ID   DYH1A_CHLRE             Reviewed;        4625 AA.
AC   Q9SMH3; Q96388;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Dynein-1-alpha heavy chain, flagellar inner arm I1 complex;
DE   AltName: Full=1-alpha DHC;
DE   AltName: Full=Dynein-1, subspecies f;
GN   Name=DHC1; Synonyms=IDA1, PF9;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS.
RC   STRAIN=21gr / CC-1690;
RX   PubMed=10459015; DOI=10.1083/jcb.146.4.801;
RA   Myster S.H., Knott J.A., Wysocki K.M., O'Toole E.T., Porter M.E.;
RT   "Domains in the 1-alpha dynein heavy chain required for inner arm assembly
RT   and flagellar motility in Chlamydomonas.";
RL   J. Cell Biol. 146:801-818(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1914-2064.
RC   STRAIN=137c / CC-125;
RX   PubMed=8889521; DOI=10.1093/genetics/144.2.569;
RA   Porter M.E., Knott J.A., Myster S.H., Farlow S.J.;
RT   "The dynein gene family in Chlamydomonas reinhardtii.";
RL   Genetics 144:569-585(1996).
RN   [3]
RP   DYNEIN COMPLEX ELECTRON MICROSCOPY.
RC   STRAIN=CC-620;
RX   PubMed=2957507; DOI=10.1016/0022-2836(87)90676-0;
RA   Goodenough U.W., Gebhart B., Mermall V., Mitchell D.R., Heuser J.E.;
RT   "High-pressure liquid chromatography fractionation of Chlamydomonas dynein
RT   extracts and characterization of inner-arm dynein subunits.";
RL   J. Mol. Biol. 194:481-494(1987).
RN   [4]
RP   SUBUNIT.
RX   PubMed=2137128; DOI=10.1083/jcb.110.2.379;
RA   Piperno G., Ramanis Z., Smith E.F., Sale W.S.;
RT   "Three distinct inner dynein arms in Chlamydomonas flagella: molecular
RT   composition and location in the axoneme.";
RL   J. Cell Biol. 110:379-389(1990).
RN   [5]
RP   REQUIREMENT OF I1 DYNEIN COMPLEX FOR PHOTOTAXIS.
RX   PubMed=9008712; DOI=10.1083/jcb.136.1.177;
RA   King S.J., Dutcher S.K.;
RT   "Phosphoregulation of an inner dynein arm complex in Chlamydomonas
RT   reinhardtii is altered in phototactic mutant strains.";
RL   J. Cell Biol. 136:177-191(1997).
RN   [6]
RP   ISOLATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=21gr / CC-1690;
RX   PubMed=9247642; DOI=10.1091/mbc.8.4.607;
RA   Myster S.H., Knott J.A., O'Toole E.T., Porter M.E.;
RT   "The Chlamydomonas Dhc1 gene encodes a dynein heavy chain subunit required
RT   for assembly of the I1 inner arm complex.";
RL   Mol. Biol. Cell 8:607-620(1997).
CC   -!- FUNCTION: Force generating protein of eukaryotic cilia and flagella.
CC       Produces force towards the minus ends of microtubules. Dynein has
CC       ATPase activity; the force-producing power stroke is thought to occur
CC       on release of ADP. Required for assembly of the I1 inner arm complex
CC       and its targeting to the appropriate axoneme location. Also required
CC       for phototaxis.
CC   -!- SUBUNIT: The I1 inner arm complex (also known as the f dynein complex)
CC       is a two-headed isoform composed of two heavy chains (1-alpha and 1-
CC       beta), three intermediate chains and three light chains. I1 occupies a
CC       specific position proximal to the first radial spoke and repeats every
CC       96 nm along the length of the axoneme. {ECO:0000269|PubMed:2137128}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. Cytoplasm,
CC       cytoskeleton, flagellum axoneme.
CC   -!- INDUCTION: By deflagellation.
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   -!- DOMAIN: A construct expressing the first 1249 amino acids but lacking
CC       the motor domain is able to assemble I1 complexes and target them to
CC       their correct location on the axoneme, although motility is not normal.
CC       Phototaxis is also restored.
CC   -!- DISRUPTION PHENOTYPE: Cells swim slowly with near normal beat
CC       frequencies but aberrant waveforms, and are unable to phototax.
CC       {ECO:0000269|PubMed:9247642}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The kink behind the wriggle
CC       - Issue 34 of May 2003;
CC       URL="https://web.expasy.org/spotlight/back_issues/034";
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DR   EMBL; AJ243806; CAB56598.1; -; Genomic_DNA.
DR   EMBL; U61364; AAC49514.1; -; Genomic_DNA.
DR   PIR; S72239; S72239.
DR   SMR; Q9SMH3; -.
DR   STRING; 3055.EDO96546; -.
DR   PRIDE; Q9SMH3; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   GO; GO:0036156; C:inner dynein arm; IDA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IDA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IDA:GO_Central.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IMP:GO_Central.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP: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; 3.10.490.20; -; 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; 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   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; PF18199; Dynein_C; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
DR   SMART; SM00382; AAA; 4.
DR   SUPFAM; SSF52540; SSF52540; 4.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Flagellum; Microtubule;
KW   Motor protein; Nucleotide-binding; Repeat.
FT   CHAIN           1..4625
FT                   /note="Dynein-1-alpha heavy chain, flagellar inner arm I1
FT                   complex"
FT                   /id="PRO_0000114646"
FT   REGION          1..1919
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          70..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1920..2141
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2201..2437
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2550..2800
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2906..3155
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3192..3494
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3542..3773
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3998..4216
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          1227..1259
FT                   /evidence="ECO:0000255"
FT   COILED          1339..1409
FT                   /evidence="ECO:0000255"
FT   COILED          3192..3297
FT                   /evidence="ECO:0000255"
FT   COILED          3400..3494
FT                   /evidence="ECO:0000255"
FT   COILED          3701..3788
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        70..84
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         960..967
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1958..1965
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2242..2249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2588..2595
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2945..2952
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         3680..3687
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   4625 AA;  522843 MW;  875F51048AF99340 CRC64;
     MDRRLEWVKE KACLGLGVEP NLFEAAIANP ESRARVTAFL DGTVTSSALL FALEEATIYV
     EEYQEVLAEE QAPEAEDGEG EEHDGQEPGE AGGEGAEGST APGDSGDGQP EDAPAAAAEA
     NGANPEDEAA APADGAADGA AGEGGEEGDG AEGDEPPAPP APKYVRRVIS VPKVVSKLNV
     ALGSLPEELS VFPVFYFILN RSGHVAAEEL DSAVEFGLLS EGPSLRILEQ MLSSVFVPIL
     VQMSGGDVAS GGVLMQSMTD NSHRELLGNM QKFHSQVTQA LQQLTGDVTL QLPDFPLEDM
     DRAAADTDLV MQLEQYMAEW SQVLASVLQR ESQKHPTGKG PLAEIEFWRE RNAVLSSLYE
     QLNLPQVKRM ILVVEKGSDD RNLMAGFKSQ LGELTKLATE ARDNVKFLTT LERHFKNIAT
     GPLGGILDTL PPMMNALRMV WIISRHYSDD QRMGSLFQRI AREIGDRVEA AVDLRHIFRM
     TSADAVELLK VCKSVLEHWL QTYMAMREKI ELSGRDARWE FPKQLLFART NYMAEICTDL
     IEMVEIVDDF FRFLGPELKT VTGDTAGIDR VVHRVVAMYE PIESISFNVF DYGNQHEWKA
     AKQQFYADNE DIKEATRELI DTSFRKLRSA EGACELLQSF KSIKSKGAIQ KQVMNKFNDI
     LEQFAREIEQ TADIFERNKD APPVTKNQPP VAGAIKWVRS LLERLKRTMA KLLSTEEEII
     RTTELGQAVE SKFKSFARSV MLTEKKWFSS WSDSINGVAM QHLKQTIFRR SAATNRVEVN
     FHPDLVRLIR ETRYLDRMGF PIPEIALNVA LQEDKFLQWL EGLNSMLFKY YESIDQLTPV
     ERELMERKLE ELESCLQPGF TILNWNSLGI TEFIGTCDKA IATFQQLVKQ VQKNSGIIEQ
     VVYAIAGAQL VTEPEEGAEV MDLQEFYEDI ERQRLAALES LVKKYRTISP LLGKIEEVVA
     GTNSGKSPAL SSYYSFWERA IFNALNTMVL CAMTKLQDMI EQRSKHAEGG RKPPLFKVTV
     SLQSVDVVVQ PPMTEVNKAL GRLVRSLVES TKAFVRWMDG TCVETPEQRG ATDDDEPIVF
     TFYWDVAANP QVIKTMLNLN QSIQRAITSV NKYAESWRRH QALWKTDKNS VLDKFKARDP
     SAAQFEDKLS KYAKMATEIS AQAKDFDQDF IRVSCHALAS SVCDEAQAWV RAIAQTMREL
     DAVTESQLRD KIAKYQTALH RPPDTLEELK QVLNTVNTIR GESMVMELRY ADLEERYRTR
     LLYATNPEEE SQCAHELASA SQVRALWTEL LNEAEAVDWS LEETKKKFSE TTRSQVSDFA
     AITAELWEKF RTTGPGLPTV ELASGLDELH KYESNLADAL RQREQLVLAE KLFGMEITAY
     PELAQLESEI RKLAQVYGVY AEHAEAVRQY GGQLWSELDV GKMMAGTEAI LTKLRKLKSL
     KLLPVYELVE KEIQGFYNSL PLMKELKSEA LRKRHWTRLM EVTGQEFDMD PKTFTLGNMF
     AMQLHKYAEE IGKITNAAVK ELTIESEIRK LADVWREQRF ELGKYMKGPE DRGWVLRSTE
     DILVLLEDMG LNLQSMMASP FVRPFLTEVR AWEQKLSLIG ECIEVWMHVQ RKWMYLESIF
     VGSDDIRHQL PAEAKRFDNI DRQWQKIMND TAKNTVVLDA CMADGRLDLL KSLSEQLEVC
     QKSLSEYLDT KRCAFPRFYF ISDDELLSIL GTSDPTSVQE HMLKLFDNCA ALVFGRGNKT
     ITGMVSSEKE GFEFRNVVPI EGAVELWMTN VEAEMRKTLY QITKEGIFFY AKTPRTKWIS
     ENLGMVTLVG SQIWWTWETE DVFRRVRDGN KHSMKEFAAK LTGQLSELTS MVRSDLSNEV
     RKKVNTLIII DVHARDIIDT YVRDSIVDAR EFAWESQLRF YWDRQQDDIL IRQCTGLFKY
     GYEYMGLNGR LVITALTDRC YMTLTTALTY RLGGAPAGPA GTGKTETTKD LAKSMALLCV
     VFNCGEGLDY KAMGSIFSGL VQCGAWGCFD EFNRIEAEVL SVVSSQIKNI QEALKNDLTR
     FQFEGKEISI DPRTGIFITM NPGYAGRTEL PDNLKALFRP VTMVVPDLEQ ICEIMLFSEG
     FDSAKVLAKK MTVLYKLSRE QLSKQHHYDF GLRALKSVLV MAGSLKRGAP DMSEQLVLMR
     ALRDMNLPKF IFDDVPLFLG LINDLFPGMD CPRVRYPQFN DVVEADLADQ GFKVLTEPSE
     QVDKVVQLYE VMMTRHTTMV VGQTGGGKTV ILNTLARAQT KLGKKTHLYT INPKAISVAE
     LYGVLDKDTR DWTDGLLSNI FREMNKPLPA ERDEARYLVF DGDVDAVWVE NMNSVMDDNK
     LLTLPNGERI RLQNHCKLLF EVFDLQYASP ATISRCGMVY VDSRNLGYKP YIYTWLNSRA
     KQAEVDILRG LFEKYAVPSV DWILEGIDGE ELVRRPKQAV PVTNLNMITQ LCNLLNATIT
     DHPRMSDPQI LEAIFIFCTI WSLGAAIVQR PESPDRDRFD AFVKHIASMG LVDGERVAAT
     QLPARSLYEY CFDTNEGVWK SWRSYLQPYE PPADGAFAKI LVPTVDVVRS TWLLNTVVAA
     GKPCLFVGES GTAKSVTIAN YLAHLDSTIN IVLNVNFSSR TSSLDVQRAI EDSTEKRTKD
     TYGPPMGKRL LMFIDDLNMP RVDTYGTQQP IALLKLFIER KGLYDRGKEL SWKNMKDVQV
     VGAMGPPGGA RNPVDPRFIS LFSVFEIQFP SNENLRTIYQ AILSRHLAKL PTDEIRDQLG
     ERLTDVTLEL YNFIIDKLPP TPSRFHYIFN LRDLSRIYEG LLLTVGDVFK TPEQFLRLWR
     NECLRVLHDR LISTDDKRVM TERLEALVQQ KFPNLAAHTL ASPVLFGDFK NVINELQGEG
     EVAPRMYDDL GDYNSIKPLF EDVMTNFYNR KRKPMNLVFF EDALEHLTRI HRTLRLPQGN
     CLLVGVGGSG KQSLSKLAAF TAGCEVFEIT LTRGYDELAF REDLKRLYAM LGSDNKRVMF
     LFTDAHVADE GFLELINNML TSGMVPALYD GAEKDGLIGS VRAEVEKKGL LATKESCWSY
     YVDKCRNNLH VVLAMSPVGE TLRSRCRNFP GMVNNTVIDW FEPWPEQALT SVASVFLAEE
     ALPEALRPQI VEHMVTVHQS VRTFSTRFLE ELRRYNYVTP KNYLDFINNY KRALATNRRT
     IEDTVTRLSG GLEKLIQAAV EVDAMQKELS QAQVVVAQAT KECNELLEVI STNTVDVETK
     AKAAAIKEAQ LKVDSEQIAI EKAEAEAALE EAIPALEEAA AALQDLSKDH ITEIRSYAKP
     PEQVQKVCEC VVILRNIKDV SWLGAKSMMA DGNFLRSLVE FDKDSLTDKQ VKKVKEYFKD
     PKAPLTYDSL RAISTAGAGL LKWVLAMVNY NNVARTVEPK RKKVAESEKN LRIAQKDLAS
     TKLELQSLND QLGKLRTQFE EKTAEQQDLK AKADLMERRL IAASKLIAGL GSERERWTRD
     IADLESRRDR LIGDCLLTSS FLSYTGAFTA TYRHAMVYEM WQDDVKARGV PVTQPFRLEA
     LLTSDVETTG WASEGLPSDE LSIQNGILTV RANRWPLCID PQMQAVNWIK SREGKMLEGK
     VKTFNDSDFL KQLELSIQYG FPFLFENLDE YIDPVIDPVL EKNLVPGDGK FVIKLGDKEV
     EWDSNFRLYM TSKLSNPHYG PEISGKTMII NYGVTQQGLT EQLLNVTLRH ERSDLEEARE
     ALIKQMSENK ATLQALEDTL LRELSNAQGN ILDNSELIAT LESAKLKAVE IAEKLEASKV
     TAAEIEETRV RYSPAAKRGA ILFFVIAGLS AITNMYEYSL ASFLVVFNGS LHSSRRDASI
     EGRLRNIIDT LTYDVYAYTC LGLFERHKLM FSFQMTCKIL EGDTPLDPQL LDFFLKGNLS
     LEKAARRKPF DWFPDAGWQD LMRLVELGQK KIGADGRMHA LGSLANDVES DEAAWRTWYD
     LEAPEEAELP CGYQSFLSDF EKLCLMRCLR MDRVTVGITR FVIGVMGEKY VQPPVLEYRS
     IYKQSTETTP IVFVLSPGAD PAFDVFKLGE EMGFRPGAKL KYMALGQGMG PKAQELIETG
     ATRGLWIMLQ NCHLLPTWLK TLEKILEKIT KPHADFRLWL TTELTDRFPL GVLQRSLKVV
     TEPPNGLKLN MRQSYSKITE EVLADCPHQA FRPLVYVLGF FHAVVQERRK YGKLGWNVPY
     DFNETDFRIS MALISTYLTK AWDAQDDLIP WGTLRYLIGE AMYGGRVSDS YDRRILTTYL
     DEYLGDFLFD TFQPFRFYAC KDYEIAIPQT GSRDTYLKAV EALPLVQSPE AFGLNANADI
     SYYTSATKAI WTDLVDLQPR TGGGGGGVAR EEFIGGVARD IAAKIPEPFD LPQLRKELGT
     PSPTQVVLLQ ELERWNSVLG VMVSSLRDLQ RALSGEIGFS SRLEELASSL YNGKLPAMWA
     RLNPATEKAL GAWMLWFGRR YRQYKDWTEH GEPKVIWLSG LHIPETYIAA LVQAACRDKG
     WPLDKSTLYT KVTKFTDPYQ VSERPKYGCY MSGLYLEGAA WDLEASQLRK QDPKVLVNEL
     PILQVIPIEA NKLKLANTFR APVYVTQARR NAMGVGLVFD ADLASAEHSS HWVLQGVALV
     LNIDQ