ID A0A1S3KFH9_LINUN Unreviewed; 4052 AA.
AC A0A1S3KFH9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=LOW QUALITY PROTEIN: dynein heavy chain 3, axonemal-like {ECO:0000313|RefSeq:XP_013421395.1};
GN Name=LOC106181527 {ECO:0000313|RefSeq:XP_013421395.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013421395.1};
RN [1] {ECO:0000313|RefSeq:XP_013421395.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013421395.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR RefSeq; XP_013421395.1; XM_013565941.1.
DR STRING; 7574.A0A1S3KFH9; -.
DR EnsemblMetazoa; XM_013565941.1; XP_013421395.1; LOC106181527.
DR GeneID; 106181527; -.
DR KEGG; lak:106181527; -.
DR InParanoid; A0A1S3KFH9; -.
DR OrthoDB; 166463at2759; -.
DR Proteomes; UP000085678; Unplaced.
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; 1.10.472.130; -; 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 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; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 1361..1500
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2004..2151
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 730..792
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2841..2903
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 89..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4052 AA; 462378 MW; CBC0D11BD7C461FF CRC64;
MALDRAKHAE TPLLSCSKTR GLPGLPPLPR SAQRERSELY QVVLKNSEHP PIMKGTSWTL
AAPFKEEKHY RTPSESIANN YTPTASDLKM RELLKRKPPH RVEGSVKSPR RRAQQVSPRD
GVQNGIQISP RSGKQKKTKE REENGHTNGV AEEPCGSRPI TPVEQLNIMK NIEDEMRQVI
GEPSDRDMER YYYYINKGIQ KSMLAPQPPE QMKNVHKLIP DAILSKPELD GMVKDLHEEV
TGDYELSLRK CIVDYILKDP TEKERLHIAW VPRPFPQRII RAPVPWHDNY AQMKEELNTH
LFTTNPIMQE LQNLWFRSFS HLRFVKLEEL LAAELPLLPT EFESLVKKQC WDAHDILTKS
WIPSCAQLFR ERPELWEYLV PEDDNESTEL VQEFFGSVAA LMSLQLRSMV VNSLADFLKF
FEIHAAGNDF DGEFDELQFV MAQVMIIKLR VEEPKILFDP PFRECKDIIL RCFSDIIASG
EGIPRVEVEM APEMRGQKLL LRSVKIEESL VTDFTDRAME IFRVNTLGPQ KYLNTYKKYS
DLLNNKADQD VTAFLKEEHS ILAFKKKIHS YIDLWNEIAL LRITVPLSMF CLDCVDLNRE
LCDRSNRLKD RLVSFEVKEN KELNKGIIRQ YDEMSETLSG KLETTADVVE LTHYLQNSTD
VTAYKLKEEV DEAGNRLMFL LDYAIFEAED LKINSKVFKW PKSVGKVFEL AQGRISNRRE
QVEEAVRAKT QAFEQKLTEY NKEVESFRKK EIMSPEEMKN NVETLTKLHD NLEAARDELE
AINEEERLLE WELSTFPILQ AMFSAKEPYD KLWKTALNFH QKNDIWTNGP FLGLNAEEIE
NEISDMYRTM HQLTKKFADQ AGPKRIAEAN RNKIDKFKQN LPILHTICNP GIKDRHWQLM
SDAVGMNIRP EPETSLNQML EYGLTKHIEK LEEIGGAASK EYSLEKALEK MKFEWQDMQF
EFVPYRDSGV CILSAVDEVQ MLLDDHIVKA QTMQGSPFVK PFEAEMKEWT EKLLLMQDIL
DSWLKCQATW LYLEPIFSSE DIMAQMPEEG RKFGIVDSYW KDIMTESVKD PHCLVATAQN
NMLGRLNESN VLLEEIQKGL NNYLEKKRLF FPRFFFLSND ELLEILSETK DPTRVQPHLK
KCFEGIAKLE FTEEQEILGM ISAEKETVPF VSKIVPAKAK GMVEKWLIQV EEQMLKSVRD
VISKAVKGYQ ETPRNKWVLE WPGQVVICTS SIYWTSEVTA AMKEKNGMKK YLDKSNEQLV
EIVELVRGKL DGGARVTLGA LTVIDVHARD VVSSLAENNV TSANAFDWLS QLRYYWEKDV
IVRMITTDIN YGYEYLGNSA RLVITALTDR CYRTLMGALK LNLGGAPEGP AGTGKTETCK
DLAKAVAKQC VVFNCSDGLD YKAMGKFFKG LAQAGAWACF DEFNRIELEV LSVVAQQIQC
IQQAIGNRLK RFIFEGTELT LDPSCTMFIT MNPGYAGRQE LPDNLKVLFR TVAMMVPDYG
LIGEISLYSV GFVDARSLAG KIVATYRLCS EQLSSQHHYD YGMRAVKSVL TAAGNLKLKY
PKEDEPVLLL KAIKDVNLPK FLAQDVPLFE GIISDLFPGV SLPKPDYDIF LDALRDNIAK
KHLQPVPWFI DKIIQVYEMI LVRHGLMIVG EPLGGKTCSY QVLADALSDL HAAGMMEENK
VMYRIINPKA ITMGQLYGCF DPVSHEWSDG VLANTFREFA VNPSDDRKWI LFDGPVDAVW
IENMNTVLDD NKKLCLMSGE IIQMSNTMNL IFEPADLEQA SPATVSRCGM IYLEPHQLGW
KPSKQSYMEH DLPKNLTADE SGMVNDLFEW LLDPCLEFLR HECKFYINTS QIHLARSMMR
LYTCLLDEIA LSGTEGQEQL TSQQITLWLQ GLFLFALVWT IGGTLTGDSR KKFDVYFRNL
ISGSDEAHPK PKSVKITKNN SFPERGTIFD FFFEKRASGM WIDWLDTLDK GLLTVPPDAN
VSELIIHTAD TARQKFFLNT YLHHQIPMLF VGPTGTGKSA ITQSHLVSMP KEKYIPNCMN
FSARTSANQT QDIIMSKLDR RRKGVFGPPM NKKCIVFVDD LNMPAKEKYG AQPPIELLRQ
WIDHGHWYDV KDTTKLFLTD VLFVSAMGPP GGGRNDISSR FTRHLNIISI DEFDDTTMTR
IFTSIVDWHF AKGFEASFTR VGKMMVAATM GVYKEAITHF LPTPSKSHYV FNLRDFSRVI
RGVLLIPSTH MQDTDKLMRL WVHEVYRVFY DRLIDSEDRL TFFNIVKTTC QDYLKVSVDK
ILSHLSPSGK VIDDHIRSLF FGDYMDEQNK VYDEVTDLKE LTSTIEGYLD DYNSISKAPM
HLVMFKFAIE HISRVARVLK QDNGHALLVG IGGSGRQSAA KLATAMAEYD MFMIEITKNY
SRNDWRDDLK KLLLKAGGDG KPTVFLFADT QIKDESFMED ISMILNTGDV PNLYPSDEKA
EIIEKMQTVA RNEGKKMDAT PLAMYNYFID RVKQNLHIVL AMSPIGDAFR NRLRMFPSLI
NCCTIDWFQY LKCDSVLDAT VVXKXLEDSV RTSVVFMCKY FHESVRKLSE RFMDVLRRHN
YVTPTSYLEL ILTFKKLLGV KQEEILTLKN RYIVGLEKLE FAASQVSVMQ VELRELQPEL
VKTSEETDKL MTKIEQETVD VEAKKEIVAA DEAVANKAAA AAQAIKDDCE SDLAEAIPAL
EASIQALNTL KPADISMVKA MKNPPAAVKL VMESVCVMLG VKAERKPDPG GSGKMIQDFW
GPSQKLLGDM KFLDRLKTYD KDNIPPAIMK NIRETYISNK EFDPKLIKQA STACEGLCRW
VKAMDVYDRV AKVVAPKKAK LAEAEGELAV QMEKLNTKRA QLKEVVDKLQ ALNDELEAMT
QKKKELEDNI DLCEKKLDRA EKLIGGLGGE KTRWTENARV LGATYINITG DVLLSSAVVA
YLGAFTVDFR QDVTKDWHDH CVEKEIPCSP NFSLNVTLGE PVKIRAWNIA GLPVDSFSVD
NGIIVANSRR WPLMIDPQGQ ANKWVKNMER ENNMKIIKLS DPGYVRTLEN SIQFGHPVLL
ENIGEELDPI LEPVLQKLTF KVGGVEMMRL GENMVEYSQG FKFYMTTRLR NPHYMPEVSV
KVCLLNFMIT PKGLEDQLLG IVAAKEKPEL EEKKNQLVLE SAANKKQLKE IEDKILEVLS
SSEGNILEDE TAIKILSSSK TLSEEISAKQ EIANVTEKEI DETRSGYLPV AVHSSILFFC
ISELANIEPM YQYSLTWFIN LYLQSIINSE PASELEERIH NLNDHFTNSI YRNVCRSLFE
KDKLLFSFVL SIGILNGSGK IDDQVWRFLL TGGVGMDNPH PNPAPEWLTE KSWSEIVRAS
NLPNLQGLFE HVRDNIGEWK KMYDSPNPHE FKYPSPYDTL GGLDKMVVLR VLRPDKIVPA
VQEFIVDNLG QSYIEPPTFD LAGSFADSHC CAPLIFVLSP GADPMAALLK YGEDRGYSTG
NNKIQTISLG QGQGPIAANM IDNAIKDGSW VVLQNCHLAT SWMPKLEKIC EETIIPESTN
PDFRLWLTSY PSNDFPVAIL QNGVKMTNEP PKGLRANLLR SYLNDPISDP AFFNSCNKPE
KWHKMLFGLC FFHALVQERR KFGPLGWNIP YEFNESDLRI SMRQMLMFLN DYEELQLQAL
TYLTGECNYG GRVTDDKDRR LLANLLSIFY NEDIIFDDNY KFSPSGIYSA PQEGQYQSYI
DYIRSLPLNV NPEVYGLHEN ADITKDNQET NQLFDNILLT LPRQSGGGGK SSEEMIEDLA
ADVLGKLPQV YNLEKVMEQY PVLYTESMNT VLRQELIRFN RLIVVVRESL QNLRKAIKGL
VVMSSELEEV FDSMLIGKVP SVWAAKSYPS LKPLGSYVAD LLQRLKFLQD WIDMGIPKVF
WISGFYFTQS FLTGVSQNYA RKYKIPIDML NFEFEVTREE KEMEEKPEDG AYVNGLFLEG
ARWDREKMLL AESHPKILFD TLPVIWLKPA KMDSIVVENS YTCPVYKTSA RRGTLSTTGH
STNFVRYIEL PSDRPQKHWI NRGVASLCQL DD
//