DYHC_ASHGO
ID DYHC_ASHGO Reviewed; 4083 AA.
AC Q9C1M7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dynein heavy chain, cytoplasmic;
DE AltName: Full=Dynein heavy chain, cytosolic;
DE Short=DYHC;
GN Name=DYN1; Synonyms=DHC1; OrderedLocusNames=ACR258W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11181180; DOI=10.1242/jcs.114.5.975;
RA Alberti-Segui C., Dietrich F.S., Altmann-Joehl R., Hoepfner D.,
RA Philippsen P.;
RT "Cytoplasmic dynein is required to oppose the force that moves nuclei
RT towards the hyphal tip in the filamentous ascomycete Ashbya gossypii.";
RL J. Cell Sci. 114:975-986(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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. May play an important role in the proper
CC orientation of the mitotic spindle into the budding daughter cell
CC yeast. Probably required for normal progression of the cell cycle.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Probably binds indirectly to the inner plasma membrane.
CC {ECO:0000250}.
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; AF287477; AAK20175.1; -; Genomic_DNA.
DR EMBL; AE016816; AAS51484.1; -; Genomic_DNA.
DR RefSeq; NP_983660.1; NM_209013.1.
DR SMR; Q9C1M7; -.
DR STRING; 33169.AAS51484; -.
DR PRIDE; Q9C1M7; -.
DR EnsemblFungi; AAS51484; AAS51484; AGOS_ACR258W.
DR GeneID; 4619795; -.
DR KEGG; ago:AGOS_ACR258W; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_7_0_1; -.
DR InParanoid; Q9C1M7; -.
DR OMA; FIMDEAN; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0000235; C:astral microtubule; IEA:EnsemblFungi.
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:0005816; C:spindle pole body; IEA:EnsemblFungi.
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:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblFungi.
DR GO; GO:0051293; P:establishment of spindle localization; IBA:GO_Central.
DR GO; GO:0000741; P:karyogamy; IEA:UniProtKB-KW.
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:0000070; P:mitotic sister chromatid segregation; IEA:EnsemblFungi.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0030473; P:nuclear migration along microtubule; IEA:EnsemblFungi.
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; 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; PTHR10676; 1.
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; Karyogamy;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..4083
FT /note="Dynein heavy chain, cytoplasmic"
FT /id="PRO_0000114637"
FT REGION 1..1745
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1746..1967
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2026..2265
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2373..2622
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2716..2980
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2987..3294
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3364..3592
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3748..3952
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 127..166
FT /evidence="ECO:0000255"
FT COILED 381..402
FT /evidence="ECO:0000255"
FT COILED 801..821
FT /evidence="ECO:0000255"
FT COILED 3015..3085
FT /evidence="ECO:0000255"
FT COILED 3223..3302
FT /evidence="ECO:0000255"
FT COILED 3527..3607
FT /evidence="ECO:0000255"
FT BINDING 1784..1791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2064..2071
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2412..2419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2754..2761
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 4083 AA; 466252 MW; 09DD11D4EF1225E1 CRC64;
MTDDQVAQAL VGYVFNVAKL FLKLGAEQDA FARTHGAKFE EWVGNGNMRT LFLVKDEEGE
VQVLEELEGP EAEGPEQSGR LLLIKNRPFV DGSAPMESQV QVLHLPPRAH FDGFKSFVSF
GVATMFDAVV STNSNLEAKQ ESINSARRKI KDLSLSLQSL QQFIEVPDIS ATAHPLIKKI
IAEGANPRNY TTYISDEQFA DSQFLNSLQK IANGWIKSAQ NLTKLTRNIE DGSATDEIRF
WINLEQSLLA LEKQIAIPEV EITLSILTAA KRFHATVTFI SDTGLRDRIL ETQSYNQIMS
DFPLADLQTA TSFTKLGEAI ESISIALKKL KVSTYPLARA VTFVEKISTE LDQKLREMLP
NLISSDFISF QEDYDHCIKI INQWEALLKE FTSLIRELMR KRSEKFIFMK IDTQTDSLKE
VLNTVAAFRK KHDILIHVLK GIGYDTLSED IQSIYEPVQY QDPLRDNASK WANAEAAYNQ
RVSLLENKLV DMLKKKLDDC KSSDSMFSIF EKYRPLMKRP RIQGAVREYQ HELLHNVKDD
LEHIHQQLSL QKWNSELSRL NDIPPVSASI IWSKQLTKKL QNLTSRLGLI LGEDWISTSE
GSQIFVECSS IMKVLNTDKL FETWVSNVSS QNFLLDEPIF KILITNEEYE LHVNFDSVVG
SLFKEVRNLM WMGFNVPSNI IKNSRRVRSL YPHAVMVSEL LQTFVSAVQS FQERPHTWLL
LKDETENIWQ LLSAMITDTW DSVPLFEDDA SHERAEDIQR DEPSILRLEH SIGELLSKFQ
QLDGLEKGLS SCLQQLEVFG KLDLQNLEVL INKIQLLVDQ ATLHGFHNMS GFIDYLNTRI
RSYLVSTVSK ILEESQLSPK KHYILQQGKK VTISPSIEET KKAWMRDFQK TLEVATNLPK
ITDKKFDITE GQMENFTDIG TDLSESLIKA FLRIEDACHA IDEHFQKWKK LELLWCLDEL
TLLERLGSDV EVSYRFLLDF MEERKAIDMV DSEITIAGDT MINNEQVYVR VSAKYDNWQR
VLCEKLLENY MDHASEFDTQ LVHSRRLLET SIINLGSLSK TTELIAYVDD IKNNLDLMFT
RYSLLLNTQK LLQKLRFRIP QNFIHAEQIE SDLVSLREIC LRKEDLINKN RDAISNKLEA
ELLKIQEVAN SLSQSWSKKK PLSVSIQPSE ALSVLNTFED SIAKVNTERE LINRAAKILL
VPIKLQNVLS PVIEEVNDYK AVWSSVDGLW NSFNATLSVK WADFESTAVK HRLEALMKKC
QDMPPKVLQY KIFQNIAGSI EATLKSMHLL KALKEPAIKP RHWSILFKQL GASHIVSGNI
DDQTFTLEDI LQLNILLNEV SVKKIVIKAR NENVLESSLS QMKARWRATK FDQFVHSSGL
VLVKGWDVIF SNCNDDLNMI TSMKNSPYFK VFEQEALEWE TKLSNFYDIV LSWVEVQRQW
MYLFGILAKK TEMKNLLPIE ASKFASLTSE YNSLLLKLYG SEIAIDILHV HSTLPTLKRM
AESLTKIRKS LNDFLETQRR LFPRFYFVGN EDLLQIIGAG DNFSEFSRHL SKLFSSVSDF
IYDESLIQGV YSLEGETLLF ANPVRVTPSS KLDQWMNEVD LEIKLTLSTL VKNCLESYRT
SGSLKHIIEK YPFQALLLAL QCTWTNKIET SMTKDNFGSI CSSIDEEMAS LAAVIDSYPT
VTEKRKVESL IVELVHLKTI TETLKNVELE QIDFHWKQTQ RFYWDDNSND PLNSITIEQS
CVSFCYGFEY IGVPERLIYT PLLDSCFNAM VLALSEHMGG CPFGPAGTGK TETIKALGQN
FGRMVLVFNC DDSFDFQAMS RLLFGITQVG AWGCFDEFNR LEEKILSAVS TQVEAIQLSL
VQGKPEIEVL DKKGSLNSNT GIFITMNPGY AGRSELPENL KKMFREFAMM KPDALVIAEV
ILTILGLENP RVLAEKIVSL FKLLNDKTTS QKHYDFGLRA LKSVLRNCLT ILRSTTDLDS
TQVLLRSLNE MVVPKLISVD EAVYEEAIAD FFPGSRIKPS NEQLLSYLAS YCESNQLVAS
DLFIKKCSQF YDIQKTQQAI ILAGDAGTGK TSVWKSVINS MKRSGAKENI VYIIDTKTLK
KEDLYGKLDP VTFDWKDGIF THLLRKTLLD TMGNFKNSNI WIVFDSDLDP NYTETLNSVL
DDNKVLTLPN GERLKIPPNL HILFEVQDLE HATAATVSRC GMIWFANNTL AAQDILISCL
SREVATLQQD ADVHDNIIAT IQDIFAQFIQ GSTLGNVIEA TYKADHIMGV DFCRFIETAV
TLLSCDIKKN KKQLSRLSQV ACVRYMSKRL ALVLIWAFVG GSDLETREKF SETICELLGI
SDIPTGSKFL LDYDVSVATQ DWVPVSAEVP KTSLESHEVL IPDLIIPTVD TVRHETLLFD
LLNADRPLIL CGPPGSGKTM TLYNTLKRSD RFNIIGINFS KDTSVELFLK TLEQHTICTP
TSRGIIMQPK AHGKQLVVFC DEINLPMLDE YGSQPVILFL RQLIEKRGFW NVQESKWVFI
ERIQIVGACN PPGHAGRVSI TPRFLRHASI VMVDYPGQIA MEQIYETFFN AIFKLTPKLK
GFASDFTKAS LQVYYDCKAT YTSEAHSHYI YSPRELTRWV RGIHFTISDS GNIDLAYMLE
LWAHESLRLF SDRLVSSSEK NIFQSILQNA ITTHFPNQPL GSLESSQLLF SNWLSLNYSK
VVKSEMYTFI KERLKTFAEE ELDTELTIYD DMIDNILRID RILKQVQGHG ILVGPNYSGK
TTITRFVAWM NGIKVVRPTI HRHFTIENFD EFLKQMLLRC GTESEKICLI IDESNILETS
FLERMNTLLA NSDVPGLFEA DEYEALLSKI GQRISQLGLL LDTEQEMYDW FTSEISKNLH
VIFNINDPDN RESTQLITSP ALFNRSVINW IGTWSSRSCL HVVNEVIKNM PLDRADYTIP
HHAAANLIVP DGNLVTIRDV VANLFVLFHE QYHRLLGNSQ GSPSAFLTSL RRFQSLYMSK
LKELEEHQRF TLVGLEKLKD TVIKVKQLNQ SLSQKQVELQ QKEKEARDTL DKMLVDQNEA
ERKQEASVEI QKILALQEKE INERRKIIMA DLAVAEPAIL EAQRGVKNIK KQQFTELRSM
LNPPDAVKTT LEAVCVILGY SCKTWKDIQL AIRKDEFVTD IVYYNTETMM TPAMKQDIET
DYLSRPKFNY ESVNRASLAC GPLYQWIVAQ ISYSEMLVKV TPLKEEMVKV ENEMLQNKAR
LMAAGEMIKE LQTSIESSKV SYSKLIREVE ITKTEMESVQ SKVERSIKLM ESLTGEKERW
IKNTEHFKDW NKNLIGNCFL SSLYESYCGP HDQSLRLKLF TIWSNTLAKF GIEYEPTYSF
ITDMVNPLTK VNWVACGLPD NELFVANFHI AMNSCHYPYV IDPSSTIVDT FANFYGRKMM
ITSFLDVGFV KQLENALRFG GCILIQDGEF FDPIISHLIA KEFKKAGGRL TVQIGDHEVD
VSTSFQLIIH SKDPNSYMSS FVKTRMAVIN FTVSKGSIEA QALQITLEKE NPELQKQRTD
LLKLNGEYKL HLRSLEDKLL ESLNESDGSI LENDSLISTL EQLKIESSEI AKKIEETNTV
IVKVEDLVNE YNVLGEQSVL IFNLLESITQ WHWFYQIPIE QFMECFSSIF ATKTRENMTR
SEHLLLALYE HVYMWFSHVF KDRDRMAFGI LLFASYHHSR ESKFFSEHFW KIIEGIASDT
LGTVEHITDT KLEQLVAAAN EKDYLKGLKS LLEFLPESSW HDSVPKYQNI IVACERGVDG
TFKVQQLAQE MGKTVHSVAL GSAESISMAE QDLIQYSGEG KWLLLQNLQM SHEWANTVLP
KKLESIKANP DFRVFMTCGI QSKPLVVPLL SRSYKIAYEG EPGVLNTVCE LWRTQSEELK
NVKPVEKLHS KFILVWFHSI IMARCRLAPI GFTKKYDFHD GDFHAGSKFL DHIFEQSSNG
KEHVDPDLVP WKLVSDTIGK IIYGGKVDDP ADLDWCKRSA RRMFSSDAYL NNFEVVQGLT
VPIDRSSYSQ YDKWFKSLDA AAERTTAWLE LSDASALQNF YAHEARMICK KIIQTNGPTS
LIH
