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Database: UniProt
Entry: A0A369S8E3_9METZ
LinkDB: A0A369S8E3_9METZ
Original site: A0A369S8E3_9METZ 
ID   A0A369S8E3_9METZ        Unreviewed;      4905 AA.
AC   A0A369S8E3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   02-APR-2025, entry version 29.
DE   SubName: Full=Dynein-1-beta heavy chain, flagellar inner arm I1 complex {ECO:0000313|EMBL:RDD42782.1};
GN   ORFNames=TrispH2_004762 {ECO:0000313|EMBL:RDD42782.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD42782.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD42782.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD42782.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD42782.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00008887}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDD42782.1}.
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DR   EMBL; NOWV01000048; RDD42782.1; -; Genomic_DNA.
DR   STRING; 287889.A0A369S8E3; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
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-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; 6.
DR   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
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; 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:SF36; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 1.
DR   Pfam; PF12774; AAA_6; 3.
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; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell projection {ECO:0000313|EMBL:RDD42782.1};
KW   Cilium {ECO:0000313|EMBL:RDD42782.1};
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:0000313|EMBL:RDD42782.1};
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:UP000253843}.
FT   DOMAIN          1036..1498
FT                   /note="Dynein heavy chain linker"
FT                   /evidence="ECO:0000259|Pfam:PF08393"
FT   DOMAIN          1694..1808
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          1940..2024
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          2106..2205
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          2522..2583
FT                   /note="Dynein heavy chain AAA 5 extension"
FT                   /evidence="ECO:0000259|Pfam:PF17852"
FT   DOMAIN          3048..3261
FT                   /note="Dynein heavy chain AAA module D4"
FT                   /evidence="ECO:0000259|Pfam:PF12780"
FT   DOMAIN          3341..3670
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          3854..4038
FT                   /note="Dynein heavy chain ATP-binding dynein motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12781"
FT   DOMAIN          4325..4435
FT                   /note="Dynein heavy chain region D6 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF03028"
FT   DOMAIN          4478..4591
FT                   /note="Dynein heavy chain AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF18198"
FT   DOMAIN          4638..4869
FT                   /note="Dynein heavy chain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18199"
FT   REGION          146..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2055..2093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2226..2247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2482..2514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          3340..3402
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3578..3615
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          4032..4059
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        146..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2060..2093
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2226..2244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2482..2498
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2499..2514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4905 AA;  563028 MW;  570665ADE2D08C1F CRC64;
     METSKSPIEH STALKFISDY KKAVDDETVD SFQYNASALI DLAKDKQELF EEDIAIIREH
     LTRLFVTVLG EESNEWQWSR LYEVLESLQP WSSSIISHQI TYYINRINRH IITNPSTPCA
     TSISDIIKAF NSSKDTTSNN KITSAVNGSK QTENVTENAS KSPRLNKQIP ARNPLKEEDN
     PYVLKIRDNQ SYIPDDELKF RDINESLPVV LQEISQRESA WPNPVGATIA AMKLNLPDHV
     KETGEKADSI DRGSKDNLIS ISISPRTKKI LKDSRAEELK INTEIKTGWD ILKLFAAGRH
     TGRLQFAYLN FDDSTKDFRP YDLVAVPKNK INPEHFVMSC YGVLHVYPDQ SAESLTLDEW
     QKEATIFNAI TKIFFFRNFL LRKLFLRWRR NSKYSQFYKT RQIISRDLLL NNNSFYSAIS
     QISSLLVDLE TIEFLPLDEH TCFTLADFVE FCQRTREKAD KFIRKFFTYS QKIMDKTFES
     SLDRLKHYEA LCKKKQPITK ESLYIMKQKA DKRQQDLEDA KNEVRRLSHL ASLIDYLTIE
     SLVKMSRANI TKFVTKTLSD ESTRRDALFK ADLVFNSEDQ LMLQPFQRHF RKIIASMLND
     IPSILCEMIK TSQSPDEPLV LQTLTNSSSF MQSPLPRISS VMNQAQDTTE VNDLEESQNQ
     QNTNAKRGVA FAPTPSNQGK EFMRLPTPTK SPSIQFSDSK RDLSTREEYV VKPNYNIEVQ
     GHSIIAQHTP LSKRNLEEKL HLDILIQEYN QKQSLLVEED LADIDQFCAK YEWLCEIHAF
     VRQWGNNQMN ELNKVNPQVF KEQFQIISQW IERVQEVPDS FITSNKLFNI HCKGIEYALL
     PRLKQIFKNL DNLISEKYHT LAVGFIRGID SLTTEMYERK FDIEKFAKFV HRVSQTNESQ
     NQLEDDLNNI KFYYEVIRKH CHQPTTEESH LLSKLNSCWR IFSVSLLDAV EFVDSEKPIM
     IEGLEEKIKA LAADAEDIGK DATSGIFLDP DQSPSHALTL MRDLRNEFQD IRTSLLNLSK
     WRESITGRPY DFSRLTAILK NIDIRQEMWK YIEVSEGRIR DWMNTSFYKL DVTKLIHKVN
     EWKNASVQLR NQLPIGDRVL DYWKKSLVDI ERHTPFLAKL STKSLKVRHW KDIFIGIGQP
     YDSTWLFTTK ELLSFDLELH TSLINSVVAR ADAEFALEGS FQQICKVWED KKLQLTKHIP
     IVQVSNVNQT PMSTDSNVNE IAKQDSRMDD DALVLMGVEE LKVQLEDHQI TLRGMLVSSH
     LADLRYQVEA WSTMLQQLNE IIDSWSNCQQ KWLLLYNVFQ RKRIKTDLSK QYQEFEKINS
     GYKDFLRSVV ENPKVLNLVN RRRSQKAHKD VHGENLLQLL FNYSDTQDQI IKHLYFLLEE
     ARNEFPRFYF ISNHQLLDIM SYADNPSALA QFVNHCFPGI LSLKLILPEQ TISVMRNTTN
     EINAAFNAHL LQVSALEGNL DEVIELTTRI KAESQPHKWF AAVETGMKES LAIILQDCLH
     SRLDGMKAPD DISSLNKLHY VIESKLTGQL QYWRYGDNII SYFMRYPSQC IELVEAIVWA
     QCVLLTCSRV TPVRFTDIKE WLISNINFLV DNLNTGIKYR VAEHAQKRIT LLITSLITRA
     VYHRDVMDRL NEFASYSPRS FEWQSTLRYD IKYMKESISP KQRYKFANQS ELSQMFNLMH
     IDCNLNIVGR QIQYGYEYSG PYSRLVLTPL TERCFIAMAS AISNYQCGAI TGSAVFGKAE
     TIRELGLSTA HHSVIFSCSS FMDISNFSNL LTGVLKSGSW LNLLRVDLLP TNVLSVLSHY
     LNQLRDGLKC LDLSQSSQYS QRGKTVYQLD YDFNEGLEEI LIPIYSRRNS INTLHSFISK
     KEDSSHHQRS TPLLHQLQRR NSTGSLSGSI QTAHRPMKKQ HSNFEYHFQH RSANDMKRSA
     IDYLKTTCNS TPPKVLPLGS ICFQQQLIQA NPHLGCFVTM EAHQILGSRL PDNFRKLLRP
     MCIIQPDIRP ITEVLLLCGG FNQITYLSSK IEKLWKMAET QLTSSLSLKL LREILNCSRQ
     KLEEIKIQQL IQSDLDQSSP TNPDNIKYSS PAPSETLTTR SASPISSTLN RSPVMSDQES
     NISIIMEESA IVYGIQTIAK AQLLINDNII IKRLAEDVFP VHRKIENIEN LSADDSTLIT
     AVKEQLKLEY LEPTPTTINK IISLNMSIKN HLGVILFGPS GSGKSTSYEM LSRVLNVLHT
     EQLYQQSPSN RPVTKGGSKT NYIGQDNEPT KAINSEELTT VSTGPQPTFP RVETIITYVK
     SLSNKQLFGS TDSKDGWQDG LVSKLFRDAA QSQRQQATQR SYSSVSKWFI FDGVMDTSWT
     ELFIKLLDRS TITLPSSEKI TLPSSCSLLF ELCDLTDASP SIVTRCSLVH NGSDGVSWKH
     LISKWRQNSI GNWHISDHDM DLLASLIENI MEPAIEFFRS HRSKTMNDFH SVGVVEGIHE
     IHSLLTILSA LFDRYMSREG LSTADSTTTD STKSFSRDIG SSRQSTPSSP LRTRYSGSSL
     AVVNLLAYAY IWSLGGNLNE ELHQQFDLLV RKCLSSYGIQ LPKMGLVFDY LYDKRTSQLV
     QWESVYSSSQ RMIPSSYFTT CNLEKYFHLL EILVASGSSV VLVGESGVGK GSMIQNRIQS
     RHSYTKITIT PNLQVDELLD TINNKLNSFE RFQIGRQNNP QQTGSRKLLF YLDDLSTAYN
     DPTANAQPIC EILRQVISIG GTFHRHRLNF RNMRHIHFII TATDPYTAGM GGGVSRYCIS
     SRFLRLFPVI RLRNSSHEQL TDLFNTSINC WLEQIVPHPL ACSNELSNAL ATATVELYTK
     IKANLKPTPL HPQYVFTLHN LHRVLSRMFS VSVNPRSVRR RSFVQFTNND KTTDRKALSS
     VSQDPNLPVI RTTIRLWCHE VSREFSDRLT NENDQHLYEE ELRQIVIKHF CSRRSPTTNL
     PSKATSNSLT IPKTPVKKPM LLTVNLPEAL STPNSSNDPL IQREALFSSR EKLRDIVFTK
     YFMPNSDGRF NRGDFNRYYT ECSLGEFRIG LEQCLATYNE ETSTQRIEFA FFPEAVEHIR
     HAVNALSIPG SHCLMIGVPG SGKSTIVKLA TFAANCEVLK IDSSMIDQEI SDTIKIACLS
     AGMYEKRTVL LVSDTLPEKW MYYISCSLMT DGIIPGLITP SELMNIWSQK ATGIGTRRID
     NPDVVYDQFT NLVRKHLHVI VSLTYRGGAE EDFSYAERSL LTMLNKFPQM LINSSCVDIY
     KPLSIASLQI FAQEWLENNF IPLIDTNVDH DYDLVSRLDK ISNAIARIYA ISRDTAIQLS
     IKDSSYDEMF TLDTYNEYLV LIRTIACDIL DKEKEITKIY ESGLKKLNEV ECEVEMIENR
     LSQLKPVLQQ NQRISQQWQA AVVQEKEDYV KARDECRDTE KEIVRIGDII RELKEDAHTE
     LNKVLPLFET ALKALKSLKP QDVDELRTYR DPPDAVVHVM NAICVLFDRE RSWFESKRLL
     YRENFFLDLE LYDKDNLSDS KHKELRRFYN NPQMKPEVVG QSSAAACSLC RWIRALYEYS
     TVYRKLTPRR QFLQEESKRL IKVETLLGDR RLTCEGIRRK LESKLQSHKD CIRQVKETEK
     RIQESNDRID SATTLIESLR LHTGDWKKKV ADSKENINSC FGDALVAAAC VCFHGPFSME
     TRLQLQQLWI DACQSGGQNA ATTENNSLQG SIPVRKNFNL AEILSSEEEQ YIWKRNGLPT
     ESIDINNALI LRTASDHRFR SWPLVIDPDD ISLEWVKALM SSETKLGQYA KRRLMMNPML
     NYKLNDIVHD MTFTSSTTTS PDISEDKIID LPSFGSMHGI FKPRTLTVSS GMNTSPSLIG
     VSSVLPEQIE TSMMIQSQER SVMVINIDSD GIQERVLEAV QNGYVLMIRH FERVVNDDSL
     ISLIQRNIVF DQYDHNKMKM RIAGELIDFN PNFRLVLISS FPLAVIRSSL SVLPFANLAI
     YNIAASDQGM LTELFNMTIS LERPEYNGQL RSLDADVHHH RQQLDVEMGR ILKKVSNYEN
     LILDDETLVE ELQKTRQNYD LYQERLQEAL KQRNNLIDRQ QAFLPVATRG AILYKIMSNM
     ISLSSLYHFR LGWFLDTFTS AISECKDSKI IGGSPDARAA ELCNFLTLSI CKRLSWSLLK
     KHSFLCISMV TISILRQQSI NQQITNEEYV LFANGPKTQL SLRNSSEFTI NVDIPAWISR
     EAWISLKQIP NYEPIVSSFL TLRNQWNEYF SSNPSLISTT PGYPTLSLSF FQKALLLRLV
     RPELTTKILE ELILYTLGTA YSVMPPYNLD ELVKSSKVHT PIMCFTENQH AEDDNKNMDN
     TALSIDALKE IMSCGARFSM NGRIVHLSLG EPDCISEAIR IIKLALRTGW WVVLQNCHLV
     QYWSTALKNL IQRIIYSKYS PQKWNIHQDF RLWFTTSINR GYEMPALFSQ HSIKVAIEQS
     VKLQDILFTS YHQSVNFLKV GLQRQHYKPL QAHAKSDFLW LLCFIHTILL KRQTFGRFAS
     IHNYQWSQED LLAAIDAVVC CINDDIASLT SLITSVFYGG AVISEFDLNT TRSVITLAIK
     DLLPLVKDRP FLSYQMSNKD WKDVLSHLDQ LVYIGLSEKV DEAVSANFGM AILHNMKLSL
     GDEKLVSIQY DEYLQLLSLL SIRIPEEIKV EDIDAQLDIG HLANGCLLRF LRDDANRYNK
     VIRMIRKEIF QLREATNGNY SLTPRLEKIC SNLRNLIVPT HWYPYLPTHL PFNQWLEDLS
     RKVATLTSYI KTSQESDLND CDLRIFYQPA GFLDSLLQDY NGLVKAGVLE IDFEVKIFND
     SEKKCDHGIH LLGLQLHNAA WDFTKCCITQ VKEAQATCPL PIIWLRPIKL SNKVKKSSYP
     TYSCPVLHSY YQDVDKNCMI RLSLATEIEV GILYLKRVAI SVMDR
//
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