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Database: UniProt
Entry: A0A0V0YDX6_TRIPS
LinkDB: A0A0V0YDX6_TRIPS
Original site: A0A0V0YDX6_TRIPS 
ID   A0A0V0YDX6_TRIPS        Unreviewed;      4947 AA.
AC   A0A0V0YDX6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Dynein heavy chain, cytoplasmic {ECO:0000313|EMBL:KRX98547.1};
GN   Name=Dhc64C {ECO:0000313|EMBL:KRX98547.1};
GN   ORFNames=T4E_10496 {ECO:0000313|EMBL:KRX98547.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX98547.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX98547.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX98547.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains. {ECO:0000256|ARBA:ARBA00011655}.
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:KRX98547.1}.
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DR   EMBL; JYDU01000020; KRX98547.1; -; Genomic_DNA.
DR   Proteomes; UP000054815; 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: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   CDD; cd05371; HSD10-like_SDR_c; 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; 1.20.920.60; -; 2.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR10676:SF314; CYTOPLASMIC DYNEIN 1 HEAVY CHAIN 1; 1.
DR   PANTHER; PTHR10676; DYNEIN HEAVY CHAIN FAMILY 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; PF18198; AAA_lid_11; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF08385; DHC_N1; 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; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00382; AAA; 3.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000054815}.
FT   DOMAIN          1906..2043
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2591..2741
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2933..3099
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          1034..1090
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1292..1322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3212..3271
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3470..3525
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   4947 AA;  567155 MW;  304D95D6E0199196 CRC64;
     MVDNINEAIV DVSSPTVEIA QVELAEARVF SLFVRRIILL LLEDASGEPC GDAYATALDE
     CLHRTDTVDV FRRFIADAQA PALLIERSCE RDSEETADAT EITEIVNYTV STEVHFSSPK
     TNGLILIKRG AVLEADKPLI QQLLLFILAD ASPYETLHSY FSTTICPYFK SFVKESGGGD
     NYRDTDKAAM SVEKKLIELE MGLLHLQQNI DIPDITLLIH PVVQSVIKQA AEENRRAKVS
     DFGKLVDDST FLNQLQNGVT RWVREMQKVT KLDRDPSSGS ALQEITFWRN LERAVFNLLE
     KRESPEVILT LEVLKHGKRF HATVSFDTDT GLKQALDTVT NYNVLMKDFP INDLLSAVEM
     DRIRAAVASI FIHLRKIRTS RYPIQRCLRL IEAISRDLQI QMLKVLGMRR ILQISFDEFD
     KVMTQAFEVF TCWDDEYEKL QALLRDLLKK KREEQLKLIW RIVPAHKKLQ FRLEEIRRFR
     RHHEQLRAVI VRVFRLTSTL HGNENDHTFD ESPRMYDAAD TSVVEEVNVA YDFVKDIDCL
     DLSKEGSDSW SSALKCYEER IDRVEGRIAT RLRDQLGSAK NANEMFRIFS QFNALFVRPH
     IRGAIREYQT QLIERVKDDI EALHERFKKQ YSHSKACSTS SIYDIPPVSG FVIWAKQIER
     QLALYLRRVE DVLGKGWENH IEGQALKTDG DIFRAKLNTQ PVFDEWVTKV QTRNLGLSGR
     VFVVESVRRR NDSKASLRLR VNFLPDFITL AKEVRNFKNL SFRVPLAIVN KAHQVNQLYP
     FAMSMIESVR TYELMTERLN EKENVAILLA GLVKEIHAQI AEGAGLVWES YKLDSYVQKF
     SEMISHFQER VEELLHLEEQ IKIQLNLLDT CQYAAPAFQQ ILSNIQKSVD ALSLYQYSNL
     DIWIKRLDEE IEQKLAIRLE EGIKSWIRAL KGEIDEENSS SEDLSAQSKF KVGGDPIIHS
     FVHEIRITQQ VMYLSPCIEE IQVNLLQQLF SWEAIVTSQA RISSSCYHVE IERSSALTKY
     RSLLAKLPHG IKYIEKAYAA IENLKIEVKD YVNEWLRYQA LWDLQADTLY DRLNTDLSKW
     MKTLQELKEA RSTFDTSETR KQFGVIVVDF ARVQSKVSLK YDSWHKEILQ RFGTILGNEM
     QSLYTVVNKA RTHLEQQSVD ISSTSEAVSF ITYVQNLKRN VLDWDDKVEC FREGQRILER
     QRFQFPSNWL YSENFDGEWS AFSDILSRKS TAIQSQVNTL QAKIRQEATA VETRSADXXX
     XXXXXXXXXX XXXDFSSTII GDQLPDVALQ TLVVYEGKLS RLKEERDNIS RAREALELQE
     TSHTSVHGER LKAAIEELND LKQVWQALNP LYNELAEIKE RLWLSVQPRK LRQNVDSLLN
     QMKEMPANYR NYDAYDHLKR LLQSYAKINF LIVELKSDAL KSRHWKQLMS LLHVHWNLNE
     LTIGQIWACD LQRYESSIKE IILVAQGELA LEEFLKQLRE FWQTYELELI NYQNKTKLIR
     GWDDLFNKLK EHINSLNAMK LSPYYKEFEE DCLVWEEKLN RITALFDVWI DVQRRWVYLE
     GIFSGSADIK TLLPTETSKF QSISSEFLGI MKKVSMSARV TEILNVPGIQ RLLERLADML
     NKIQKALGEY LERERSEFPR FYFVGDEDLL EIIGNSKNIP RLQKHFKKMF AGVACILFNE
     DYTLIHGVAS REGEEVNFLH SISIKETPRV NEWLGLVEKE IQNTLAQLLV TCLQEFQKFK
     VHPIDADSYY NWLDKFPLQV ITLAAQIAWS EDVELALGKN ANLESILKFV ENTLNLLADS
     VLHEHPPLRR KKIEHLITEF VHKRCIMRYL MDCGVNSNQS FYWLKQMRFY LNADEVDPQK
     KLTIRMANAQ FYYGFEYLGI QEKLVQTPLT DRCFLTMTQA LESRLGGSPF GPAGTGKTES
     VKALGNQLGR FVLVFNCDEN FDFQARRIFI GLCQVGAWGC FDEFNRLEER MLSAVSQQIQ
     AIQETLRLTQ TKNDASVELL GKRVWVSPQM AIFITMNPGY AGRSNLPDNL KQLFRSLAMT
     QPDKQLIAEV MLFSQGFRLA EKLASKIVPF FTLCSEQLSN QTHYDFGLRA LKYVLVKAGN
     VKRDHVQQLK EQFQQVDRSF SEGVIGEQLP EQEILIQSVC ETLVPKLVAE DIPLMFSLLS
     DVFPGIPHTK AEMKRLREEI RKVCRERYLC YSEVEGELGY TWAEKVIQLY QIVQLNHGLM
     MVGSSGTGKT KAWQVLLAAL GRVDGVDGAV HVIDPKAITK DALYGTLDPN TREWTDGLFT
     HILRKIIDNV RGESTKRQWI IFDGDVDPEW VENLNSVLDD NKLLTLPNGE RLALPQNVRI
     MFEVENLKYA TLATVSRCGM VWFSADCVTE EMCFENYLQK LRNVSLDAHE NSGMPVSNLP
     VTQAQTNLTD QILPSLQVQR DIANILAPYL SSDGLVARCL EFAENQVEHI MEFSSCRALS
     SFFSMISQCI MKILFYNQQH SDFPMAFDQM ERYITRSLLL SIVWSFVGDA RAKYRDDMCE
     MIRSLTAIAL PAQENVSLIE FEVSVDGEWS SLHNRVPQVE VESHKVGAPD VVIPTIDTVL
     HEQLLYTWLA DHKPLVLCGP PGSGKTMTLF SSLRSLPDME VVGLNFSSAT SPELLLKTFD
     HYCEYKRTPN GIVLSPVQLG KWIVLFCDEI NLPNYDKYGT QRVISFLRQM VEHGGFYRSS
     DQAWVTVERI QFVGACNPPT DPGRKPLSQR FLRHVPVVYV DYPGELSLKQ IYGTFNRAML
     RMIPSLRSFA EPLTAAMVEL YLLSQDRFTP ELQPHYVYSP RELTRWVRGI CEAIRPLETL
     NVESLVKLWA HEALRLFQDR LAEEDERRWT DEQIDLIAAK HFPNVDVSVV LRRPLLYSCW
     LTKDYLPVER EELRNFLQAR LRVFYEEELD VRLVFFDEVL DHVLRIDRIF RQPQGHLLLI
     GVSGSGRATL SRFVAWMNGL SVFQVKIHNK YSAENFDDDL RLVLRRVGCK GEKLCFIMDE
     SNLLDSSFLE RINTLLANGE VPGLFEGDEY TTLMSQIKEA SQHEGLILDS SEELYRWFTQ
     QVMRNLHVVF TMNPSSEGLK DRVSTSPALF NRCVVNWFGD WSKSALFQVG RELTSNLDMD
     NTAYRSPDYF PYACDLVSRP PTYREAVVNA YVYVHETLHQ VVLQLTKRDH RTVLITPRHF
     LDFINHYVKL FHEKRKDLVD QQRHLNIGLS KIVETEQQVT ELQKSLSLKS KELEEKNALA
     NEKLKQMLSN RQEAENQKHM SEQIQSNLQQ QLAEVAAKKS DVMKQLAQVE PAVIDAQNAV
     KSIKKQHLVE VRSMANPPGL VKLALESICL LLGENCTEWK LMRAVIVKDD FISRIVNFDT
     DSVTNIRRQH LGEIRYLSSP PATVKLALEA VIFLFTGSST LDWKSIRGYL LRDDFVSQIL
     NFDTERITED IRQKMKAKYL DNPEYNYEKV NRASQACGPM VKWATAQINY AEMLHKVEPL
     RNELKKLEND AEVNKRKVED VNAVINQLEK SIASYKDEYA LLISEVQSIK ADLIAVQTKV
     DNEISFYKTC YFDQQIRLSL FMNWSRHLDE AGIQFRPDIS LVEYLANPDE RLRWQQHALP
     VDELCVENAI MLKRFTRYPL IIDPSGQAIE FLMQEYGERK IIRTSFMDDA FRKNLESALR
     FGNSLLVQDV ECYDPILNPV LNYEVKRAGG RVLITVGDQD IDLSPSFQIF LSTRDPTIQL
     TPDICSRVTV INFTVTRSSL QSQCLNHILK AERPDIDSKR SDLMKLQGEF ALRLRHLETS
     LLQALNDVKG RILDDDSIIS TLETLKKEAA EVSRKASETE TVMMEIEKTS QLYTPFSSYC
     ASLYFTLDHL NQMHFLYQYS LQFFMDIFMH VLNKKSILDG ISDYSQRLNV ITKNIFKTVY
     KRVSLGLLHH DRLGFALLLS RIYLKGMSES DCSFDDEFSH LLMKSDSLKT ADTTPFSISG
     QLKLSKEQKE KLAQLVVTLP AFASLAERLT QTEGVLEWME SSNPEINCPI LWDESKTTTP
     VSQALYRLLL IQALRPDRLL SAAHMFIDVA FGENFMSTGE NILNLKTIVE NEISCNMPLL
     LCSVPGYDAS GRVDDLSSEL DRGLTSIAMG SAEGFDAAEK AVNSSAKTGR WVLLKNVHLA
     TGWLIHLEKK LHSLVPHPNF RLFLTMEIHP KLPVNLLRAG RIIVYEPPPG IKANLLRTFG
     TIPPGKMTKP PAERPRLFFL LAWLHALVQE RLQYVPLGWT KKYEFSEADL RAAWECVDTW
     VDAAAHGRAN LPAEKVPWNA IRTLLSQCIY GGHLDNEFDQ ILLDCFIEKL FSEKSFQPDF
     ALVNNVDSFG NKLTVPDGVR REQYVNWVES IQALQSPTWL GLPSNAEKVL LTIRGQTMVK
     KLLKMNDEDE ELAYTPIGEQ FEGENHKPHW LKQIREAADH WLNSLPTSLA PLKRSVSNIK
     DPLYRFFERE VNIASRLLNN VRHDLADLIS IVEGNKKPTN HHRDLFAHLN KGLVPETWIK
     YTIPSTTTIT QWVHDFAERL AQFQLIVDAI SSGRIKNLKN RLWIGGLLSP EAYLTATRQH
     VAQLNEWSLE ELKLDVQVAN NFDNLEMDDC SFGVTGLKIM GVSCSEQGRL KISPKIWTDL
     LAVQLRWVHG MGAEKQKLNN TVRLPVYLYT DRQRVLFSLD FQTDPAVSSV NEFYERGVAI
     VCSGLMQMVL AKSRNLVALI TGGASGLGKG CAEQLLKMGS KIVLMDLPTS SGAEVANSLH
     KTDVVFSPGD VASESDVSKT LEFCRQKFGK LDAVVNCAAI GIAFSIYNNT KKQPHPLEPF
     ESVFRVNVLG TFNVIRQSIG MMLEKELGED EERGVIIMTS STAAFEGQQG QAAYAACCGA
     LNSMTLPLAR DCSRHRIRVV TIAPGLFDTP LTSFLPEKVQ QFFGRLTPYP HRFGQPAEFG
     HLVQSVIENP MINGEVIRID GGLRMPP
//
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