ID A0A2J6TIG7_9HELO Unreviewed; 4345 AA.
AC A0A2J6TIG7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dynein heavy chain, cytoplasmic {ECO:0000256|ARBA:ARBA00022197};
DE AltName: Full=Dynein heavy chain, cytosolic {ECO:0000256|ARBA:ARBA00033439};
GN ORFNames=K444DRAFT_558087 {ECO:0000313|EMBL:PMD62815.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD62815.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD62815.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD62815.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613783; PMD62815.1; -; Genomic_DNA.
DR STRING; 1095630.A0A2J6TIG7; -.
DR InParanoid; A0A2J6TIG7; -.
DR OrthoDB; 312195at2759; -.
DR Proteomes; UP000235371; 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; 2.
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; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 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; 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; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 4.
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:UP000235371}.
FT DOMAIN 1926..2064
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2218..2447
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2583..2737
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2925..3091
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 3176..3249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3413..3454
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 4345 AA; 491878 MW; 2C3CBF3F5E4D1668 CRC64;
MTEVDSPASP NGVAKDAFAV DPILIVEYLS KVIEITLGAT RKDLESGNNL LSKIRYQDTI
SRCTRFASEN QVALYVTKDI ASAGGLDGSL DGTNSLSYSY SMATDISFSP ANMASIALLK
RPQPIDPTIP IISQIQIINL PGVATLNSTA NGQGGASVSP FEILHSVVHL ALGPYFDAYT
KTQQTTNGVR GRSDVEAKTG IPVTKKRIAE LELSLLHLQQ NIEIPDLILP LHPMIQNAIE
EAAARNIKPS AELIPQALLS DSQFLNNLQS IVNGWIKSIQ TITKMSRDAN SGTATQEINF
WLSMESALEG IEAQLRGEGV ALTMEILRTA KRFQATVSFT ADTGLKEATE KVQKYNQLMR
DFPLDELLSA TSLPKIQDAI GLIFAHLNKK LRICPYPIRR ALPLVEAISA DLDLQLHSLL
HGRSLMHLDY REFNNLIATT ESIWKAWDEN VKEFTNVARE VTRRRNEKFI PIKISPKHAD
LQARLKYVST FRDNHEQLQR TIVNVLGPKS GEGDGNTNGA VIVEEMGDVD AVEEVQQAYA
ALNNVDLLDV TPEGTRIWVQ AEITYNERTS RVENSIIARL RDRLATAKTA NEMFRVFSKF
NALFVRPKIR GAITEYQTQL IDNVKHDISS LHERFKQQYG HSEAHAMAQL RDLPPVSGAI
IWARQIERQL DGYMKRVEDV LGNDWALHSE GQKLQSESNL FRKKLDTRPI FEAWLHDVQR
KQISIAGRLF NINKIRSANN ALELAVNFDP QVIALFKETR NLLWLNYAVP HQINNISKEA
KRVYPYAVSL MESVRTFAQT SRQIAEMSDV SILLSGYQNE VQALISKGVP LKWESFVHSF
DLHIKQTPYL SNGTVDHSAG RNESKHVQFV REFAASVSLL QNKTATLAAI NITIQKALIE
LQTCPYDSES FKQLLETIQR AVDQLNLENY VNLSYWVREM NARIKTTLLL RVRQAIGAWI
ESFENERSEG VNDDSRRKHL SGVPGAVKDE TPTLKRLVHE VSMRNQVIYL EPPLEDARAN
WFQQLHNWLG VVCNLPKVKA SRYEMSLSTT NETEARFTDL PASCTDSLSR VYSSIETKLR
EISTYVDKWL QFQSLWDLQS EQVYELLGEQ LSKWLQLLQE IRKARSTFDT TEVSRSFGHL
TIDYDQVQTK VNAKYDQWQH EILTKFAVRL GTRVREVYSE IEKARKDLEV QSLEATSTAQ
AVQFITIVQT CKRKVKAWGP EVETFRQGQT TLVRQRYQFP ADWLGVEQVD SEWTSLNEIL
NRKAKIVQDQ TDALRAKITA EDKVVGDKIA EITSQWNEEK PVSGTIAPDV ASATLMSFET
RITKLHEESE MVSRAKEALD LPATADTALA AILEEVQDFK SVWAALSTIW KSLNDLRETL
WNSVQPRKLR SAIDGLIKMT KEMPSRMRQY AAFEHIQNVL RQFLKVNPVL TDLKSEAVRD
RHWNKIFKAL KPGKRYSPIS MTLGDVWDLN LAASEVVIRD IIAQAQGEMA LEEFLKQVRE
VWTNYSLDLV NYQNKCRLIR GWDDLFAKCS ENLNSLQAMR HSPYYKEFEE EASSWEDKLN
RVHVLFDVWI DVQRQWVYLE GVFTGNADIK HLLPIESSRF QNINSEFFAV MKKVYKQPFV
LDVLNISGVQ KSLERLAELL NKIQKALGEY LERERVSFPR FYFVGDEDLL EIIGNSNDTL
RIAKHFKKMF AGLSGLIMDE DHIISGFTSK EGEEVRLKKE ISLIKTPKIN DWLALLESSM
KSTLAELLAE AIERYEPVFT ADEIDQTALS KYIASFPSQI VVLATQAVWT STVEKSLETG
GSTLQSLYEQ EVKVLQLLAA TVLGDLDPIQ RKRCEHLITE CVHQRDVIEK LIGLNATTPN
HYMWLLQMRY VYKAEGDFLQ RLYIKMANAK LNYGFEYLGV AERLVRTPLT DRCFLTLTQA
LCQRLGGSPY GPAGTGKTES VKALGVQLGR FTLVFCCDDT FDFQAMGRIF LGICQVGAWG
CFDEFNRLEE RILSAVSQQV QNIQLGLKQG LEDEKSQIEL VGRQLRVNAN TGIFITMNPG
YAGRSNLPDN LKKLFRSVAM SKPDKELIAE VMLYSQGFNQ AKQLSKQTVP FFDRCSAKLS
KQAHYDFGLR ALKSVLVSSG GLKRARLTRT GGDLGLEEEV EPQIIVQSIR ETIAPKLIKS
DVEIMRTIEA ESFPGVEYVP ASLEKLQDAI HSIAKERHLV VNDTWMTKIL QLFQIQGIHH
GVMMVGNSGS GKSVAWKLLL QALQQVEGVE GVCHIIDSKV MSKEALYGNL DSTTREWTDG
LFTSILRKIV DNLRGEETKR HWIVFDGDVD PEWVENLNSV LDDNKLLTLP NGERLNLPLN
VRIMFEVETL KYATLATVSR CGMVWFSEDT VTSNMMVSNY LDTLRKVAFE DLDEDAVATG
QTAAKALAIQ AQVADLLQAF LTTEDFISNA LERAEGFNHI MEFTISRVLN TLFSLLNKCV
RDVIEYNTQH VDFPLDPEQV ESYVAKKLLL ALVWSLTGDC PLGDRKSFGD CLAGMATFGS
PIMGDNSSLI DFDVTLPKAE WTSWQNSVPS IEVNTHSITQ TDVVIPTLDT ARHEDVLYSW
LAEHKPLLLC GPPGSGKTMT LFSALRKLPN MEVVGLNFSS ATTPDLLIKT FEQYCEYKKT
LNGVILSPTQ IGRWLVLFCD EINLPAPDKY GTQRAISFLR QLVEQNGFWR TSDKTWVTLD
RIQFVGACNP PTDAGRTPMG ARFLRHAPLI MVDYPGELSL HQIYGTFNSA VLKIIPSLRG
YSESLTKAMV QFYLESQQRF TPKIQPHYVY SPRELTRWVR GIYEAIRPLE TLSVEGLVRI
WAHEALRLFQ DRLVAEDERN WTNEAVHRIA LDFFPTIEED KALGGPILFS NWLSKNYIPV
DREQLREFVK ARLKTFCEEE VDVPLILFND VLEHVLRIDR VFRQPQGHLI LIGVSGSGKT
TLSRFVAWMN GLKVFQIKVH GKYSAEDFDD DLRDVLRRSG CKGEKICFIM DESNVLDSGF
LERMNTLLAN AEVPGLFEGD ELASLMTACK EGAQRQGLLL DSQEELYKWF TQQIVKNLHV
VFTMNPPEDG LSSKAATSPA LFNRCVLNWF GDWSDQALFQ VGTELTQAVD LDRPNFQAPD
SIPVAYRELT LPANHRAAVV NSMVYIHYSL HRFNIKLLKQ QGRVTYLTPR HFLDFVAQYV
RLYNEKREDL EEQQRHLNVG LEKLRDTVDK VRDLRASLAE KKGQLERKDA EANEKLQRMV
ADQREAEQRK TTSLEIQAAL EKQEAEVAQR RELVLNDLAN AEPAVIEAQK SVSNIKRQHL
TEVRSMGNPP QGVKLALDSV CTLLGHKVDS WKTVQAIVRK DDFIASIVNY DNEKQMTKNL
RIKMRNEYLS NDDFTYEKVN RASKACGPLV QWVQAQVNYS EILDRVGPLR EEVGMLEEQA
LQTKAEAQAV ENTINALEQS IATYKTEYAA LISETQAIKT EMSRVQFKVD RSVRLLDSLS
SERVRWEEGS KSFETQIGTL VGDVLVAAAF LAYSGLYDQQ FRKNMMEDWL HQLQLSGINF
KLHNPMTEYL STADERLGWQ ENSLPVDDLC TENAIILKRF NRYPLIIDPS GRVTEFLQKE
SKDRRLTVTS FLDDSFTKQL ESSLRFGNPI LIQDAEYLDP VLNHVLNKEY QKTGGRVLIQ
LGKQEIDFSP AFKIYLSTRD PSATFAPDIC SRTTFVNFTV TQSSLQTQSL NDVLKSERPD
VDERRSNLIK LQGEFKVHLR QLEKRLLQAL NESRGNILDD DNVIETLETL KKEAAEISTK
MSNTEGVMTE VDEITLQYNI IARSCSAVFA VLEQLHYLNH FYQFSLQYFL DIFHSVLHGN
KRLASETNHN VRRDIIIEDL FVTTYQRTSL GLLQKDRITL AMLLAQAAPY KMDKSLIDVI
LDEGIEGVDV STESHRKDEV LARASRIPVL KGKLEVISNA AWERFLFEEI GENHVPQVWG
ASTEKRDQEL MSLLLIKLFR LDRFVPAAER FVTAVFGQGL LDTTEDLKQT VDQVSASSPI
ALCSSPGFDA SYKVDNLVER SSATCTNIAM GSNEGLASAD KAISNAAANG SWVLVKNVHL
APTWLQSLEK RMDSLKPHAN FRLFLSMESS PKIPVNLLRA SRVLMYEQPA GVRANMKDSM
ASLSTRATKN PVERTRLYLL LSFLHAVVQE RLRYAPNLGW KGFWEFNDSD YECSAFIIDT
WIETVALGRT NVAPQNLPWD MIRTLIVETY GGKIDDEGDF ARLTQLVNSF LTPSAYDIGH
KLVEGIAGSG LDEDDGSLVV PSGTTLKEFT DWIQKLPERE PPTYLGLPAN AEKLLLVGQG
LSMIQNLGKI TELLDEGEQI MAEAV
//
