLEE GYENSMKEYY KKQCNQLTTL
     ITLIQGELSK LDRQMIMTVC TLDVHARDIV GKLVQEKAEN AQCFSWQSQL RLRWDEEKRH
     CIANICDAQF TFCYEYLGDT PRLVITPLTD RCYITLTQSL HLIMGGAPAG PAGTGKTETV
     KDLGRALTVM VYVFNCSEQM DYRSIGNIYK GLAQSGAWGC FDEFNRISVE VLSVVATQVK
     SIEDGLRAKK KRFIFQGEEI SLEPTVGFFI TMNPGYAGRT ELPENIKALF RPCSMVVPNL
     ELICEIMLMA EGFVEASILA RKFHTLYKLN KELLSKQDHY DWGLRAIKSV LVVAGSLKRS
     DPGVPEEHVL MRALRDFNLP KIVTDDLQVF NGLINDLFPK IDIPRKRNLD FENDIKKSTI
     ACGLQAEETF VLKVVQLEEL LAVRHCVFII GNAGSGKSEI WKMLAKTYIN NGKKCVYADL
     NPKAVSTNDL FGYINPATRE WKDGLFSSIM RDMFNISGPD PKWIILDGDI DPNWIESLNT
     VMDDNKVLTL ASNERIPMKP AMRLIFEIGD LKYATPATVS RAGILYVNTS DLGWNPYVQS
     WLAKLEDQSE RTTLSVLFDK YVNTILDTIH SGRFKMAPVE DNSMVITLCN ILEGLIFNQT
     SLKGCDKEIY EIYFVIQDQL VDYRVEFSKW WNSEFKTVKF PPVGTVFDYY IDNTTRQFAL
     GQIKFQNSSI LEKPLEKKAG RNYGPPGTKK LIYFLDDLNM PEVDCYGTAS PHTLLRQHID
     YNHWYDRTKL TLKDIHNCQY VACMNPTAGS FTINPRLQRH FAVFSVSFPT LEKKIVNAAL
     QLHKKVSQVF LPTAIKFHYV FNMRDLSNIF QGILFSTKEA LKEPTDLIRL FLHETRRVYG
     DKLLETTDME QLVNFQLLLR RKSKDWASLK KILDDALDQY NEINAAMNLV LFEDAISHIC
     RINRILESPR GNALLVGVGG SGKQSLSRLA SYISSMDVFQ IVLRKGYGVA DLKLDLAALF
     QKCGLKQQQI VFLLTDAQIA DESFLVLIND LLASGNVPGL FPDDETETII NAMRNEAKAQ
     GLLDTRENLK VVLCFSPVGN LLRSRCRKFP AIVNCTSIDW FHEWPEEALT GVAKRFISAC
     ERVPEELRDP VTKFMAYAHL SVNEVSKKYL LNEKRYNYTT PKSFLALINL YEEMLEKKHA
     ELIKSMDRLE NGLTKLQSTS SQVDDLKAKL AVQEVELKQK NEEAELLIER VSVDTEKVNK
     EKAIADQEEK KVDQITKEVS EKQAQCEQDL LAAEPALEAA SQALNTLNKA NLTELKSFGT
     PAEDVKNVVS AVMENIDQSN LDALAPYLAD PNFNADYIRT KSFAAAETIA LANRLVNGLA
     SEKVRWSDEV ANFKEQEKTL AGDVLLAAAF ISYVGCFSKS YRNELLEEKW LPYMRQTNAD
     GKPFIPMSAE LDPLDILTTS AEIARWNNEE LPTDRMSLEN ATMVTKCKRW PLIIDPQLQG
     IKWIKAREGD SLKVIRLGQR DIGIEIDPVL NDVLGRNTIK KVENLETTKS TSTDIEKQVK
     EAKLTEKSIN ETRELYRPVA ARSSLLYFLL NDLYQIHPMY QFSLNAYKVV FQNAIHNAEP
     SEDIKERVNS LIDNITYSIM ITQNEIDMNE FNFLLRAPRA PNVTSPFDWL NNQSWAVIKA
     LSDLDEFKSL ANDIEVPENE KLPQEWKNKN AIQKLCILRA LRPDRMTYAV RNFIVQKMGA
     KYVDSTRQPL SQTYTEMNPS TPIFFILSPG VDPVKEVELL GKQLNFTEDN GNFHNVSLGQ
     GQEIIAEQKL DLAYEKGGWV MLENIHLVAK WLPTLAKKLE ALSVGAHKDF RVFLSAEPAG
     NPSCHVIPTS ILQVSIKITN EPPTGMKANI HRALDNFSQE TLERCSKDIE FKTILFTLCY
     FHAVVLERRK FGTQGWNRSY PFNTETFPKV PWTDLRYMFG DIMYGGHISD DWDRRLCSAY
     LDVYLKEEML DGNFELAPGF SLPPPSDYKI RSLKELDLGL KGDLTISEPM ETLMNAIYLN
     TVPATWERLA YPSLQSLSNW YVDLLQRIRE LENWVQEFSL PTVLWISGLF NPQSFLTAIM
     QTTARKMEWP LDQNREEYNT PPREGAAICG LFMEGARWDT QTGMIQESQM KVLTPAMPVI
     QVKAIPVEKK EVKGIYECPL YRTRNRGPTY IWTFNLKTKE VPQKWVLSGV CLLMSVD
//
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