DYHA_CHLRE
ID DYHA_CHLRE Reviewed; 4499 AA.
AC Q39610;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dynein alpha chain, flagellar outer arm;
DE AltName: Full=DHC alpha;
GN Name=ODA11; Synonyms=ODA-11;
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], AND SEQUENCE REVISION.
RC STRAIN=21gr / CC-1690;
RX PubMed=9186009;
RX DOI=10.1002/(sici)1097-0169(1997)37:2<120::aid-cm4>3.0.co;2-c;
RA Mitchell D.R., Brown K.S.;
RT "Sequence analysis of the Chlamydomonas reinhardtii flagellar alpha dynein
RT gene.";
RL Cell Motil. Cytoskeleton 37:120-126(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1142-4499.
RC STRAIN=21gr / CC-1690;
RX PubMed=8006077; DOI=10.1242/jcs.107.3.635;
RA Mitchell D.R., Brown K.S.;
RT "Sequence analysis of the Chlamydomonas alpha and beta dynein heavy chain
RT genes.";
RL J. Cell Sci. 107:635-644(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; L26049; AAA57316.2; -; Genomic_DNA.
DR PIR; T08164; T08164.
DR SMR; Q39610; -.
DR STRING; 3055.EDP01520; -.
DR PRIDE; Q39610; -.
DR ProMEX; Q39610; -.
DR eggNOG; KOG3595; Eukaryota.
DR eggNOG; KOG4152; 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:0003824; F:catalytic activity; IEA:InterPro.
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:0030030; P:cell projection organization; IEA:UniProtKB-KW.
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; 2.120.10.80; -; 4.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR042228; Dynein_linker_3.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011498; Kelch_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
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; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 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; PF00630; Filamin; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF12777; MT; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00382; AAA; 3.
DR SMART; SM00557; IG_FLMN; 1.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 2.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Flagellum; Kelch repeat;
KW Microtubule; Motor protein; Nucleotide-binding; Repeat.
FT CHAIN 1..4499
FT /note="Dynein alpha chain, flagellar outer arm"
FT /id="PRO_0000114648"
FT REPEAT 29..84
FT /note="Kelch 1"
FT REPEAT 86..135
FT /note="Kelch 2"
FT REPEAT 137..183
FT /note="Kelch 3"
FT REPEAT 199..245
FT /note="Kelch 4"
FT REPEAT 253..304
FT /note="Kelch 5"
FT REPEAT 307..358
FT /note="Kelch 6"
FT REPEAT 425..534
FT /note="Filamin"
FT REPEAT 562..608
FT /note="Kelch 7"
FT REPEAT 610..661
FT /note="Kelch 8"
FT REPEAT 750..801
FT /note="Kelch 9"
FT REPEAT 864..913
FT /note="Kelch 10"
FT REPEAT 2269..2317
FT /note="Kelch 11"
FT REPEAT 3070..3117
FT /note="Kelch 12"
FT REGION 1..1677
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 653..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1921
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1981..2225
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2331..2577
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2679..2928
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3003..3262
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3320..3550
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3614..3687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3843..4082
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 1261..1334
FT /evidence="ECO:0000255"
FT COILED 1382..1450
FT /evidence="ECO:0000255"
FT COILED 2655..2688
FT /evidence="ECO:0000255"
FT COILED 3003..3023
FT /evidence="ECO:0000255"
FT COILED 3170..3262
FT /evidence="ECO:0000255"
FT COILED 3486..3515
FT /evidence="ECO:0000255"
FT COMPBIAS 3623..3649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1716..1723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2019..2026
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2369..2376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2717..2724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 4499 AA; 503617 MW; 319AC7FD30F1591A CRC64;
MSIFWEVPNA QGEAPCPRSG HSFTVLGERF VLFGGCGRKD GKAAAFNDLY ELDTSDPDEY
KWKELVVANA PPPRARHAAI ALDDKRLLVF GGLNKRIRYN DVWLFNYDDK SWTCMEVEGA
APEPRAHFTA TRFGSRVFIF GGYGGSGQVY NEMWVLHFGE DGFRWQNITE SIEGTGPAPR
FDHSAFIYPV TPNSDTYDKL LIMGGRDLSQ MYQDSHMLDL NKMAWENETQ PPTLPYEICN
NVCDGIESVP YHKVFSFGGR KGMMQYLNTV EVMDCGTQMW STPPVDHGVA PVGREDTAWV
FDVKTCSLLI FGGWANRWLG DLHKLNVSPI IGPPYACTAI QPEMGPVFGS TELVIRGLRF
RDGKVQVKFG LSEKNEVVVE GTYVDQETIR VQTPNYEQFG ALTVDVRVSI NGEGWTVNKI
KYAYFANTAA RNCIAYGPGL LAETISGVEV PFIIQAKDTL NDKRTSGGDV FKVTVVSADG
KNEGVSRVRD LQNGQYEVQY AAPTAGPYLI HVAFNELGTS DFVPIRGSPF TVKCTDSWTK
HRVMGAAPAK RKGATICTMG NELVLYGGDK SGVTVLNTEG AEWRWSPATV SGSTPPDRTA
HSTVVLSDGE LVVFGGINLA DQNDLNDIYY LRKQGEGWVW SCPSESRPYI RHPKGAAAVS
AEPSAEPAAE PAAEPAAEPD ADAPAAEPAA EGEEGAVPAE GEEGAEGATG SRPVSAKPAP
AAAAPAAEAL PELPVSARNS HVAVAIDKDL YVMMGDHDGD LMTELAMVDT SDRTCAHWLE
PILKGDVPVP RKACAAAATG NTIVLFGGQT QNADGEATVT GDLVIMEVTG PNSIQCAVNP
AAPGASGSPA ARYGAVMQEF SNGKLFLHGG MDAASKPLND GWLFDVPSKT WQCVYVGSSD
VVLPTGQLAT LSGNRIVLVS AAVGSPKLDS VQSLDFQELR DQAGVHAKMR ASTETLLKGL
EDWVDTQAHG MELARSPEKL SKDFENGLRK VMDALFQVKS QRSQTDLLID QLHEAFAQLA
EEKVPGINKM EKRLEAAAHK WDEIKKAQPQ VKTDVEPIQA AKGEDIKKEI ETFAAKVRNY
RADFRRRGFF KYATGFDGAY PLLDAAAHEL AELKKECDRL SELASVFEFP QAIEPVTVAI
KETVEDLVMV KDVWDTAVLC ELQFQDWRQT LWSDIRTDIM EEGAKQFVKE VKSLHKKVRD
EDVFRGVDQV VKNFLVSVPL VADLRSPAMR DRHWEQLMAT TKMTFNVKDP NFKLDDLLAL
ELHKFEEEVG EIVDRAQKEE KMEIAIRKLN DTWTRVEFQF HRHKDYDVHT VKMAEEDFEA
LEDNQVQVQG MIANRYMATF KDEILGWQKK LNDVADVNQI MAEIQRTWAY LESLFIHSEE
VKKELPQATE RFAAIDTEVK KVLREFQQLK NCVSCCNREG LYANLETQER ELEICKKALN
DYMESKRRAF PRFYFVSSAD LLDILSNGNN PMRVQIHMNK CFQAIDNVRL DSEEVVPGRR
PKALGMESCV GIEYVPFSSL PLENKVEQYM NDIIAKMRND VRMVLKASVE DYPSKPRDKW
LFDWPSQIIL VVNQIYWCLE VEQAFTEMAR GDKGAMSKYN EFQVKQLTKL IEVTRTDLSK
PDRQKIMNMI TIDAHSRDMV LAGADQPDSF QWVSQLRSYW DRDISDCRIR ICDASFPYGY
EYLGNGPRLV ITPLTDRIYI TATQACWLSL GTAPAGPAGT GKTETTKDLS AQLGKSVYVF
NCSPEMDYRT MGDIFKGLAA SGSWGCFDEF NRLVPEVLSV CSVQYKCVTD SQKKKTMLPG
RGLEYIKDGV KHPAVEHWSF IAADGVEMPL EEGTSAFITM NPGYIGRAEL PESLKALFRP
ITVMVPDRQL IMENMLMAEG FVEAKMLAKK FASLYYLLED LLSPQKHYDW GLRAIKSVLV
VAGSLLRAEA GQVEADVLFR ALRDFNIPKI LAQDMVIFMG LLNDLFPGID PPRKRDMEFE
DVIVSTIKDL GLTPEDDFVL RVVQFSELLA IRHCVFLMGP TGTGRTECYR VLAKAITKGC
NNPVNDYLKM TNKKKVVIRD INPKSISTYE LYGQVNQATR EWKDGLLSYY MRDVANMPGD
DPKWLLLDGD LDANWIESMN SVMDDNRLLT LPSNERIRVL PHMKLIFEIR DLKFATPATA
TRAGILYISE GQQWHNMAMS WINRVVKPYA ERAKWKDPQL PCTWLREMFD KYIPPTLLEM
KKSYSHITPL AQMNFISTLV NIMEGVLKPE NLSNKADQAM FEMYFVFAMI WAFGGGLVEK
DGIPYRRNFD KWFKQTWTTV KIPGKGTVYD YFVNPKTQKF QPWAELVTDI DYDGSRPMST
VFVPTAETSS LRFFLDMMVD LRKPIMFVGG AGVGKTQLVK GKLGSLNEEQ ISLSISFNYF
TDVVSFQKVL ESPLEKQPAG INYGPPGTKQ LIYFVDDLNM PKLDLYETAM PISLIRQHLG
WGHWFDRAKL TPKNINNTQY VACMNPTAGS FIINPRLQRL FMTLAVDFPG QDSLMKIYGT
FLQGHLKKFS ESIQDMGTKI LQAALALHDR VSQTFRKTAI NFHYEFTVRH LANVFQGLLM
STPEAFNSPT KWGKLWLHES ERVYADRLVS LYDLDAYNKA ATAIAKKYFS VADIDDYYKK
KDPKPLIFCH FARGLADKAY DEVADYTSLY KTLTEALNEY NETNAAMDLV LFEDAMKHVC
RISRIVSNPS GHALLVGVGG SGKQSLARLA AHICGYATQM IVISGSYSMN NFKEDIQKMY
KRTGVKGEGV MFLFTDSQIV DERMLVYIND LLSSGEIPDL FPQEDRDEIV NALRSETKSL
GLLDTAENCW ATFIQKVKTN LHMVFTASPV GENFRVRSQR FLATVTSTVI DWFQPWPESS
LFSVAKRFLD EVDLGEDAVA NAVVEFMPYS FQLVNKVSIK FREQERRYNY TTPKTFLELI
KLYKNVLAAK RKANQDNTER LENGLHKLHK VQADVDILVE EAKVKAVEVE HKVASANIFA
EQVGVEKEKV NAENAAAQVE AEKCAVIAKE VSEKQASCEK DLAAAEPLVA EAMAALETVT
KKDLGEAKSL KKPPPGVDDI TAVVIILLEN NPKDKSWQAA QKLMNNVDKF LERVKSFKSV
IDAGQVARKT VDACRPYLAL EWFNREAIGK KSAAAAGLCE WAVNIIKYYD VVQEVEPKRQ
ELAAANAKLE EANVTLAAVE EKVALLNAKV QELEQQYKEA NDDKEAAIRE SERCQRKLEL
ANRLINALAS EGERWALTVE QLRKSYEVLT GDMLLAAAFV SYAGPFTAKF RAHVIDDWIL
FLRERHMPMT EGITDPLKVL VDDALVAGWI REGLPSDPTS VQNGTILTNS ERWSLMMDPQ
LQGILWIKER ESKNNLQVTR MGASNMLQVM ERAIEAGHSV LVENMGETID AVLNPIITRS
TFKKGRSLYV KLGDKECEYN KNFRLFLHTK LSNPHYPPEI QAETTLINFT VTEAGLEDQL
LALVVNKERP DLEETKTQLI IQNTEFTIKL KELEDGLLLK LSTAEGDITE DVALIESLED
AKRVSTEISE KVKESRETEA AINENRNKYR TVAARGAMLF FLLNSLNKIH AFYQFSLNAF
VTVFSRGLDL APGGRKKGKG LKKTPSLRDQ PMDHQSLMEK ARRSSGVGDR RPSQEGLPGP
EASQASLAES QGGRGSQVGD AEDEDDESFA MAPEALEQRL VNLLETCTFT VYNYTRRGLF
DRDKLIVLSL LTFTILLRSQ AVDASEYEAL CRGMRNPTPP PITDDLSRWM AESQWAALDV
LTTLPCFAHL AKDMEKNSDD WFNWCNNEAA ERAPMPGEWG KLTEFRQLLI IRALRPDRIT
NALQNFCEHM MGSDYVNQDA FSPAAMMDES SSATPIFFIL FPGYSPSKEI EVYANKCGYS
VANGRLCLIS MGQGQEAPAE AVLDKYTREG GWVFLDNVHL MQGWIPKLER KLEIAAESAH
PDFRCFFSAE PINGAPHANI IPESILQTCI KISNEPPSDM KSNMRRAFAA FTPEQCDRPS
TPAKRVAFRA ILFGLCFYHS LLLGRKKFGV GIGTGSGSGL GFCRGYSFNI GDLTTCGDVL
YNYLEAYEQI PWRDLQYMFG EVFYGGHITD SMDRRCCTTY LEVLIRNEIL PKGNPDEVEA
WEAPTLELAP GFFAPKPVDY PTLKEYIETS LPAESPVVYG MHPNAELSLL TSLGETLFKT
VVEVAGGGGG GGGGGGGGEN AVRQALETFK ERLPEPFNMV EVELRVKEKT PFVVVALQEA
TRMNALLSEM KRSMEELQLG LDGALNMSDN MEKLAKGIAS NTVPELWMSC MSTRVQEVYT
LTAWYQDVVK RHDQLSAWTA GDIITPHSVW LPGLFNPKAF LTAVMQTFAR ANKLPLDVMK
FMTEVTRMTS PEQVTEAAPL GVYVHGLVLE GARWDREDGC LRDSKPNELH PAMPVLQVKP
VTADQFNLEG YYECPVYTNM QRANVYSPVV STFTLRTQDM PAKWVLASVA LLLQDDLAG
