ID   DYHC_NEUCR              Reviewed;        4367 AA.
AC   P45443; Q7RVH1; V5IQJ3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Dynein heavy chain, cytoplasmic;
DE   AltName: Full=Dynein heavy chain, cytosolic;
DE            Short=DYHC;
DE   AltName: Full=Ropy-1;
GN   Name=ro-1; ORFNames=NCU06976;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=7929559; DOI=10.1083/jcb.127.1.139;
RA   Plamann M., Minke P.F., Tinsley J.H., Bruno K.S.;
RT   "Cytoplasmic dynein and actin-related protein Arp1 are required for normal
RT   nuclear distribution in filamentous fungi.";
RL   J. Cell Biol. 127:139-149(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Cytoplasmic dynein acts as a motor for the intracellular
CC       retrograde motility of vesicles and organelles along microtubules.
CC       Dynein has ATPase activity; the force-producing power stroke is thought
CC       to occur on release of ADP. Required to maintain uniform nuclear
CC       distribution in hyphae.
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC       (which binds cargo and interacts with other dynein components), and the
CC       head or motor domain. The motor contains six tandemly-linked AAA
CC       domains in the head, which form a ring. A stalk-like structure (formed
CC       by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC       and terminates in a microtubule-binding site. A seventh domain may also
CC       contribute to this ring; it is not clear whether the N-terminus or the
CC       C-terminus forms this extra domain. There are four well-conserved and
CC       two non-conserved ATPase sites, one per AAA domain. Probably only one
CC       of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC       regulatory function.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR   EMBL; L31504; AAA64908.1; -; Genomic_DNA.
DR   EMBL; CM002239; ESA43035.1; -; Genomic_DNA.
DR   EMBL; CM002239; ESA43036.1; -; Genomic_DNA.
DR   PIR; B54802; B54802.
DR   RefSeq; XP_011394207.1; XM_011395905.1.
DR   RefSeq; XP_011394208.1; XM_011395906.1.
DR   SMR; P45443; -.
DR   STRING; 5141.EFNCRP00000007047; -.
DR   PRIDE; P45443; -.
DR   EnsemblFungi; ESA43035; ESA43035; NCU06976.
DR   EnsemblFungi; ESA43036; ESA43036; NCU06976.
DR   GeneID; 3878786; -.
DR   KEGG; ncr:NCU06976; -.
DR   VEuPathDB; FungiDB:NCU06976; -.
DR   HOGENOM; CLU_000038_7_0_1; -.
DR   InParanoid; P45443; -.
DR   OMA; FIMDEAN; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0072382; P:minus-end-directed vesicle transport along microtubule; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.10.8.720; -; 1.
DR   Gene3D; 1.20.140.100; -; 1.
DR   Gene3D; 3.20.180.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 5.
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; 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   Pfam; PF12774; AAA_6; 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; 3.
DR   SUPFAM; SSF52540; SSF52540; 4.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..4367
FT                   /note="Dynein heavy chain, cytoplasmic"
FT                   /id="PRO_0000114640"
FT   REGION          1..1904
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1905..2130
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2202..2460
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2566..2815
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2909..3179
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3193..3481
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3565..3794
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          4003..4215
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          676..693
FT                   /evidence="ECO:0000255"
FT   COILED          1176..1215
FT                   /evidence="ECO:0000255"
FT   COILED          1327..1351
FT                   /evidence="ECO:0000255"
FT   COILED          1557..1574
FT                   /evidence="ECO:0000255"
FT   COILED          1637..1668
FT                   /evidence="ECO:0000255"
FT   COILED          2195..2218
FT                   /evidence="ECO:0000255"
FT   COILED          3193..3296
FT                   /evidence="ECO:0000255"
FT   COILED          3423..3481
FT                   /evidence="ECO:0000255"
FT   COILED          3778..3809
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1943..1950
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2240..2247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2605..2612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2947..2954
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   4367 AA;  495578 MW;  1E10F3E2D170D6DF CRC64;
     MMDSVPSPPP QPSPDANGVA TTPFAAVDPV KVVDHLVLLL EATLGAKRDE LEAPGSLLSK
     VRYSDTVQRC SRFALDTQVA LYIQKDLAPT TTLDGDNGAE AEEPEPTHVY TISSDLTSSP
     TTVAYLVLLK RPQPLDPIVP LTSQIQMLNL PGPAYLSTSG SEQGPTSSPY EILQLYLHNG
     LAPYFDASTK SQQLLNGARG RPDVDAKTGI PVTKKRWTEL ELSLSHLQQN VEIPEVSLPF
     HPLVQSTLEE AATKNVKPSI DLLPATVLAD STFLNNLQAT VNNWIKSIQV ITKMTRDPTT
     GTANQEINFW LSMEAALEGI ENQLRSEGVM LTLDILKHAK RFQATVSFTA DTGLKEAMEK
     VQKYNQLMRD FPLDELLSAT TLTKVQESIG QIFGHLNKKL RICPYPIRRA LPLVEAISGD
     LDEVLHRLLP GTELVKLDYE EFKGVMKQAG SIFRAWDESI KEFTNVAREV TRRRNEKFIP
     IKINPRHAEL QSRLDYVHNF RDNHEQLQRT IINVLGPKAT VNGIVTASGA NGVAVVEEIG
     DVDAVDEVKQ AWEALKDVDL LDCTREGTEK WVRAENIYNE RTARVENSII ARLRDRLATA
     KNANEMFRVF SKFNALFVRP KIRGAIAEYQ TQLIDNVKQA ISSLHERFKQ QYGHSEAHAM
     AQLHDLPPVS GAIIWARQIE RQLDQYMKKV EQVLGSDWAL HTEGQKLQNE SDLFRKKLDT
     RPIFEAWLHD VQRKQISISG LLFTINRIRS AGNILELAVN FDAQVIALFK ETRNLLWLNY
     PVPHSVNNVA KEAKRVYPFA VSLMESVRTF AQTNRQISDM SEVAVLLSGH RNDVYTLISK
     GIPLRWETFV NTYEVHFKPT FNPNTPLGQT GSKVSETKHV MFIREFAASV SLLQSKTLLL
     ANIYVTVQKA LNELKTCPYE ASAFQSRLET IQHAVDQLNL EQYVNLGYWV ERMNRQIKDV
     LYTRLQVAIQ AWIQAFEDED VERPSERKRL LEIASPDAAK SIGPVIKSLV HEITMRNQVI
     YLDPPLEYAR ASWFAQLQDW IGVICNLKKI KATRYTMSLS TEVVDEPRFN DLPGDCTEEL
     LRVQTSVEKK IREIGAYVDK WLQFQSLWDL QSEHVYDVLG DQLSRWLQLL QEIRKTRQTF
     DTTEVSRSFG HITIDYDQVQ TKVNAKYDQW QQDILIKFAS RLGNRMREVY AELEKARKDL
     EGQAMTANST AEAVRFITIV QSCTRQVKLW APEIETFRQG ESTLVRQRYH FQNDWLHAEQ
     VDGMWDMLNE LLARKSKIVT DQSDALRAKI TAEDKVVNDK IAEIAHQWNE EKPVSGTIAP
     DVASATLTHF EQRITKLQEE SAMVAKAKEA LDLAPTPDTS LGVILEEVQD FKSVWASLST
     IWKNLNELRE TLWNSVQPRK IRASIDNLIK MTKEMPSRMR QYAAFEHIQN VLRQLMKVNS
     ILGELKSEAV RDRHWTKIYK QIKPGKRYSP VSMTLGDVWD LNLVATEVIV KDIIIQAQGE
     MALEEFLKQV RETWTNYGLE LVQYQQKCRL IRGWDDLFAK CSENLNSLQA MKHSPYYKEF
     EEEASSWEEK LNRVHVLFDI WIDVQRQWVY LEGVFHGNAD IKHLLPIESS RFQNINSEFL
     AVMKKVYKQP NVLDVLNIPN VQKSLERLAE LLNKIQKALG EYLEKERVSF PRFYFVGDED
     LLEMIGNSND TMRIAKHFKK MFAGLNGLVM DDEGVISGFT SKEGETVRLK KEINLVKTPR
     INDWLALLEN GMKVTLAELL AEAVDEFTPI FSSENVDRDA LIKFMNTYPS QIVVLATQVV
     WTTAVDQALA DGGKDLQLLF DREVQVLRML ADTVLGDLEV LLRKKCEQLI TECVHQRDVI
     EKLVKLNANS NTHYMWLLQM RYVYNPEGDF LQRLHIKMAN AKLNYGFEYL GVPDRLVRTP
     LTDRCFLTLT QALCQRLGGS PYGPAGTGKT ESVKALGLQL GRFTLVFCCD DTFDNQAMGR
     IFLGICQVGA WGCFDEFNRL EEKILSAVSQ QIQDIQLGLK MGAEDEKAQI ELDGRQIHVN
     ANAGIFITMN PGYAGRSNLP DNLKKLFRSV AMSKPDKELI AEVMLYSQGF NQAKQLSKHT
     VPFFDQCSEK LSKQAHYDFG LRALKSVLVS SGGLKRARLL ETGDAESLGP EDVVEPEIIV
     QSIRETIAPK LIKSDVEIMM EIESVCFPGV KYVPASLEKL QEAIRRLAAE RQLVVNDIWM
     TKVLQLYQIQ KIHHGVMMVG NSGSGKSAAW RLLLDALQQT ENVEGVSHVI DSKVMSKEAL
     YGNLDSTTRE WTDGLFTSIL RKIVDNLRGE DAKRHWIVFD GDVDPEWVEN LNSVLDDNKL
     LTLPNGERLN LPPNVRIMFE VENLKYATLA TVSRCGMVWF SEDTVTPDMM VSNYIETLRT
     VAFEDLDEDA VATGQSSAKA LAVQSQAADL LQEFLTRDNL INEVLKEAAN YEHIMEFTVA
     RVLSTLFSLL NKAVRDIIEY NSAHVDFPMD PEQVEGYIAK KVLLALVWAL TGDCPLKDRK
     AFGDKVAGLA SFGSPPLDGT SSLIDFTVTM PQGEWQTWQQ HVPTIEVNTH SVTQTDVVIP
     TLDTIRHEDV LYSWLAEHKP LLLCGPPGSG KTMTLFSALR KLPNMEVVGL NFSSATTPDL
     LIKTFEQYCE YKKTLNGVML SPTQIGRWLV IFCDEINLPA PDKYGTQRAI SFLRQLVEHN
     GFWRTSDKAW VTLDRIQFVG ACNPPTDAGR TPMGARFLRH APLIMVDYPG ELSLMQIYGS
     FNAAVLKVIP SLRGYAEALT QAMVRFYLES QERFTPKIQP HYVYSPRELT RWVRGVYEAI
     RPLETLSVEG LIRIWAHEAL RLFQDRLVDE EERKWTDDAV RRIAMEYFPT IDEHKALGGP
     ILFSNWLSKN YVPVDREQLR DFVKARLKTF CEEEVDVPLI LFNDVLEHVL RIDRVFRQPQ
     GHLILIGVSG SGKTTLSRFV AWMNGLKVFQ IKVHGKYSAE DFDEDLREVL RRCGCKGEKI
     CFIMDESNVL DSGFLERMNT LLANAEVPGL FEGDDLAALM TACKEGAQRQ GLLLDSQEEL
     YKWFTGQIVK NLHVVFTMNP PGEDGLSSKA ATSPALFNRC VLNWFGDWSD QALFQVAHEL
     THSVDLDRPN WTAPDTIPVA YRGLNLPPSH REAVVNAMVY IHYSLQRFNA KLLKQQGKIT
     FLTPRHFLDF VAQYVKLYNE KREDLEEQQR HLNVGLEKLR DTVDKVRDLR VTLSEKKAQL
     EQKDAEANEK LQRMVADQRE AEQRKNISLE IQAALEKQEA EVASRKKVVL EDLARAEPAV
     EEAKASVSSI KRQHLTEVRS MPTPPSGVKL ALESVCTLIG HKANDWKTIQ GIVRRDDFIA
     SIVNFNNEKQ MTKSLRVKMR NEFLANPEFT FEKVNRASKA CGPLVQWVEA QVNYAEILDR
     VGPLREEVML LEEQALQTKA EAKAVEQTIS TLENSIARYK TEYAALISET QAIKAEMSRV
     QFKVDRSVKL LDSLSSERTR WEEGSRSFET QISTLVGDVL VAAAFLAYSG LYDQTFRKSM
     MEDWLHQLHL SGVQFKQHNP MTEYLSTADE RLSWQENTLP VDDLCTENAI ILKRFNRYPL
     IIDPSGRATE FLNRESKDRK LTVTSFLDDS FTKVLESSLR FGNPILIQDA EHLDPVLNHV
     LNKEYQKTGG RVLIQLGKQQ IDFSPAFKLY LSTRDPSATF APDICSRTTF VNFTVTQSSL
     QTQSLNEVLK SERPDVDERR SNLIKLQGEF KVHLRQLEKK LLQALNESRG NILDDDHVIE
     TLETLKTEAA EISAKMSNTE GVMAEVEQIT LQYNIIARSC SAVFAVLEQL HYLNHFYRFS
     LQYFLDIFHS VLRGNPHLAN ETNHNVRRDI IVKDLFVATF KRTALGLLQK DRITLAMLLA
     QASPYKMDKG LLDIILDERI EGKDVSIDQN TREEAFARAK KIPALKNKID AVPEADWEKF
     FTEELAEDFV PKIWNDETEP NDRALMSLLL VKLFRLDRFV PAAERFVTLV FGSDLFDIVE
     DLKQTVDQVS AILPIALVSS PGFDASYKVD GLVERMRVRC TNIAMGSAEA EGSADKAIAN
     AAQTGSWVLI KNVHLAPGWL QGVEKKMETL NPNPEFRLFL SMESSPKIPV NLLRASRVLM
     YEQPAGVRAN MKDSMSSIST RSLKSPVERT RLYLLLSFLH AVVQERLRYA PNLGWKGFWE
     FNDADYECSA HVIDTWIDTA AHGRTNIAPS NIPWEMIRYL IVETYGGKID DENDFKMLNQ
     LVHTFLTPSA FDIGHKLVEV SHDAEDEQKD AATGGDLVVP SGTSLQEFMS WIQKLPEREP
     PTYLGLPANA EKLLLVGLGK SLIGNLKKVT DLLDEGEAIM AEASEAA