GenomeNet

Database: UniProt
Entry: A0A139WBF9_TRICA
LinkDB: A0A139WBF9_TRICA
Original site: A0A139WBF9_TRICA 
ID   A0A139WBF9_TRICA        Unreviewed;      4209 AA.
AC   A0A139WBF9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Dynein heavy chain 2, axonemal-like Protein {ECO:0000313|EMBL:KYB25181.1};
GN   Name=AUGUSTUS-3.0.2_31238 {ECO:0000313|EMBL:KYB25181.1};
GN   ORFNames=TcasGA2_TC031238 {ECO:0000313|EMBL:KYB25181.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB25181.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:KYB25181.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB25181.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:KYB25181.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB25181.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00008887}.
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DR   EMBL; KQ971372; KYB25181.1; -; Genomic_DNA.
DR   STRING; 7070.A0A139WBF9; -.
DR   EnsemblMetazoa; TC031238_001; TC031238_001; TC031238.
DR   eggNOG; KOG3595; Eukaryota.
DR   InParanoid; A0A139WBF9; -.
DR   OMA; MYPALIN; -.
DR   Proteomes; UP000007266; Linkage group 9.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis 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:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.287.2620; -; 1.
DR   Gene3D; 1.10.472.130; -; 1.
DR   Gene3D; 1.10.8.1220; -; 1.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.20.1270.280; -; 1.
DR   Gene3D; 1.20.58.1120; -; 1.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 6.10.140.1060; -; 1.
DR   Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
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; 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; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR45703:SF32; DYNEINS HEAVY CHAIN; 1.
DR   Pfam; PF12774; AAA_6; 1.
DR   Pfam; PF12775; AAA_7; 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; PF18199; Dynein_C; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Dynein {ECO:0000256|ARBA:ARBA00023017};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          1849..1985
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2128..2264
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2463..2610
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2808..2866
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3038..3100
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3351..3378
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4209 AA;  485467 MW;  6E1384AC0697596A CRC64;
     MTTPSPLDEA EEKDSLFSDK SEDKAVKIQT PEAETSEHVK VSYTDEDLDK LVGFVRNLTT
     LYDLRPDDWK EENYEVIKRF FLTPTEPILT IYFVNDDLIC SLGPPVKSVM DLTYFLRQPF
     EVFEVATFFD NINFGTMDDN IEGSILNIVE NIYAPVFFKS NHWPESVKND FSHNLHMFLS
     KFTDVHSRLF GLTVLYIPRE ALDIPVDVAS LDKELVKRME AIVVYWTKQI RVGLQDQDQN
     TPDDLLTPLD EYDFWVYRFE NLSGLNYQLT NESLKHICNI LIAVQSTYVH QFLILADEIE
     RNVKESMSNI EYLAVLRKPC TELSEIENPN EMHTKLAEIL HLIRFIWMNS PYYNTIEKIT
     SLCRALSNQV ILQCTKYINM DILFEEKKSR EGIKMFETCI ECLTNYIRTY VLISESHTMF
     GPSPWLLDKA PIFNHVDSFI QRCKDMIEIC EAMINFGRHD ETEEIPKPNF GGSRRIEFLN
     WCNKVEDMFA ESLKSVQEVK HLILDVQVST WYDQMLQFKN RMKDIEVVIE NLTNAVFEEV
     ANVEEGIESL AALYNYSKRE SLKALFDGKT LFVYEMFKEE IHGVKKELTE SEMYPARLPY
     YAGRAMIANM KKNRLVLIRK FFDDAKWMLP CSVSQEIFSQ YEKLVSSIDE RILGLYRKWN
     DRLGEDVAKR LHRPLMCKSI SKPGLLECNI DRSLLEIFTE ARYWESLNYE VPSHIKSVYD
     KANNVRFVYE SVLAVVLDYN KILASLSDDE RLLFKPLITI VEKKIAPGLS KLTWASEVSD
     EYIAECSHNT AELQQFLDDY KSCNLQIVTI CEKVCDTYMF RITPNYVFNI RELIIEISTQ
     LEKTMEKLVI HYQNIIQFLI LVFEGFENYM TVMANQWITY INNFDTLVEE ALKISCRNTL
     NHMYECLHGD DTLGPNPVLE LTASLKANRI NFEPTLSEVA KVVHNILPNM VEALTTLPRL
     NDKFHVAETD FTPYWGIIEQ DAECQKIQKM LNDEMSLNVK KIQEYMTIWE PFRDLWEIDK
     DLFMTKYETE NPTAAQFDAN IGRYTEVANN VQIQEGVTVV HFIRINCSEL KKSIIEHCLQ
     WQMKLCQLLY KLTVRNIDDV YEYIKVNTEA VLKEPQNLIE MEKAIALHER LVNEVSQKEE
     TFPFITDQML VLEKYNVSVS NEVRNREKAI PNEWSRYLDV LSDADKMLGY SKDTFKTRLL
     EDAEVLKKDG KKLLDDFLAT GPFSSDWSAE DALKYIADIK AKLAYLREHE KDLRGDLGIF
     GLSLPDTIEL TKLEREIAAI ELVWQLTDEW NKAWEKYKSG EFWTIETEEM EVTAQTLFRK
     LTRLSRELKD KNWEIVDHTR QRVDAFRRTL PLIGDLKNPS MRPRHWDRVR KVVGKDFDEN
     GPEFNLEAIY AMEMHKYAEE INDISNAATM ELQIEKGLAN IAHIWKDIKI EMVPHKDKGL
     YRIKSVEECF QTLEDHMLQL STMKSTRFVE PFAKEVDYWE RTLSYILETL EAALTVQRQW
     LYLENIFFGE DIRKQLPRES EGFDRLSEEW KNITIHMHAG KTAMKATQYE PAPYLYNKLN
     RMNDKLELIQ RALERYLETK RHIFPRFYFI SNDDMLEILG NSKKPEAVQP HLKKLFDNLT
     KLKMQRNLVT GKQEAMGMFS EDGEYMDFTK LIVLDGPVEM WLLEVEAQMR AALKKEFKPC
     RSALKKMLSK RDKWLLSYCG QLCNACSQIQ WTTDCTKALV HAKITDSKKP LKKLRKKQNQ
     VLSKLSELSR RELTKLQRLK ANALITIEIH SRDVIDKMYK ANCRDTNSFE WFSQLRFYWD
     RDLDDCVIKQ TNTAFMYGYE YNGNSGRLVI TPLTDRCYIT LTTALHLFRG GSPKGPAGTG
     KTETVKDLGK AMGMWVIVNN CSEGLDYKSM GKCFSGLAQT GAWGCFDEFN RINIEVLSVV
     AQQILSILSA IARKMKQFVF EGTEINLKLT CGIFITMNPG YAGRTELPDN LKSMFRPISM
     MVPDSAIIAE NILFSDGFQN TKTLSKKVFT LYQLAMQQLS KQDHYDFGLR SMVALLRYGG
     RKRRQFPHFP EDEIIYLAMR DMNIARLTSD DLPLFNGIMS DIFPGVSIPK VDYVDMTDAI
     VSHMKENGLQ PIENAITKII QLYETKSSRH SVMILGQTGS AKSTTWKTLQ GALGILHKAG
     KPGFNVVHVY AINPKALNLG ELYGEYNLST NEWLDGVISA VMRTTCAEET PDEKWILFDG
     PVDAVWIENM NSVMDDNKIL TLINSDRITM PEQVSLLFEV GDLSVASPAT VSRCGMVYND
     YKDWGWLPYV TSWVQKQHKR GKEFQDIMMD FFHVYLQKIL DFKRLHCEEA AGCVELNLVM
     SLCKLLEILA TVENGVNPHD EDNFADMAKN WFLFCLIWSV CCTTNEEGRK KIDNFIREKE
     GVFPIKDTIY EYFVDVPNKS FALWEVKLPY DWKYDPGCAF FEIIVPTVDT VRYEYITNAL
     LSHGYPVLLT GPVGTSKTST AQSVLASLSS EKYTVLNINM SAQTSSLNLQ EAIESRLEKR
     TKGVYAPVGG KLLITFLDDL NMPAKETYGS QPPLELLRQW LDYNFWYDRQ KQTKKFVINM
     HILAAMGPPG GGRNVISERL LSIFNVINIT FPDETNILRI YGTMLGQHLA DFNEVVKIVG
     REITETTIDL YNNIKSKLAN AAKKAGVFPT SEAMYNFLIK RVRANLHIII CMSPIGDAFR
     NRLRQYPALV NCTTIDWFCE WPKVALLEVA NKYITDVNFV QTITGEVLGK RRASVLLSSQ
     DRLREAVAST FATIHDSVAK CARRMAIEMK RHSYVTPTNY LELVAGYKKM LQEKRDEVSA
     QANKLRNGLW KIEDCRNKVQ SMSIELEEAQ VKVAEFQQQC DEYLVIIVAQ RKQADEQQKE
     VTQKSIKIRE DEVQCQKLAD VAQADLDEAM PALEEAIRAL DSLSKKDISE MKSYGKPPAK
     VEMVMEAIMI LKQVEPTWAE SKRQLGEINF LKDLKDFDKN HISDRTLKKV ANYTQNPEFI
     PEKVGTVSFA AKSLCQWVIA IEKYARVWKI VEPKQMKFDE AMASLREKQA MLAEAQAKLA
     ELNIMLARLQ KEYEEKLEQK EELNRKAELL KIKLERAYIL VECLAGEKTR WEETVAKLDI
     SFDCLPGDCL LATAFLSYLG PYVSNYREEL MEMWKNEVAT LEIPYSTNFE IISFLTDPTT
     VREWNLQGLP ADGFSTENGI IVTTGQRWPL VIDPQCQAQK WIKNMEAVNN LKVVDFGMHS
     YMKILEDAVQ NGKPVLLQNI LETMDPSLNS ILAKAVVKQG GMNLIKIDDK MVSYNDDFRF
     FITTKLTNPH YPPEISTKTT LVNFAVKEQG LEAQLLGIVV RKERPQLEEQ KDKLVTAIAK
     GKRQLIDLEN ELLRLLNETR GSLLEDAELF NTLQTSKATS IAVAKSLETA ETTEVQIDMA
     REGYRPCAER ASILFFVLND LGRIDPMYQF ALDSYIFLFE KSIQNSTKSQ ILSERIMELN
     DYHTYSVYRN TCRTLFEHHK LMFSFHMCVK ILENMGKVVK AEYNFLLRGG VVLDKENQMD
     NPCAAWLSDE GWDNITELDK IAGFHGIIDT FEQYPREWHA WYTHTEPETL PLIAEWNEIC
     NNFQKMLFIR SLRQDRMSFC ITNFIINQLG SKFVEPPVLD IKAVLEESVA QTPLIFVLSP
     GVDPTTALMQ LAESAGMMGA FQSLSLGQGQ SPIATRMIQR GAKEGHWVFL ANCHLSLSWM
     PQLDKIVETL QTGKINPRAN LTRLYQLITE EQFSVCQCQE KYKKLLFSLC FFHAILLERK
     KFQQLGWNVI YSFNDSDFEV SENLLTIYLD EYENTPWDAL KYLIAGVNYG GHVTDDWDRR
     LLLTYINQYF CDDVLNIPYH RLSSLPTYYI PRDGSLQTYQ DYVRLLPTID RPEAFGQHPN
     ADITSLITES RMFCETLMSL EIQSSSGESE SQEDKVSQLA AEVLSKIPNP IDYETTEKLI
     GVDKKPLDVV LLQEILRYNT LLVDIRTSLD ELQKGIKGLV VMSSQLEEIF TCIFEGRVPS
     DWLKAYASLK LLGSWTRDLI ARVEHFETWA STTHPPMFFW LSAYTFPTGF LTAVLQTTAR
     ANEVPIDTLS WEFTVITVDE SQLIERPENG VYVKGMFLEG AGWDRKNACL IEPQPMQLVC
     AMPVIHFKPQ EVLKKKTRGL YSCPCYYFPI RTGAPNRPAF VVAVDLKSGA ENADFWIKRG
     TALLLSLSN
//
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