ID   DYH1B_CHLRE             Reviewed;        4513 AA.
AC   Q9MBF8; Q9ZPC2;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Dynein-1-beta heavy chain, flagellar inner arm I1 complex;
DE   AltName: Full=1-beta DHC;
DE   AltName: Full=Dynein-1, subspecies f;
GN   Name=DHC10; Synonyms=IDA2;
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 DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=21gr / CC-1690;
RX   PubMed=10888669; DOI=10.1091/mbc.11.7.2297;
RA   Perrone C.A., Myster S.H., Bower R., O'Toole E.T., Porter M.E.;
RT   "Insights into the structural organization of the I1 inner arm dynein from
RT   a domain analysis of the 1 beta dynein heavy chain.";
RL   Mol. Biol. Cell 11:2297-2313(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1820-1901.
RC   STRAIN=21gr / CC-1690;
RX   PubMed=10069812; DOI=10.1091/mbc.10.3.693;
RA   Porter M.E., Bower R., Knott J.A., Byrd P., Dentler W.L.;
RT   "Cytoplasmic dynein heavy chain 1b is required for flagellar assembly in
RT   Chlamydomonas.";
RL   Mol. Biol. Cell 10:693-712(1999).
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, AND DISRUPTION PHENOTYPE.
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).
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 encoding the first 989 amino acids but lacking the
CC       motor domain is able to assemble I1 complexes and target them to their
CC       correct location on the axoneme, partially restores motility and fully
CC       rescue phototaxis.
CC   -!- DISRUPTION PHENOTYPE: Cells swim slowly with aberrant waveforms, and
CC       are unable to phototax. {ECO:0000269|PubMed:10888669,
CC       ECO:0000269|PubMed:9008712}.
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DR   EMBL; AJ242523; CAB99316.1; -; Genomic_DNA.
DR   EMBL; AJ242524; CAB99316.1; JOINED; Genomic_DNA.
DR   EMBL; AJ242525; CAB99316.1; JOINED; Genomic_DNA.
DR   EMBL; AJ132799; CAB39160.1; -; Genomic_DNA.
DR   SMR; Q9MBF8; -.
DR   STRING; 3055.EDP03736; -.
DR   PRIDE; Q9MBF8; -.
DR   EnsemblPlants; PNW73250; PNW73250; CHLRE_14g624950v5.
DR   Gramene; PNW73250; PNW73250; CHLRE_14g624950v5.
DR   eggNOG; KOG3595; Eukaryota.
DR   OMA; DPKMRSW; -.
DR   GO; GO:0005930; C:axoneme; IDA:BHF-UCL.
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; 3.
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..4513
FT                   /note="Dynein-1-beta heavy chain, flagellar inner arm I1
FT                   complex"
FT                   /id="PRO_0000114647"
FT   REGION          1..1806
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1807..2028
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2089..2350
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2458..2706
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2808..3059
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3107..3384
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3443..3674
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3890..4109
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          192..223
FT                   /evidence="ECO:0000255"
FT   COILED          1544..1577
FT                   /evidence="ECO:0000255"
FT   COILED          1704..1727
FT                   /evidence="ECO:0000255"
FT   COILED          3107..3193
FT                   /evidence="ECO:0000255"
FT   COILED          3301..3384
FT                   /evidence="ECO:0000255"
FT   COILED          3499..3519
FT                   /evidence="ECO:0000255"
FT   BINDING         1845..1852
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2127..2134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2497..2504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2848..2855
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   4513 AA;  510667 MW;  F2A3E10767FD6719 CRC64;
     MEPGDEGKGH QLTADATCIA WVRSKLQLLK PESLGDSDGA EWLSSVWHND VHTPVVSTFL
     MSVKATRMFA ALDGGHEGGS SPKLVLALEV PKQFEQMVYF VRDPSKFVTR ENVGSVIFFG
     VMRGGDPLHS LLNIMHGLYV PVVVANTTWP ETVKSDFTAQ MHKFMANLTE TVYEVKGKTI
     LYIPQEDLRD PKAAAKQKDL VQRLESTIIH WTRQVKELLN QQDSVDASEQ AGPLAEIEFW
     RERSVDLSGI RAQLDDGAVS SIVSVLEYAK SSYLAPFLSL RNLIHREAVA AEDNLKFLLC
     LEEPCQQLAS AHPQTIPSLL PPILNCIRMV WNLSRFYNTP ERLSVLLRKL SNEIINRCCS
     VISLPDVWSG DVDNVMVALR QSMEAGERWK ELYKRTAAAV AVRSPKPWDF DISSIFAHID
     AFLQRCNDLL EVCEAQLQFA PRTPLPVFGG TYGPEVKKSI LDIQESFQGL VQGLQALKYD
     ILDVKATRWH DDFNGFKGGV KDLEVMMANV IQRAFDTQPC LAARGELLEG FQTMAKRDYI
     RRFVEKKTVE FFALFNAEIN TVKKLFDAVK RSQPKSPILP RYAGLAKYAM NLMRRLEQSH
     KVVDSVRYTL PQVSEAADVM QQYELAHQAI EQYISNTHND WFSTIESSIA KELQACLLTQ
     DKASGGLLSM NFHKDLLSMG QEVHFWERMR LAVPLVAMEI NAQREKYRVL RDNILMVVRD
     YNKILTALDK EERKLFHDRI RYLDRRIMPG VTKLQWTADK HALEFYYREA RKFCRDADMA
     VGDYKTANSR LDAICRSISE LVLVDVEKKK IYQHAEFANL QESHHAKIKD RLVSAVDEIR
     DIMASIHRVF EQDSEEVQRE WVRFTQKVDR KLEDALRHVI KKSLQELSRL LNGDNKTEVM
     PIFHVTMVLE RTNRVELRPT IQALFDTINS VARNLILVLQ SVPRVALQLT DKQRRDMEDA
     GLPLPKPLPT LYETISADED AVLRTIMQIT SGITSIIDKV QAFLTYWEKK YRQVWEADRD
     AYIRRYEKAQ KPLSSFEADI SRYLQCIDEI RGEDGATNMR FLRIDCGPLK LTLVGHCEAW
     VSKFTGLLGQ LAATELRTLH TYFRENKDSL MLAPSTLEQL AELVGLHRRL ADERRRTEAR
     FEPLRDKYKL LERYEVGAKE EEAALLEGLE PAWTQFQALL DETAGKLERY KDNFREKVKS
     LLDTFLKDVA QLCEDFSRDA PYSSEVPTPD ALDFIQASKQ ADEDTRKRAA EIKNGMDIFN
     IPQPQYKDLA AMEKDLDFLD RIWGLKDEWE QLYYGWKDGS FTDIKVEEME EAAVRIGKNV
     AKLGRDIRQW TVWSSLKDTL DAFKRTMPLI TDLRNPAMRP RHWQNLQDHI GVRFDPHSRD
     FTLDSLVALR LDQHVEFVAE LSVNATKELA IENNIKAIAA TWSALGLDMA EYKSTFKLRS
     TEEIFTSLEE NIVTLSTMKA SKYFIVFEKD IAYWEKTLSH ISETIEIILQ VQRNWMYLEN
     IFIGSEDIRK QLPQESQMFD AVHNNFMRLM KQLYSTANCL KACTAQGLLE SFQDMNNKLE
     RIQKSLDNYL ENKRQQFPRF YFLSSDDLLE ILGQAKDPLN VQPHLKKCFE GIKKLDMHLP
     GEDRKQTISV GITSPDGEYL PFANPVITEG RPEEWLNRVE DAMFLTTKKH LYKVLEESKA
     QKKEKWVKEN QGQMIITAGQ IVWTHECEKA LADADSARKN LKLLKKKWIS YLNKLTAVTR
     SKLNKIERNK VVALITIEVH ARDVIEKLGK SNCSSTNDFE WVSQLRFYWD REKNDCIVKQ
     VLSVFYYGYE YQGNNGRLVI TPLTDRCYMT LGAAMFTRRG GNPLGPAGTG KTETVKDFGK
     ALARYVIVFN CSDGVDYKMT GKMFSGLAQT GAWACLDEFN RIEVEVLSVV ATQIAAVMQA
     IKESKKRFLF LGQEIRLNPS CGIFVTMNPG YAGRSELPDN LKAMLRPVSM MVPDFTLIAE
     IMMFSEGFSS AKVLAKKMIA IMELSQQQLS KQDHYDYGLR SFVIPIARAA GSLKRLDPEG
     SEEVILYRTM LDLIKPKLVY LDLPLFMALL SDLFPGVELP PADGGSLRRA IEAELRESNL
     QIVPEFVTKI IQVFDCKVAR HGNMIVGRTG SGKSEAWKCL QRALGRLRKE EPDDDRFQKV
     HVHTINPLAL SNDELYGCFE AATHEWQDGV LARIMRTVCK DETHEQKWIL FDGPVDTLWI
     ESMNTTLDDN KLLTLLSGER IAMTPAVSLL FEVEDLSQAS PATVSRAGMI YLNVEDLGWR
     PFITSWLAAK QAAPGADAAI IDQVSKLVDK YMEAALEHKR LHCRELVPTD RLSCVRAFTR
     LWDALAVPEN GVGTMPVDES AGPPGSKAAA AAAAAAAAAA PPEETSGGTG GNLVEMWFLF
     CLIWGIGGPL DEEGRKKFDA FMREMDTRYP SSDTVFEYFV EPKAKSWLAW ETKLTGAFKP
     AMDQPFFKIL VPTVDTVRNR FVGSALVRVS QHTLIVGNVG VGKTMIVGSL LEGLPGDRMS
     SMTINFSAQT SSNSLQDTIE GKLEKRTKGV FAPAGGKRLV CFIDDLNMPQ KSKFGFIPPL
     ELLKLWVDNG FWYDRAKCEV KHIKDMQLLA AMAPPGGGRN AFSQRVQACF ATLNVTAPND
     NQLKRIFGTI LNAKLADFDD EVKPLSEPIT MATIGIYRAV SKELLPTPSK SHYLFNTRDL
     AKIIQGMMQA TKAFYNSKEE VLQLWCHECM RIIADRMWDH ADKEWLVRQL DEKLGTTFST
     SFGTLFEAYN ETVPPFVTFM RQNVDVPVYE AVRDMVALKD LLTERLEDYA LEPGHSAMDL
     VLFRDALSHV CRIHRILGQP RGNALLVGVG GSGRKSLARL AAFVAELKCF TIEITKNYRQ
     TEFREDLKGL YRQAGVANKP TVFLFDETQI VYETFLEDVN NILTSGEVPN LFPKDELGSV
     LDELRPAAKA AGAGETADAL YGFLLERVRT NLHVVLCLSP VGEAFRERCR MFPGLVNCTT
     IDWFTEWPAD ALFEVAQKQL MDVDLGSTEV KTAVCKVFVT AHQSVENTSA KMFAALKRRN
     YVTPTNYLET VRGYKGLLAE KRTELGEKAA KLQGGLHKLD ETSVQVAAMK KVAEEKKVVV
     AQAKADCEEL LVEIVQDKRV ADEQEKQVNA EAQKIGKEAE EANIIAAQVQ QELDKALPAL
     REAEAALDVL TKKDMSELKA YAKPPEKVEM TLNAVLTVLR RPPNWDEAKK RLSDANFMQS
     LKEFDKDKLD DSLLKKIGKF TANPDFTYEK INTVSAAASG MCKWVHAMET YGYVAKDVAP
     KRAKLKSAQD TLARKQAALA LAQEQLAVVL AKVQALKDKY DTSIARKQAL EEELADLEGK
     LERAEKLVTG LAGERVRWEA SISEYNIALG CLPGDVVVAA AFMSYAGPFP SEYRDELVKH
     TWLPQVKALN IPASEHFDFA LFLANPAMVR DWNIQGLPSD SFSTENGVMV TRGRRWPLMI
     DPQGQANKWI KNMEGRGGRL KVLNLQMSDM ARQIENAIQF GQPVLMQDIL QEIDPILEPV
     LAKSFIKRGN QTLIKLGDKE VDYNFDFRLY LTTKLANPLY TPEISTKVMI VNFAVKEQGL
     EAQLLATVVK NERPDLDKQK NDLVVKVAAG KRTQAELEDT ILHLLSTATG SLLDNVTLIN
     TLDQSKTTWE EVNASLAVAE ETQKKIEAAS QLYRPCSVRA SVLYFVLNDL STIDPMYQFS
     LDAYNDLFLL SIKNSPKNDN LAERIKSLND FHTYAVYKYT SRGLFERHKL LLSLQMCVRI
     LQTANQVNTE EWQFFLRGGT VLDRSSQPNN PSQEWISEEA WDNITELDAL PNFKGVVSSF
     ESNLGEWEAW YRKGDPEASE LPAEWESKCN ELQRLILVRC LRPDRVIFAA TTYVSNALGR
     KYVEPPVLDL AETLKDSTAL SPLIFVLSAG VDPTDNLRKL ATEKGMTSRF FTVALGQGQA
     PTATRLIEDG LREGNWVFLA NCHLMTSWLP TLDKIIEGFE TKQPHENFRL WLSSNPSPSF
     PIAILQRGIK MTTEPPKGLR ANLLRLYNSV SDASYAQCKT QIKYQKLLFA LTYFHSVLLE
     RRKFRTLGFN IPYDFNDTDF SVSDDLLKSY LDSYEQTPWD ALKYLIAEAN YGGRVTDELD
     RRVLASYLNK FYCEDALAVP GYLLSPLSTY YVPENGPLQS FKDYILTLPA GDRPEAFGQH
     PNAEISYLIE DSKVLLDSLL SLQPRTEGAA GGAGTRREDV VMAIATDLLD QVPQPFNLEE
     VMKAKADDPS ALHVVLFQEV ERYNALLVAV RRSCVELQRG IKGLVVMSAD LDLIFESLYA
     AKVPAAWLKT YPSLKPLGPW TRDLLQRIEQ LATWVEETYP RVYWLSGFTY PTGFLTAVLQ
     TTARKASVPI DTLSFEFSII NLDEREINAP PKEGVYIKGL FLEGAGWDFE NGCLCEPNPM
     ELIVPMPILL FRPVENKKRT AKGIYTCPLY LYPLRTGTRE RPSFMINVDL RSGSADPDHW
     IMRGTALLLS LAT