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Database: UniProt
Entry: A0A1L9NLR3_ASPTC
LinkDB: A0A1L9NLR3_ASPTC
Original site: A0A1L9NLR3_ASPTC 
ID   A0A1L9NLR3_ASPTC        Unreviewed;      4344 AA.
AC   A0A1L9NLR3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Dynein heavy chain, cytoplasmic {ECO:0000256|ARBA:ARBA00022197};
DE   AltName: Full=Dynein heavy chain, cytosolic {ECO:0000256|ARBA:ARBA00033439};
GN   ORFNames=ASPTUDRAFT_111685 {ECO:0000313|EMBL:OJI90177.1};
OS   Aspergillus tubingensis (strain CBS 134.48).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI90177.1, ECO:0000313|Proteomes:UP000184304};
RN   [1] {ECO:0000313|Proteomes:UP000184304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   EMBL; KV878176; OJI90177.1; -; Genomic_DNA.
DR   STRING; 767770.A0A1L9NLR3; -.
DR   VEuPathDB; FungiDB:ASPTUDRAFT_111685; -.
DR   OMA; NERQMTR; -.
DR   Proteomes; UP000184304; 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; 2.
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; 1.20.58.1120; -; 1.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 1.20.920.30; -; 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; IPR042222; Dynein_2_N.
DR   InterPro; IPR043157; Dynein_AAA1S.
DR   InterPro; IPR041466; Dynein_AAA5_ext.
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; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR45703:SF34; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 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; PF08385; DHC_N1; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF17852; Dynein_AAA_lid; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   Pfam; PF12777; MT; 1.
DR   SMART; SM00382; AAA; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   4: Predicted;
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:UP000184304}.
FT   DOMAIN          1933..2071
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2225..2546
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2589..2739
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          2931..3097
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          1633..1660
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3193..3244
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          3419..3460
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   4344 AA;  492560 MW;  27F83F6471791832 CRC64;
     MEVANAEVSN GVPAPAQTPL VDSNAVIEYL SEVLRVTLGA LRSELESTGS LLSPARYNET
     VQRCTRFASE SQVAIYVQKD VVASEEANGT ETSEDLSSKY VYNLSAEISS SSTTVATVVF
     IKRPTAIDPS LPIPSQIQVV NFPGPASLSN AQSQQGASQS PYEILHLMVH HGLNAYFEAN
     TRSQEAAGGA KPRTDTEAKT GVSSTKKKFA ELELGLRHLL QNVEIPALNL PLHEVVQAAL
     VDAEKRGVKP SVELIDSAIL ENSTFVNSIQ NTVNAWIRSI QTITKMSRDA DSDSAAQEIN
     FWLSMETALE GIENQLRGDG VQLTMDILRH AKRYQATLSF VADTGLREAT DLVQKYNQLM
     RDFPLDELLS ATTLQKVQES LNLIFNHLNK KLKICPYPIK RALALVEAIS GDLDNQIHSL
     LHGRTILHLD YREFRSLMKT AGAIWRTWDE NLKEFTNVAR ESTRRRNEKF IPIKIAARHE
     KTQERLKYIN TFRVNHEQLQ RTIVNVLGPK TSTAGDTAAG AGSDGAVIVE EIGDVDAVEE
     VAQAYAALRN VDVLDVSPEG TQQWIKEEIA YNERTSRVEN SIIARLRDRL ATAKNANEMF
     RVFSKFNALL VRPKIRGAIG EYQTQLIENV KQDISSLHER FKQQYGHSEA HAMAQLRDLP
     PVSGAIVWAR QIEHQLDGYM GKVANVLGED WALHSEGQKL LAESNLFRKK LDTRPVFESW
     LHDVQRRHIT ISGRLFNIIR NRAAGNTFEL TVNFDAQIIA LFKEVRNLIW LNFQVPHAVS
     NISKEAKRVY PYAISLMESV RTLLQTNRSI AAMTEVAILL NGYVNDTQSM IIKGVPLRWE
     SFVHSYELHV KQSALANGAI DAAIPTRGES KHVQFVREFA GSASVLQSKT AVLASINESI
     QKATHELKTC PYEAAAFRQR LDAIQVAVDK LNLENYVNLG YWVANLNQKI EGILRERLHR
     AIREWINSFQ EATYSSQSLQ TSSGVQTGEG ETLSYNIEFP ELTHEISMRN QFLHLDPPLQ
     YARASWFAHF DNWLGVICNL EKIKSSRYQI SIDVQKVQLS EACFATLPQH CTNELGQVYN
     AVESRLSEVS AYVDKWLQFQ SLWDLQSEQV YDILGDDLSQ WLQLLQEIRK SRATFDTSEV
     SKSFGNIKID YEQVQTRVNA KYDQWQHEIL LRFGSKLGGR MREVHSEIAA ARRDLEGQTL
     EAASTAHAVS FITIVQQCKR KAKVWEPEVD LFRQGQATLA RQRYQFPSDW LHVENVDGEW
     AALNELLARK SKIVQDQTEG LRAKISAEDK VISDKITEVI SQWNEEKPVS GTIPPEEASR
     TLSMFQSRLE SLQSEYEMVS KAKEALDLPA GVESSLPAIL EEVQDFMSVW AALSTIWKSL
     NDLRDMLWTS VQPRKLRQSI DGLIKMTKEM PSRMRQYAAF EHIQNVLRQL LKVNPLLSDM
     KSEAVRERHW QKIYKALKPG KRFSLVSLTL GDVWDLQLTA SEVIIRDIIA QAQGEMALEE
     FLKSVRETWQ NYSLDLINYQ NKCRLIRGFD DLFAKCSENL NSLQAMKHSP YYKEFEEEAT
     SWEDKLNRVH VLFDVWIDVQ RQWVYLEGVF TGNADIKHLL PLESSRFQNI NSEFFAVMKK
     VYKSPFVLDV LAINGVQKSL ERLAELLNKI QKALGEYLER ERVSFPRFYF VGDEDLLEII
     GNSNDIVRVA KHFKKMFAGL SGVLMDDDNN IVGFTSKEGE EVRLKKEVNL VKTPRINDWL
     TAIETNMKLT LAELLAEAVE QFEPLYNASE VDQTAFNDFL ANYPAQIVVL ASQVVWTRAV
     QRSLENGGST LQSLFDAQVR ILELLAATVL GELDAISRKK CEHMITEFVH QRDVISKLVT
     ANATTPMHYL WLLQMRYVYQ PEGDFLQRLY VHMANAKLNY GFEYLGVPER LVRTPLTDRC
     FLTLTQALCQ RLGGSPYGPA GTGKTESVKA LGLQLGRFTL VFCCDDTFDF QAMGRIFLGI
     CQVGAWGCFD EFNRLEERIL SAVSQQIQNI QIGLKNGETD EKAQIELVGR RLSVNPNTGI
     FITMNPGYAG RSNLPDNLKK LFRSVAMSKP DKELITEVML FSQGFKQAKH LSKQTVPFFD
     HCSTQLSKQA HYDFGLRALK SVLVSSGGLK RTRIASSEED LGPDEVIEPQ IIVQSLRETI
     APKLVREDVD RMLEIQKQDF AGVEYVPANY EKLTAAIRDI AKEQHFVDSE MWITKALQLY
     QIQSIHHGVM MVGKSGAGKS AAWKILLQAL QRTEGVESVS HIIDSKVMSK EALYGSLDAT
     TREWTDGLFT GILRKIVDNL RGEDSKRHWI VFDGDVDPEW VENLNSVLDD NKLLTLPNGE
     RLNLPPNVRI MFEVETLKYA TLATVSRCGM VWFNDDTVTP SMMISNYVES LRTRTFEDLD
     DDSAPSGQAA IKTQDAQDML ATILKHLLQT EDLVLQALEE AKKYNHIMEY TFIRALNTLF
     SLLNKACRNV LEYNIQHVDF PLDYDQIEAY ISKKLLLALV WSFTGDCPLA DRQSFGQFVS
     ALTTIDLPPD GAASIIDFDI TLPKCEWASW QSQVPTIEIN THSITQTDVV IPTVDTVRHE
     DVLYSWLAEH KPLLLCGPPG SGKTMTLFAA LRKLPNMEVV GLNFSSATTP DLLIKTFEQY
     CEYKKTLNGV VMSPNQIGRW LVIFCDEINL PAPDRYGTQR AISFLRQLVE QNGFWRTSDK
     TWVTLDRIQF VGACNPPTDA GRTAMAERFL RHAPLVMVDY PGEVSLNQIY GTFNSAILKI
     LPLLRGYSES LTKAMVQFYL ESQARFTPKI QPHYVYSPRE LTRWVRGVYE AIKPLETLSV
     EGLVRIWAHE ALRLFQDRLV TEDERNWTAD AVRRIALDNF PTIDDQEALK GPILFSNWLS
     KNYVPVEQER LRDFVKARLK TFCDEEVDVP LVLFNDVLEH ALRIDRVFRQ PQGHLILIGV
     SGSGKTTLSR FVAWMNGLKV FQIKVHGKYS SEDFDDDLRT VLRRAGCKGE KICFIMDESN
     VLDSGFLERM NTLLANAEVP GLFEGDEFSS LMTACKEGAQ RQGLLLDTQE ELYKWFTSQI
     VKNLHVVFTM NPPEEGLSSK AATSPALFNR CVLNWMGDWS DQALFQVGSE LTQSVDLDKP
     NFIAPDSIPV AYRELSLPAS HRDTVINAMV YIHYSLQRFN QRLQKQQGRT TFLTPRHYLD
     FVAQYVKLFN EKREDLEEQQ RHLNVGLEKL RDTVDKVSDL RASLAQKKTQ LEKKDTEANE
     KLQKMVADQR EAEQRKAVSL EVQAALEKQE AQVALRREVV LSDLAKAEPA VIEAQKSVSN
     IKRQHLTEVR SMGNPPASVR LALEAVCTLL GHKVDSWKTI QGIIRRDDFI ASIVNYDNER
     QMTRNHRIKM RNEFLSKEDF TYERVNRASK ACGPLVQWVE AQVNYSEILD RVGPLREEVD
     QLEEQALQTK AEAQTIENTI KGLEDSIATY KAEYAALISE TQAIKTEMSR VQFKVDRSVR
     LLDSLSSERT RWEEGSRSFE TQISTLVGDV LIAAAFLAYA GFYDQQFRKA MIDEWVTHLT
     QAGINFKPHN PITEYLSNAD ERLAWQDHSL PVDDLCTENA IVLKRYNRYP LIIDPSGRVT
     EFLEKESTDR KLTVTSFLDD SFVKQLESAL RFGNPILIQD AEHLDPILNH VLNKEYQKTG
     GRVLIQLGKQ EIDFSPSFKL FLSTRDPSAT FPPDVCSRTT FVNFTVTQSS LQTQSLNEVL
     KFERPDVDAR RTDLVKLQGE FKIHLRQLEK RLLQALNESR GNILDDDNVI ETLETLKKEA
     AEISKKMVET EGVMTEVENI TLNYSIIARS CSAVFAVLEQ LHHVNHFYQF SLQFFVDIFN
     SVLYQNKRLA QEKDHAARVQ IILRDLFVTT YQRTSLGLIQ KDRITFAMLL AQAAPYPMDK
     RIIDMILDES MESVDLSTSP ELKEQVLNKI ANMSLYKSIF PTITSEQWEQ FFSDELAENS
     IPVVLEETTE NIDRLLRSLL LVKLCRMDRF VPTAERFIEA VFGRELFEGS TDLKDIVSQV
     TATTPIALSS SPGFDASYKV DALVERMNAT CANIAMGSNE GLESADKAIS NAAAAGNWVQ
     VKNVHLAPSW LQSLEKRLES LKPHKDFRLF LSMESSPKIP VNLLRASRVL MYEQPAGVRA
     NMKDSLSSLS TRASKAPVEK ARVYLLLCFL HAVVQERLRY APSLGWKGFW EFNDSDYECS
     AHIIDYWVDT IAQGRSNVAP QKLPWDMIRT LVTETYGGKV DDFADFKQLE SLVTNLLTPA
     AFEDEHKIVS GVENDDCLTL PGGTSIRDFV EWVNKLPERE PPTYLGLPAN AEKLLLVGHG
     NKMISDLSRV TTLLDEGEQL MIEA
//
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