ID   DYHG_CHLRE              Reviewed;        4485 AA.
AC   Q39575;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Dynein gamma chain, flagellar outer arm;
GN   Name=ODA2; Synonyms=ODA-2;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=1132D;
RX   PubMed=7516341; DOI=10.1242/jcs.107.3.497;
RA   Wilkerson C.G., King S.M., Witman G.B.;
RT   "Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar
RT   outer-arm dynein.";
RL   J. Cell Sci. 107:497-506(1994).
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.
CC   -!- SUBUNIT: Consists of at least 3 heavy chains (alpha, beta and gamma), 2
CC       intermediate chains and 8 light chains.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. Cytoplasm,
CC       cytoskeleton, flagellum axoneme.
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; U15303; AAA50455.1; -; mRNA.
DR   PIR; T08044; T08044.
DR   PDB; 6L4P; X-ray; 1.70 A; B=3125-3268.
DR   PDB; 7KZM; EM; 7.50 A; C=1-4485.
DR   PDB; 7KZN; EM; 4.00 A; C=1-4485.
DR   PDB; 7KZO; EM; 3.30 A; C=1-4485.
DR   PDBsum; 6L4P; -.
DR   PDBsum; 7KZM; -.
DR   PDBsum; 7KZN; -.
DR   PDBsum; 7KZO; -.
DR   SMR; Q39575; -.
DR   IntAct; Q39575; 2.
DR   PRIDE; Q39575; -.
DR   eggNOG; KOG3595; Eukaryota.
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:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
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:0036158; P:outer 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; IPR026983; DHC_fam.
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   PANTHER; PTHR10676; PTHR10676; 3.
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   3D-structure; ATP-binding; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Dynein; Flagellum; Microtubule; Motor protein;
KW   Nucleotide-binding; Repeat.
FT   CHAIN           1..4485
FT                   /note="Dynein gamma chain, flagellar outer arm"
FT                   /id="PRO_0000114650"
FT   REGION          1..1780
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1781..2002
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2061..2279
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2384..2638
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2763..3013
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3077..3343
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3412..3643
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3857..4071
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          449..469
FT                   /evidence="ECO:0000255"
FT   COILED          804..838
FT                   /evidence="ECO:0000255"
FT   COILED          1093..1114
FT                   /evidence="ECO:0000255"
FT   COILED          1275..1297
FT                   /evidence="ECO:0000255"
FT   COILED          1699..1727
FT                   /evidence="ECO:0000255"
FT   COILED          3077..3099
FT                   /evidence="ECO:0000255"
FT   COILED          3196..3227
FT                   /evidence="ECO:0000255"
FT   COILED          3265..3343
FT                   /evidence="ECO:0000255"
FT   COILED          3569..3663
FT                   /evidence="ECO:0000255"
FT   BINDING         1819..1826
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2099..2106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2425..2432
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2802..2809
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   HELIX           3130..3141
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3145..3153
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3159..3171
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   STRAND          3181..3184
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   STRAND          3187..3190
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3194..3201
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3206..3211
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3215..3217
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3220..3230
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3237..3244
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3245..3248
FT                   /evidence="ECO:0007829|PDB:6L4P"
FT   HELIX           3249..3264
FT                   /evidence="ECO:0007829|PDB:6L4P"
SQ   SEQUENCE   4485 AA;  512846 MW;  974B79328B403677 CRC64;
     MALDNRHRLI VGKLAEAFGL PENVIEKTLT QDKQAVNSFF TPAGPPSLVF VYQVKEDKLK
     DGSVGPVDNK PTLHRIGPHE RIHNSVYFTR LNPKGINEKT LEADMGSGEL SVLWALENFK
     AIVSDLYLPI MQEQQQWGKM STEYLEDFLS STAKFGSMLT EAVATVSGGV EPMPDPRYID
     QYGDLRPAGI TQAAGDDDTL QEMEECLTEW CREAELLLNQ TNKIKDGEER GPDTELEYWR
     TRMSNFNSIT EHLKTKECKL VLGICSHAKT KAYLRWRGLD VQITDAANES KDNVKYLATL
     EKSMEPMYQG RVTDITESLP ALMTNVRMMY TIARFYSTAE HMTRLFTKIT NQLVRRCKEQ
     IMENGKIWDQ DKVTLIGNMK VSVELANVYR QQYRLAKETL AAQPKSKQFD FDEQAIFLKF
     DLSSKALHKL IDMFTTIHQF SSLEQHTHIE GLDTMLKSLN NIIDDVKRKP YDLLDYSRNA
     FDTDFLEFNV QINDLELQLQ GFVNASFEHI TSTEHALSLL AQFQAIMQRE TLQQDLENKY
     MVIFQNYAKD LDAVQKLYEK NKYEPPVPRN APPVAGNIMW ARQLLRRIEA PMQLAQNKNL
     LAAKESKKNI KTYNKVAKAL IEFETLWHQA WIKSIEQCKA GLAAPLLVQH PDTGKILVNF
     DKEIMQLVRE AKYMQRFNIR CSSPSQMVLL QEEKFKFYHN QLTHLVREYE HVLGRGATIK
     PLLRPHLDDM ERKIAPGFAV LTWTSLNIDG YLHRFKQGLA RLEELVRKVV DLTENRVDSN
     LGAISSTLLV ELPTDRSFTY EGFVEQNRFQ KKQAELLAIR NEEVRRAIED LYTLVRNYPR
     ENTEDVLDEK EVSLLVRHYS KNMYNAIMQC TLNSLQAMKR RLGSKTTTGI FFMERPFFDV
     DVELKVPSVC MNPTLEEIQA AINQCAKKVL TISKQLPAWG MDNVATYHEM MRGDRRWVKA
     VLRLTGSVEG IKTQVGEYIR TFDKYDFLWK EDLQAAYDHF MRSNPTLEAF EAELKKYMAI
     ETEVTMINGV NNIGALSLET HPLKNSLKAE AVSWKTQFAQ NLHKQCSDDL KLDNYIRDTN
     SKFHRKIEDL EDVRNVMAVL KEVREKESEI DNLIGPIEEM YGLLMRYEVR VPKEETTMVS
     DLRYGWKKLK KVATEVSDNL TRLQVGFKRE LIKEVKTFVV DAQMFRKDWE ANAMVPGLDP
     QEAVDRLRKF QQMFEVRKRK WENYSSGEEL FGLPVTQYPE LEQTEKEIQM LDRLYSLYVA
     VITTIKGYGD YFWVDVVEKI DEMGEQVQQY QNQSKKLPKL RDWPAYNACR KTIDDFLEML
     PLFQALTHKS MRERHWKEVM RVTGHELNLA EDHFKLQHLL DCNVLRYRED IEDLTGAAVK
     EEIIEVKLNQ LKADWATANL ALAEYKNRGP VILKPSDTSE LMEKLEESQM TLGSMATNRY
     SAPFRDEVQA WSIKLSTVSE IIEQWLMVQS MWQYMEAVFS GGDIVKQLPQ EAKRFLNIDK
     NFMKIVSNAL ETQNVINTCF GNELMKNMLP HLHEQLEMCQ KSLSAYLEQK RAEFPRFTCV
     GPHLLEICRW AHDPPSVVPH FQSGLFDSLS NVTFDRIDKT RMTEMFSQQN EKVEFERPVD
     AKGNIEVWLQ RLVDGMEDTV KQIIKRAVRN VAEMPLEDFV FGHPAQVSLL GIQFQWTAET
     QMALSSAKVD KTIMNKNMKK VDALLRDMVN ITVRLDLTKN QRTNLETCIT VHMHQKESTE
     DLVKKKIKDP TDFEWLKQVR FYWRDDKDTV IISICDVDFE YSFEYLGVKE RLVITPLTDI
     CYITLSQALG MFLGGAPAGP AGTGKTETTK DLGNTLGKYV VVFNCSDQFD YTYMGKIYKG
     LAQSGLWGCF DEFNRINLDV LSVCAQQVYC ICRTRERKKS FQFTDGTTVS LDPRVGFFIT
     MNPGYAGAQE LPENLKALFR GVTMMVPNRQ IIMKVKLAAA GYQENDILSK KFFVLYGLCE
     QQLSKQAHYD FGLRNILSVL RTAGASKRQS PDKSEVFLMM RTVRDMNMSK FVAEDVPLFL
     SLIDDLFPGL KADATRPDVN KDAEKVVLER GLQVHPTWMN KCIQLYETYL VRHGIMLVGP
     SGSGKSAICE CLAAALTELG TKHVIWRMNP KAITAPQMFG RRDDTTGDWT DGIFAVLWRR
     AAKNKNQNTW IVLDGPVDAI WIENLNTVLD DNKVLTLANG DRILMSAAMK AMFEPENLNN
     ASPATVSRAG IIYVSDVELG WEPPVKSWLQ KRDPTEACWA RLFSKYIDRM LEFVRISLKP
     VMYNEQVSIV GTVMTLLNGY LKSMKEAGTA MNDAKYERVF LYCMTWSLGG LLEMKERPLF
     DQELRTFAHN MPPKEEDSDT IFEFLVNTTD AEWLHWRHCV PVWTYPKNEE KPQYAQLVIP
     TLDSVRYGAL LNLSYNVDKA TLLVGGPGTA KTNTINQFIS KFNAETTANK TITFSSLTTP
     GIFQMSIEGA VEKRQGRTFG PPGGKQMCIF VDDISMPYIN EWGHQVTNEI VRQLLEQGGM
     YSLEKPIGDM KFITDVRYVA AMNTPGGGKN DIPNRLKRQF AIFNVPLPSV AAINGIFGKL
     VEGRFSRDVF CEEVVYVASK LVPLTITLWN RIQTKMLPTP AKFHYLFNMR ELSKVFQGVI
     LATRDRFNLA AGDSAVFGGN VASPEGYLLG LWIHECRRVF SDKLISYEDK NWVDKAVFDL
     CRDNFSSDLV KQVEEPIYFV DFLREPAVMM RPVEIVTPHP SFYYSVPGGL PEVRARVEGL
     QRKFNEESKV MKLELVLFTD CVTHLMRITR LLAWPGLGLL VGVGGSGKQS LSRLSAYIAG
     PTFYITKTYN VSNLFEHIKG LYKIAGFKGQ PVYFIFTDAE VKDEGFLEYI NQILMTGEVA
     GLLTKEDQDM IVNDIRPVMK HQAPGILDTY DNLYNFFLNR VRDNLHVVLC FSPVGAKFAR
     RAQQFPGLIN GCTIDWFCPG PKKRLTSVSG KFIDKFTMAC PKEVKNQLEL LMGHAHVFVT
     AACKEYFEKY RRYVYVTPKS YLSFLQGYKE LYAKKWSFTK ELAYQIEVAC QKMFEPKADV
     NKMKAELAVK NQTAVSAKEA EALLKQISES TAIAEKEKQK VAVIVDAVTK KASEIATVKD
     DAERDLAAAK PALDAALEAL NSIKDGDIKN LKALKKPPQI ITRIFDCVLV LRMLPVTKAE
     YTDEKGRMVQ VGNYPEAQKM MNQMSFLQDL KDFAKEQIND ETVELLEPYF MSEDFTFENA
     QKGSGNVAGL CNWAESMAKY HNVAKVVEPK IAKLREAEAE LKLATKEKNA AEERMAKVQA
     KLDEMQAQFD AAMAHKQALE DDAAATQRKM DSANALIGAL AGEEARWTAQ SKEFDVQIQR
     LTGDCALASA FVSYLGPFNK EFRELLLNRD FYGDCMKLNV PVTPHLQITK FLVDDSEVGE
     WNLQGLPTDE LSIQNGIMVT RASRYPVLVD PQGQGREWIK NREEANQLKT TQLNDKLFRN
     HLEECLAFGR PLLIENIEEE LDPLLDPVLE RRLVKKGKTW VVPLADKEVD FTETFRLFCT
     TRLPNPHFTP ELSAKVTVVD FTVTMAGLED QLLGKLISKE KKELEDQRQQ LLEEVQSYKK
     RIKQLEDDLL CRLSNSQGNL LDEHQELIDV LAVTKQTAQD VSEKLANASE TNKRINEACE
     EYRPVAHRAT LLYFLIAEFS VVNCMYQTSL AQFNQLYELA IDRSEKANMP SKRIHNIIEY
     MTYEIYLYVQ RGLFERHKII FALMLTNKVL TSAGKVKATD LDVFLKGGAA LDINSVRKKP
     KDWIPDLVWL NIIALSAMDA FRDIPDSVFR NDGLWRQWYD QEAPEMAKVP DYEDRLNKFE
     RMCVVKTFRE DRTLIAAADY IAEALGQRFV ESVPLNMEKR PGRRAMAKCP LICLLSPGPD
     PTKLIEDLAK KKKIKTLGVS MGQGQEVIAR KHMAAASLEG HWVLLQNTHL GLGYLTEVET
     FLVKEENVHE DFRLWITAEP HPQFPIGLLQ MGIKITNEAP VGIKAGLRAS YQWVNQDMLD
     MVSRQEWRQL LFVMCFLHSV VQEPQFGPIG WNVPYEFNQS DLSACVQFLQ NHLSEMDAKK
     APQPTWETVR YMISAIQYGS RITDDFDKLL MDTFAEKYFL QPVLQPSYEL FKDTRSSDGF
     SYRVPDSTDI ETFGSYIETL PGTESPEIFG LHPNADITFR TLQVQESIVT ILDTMPKGAG
     SGSGLSREDV VDKICEDLLS KAPPLFDKEE TKEKLKKLPG GPTLPLTVHL RQEIDRLNIV
     TRLTTTTLKN LALAIAGTIA AERGLIDALD ALFNARIPQQ WLSKSWEAST LGNWFTGLLQ
     RYDQLNKWLN LGRPKAYWMT GFFNPQGFLT AMKQEVNRKH RDKWALDDVV MSSEVTHRPK
     DFESLKEGAP EGVYVYGLYL DLRLDGRENR LMDSDPKKLF NPLPVLHVDG VLAKDKKRSG
     LYEAPKPYRV KARKGLNFIT TFSVRTEDDK SKWILPGVGI LCSID