ID   DYHC_FUSVN              Reviewed;        4349 AA.
AC   P78716;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Dynein heavy chain, cytoplasmic;
DE   AltName: Full=Dynein heavy chain, cytosolic;
DE            Short=DYHC;
GN   Name=DHC1;
OS   Fusarium vanettenii (Neocosmospora pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=T213;
RA   Inoue S., Aist J.R., Turgeon B.G., Yoder O.C.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
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.
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; U84215; AAC33176.1; -; Genomic_DNA.
DR   SMR; P78716; -.
DR   PRIDE; P78716; -.
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:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; IPR041589; DNAH3_AAA_lid_1.
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; 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; 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; Repeat.
FT   CHAIN           1..4349
FT                   /note="Dynein heavy chain, cytoplasmic"
FT                   /id="PRO_0000114639"
FT   REGION          1..1907
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1908..2133
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2201..2459
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2565..2814
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2908..3177
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3186..3477
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3563..3792
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          4001..4213
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          459..480
FT                   /evidence="ECO:0000255"
FT   COILED          1178..1215
FT                   /evidence="ECO:0000255"
FT   COILED          1266..1293
FT                   /evidence="ECO:0000255"
FT   COILED          1334..1354
FT                   /evidence="ECO:0000255"
FT   COILED          1560..1577
FT                   /evidence="ECO:0000255"
FT   COILED          1640..1670
FT                   /evidence="ECO:0000255"
FT   COILED          2194..2217
FT                   /evidence="ECO:0000255"
FT   COILED          3186..3294
FT                   /evidence="ECO:0000255"
FT   COILED          3420..3477
FT                   /evidence="ECO:0000255"
FT   COILED          3774..3807
FT                   /evidence="ECO:0000255"
FT   BINDING         1946..1953
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2239..2246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2604..2611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2946..2953
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   4349 AA;  493463 MW;  FCB3C7152B36A1BF CRC64;
     MEVTSAAAPS TGSSANGVTA AAPFPTIEPE RVVEHLAAVC EIALGATRDE LEQLGSLLHK
     ARYGETVSRC TRFASDSQNV LYIQKDIANP SAVEAGADPA APVTYNYTLS TEISSSSTTV
     SSLVLIKSPQ PIDPTRPLTS QIFITNLPGP ASLNAGVGEQ GTALSPWEVL HSQVHHALVP
     YFDANTKSQQ LANGSRGRAD VDAKTGIPVT KKRLNDLELS LLHLQQNVDI PEISLTFHSI
     VQNVLDDAES RHTRPSLDAI PQIFSQDSTF LNRLQANVNT WIKSIQGITK LTKDPSSNAN
     QEFNTASQEV NFWLSMESAL EGIEGQLRSE GVLLTLEILK HAKRFQATVS FTADTGLKEA
     MDKVQKYNQL MRDFPLDELL SATSLSKAQE AIAQIFGHLN KKLRICPYPI RRALPLVEAI
     SADLDEVLHR LLPGTELVNL DYQQFQTIMQ TCDDIFRTWE ENVKEFTNVA REVTRRRNEK
     FIPIKINKKH SELESRIKYV STFRDNHEQL QRTIINVLGP QATIPGVTET TGSNGIVMEE
     MGDVDAVEEV KQAWEALHNV DLLDVTDQGK ERWVRAENLY NERTTRVENS IIARLRDRLA
     TAKTANEMFR VFSKFNALFV RPKIRGAIQE YQNQLMDHVK QAINGLHERF KQQYGHSETH
     AMAQLRDLPP VSGAIIWARQ IEFQLDGYMR KVEAVLGPDW TMHTEGHKLQ EESELFKQKL
     DTARIYEAWI ADVGRRKISI SGQLFEIARV RSAGGILELT VNFDPQVITL FKETRNLTWQ
     SYSVPHAVTT VSKDAKRVYP YAVSLMESVR TLSQTLRQIS VMGEESVLLF GYRNDVYKLI
     SEGVPLRWES FINSHELFYS DNRQTRPLLP GGTDFGLAKN TESKHGMFIR GFAAAVSVLQ
     QKAVSLNFIH ATVEQALKEL NTCPYEEAAF HSRLDTIQAA VDQLNLEQYV NLDFWVRGLN
     SKVQSILLTR LQSAVHAWIE AFEDDTPDDE MRRKVNNNNE EAKPDGPTMK RLVLELAMRN
     QVIYLDLLLE FARASWFLHL HEWLGIVCNL RKIKATRYQM SLTTTANDEP RFTDLPSECA
     GLLQRVYVSV EKKLHEVSAY VDKWLQFQSL WDLQSEQVYD ALGEQLPRWL QLLQEIRKTR
     STFDTQEVSR AFGHLTIDYD QVQTKVNAKY DQWQHEILMK FASRLGNRMR EINAEIEKAR
     KHLESQSSDA SSTAQAVQFI TVVQSCKRNV KTWAPEIDMF RQGQSTLVRQ RYQFPNDWLH
     IEQIDSQWEA LKEILEKKSR IVQDQTDALQ AKIVAEDKLI NERIAEIAAQ WNEEKPVSGT
     IQPDVASATL SSFESRISKL QDDAQMVAKA KEALDIPASP DTSLEATLEE VRDFQSVWSN
     LSTIWASLNE TRDVLWTAVQ PRKIRSKVDD LIKSTKEMPS RMRQYAAFEH VQGILRGFLK
     VNSILSDLKS DAIRERHWHK IYKQIKPQKR FSPSSMTLGD VWDLNLVATE VIVKDIIAQA
     QGEMVLEEFL KQVRETWQNY ALEMVNYQNK IGLIRGWDDL FAKCSENLNS LQAMKHSPYY
     KEFEEEAVAW EDKLNRVHVL FDVWIDVQRQ WVYLEGVFTG NADIKHLLPI ESGRFQNINS
     EFLAVMKKAN KSPYVLEVLN IPNVQKSLER LAEMLNKIQK ALGEYLEKER VSFPRFYFVG
     DEDLLEMIGN SNDTLRIAKH FKKMFAGLSG LVMDDETVIS GFTSKEGEVV RLKKEISLAK
     TPKINDWLAL LEGGMKSTLA ELLAEAVDQY TPIFESETID REALNGFMDA YPSQIVVLAT
     QVVWTTAVHK SLTTGGETLK AIFDREVRVL RVLADTVLGE LEVILRKKCE QQITECVHQR
     DTIEKLINAK ANSTNHYLWQ LQMRYVYEPQ GEYLDRLYIK MANAKLNYGF EYLGVPERLV
     RTPLTDRCFL TLTQALCQRL GGSPYGPAGT GKTESVKALG VQLGRFTLVF CCDDTFDFQA
     MGRIFLGICQ VGAWGCFDEF NRLEERILSA VSQEIQNIQL GLKQGVEDDQ SQIELVGRHL
     HVNENTGIFI TMNPGYAGRS NLPDNLKKLF RSVAMSKPDK ELIAEVMLYS QGFNQAKQLS
     KQTVPFFDQC SGRLSKQAHY DFGLRALKSV LVSSGGLKRA RLGEGSLGAE EVVEPEIIVQ
     SIRETIAPKL IKSDVDIMAT IETDCFPGVQ YVPANLEALE NAIRELAAER HLVVNELWMT
     KVLQLYQIQK IHHGVMMVGN SGSGKSAAWR LLLDALQKVE GVEGVSHVID SKVMSKEALY
     GNLDSTTREW TDGLFTSILR KIVDNLRGED SKRHWIVFDG DVDPEWVENL NSVLDDNKLL
     TLPNGERLNL PANVRIMFEV ETLKYATLAT VSRCGMVWFS EDTVSPTMMV QNYLSTLRSV
     PFEDLDEDSV ATGHTPAKTL AVQSEFASLL HVYLTDENFI LPALQRAEGY NHIMEFTTAR
     VLTTLFSLLN KAVRDAIEYN GQHSDFPLES EQIESFISKK LLLALVWALT GDCPLTDRKS
     FGDDICALAN FGSPPLDGNS SLIDFDVTLP KAEWAPWQNQ VPSVEVNTHS ITQTDVVIPT
     LDTVRHENVL YSWLAEHKPL LLCGPPGSGK TMTLFSALRK LPNMEVVGLN FSSATTPDLL
     IKTFEQYCEY KKTLNGVMLS PTQIGRWLVI FCDEINLPAP DKYGTQRAIS FLRQLVEHNG
     FWRTSDKSWV TLDRIQFVGA CNPPTDAGRT PMGARFLRHA PLIMVDYPGE LSLNQIYGTF
     NSAVLKIIPS LRGYAEPLTH AMVRFYLESQ QRFTPKIQPH YVYSPRELTR WVRGVYEAIR
     PLEALTIEGL IRIWAHEALR LFQDRLVAEE ERQWTDESVR RIALEFFPNI DEEKALGGPI
     LFSNWLSKNY VPVDREQLRD FVKARLKTFC EEEVDVPLIL FNDVLEHVLR IDRVFRQPQG
     HLILIGVSGS GKTTLSRFVA WMNGLKVFQI KVHGKYSAED FDDDLRDVLR RCGCKGEKIC
     FIMDESNVLD SGFLERMNTL LANAEVPGLF EGDEYAALMT ACKEGAQRQN LRLDSPEEMY
     KWFTQQIVKN LHVVFTMNPP EDGLSSKAAT SPALFNRCVL NWFGDWSDQA LFQVGHELTQ
     SIDLDRSNFE CPDTIPVAYR GLQLPPSHRE RVVNSMVHIH YSLQRYNEKL LKQQGKVTFL
     RPRHFLDFVT QYIKLYNEKR EDLEEQQRHL NVGLEKLRDT VDKVRDLRVS LAEKKKQLEQ
     KDAEANEKLQ RMVADQREAE QRKNTSLEIQ ANLEKQEAEV ASRKKVVLED LAKAEPAVEE
     AKASVSNIKR QHLTEVRSMG NPPQGVRLAM DAVCTLLGHR INDWKAVQGI LRKDDFIASI
     LMFDNAKQMT KGLRNKMRND FLSNPEFTFE KVNRASKACG PLVQWVAAQV NYFDILDRVG
     PLKIEVEQLE DQALETKAQA KSVQNNIADL EASINTYKTE YAALISETQA IKAEMSRVQF
     KVDRSVRLLD SLSSERVRWE AGSKSFEIQI STLVGDVLVA AAFLAYSGLY DQTFRKSMMD
     DWFHQLHLSG IQYKSPNPVT EYLSTADERL GWQENALPVD DLCTENAIIL KRFNRYPLII
     DPSGRVTEFL QKECKDRRLT VTSFLDDTFT KQLESSLRFG NPILIQDAEH LDPILNHVLN
     KECQRTGGRV LIQLGKQEID FSPAFKLYLS TRDPSATFAP DICSRTTFVN FTVTQSSLQT
     QSLNDVLKSE RPDVDERRSN LIKLQGEFKI HLRQLEKRLL QALNESRGNI LDDDNVIETL
     ETLKTEAAEI SAKMSNTEGV MAEVEEITQQ YSIIARSCSA VFAVLEQLHY LNHFYQFSLQ
     YFLDIFQSVL HGNKNLANET DHNARRDVIV HDLFVNTFKR TALGLLQKDR ITLGMLLAQA
     SPYKMDKSVI DMILDNRVEG KDLSSHPDDR ENAFAQAKKL SAIKDKIDAI STEDWDKFFT
     EELAENAVPH IWDEKTEAID QALLSLLLVK LFRMDRFVPA AERFVAQVFG SDIFDIVEDL
     KQTVTQVSAT LPISLVSSPG FDASYKVDNL VERMRVKCTN IAMGSNEGLA SADKAISNAA
     QTGSWVLVKN VHLAPTWLQS LEKRMESLNP HSDFRLFLSM ESSPKIPVNL LRASRVLMYE
     QPAGVRANMK DSMSSLSTRA TKSPVERTRL YLLLSFLHAV VQERLRYAPN LGWKGFWEFN
     DSDYECSAYI VDTWIDGVAG NRTNLAPQNI PWEMLRYLVT ETYGGKIDDE GDFKLLSQLV
     TSFLTPAAYE VDHKLVDGPE GGLVVPSGTS FQDFNAWIHR LPEREPPTYL GLPANAEKLL
     LGGLGRSLIG NLRKVTELLD EGEQLVTEV