ID A0A182NV02_9DIPT Unreviewed; 4265 AA.
AC A0A182NV02;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR011503-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR011503-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR011503-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR STRING; 7168.A0A182NV02; -.
DR EnsemblMetazoa; ADIR011503-RA; ADIR011503-PA; ADIR011503.
DR VEuPathDB; VectorBase:ADIR011503; -.
DR OrthoDB; 166463at2759; -.
DR Proteomes; UP000075884; 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:0004222; F:metalloendopeptidase activity; 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; 1.10.472.130; -; 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; 1.20.920.30; -; 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; 5.
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; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR019165; Peptidase_M76_ATP23.
DR PANTHER; PTHR46961; DYNEIN HEAVY CHAIN 1, AXONEMAL-LIKE PROTEIN; 1.
DR PANTHER; PTHR46961:SF9; DYNEIN HEAVY CHAIN, CYTOPLASMIC-LIKE PROTEIN; 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; 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; PF12777; MT; 1.
DR Pfam; PF09768; Peptidase_M76; 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, 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}.
FT DOMAIN 1560..1699
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2211..2358
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 953..980
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3069..3103
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 4265 AA; 487991 MW; 715FEC72DEF982BA CRC64;
MAANRTGKEP DKTSDPRSPP IPNAVIDRSD REGDEKKWGY DLYPERRGEK YKPSWGRVLL
GMEGTESLDK IKCERNVYAC VKKSPMVKLM MGALKSSGCE IDIRRHIACE VCDTSVSGGY
DPVLNQVVVC QNIARNEGIV QGVLTHEMIH MFDYCNNNLD FKNIDHLACT EIRAANLTHC
SFLSACTQGD ASPFKIKQAH ADCVKTKALN SVLAVRKVTP EEAIAAVERV FPRCYNDLEP
IGRRIRRNSK DMYKAYMEGP MYGMKPSTDR RASAPGRKRT QDGARSVGSM ETPGPSGLLR
INRKAHPEHN TKQIWRELNM PTDCDFLGPN VFSLPEKLLR HSTKMRPSPL ARPKPDRNAD
KKKIRSYTAL RKDREDFRCR LVRLIVRKEH EKDDPENTFP NVEEREMLRY YHYIRHGIDT
VHVSPIDKRV LQRILRLIPK NLSKWKQALR DIIGEIKEDY SFAVRKAVVD FVLGDAMTKY
ARKEEITPGR LEIKELRLKW KHRYDENQAK IKRNLFSINV CSEQILELWD TTFKKMLLVN
VTDLEAKGEA YDLTEFTSTV NQQIEETRLT LSEKWYGAIK TIFQKGIKKK LIPDDSKPKM
LKKFFNSLAT LMTRQLQNLC ISSIESYTHY ICDVGRSNQG FRLTILLENQ DTLSFIPSFP
RFQIEILKII DNIIKSVKSF PRIERQIYPD LPCPHDTLRP EIPPEVINVC KERIHDVLEE
QRIGPELRMQ DFDNYMTLMN GTDIDDIERF MEKRPSFEEY CTYIQRYKKM ENDVAREIYG
VVSMGFYEFH REGLIDTLEG LAKFMQQELI AKMTADQQSG AHQLAIEYEA ISTKIITIPK
DTVELMTLKA YAIRMEETTI PEMEERLKKN LNHLLYLTDY TIFTPLEIKQ NNNTFQWYMK
MPTIFQDHKN IIAEKVIEYQ DALKRRIESF RRDLELFWQQ VKEYDSWGDI KNLQKYKKKA
TALDNKLVAA MEKIDHINEE ETAYGWELSQ YPIRKQCHDK LAPYKQLYDA GQEFMDKHDL
WMHSQVGSHD PEQIDETVGS LYRTVYKLEK HFSDSYQTQR LAHDIKNRID QFKTHMPIVQ
TLGNQGMKER HWEQVSEIIG FPIRISAELT LERVIDYGLD DYIQRFETIS ESATKENNLE
KAMIKMVNEW SDMAFVVLPY RDTGTYILAA IDDIQVLLDD HIIKTQTMKS SLYIKPFEKD
IIAWEKKLML LQDILDDWLK VQATWMYLEP IFSSPDIQSQ MPEEGRRFSA VDKIWKDLMK
SVQADTKVLV VLEIDKMSEK LKKSYGLLEI IQKGLNEYLE KKRLYFPRFF FLSNDELLEI
LSETKDPTRV QPHLKKCFEG IASLHFTDAL DITVMRSSEG EEVDLVEEVS TGKAKGQVEK
WLLDLEQSMK KSIHLKVGKS YEAYTETERH KWVLMWPGQC IQCISCAFWT LETTMCFDSE
DPLEALEEYL ETCKVQISYI VDLVRGKLAM QNRLTLGALV VLDVHARDVL LDMIEQRTTQ
VDDFNWLAQL RYYFEEQNLA TRMINSTLMY GYEYLGNTAR LVITPLTDRC FRTLFGALHL
HLGGAPEGPA GTGKTETTKD LAKAVAKQCV VFNCSDGLDY IALGKFFKGL ASCGAWSCFD
EFNRIDLEVL SVVAQQILTI QRGINAGSPT MVFEGTTLTL DPSCAVFITM NPGYAGRSEL
PDNLKALFRS VAMMVPDYVL ISEIELYAYG FLNAKPLAVK IVATYRLCSE QLSSQPHYDY
GMRAVKSVLK AAGALKLRYP DESEDILVLR SIKDVNLAKF LNQDVPLFQG IISDLFPGVV
LPQPDYAVFD AAVQRACEKH NKQCTPFFLE KVQQLYEMIV VRHGLMIVGP PLGGKTTAYR
LLADALATIE ERGEMSEHRA QYTVMNPKAI TMGQLYGQFD PVSHEWSDGI LAVSYRQYAQ
STSPDRKWLV FDGPVDAIWI ENMNTVLDDN KKLCLMSGEI IQLAATTNLI FEVMDLDAAS
PATVSRCGMI YMEPSSLGWE PVLESWKNTL PPALHSVNKQ VITQMFHRFC PLLLWFVRRG
GGLREMMPTS DANLVQSVMR LFDCFMDDYR NETYMKAVSE VDVRAQLEGV FFFSCIWAIG
GPLETESRAR FSELFRALTE KVFPPELNER FRIPVHLQVQ PLSKPFIFQI PKGGTVFDYR
FTKEGKGKWR PWAEEISQST SIQRDVPVNQ VIVPTIETIR IGALLELLVQ HGKCLLLVGP
TGTGKSVYTI DFLLKRNDTN VFKPLLISFS AQTTANQVQD IIMSKLDKRR KGVFGPPLGK
KCVVFIDDVS MPLKEAYGAQ PPIEIVRMWL DHCLWYDRKD VTAMKLVDLQ LMCAMGPPST
GNTVSPRFSQ HFNAIAMDEF DDQTLIGIFS KIVLWHLDTR GFSKEFDPCI DEIVLSTLQI
YRQARAILLP TPAKCHYLFN LRDFSRVIQG VLLSVPEGTE TLNSMRRLWA HEILRVYGDR
LVDDGDREWL FQELSTVIRE YMKEDPKVLF ERFVEGSELT ETSLRALMFC DFTNPKADTK
LYLEVMDIEE LSFVVESYLV EYNNMSKKPM SLVLFRFAIE HLSRICRIIK QPRSHALLVG
VGGSGRQSLA RIASHICSYE LYQVEISRQY GMTEWREDMK NLLKKVCSSD QHICFLFTDT
QVKEEGFLED INNLLNSGEI PNLFTNEEKS EIIEKMRQMD RQKEKSQQTD GSLVALFNLF
VTIIRDQLHI VISMSPIGDA FRNRVRKFPS VVNCCTIDWF QPWPKDALTA VATKFLSSVE
MTDMERQCCI DMCMEFHTST QLLSDEFLLR LKRYNYVTPT SYLEMIHTFK TLLDKKRTEV
LTGKNRYLTG LKQLEIAAQQ IGVMQEQLEA VQPQMKIAAE TVAHQMAKVQ ADSEVAAEQK
QMVEKDEAAA QEQAAAANAI KEVCDAKLAD AMPILDAAME ALNTLTPADI TIVKTMKSPP
VGVKVVMEAV CILKDLKPDR VQNPSGMGMV EDYWGPSKRL LGDIKFMDGL LNFEKDDIPP
KVIQKLEERV FTNENFDPEK VKAASTAAEG LCKWVIAIAK YDKVAKEIAP KKAALAEAQA
SYNSAMTILN AKLEQLRIVE ENLADLQRKL DEQIAQHAKL QANVELCMKK LERATEIITG
LGGEKDRWQT AADTLAQIYD TLTGDVLIAS GIVAYLGPFT MQFRAQQIGQ WIERCTDRGI
ICSRDFQLVN VLGNPVDIRA WNIFGLPSDA FSIESAIIIH NARRWPLMID PQGQANKWVR
NMEKANRMCI IRLTQPDYTR VLENAIQFGL PVLLENVGEE IEPMLEPILL KQIFRQGGTM
CIKLGDSIIE YNDSFKFYIT TKLRSPHYLP EIAVKVTLLN FMITQTGLQD QLLSITVARE
RPDLETEKNS LIVQGAENKR QLQEIEDKIL QVLSSEGNIL EDETAVSVLS SSKTLANEIN
EKQIIAEVTE RQIDVARLQY TPIAAHSTVL FFTIADLACI DPMYQYSLAW FVNLFTAAID
NTEKVDEVPA RLEDLRTYFT YSLYENICRS LFEKDKILFS LLLATNLQQD AGQLSTPELM
FLLTGGVGLD NPDPNPGAGW LPDRNWDEIC RLTVAFEVFG ALKAHVVDNL ESWKQYFDDD
TPHAATMPEP WNDKLSPFQK LLVLRCFRAD KLVPAIELYV AETMEPKYVE PPPFNLGASY
DESNCCVPLI FVLTPGTDPT ATLIKFADAQ GLGANRLFSL SLGQGQGPIA TKMIDEGTKF
GNWVLLQNCH LAQSWMPTLE KICESFQPDT THPDFRLWLT SYPTEHFPVV VLQNGIKITN
EPPKGLRMNV TRSFMSDPIS NVEWFEASKQ PANFKKLLYS LCFFHGLVQE RRQFGPIGWN
IPYEFNETDL SISLTQLRMF LDEYEEVPYV ALRYLTGECN YGGRVTDDWD RRCLNTILAR
FYNPEVLENE SYIFDEVGLY TVPELKEHEE FVTFIRELPV IARPGVFGLH ENADIIKDQK
ETDMLLASAL KTQNTSTGVF KETPAELVIR VSSDILNRLP AEFDRDAALE KYPTDYHQSM
NTVLVQEMVR FNNLLSCIRG SLQTARSAMQ GLVAMSPTVE EVVGAVLVGK IPAVWAKRSY
PSLKPLGSYI VDFIARLEFL QKWYDEGPPA TFWVSGFFFT QAFLTGAQQN FARKYVIPID
LLVFDNEVLA ETELTEPPED GVYVYGLFLE GTRWDREKGY LQDPVPRVLF DTVPHILLKP
MKKDDFVSRH TYRCPVYKTA ERRGTLSTTG HSTNFVIALL LNCDPGVIPD HWVMRGAAML
CQLSH
//
