ID B4HUB7_DROSE Unreviewed; 2700 AA.
AC B4HUB7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=GM14682 {ECO:0000313|EMBL:EDW50538.1};
GN Name=Dsec\GM14682 {ECO:0000313|EMBL:EDW50538.1};
GN ORFNames=Dsec_GM14682 {ECO:0000313|EMBL:EDW50538.1};
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN [1] {ECO:0000313|EMBL:EDW50538.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {ECO:0000313|Proteomes:UP000001292};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR EMBL; CH480817; EDW50538.1; -; Genomic_DNA.
DR RefSeq; XP_002035402.1; XM_002035366.1.
DR STRING; 7238.B4HUB7; -.
DR EnsemblMetazoa; FBtr0197667; FBpp0196159; FBgn0169603.
DR HOGENOM; CLU_000038_5_0_1; -.
DR OMA; LEDKHVN; -.
DR PhylomeDB; B4HUB7; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0005930; C:axoneme; IEA:UniProt.
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 Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.30; -; 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; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
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; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF1; DYNEIN HEAVY CHAIN; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000001292}.
FT DOMAIN 1638..1775
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2269..2415
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 2700 AA; 313585 MW; CED4FE812D2227C2 CRC64;
MQKKVAPERR PYCDPRLQDD KLRRKRTLHL PRVSQAQKKG EKRQLNDCPF YNLTYGFDQL
PLDPVKEFLQ EKISHMQTDK IVGHCNREFD FHRYDLDNVK EEYDECDDDS LQELQLEDII
MPEQFEMLRD AKDHVFNFDS TVRPSEQEIY EMTSHLLELY CNRRVRIFYP GCGTSSSLWT
NQLRRQHGSP SELIGAYRTP SARHMRVNNM IGPPKKEKFT AGDHYAFRTP QECRNELMRV
GKIIDELIEP VLKAAEHKIG HGLTKYPDPP SCKDNTNRIL KSAGILVGKK KNCYVGKCRI
HRKDFATNEE FLRCLKRMEA THFPYMQPLQ PVDPDDQKIK MMAKYRVELA KAEKLFTLKI
QKRYQCLLKS MSIVQLATYP SHLIRKAFRR INPRSALLQD AYQFIVKEKK DWPKLPPEVI
LMDYLFVGDR GVRQDLAILI IVCLIDLQED FRHYVKRSFL NYLLSSNMER RRLQLEREPP
EFPILTISPP VSWRSNLLRG KARIGEVLMT THPTVQALNR LWHDLYEDLV VVDLGQLLLA
QRPLDADTVQ VFIEKSCADV RDLLLNDWLP RCADLMNEMR GTWKDLVPMS GKYGGRAAML
FRCIHSAMSR HLNSLISKSI NYLFKVLCAF KDGNRIEKYS MFDAKLKRIP LMTLIASVVG
AHFDHEPINM GPGVRPASNI YVYDEDDADP FQQPQVNQFV ENLPDIDDVA QFELDHSNKL
YIYPYMQELP RIFTEHFKSI LAVGYEIPRL EFVMSGGEPE TKGFLLFIDE DHVDFLELCE
KVEQIVKVNW QGVHVYLKPV YKYYFGLFQK LILPMVQKVW TENNLPELGA VQELLKKLHA
VSDTTYYLRD FIPLNLFMLD NRHVKLSLRM YVREIYDFII DFYKALNWNE NRAICEELEE
MSMKAGERPE ETPEVVALQN YINDCREMRI FAIKDEIKNV LKRVVFLLTH TYLSSDELHL
NSRTFILPGE LEEVLDLSAA RLSVVRDNLE LALRERRLEF EKLLAQEKRT MDGFRIREIR
DVLTLEELKE RVDTVDLLFT TIENLSREAK AINTEETLLQ IDVSAFPLLA EIIEKMEPIE
KLWKTSYEFE KDYLIWMFER FECLNADGVR EQVENMHKIM YKLSRQLAYN PVAKRAAEQM
RMKIEKFRVY LPVLDSICRH GLEKRHWDQI SKILGRKVNP KLFPTLKDMI DVDIMSILPQ
LEEIANAAGK EYDLNNGLRI MQADWRDVMF EVLQYRDSDT HILASLDDIQ TLLDDHIMRT
QAMKRSPFIV ALGSKADDWE ARLLLIQNII DAWTQVQITW MYLEPIFSSE DIMRQMPLEG
RNFKAVDKLW RKIMKHTLKD RHVMAATEYP EMLEVFTKAI EDLETVTKGL NTYLEQKRLF
FARFFFLSND ELLEILSETK DPMRVQPHLR KCFEGIGSLT FDDNMEIVEM VSDEEERVAL
VRKINPQLAN GLVEMWLKEV EMVMLDSVKE QMREAWEDYA MVERISWVVS WPGQVVQGIS
CMAWTYEVEE AIETRELPAY LEKSNLQIAD LVQLVRTDLQ AGVRIAVEAL IVLDVHDRDV
VKYLTDCRIT NIQDFDWISQ LRYYWKVNEK NEDWVCVSMV VTDVEYGMEY LGNLPRLVVT
PLTDRCYRTL MGALKLCLGG APEGPAGTGK TETCKDLAKA VAKKCVVFNC SDGLDYKALG
KFFKGLAQSG AWACFDEFNR IELEVLSVVA QQILTIQRAI GRKVVKFFFE DTMLKLDPTC
SIFITMNPGY AGRTELPDNL KVLFRTVAMM VPDYAMIGEI TLYSNGFDMA RNLSQKIVQA
YKLCSEQLSS QSHYDYGMRA VKSVLLASAS LRRLYVDLPE PEIVLRAIVD VNLPKFLEQD
ISLFIGIYMD LFPGVELPMP QRGDILKWLH INLADRNLQA TPWYLEKILQ IYEMLLVRHG
LMIVGGSMGG KTTAYQVLAQ TLRNVSNDEE ATLKEFPVTF RIINPKAITM GQLYGRFDPV
SHEWYDGVLA KTFREQVQGP KGERAWVMFD GPVDAVWIEN LNTVLDDNKK LCLMSGEIMQ
MTKLMNMMFE PADLEQASPA TVSRCGMIYM EPSQLGWRAL HKSFINVLVN KVGLSEIYMT
LFEDMTEWLV PAALEFLPQC KQMLELSPIY QYQTFSRFFL HFLEKHKQFN QAWFQQMFLF
CFAWAYCSAL TGQGQKTFDA LLRKVIYGSN ENFPKPKYFS LNRGQMFPEK LLFLDYRFDE
AENWWTWQKS DDSASTTSNF PENAQISELI VPTKETGYIS YWQDFCISKS YAMLVVGPTG
TGKSAIITSN LLAMPKFANL VNVINFSART SAQMVQDTIM SKLDRRRKGV FGPSLGKKCT
VFCDDVAMPS KDTYGSQAPL ELLRTWLDHG YWSDLVDTTK IELVDMTLMC AMGTLGGSNF
IFPRLYRHMF VVAVDSFEDS TIVRIFTTIG DWHFSKGYPE KVALLSRGLS EAMVSVYRDA
IRSFLPTPAK SHYSFSLRDI TRVFQGIVMV PPKRLPDPEK LGRLWAHETY RVFYDRLVDQ
QDRDRLLVMA VDACKSNLRF PLEQAFGERI EPGEKLTDND LRNLFYGNYM EPDAEPKFYD
EGDTYEKLEK LMKYYLREYN SFSSTPMDLV MFRFAIEHVS RVSRVLQMPR GNILMVGMGG
SGRRSSARLA AYIADCRLMT VQVSKSYTIT DWRDDLKKIL MSASFNLNHT VFLFSDAQVS
//
