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Database: UniProt
Entry: A0A6J1R2A5_9HYME
LinkDB: A0A6J1R2A5_9HYME
Original site: A0A6J1R2A5_9HYME 
ID   A0A6J1R2A5_9HYME        Unreviewed;      4744 AA.
AC   A0A6J1R2A5;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=Dynein-1, subspecies f {ECO:0000256|ARBA:ARBA00077719};
GN   Name=LOC112464273 {ECO:0000313|RefSeq:XP_024886930.1};
OS   Temnothorax curvispinosus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Temnothorax.
OX   NCBI_TaxID=300111 {ECO:0000313|Proteomes:UP000504618, ECO:0000313|RefSeq:XP_024886930.1};
RN   [1] {ECO:0000313|RefSeq:XP_024886930.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole body {ECO:0000313|RefSeq:XP_024886930.1};
RG   RefSeq;
RL   Submitted (MAR-2025) to UniProtKB.
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. Required for assembly of the I1 inner arm complex
CC       and its targeting to the appropriate axoneme location. Also required
CC       for phototaxis. {ECO:0000256|ARBA:ARBA00054075}.
CC   -!- SUBUNIT: The I1 inner arm complex (also known as the f dynein complex)
CC       is a two-headed isoform composed of two heavy chains (1-alpha and 1-
CC       beta), three intermediate chains and three light chains. I1 occupies a
CC       specific position proximal to the first radial spoke and repeats every
CC       96 nm along the length of the axoneme. {ECO:0000256|ARBA:ARBA00063032}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton, cilium
CC       axoneme {ECO:0000256|ARBA:ARBA00004430}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00008887}.
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DR   RefSeq; XP_024886930.1; XM_025031162.1.
DR   GeneID; 112464273; -.
DR   OrthoDB; 64868at2759; -.
DR   Proteomes; UP000504618; Unplaced.
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-ARBA.
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   FunFam; 3.40.50.300:FF:000153; Dynein axonemal heavy chain 1; 1.
DR   FunFam; 1.10.8.720:FF:000005; Dynein axonemal heavy chain 10; 1.
DR   FunFam; 1.20.1270.280:FF:000005; Dynein axonemal heavy chain 10; 1.
DR   FunFam; 1.20.920.30:FF:000007; Dynein axonemal heavy chain 10; 1.
DR   FunFam; 3.10.490.20:FF:000006; Dynein axonemal heavy chain 10; 1.
DR   FunFam; 3.40.50.300:FF:000884; Dynein axonemal heavy chain 10; 1.
DR   FunFam; 1.10.8.1220:FF:000001; Dynein axonemal heavy chain 5; 1.
DR   FunFam; 3.40.50.300:FF:002141; Dynein heavy chain; 1.
DR   FunFam; 1.20.58.1120:FF:000008; Dynein heavy chain 10, axonemal; 1.
DR   FunFam; 1.10.8.710:FF:000002; dynein heavy chain 17, axonemal; 1.
DR   FunFam; 1.20.140.100:FF:000001; dynein heavy chain 17, axonemal; 1.
DR   FunFam; 1.10.287.2620:FF:000002; Dynein heavy chain 2, axonemal; 1.
DR   FunFam; 1.20.920.20:FF:000001; dynein heavy chain 2, axonemal; 1.
DR   FunFam; 3.40.50.300:FF:000044; Dynein heavy chain 5, axonemal; 1.
DR   FunFam; 3.40.50.300:FF:000049; Dynein, axonemal, heavy chain 5; 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; 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.
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; PTHR22878:SF63; DYNEIN AXONEMAL HEAVY CHAIN 10; 1.
DR   PANTHER; PTHR22878; DYNEIN HEAVY CHAIN 6, AXONEMAL-LIKE-RELATED; 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; PF08385; DHC_N1; 2.
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; 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   Flagellum {ECO:0000256|ARBA:ARBA00022846};
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:UP000504618};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          2074..2212
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2355..2641
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2719..2872
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1014..1041
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3375..3406
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3533..3626
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..27
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..258
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4744 AA;  546940 MW;  242B61739D0EDCAA CRC64;
     MSTSTLHTSS VQDSSEEEEE EEEDDGEQTG SGDFLSYPKK KADLKSASID SSAVSAPPLG
     EEDKYVLTKK MVEKVRQVPV LHMICGQVDG NRADLQDVTF FYFMRTSDEG IPSFDTYEEC
     LNEITSYLVV GSLDRKFLSS LNSILVNVFK PLVENQFRTP DTGERWQTKS ADNGKRKNVD
     VEARSMLRRP SHFVTASSLV SRQNLDAKRK GDDEGNATIS VATLQDEIPR NRKQKSSLKG
     FDKRSVPSVS ESKSSKSISS KEIKKQPAGE QIKKDILDYL DNLIEKTEWT LEHVESDILL
     TMPKIPELND PAITDDMLLK NKDIVEQMEE VVMLWEKHIQ KVMESYESKV LPKKGPIAEH
     QYWQDCETGL TILVEQLKMP IVKRILTLLD QALSPIASSF HYYQTELWKH YVEARDNNKF
     VQTLLRYFKL MTESDSFESI SDCIPSLMEG LRMLWVLSSY YCHEEKIMLL MDRISWQLCE
     NVKQNLAIVL LFKKPLEEIL EKTSMASAML RQWKRSYLKT RLDIELSGKG ARWEFDQKRL
     FQNTEYIAEV CSDLYKIADV LQDFYNIFGP DLKSIINDPA QIDAVIKRVD ALVVPIEEAD
     FDIFNVFNKE NWEALTAWFY EQVTFLEDQA KFYIDECFMV LISAENSLEM LLKFKNMKTR
     AAIQRQLLRK FDVIMQQFSK EVNIVESIFH RGKWHPPLLT YHPPMAGAIF WVKQLFHGLR
     RPVLIFQEVR ELKHSELKLL AFSQYLDLAK QLKNFEEAKF NMWLDKALLT VTAIMKKSVL
     RIVRVERDSP VALTFPDEER VTKNLQLIHV ASKAKGKDVG SFLSTPRESL LKLDGVMSKP
     SAEIESSIAA GSRIISMTQP RAEVKADARG SSLKDCKTST VSFDKHDARA KIAWPEFMSG
     AILVECQLRF QVNFDWEVFE VIREAELMEH LGFELPATIR NVGIQKNRLR TDIDATTKMI
     SQYNNTLDTL DRADIQLLKQ TLQDVEKHIQ PGVTRFNWNS LSISDYASTC SRILKNLNSI
     VEQVNQIKKE LDNRIESELQ SYHLFSTKKE VADSEVLLPC KCYFTEIKNR RSELVSSMLK
     TYQSISPMLV KLESLVLGTS TGTSPAMQLL YEKYEKKIFA AFIICMVRNM EVLNKILNNT
     KPIFQVDALL ITSEVILRPS PNEIYNTICY DVRNLLERLK EFSRWMNGTC LECKPQRREL
     SEDLVVFSFF EDVMSVRIIN ELVRVVHDTA YRISMECSRY LYRWKKYSNL WSFDKNLACE
     KFASTKPTLL QYDEKFTFYE GILEELEDMS SYFDINSVRL NLKPLLSGIE RQAKEWKQVL
     GNYLLSDTVL AMSELKTQID TFRGEIELVI TGLDRFVSIM QAIADVRNMA IQAEVQFLCY
     QECFQTMRAH GIVFPLSDEA MAYELQHDWE SLYLGALYRA STLESTSEKF AELTREQIQQ
     FLVETEMFAE DFEAHGPGSI GNDLELGLKK MDEYGKLIHN YEERRLSLIK LENLFDLLST
     DYSTLLKIKT EYEGMDVLYN LYKEQRSARE IWAKTLWVNL NPQQLIEGME HFIREFRRLP
     KSIRATNVGH ALETNIKNFK NSVPLFIELK NEAMRERHWQ ELMRRTGQYF DMDPDRFTLE
     NMFAMELGKY QDIAQDIVMY AVKELAIERG VKELAEVWKS MEFNIVKHYK GTEDRGFILG
     PLDELNLVLE DNMLTVHSMA ASQFIGPFLN VVQKWERTMH TISEVLEVWV DLQRKWLYLE
     GIFVGGDIRF QLPDETKRFD DIDQAFRKIM TDTSKRLNVL ECCTIYGRKD EFEAMIAALE
     KCQKSLTEYL RNKRIIFPRF NFISDDELLS ILGSGNPMAI QEHVGKMFDN LDKFALVSDN
     MDRLMATALI SCEREVMDFR NPVSTEDQIE IWMGLALEEM KRSNRYLTKK AIYDYGKVRR
     PRTQWILEFQ GMMILVANQI WWTAEVENVF EKISQGNTRA MKEYLQQLNT QLDEVVTLMG
     TGTLTNNDRK KIDMVLTIDV HIRDIIEGFV RDSIVDPTEF KWESQLRFYW VHDLDNVWMN
     QCTGTFEYGY EYMGLNGRLV ITPLTDRIYL TITQALSMHL GGPAGTGKTE TVKDLAKALG
     LLCIVTNCGE GMDYITIGKT LGGLAQCGAW GCFDEFNRID SSVLSVISTQ LQTIRSALQV
     KAQRFTFENQ DIVLDTKVGI FITMNPGYAG RTELPESVKA LFRPVVCIVP DNELICQIKL
     FSAGFLTAKL LAKKMTVLYK LASEQLSKQT HYDFGLRALK SVLNMAGQLK RTSNDLPENV
     VLMRALRDMN LPKFIYDDVP LFLGLIRDLF PDLDCPRVRY PDFNEAVEAV LEKHGYIVLP
     EQVDKVIQLY EVMMTRHSTM VIGPTGGGKT VVIETLCRAQ THLGKLTKLH ILNPKACTVI
     ELYGTLDPTT RDWTDGLLSS IFREINRPLD PGKDERRYIL LDGDVDALWI ENMNSVMDDN
     KLLTLANHER IKLQNHCSLL FEVGDLQYAS PATVSRAGMV YVDPKNLGYQ PYMDKWIQAQ
     SKADQDFLRE MCEKYVHGSL RLITEGMLGL QAVEPLQTII PQTGLNMVTQ FCYVFDGLLS
     SLKDELTRKK SEVDQEEEDS LLTTKEELWE AMYIQACYWS FGASIVNEAR SKFDEYIKKI
     CGLILVQDTP TKPATAKSIP VSFPTIYDYI LDVNKRVWMA WKWLVPAYLH DREKNFSDIL
     VQTIDTLRTT WFINLMQNQQ RPVLLVGETG TSKTAIIREF LRNLNPEKYE QLLINFSSRT
     TSMDVQRNLE SAVEKRSREI FGAPPGRKLI VFMDDMNMPI VDIYGTQQPI AFLKLLFERG
     GFYDRGRDLN WKYLKDIYYL AAMGEPGGSR NEVDPRFISM FSVCNVTFPT SETLNYIYTS
     ILSGHLQTFS EAIQSIANGL VQLMLELYKT VRKELLPTPS KFHYIFNMRD LSRIMAGLLQ
     SHPDFFSGVK QFVRLWRNEV TRVMCDRLIS VQDENLVIEQ LNGKIRNYWE QEPEVIQYSL
     RDPILYGDFR NACNEDEPRF YEDLLDYEAV YNLFLEIFEE YNERNRTKLH MVLFNDALEH
     LTRVHRALRM HRGHVLVIGT GGSGKKSVIK LASFAAGYQL FQIVLSRGYN ESFFREDMKN
     LYNIVGLENK KVVFMFTSAH IKDESFLELV NSMLTMGFVP ALFNDEEKDT IVTACRDAAV
     KAGFDVSKKS VWSYFGKTCT ANLRIALAMS PSGDTLRTRC RNYPGLINNT TIDWMFPWPQ
     QALVAVANVF LRDNPIVPQE YKEVIVSHIV YVHTSVLQYT VDFAAKLRRR NYVTPRHFLD
     FINTYLKLLV EKKNFINSRC ARLSGGLQKI MEASVTLTEL NKVLAVQRVK VDDQTRSCEL
     LLASIGESTD VAMEKKNLSE EKRKEIEDKK KMIAKEEAEA KQALAEAQPV LDAAKLALGE
     LEKADITEIR SFATPPEPVQ IVSECVAILR GVKDVSWKGA KGMMSDPYFL RHLQEMNCDQ
     ITLRQQQVVR AHLKKTDKLD QMQVISKAGY GLYKFVLAVL DYCAVYREVK PKIDRVQALE
     AESEKARRAL EKEERELQRL EKTIQELNAK YDIAMTERQN LQDETDLLQR RLSAADKLIS
     GLSSENERWR KDLEILQDDL EKITGNCLLG ASFLAYSGPF SYEFRNEMYS DWERSILEKE
     LPLSKPFKLE TQLSDDVEIS KWNSEGLPPD ELSVQNGILT MKASRFPFCI DPQQQALNWI
     KKREQKKTLK ILSFTDADFL KQVELAIKYG LPVLVQDADE VDPILVNVLS RNVQTVAGQT
     FVIFGDKEID YDPRFRIYLT TKMTNPMLDP ALYAKAVVIN YMVTTAGLEN QLLSVVVRTE
     RPDIEEQRET LILETSENKN LLQQLEDSLL REIAADQGTM VDNIELIETL ENIKSSANDV
     MKKLLLAEVT SADINKLREN YRPVAERGAI LFSVLVDMAT VNAMYQYSLI SYVEVFIHSL
     KRSLPDPVVA KRLKNIIPML TKNVYDYGCT GIFARHKLLF SLQTCVKIEQ SMGNVNQKQL
     DFFAKGSTVL ERSPRSNPTR WLPLSGWEDI LKLASGFPEK FEQLPEELRD YEDEWKKWYD
     SDTPELEELP CDYSVRLTSF ERLMLIRCFR VDRVYRGIVN YIIEIMGEQY ITPPHVSFDM
     IFDESTPTMP VVFILSPGSD PTAELMKLAD RYGCGGGKFR HLSLGQSQDK IAMELLKTAI
     TRGQWLMLQN CHLLLSFTKN LEKIVENLEK PHPDFRLWLT TEPTPNFPIG ILQQSLKVVT
     EPPSGLKLNL QNTYFNMRPQ LLESCPHPLY KHLIYVLAFY HAVIQERRKY DKIGWNIKYD
     FNESDFNVCV TILDTYLTKA LATNESRVPW NSLKYLIGEV MYGGRVIDSY DRRVSYTYMD
     EYFGDFLFDE FQPFHFYKDD FVDYVIPPEG GRDDYLRFID ELPLVNSPEV FGLHPNAEIG
     YFTQAIKRMW RHLIELQPQT AVSLTGVSKD ESIDNVAREI LTKIPAPYDI SKVKRNFGVA
     VTPTAIVLFQ ELERFNKLIE TITRTLNQLR KAIAGEIGMD AVLENISVAL YNGTLPKEWA
     RLAPDTRKNL AGWMDHFQKR IDQYTNWSGA NEPVVLWLSG LHVPETYLAA LVQMACRKNN
     WPLDRSVIYT TVSKFSKPDD VEERPDQGCY VYGLYLEGAR WDIEEHRLKR SHPKVLIEEL
     PILTIVPIEV HRLKLQNTFK TPVYTTSNRL NALGVGLVFE ADLATPEHIS HWILQGVCLV
     LNTD
//
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