ID I7M304_TETTS Unreviewed; 4564 AA.
AC I7M304;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Dynein heavy chain, amine-terminal region protein {ECO:0000313|EMBL:EAS01815.2};
GN ORFNames=TTHERM_00565600 {ECO:0000313|EMBL:EAS01815.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS01815.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG662556; EAS01815.2; -; Genomic_DNA.
DR RefSeq; XP_001022060.2; XM_001022060.3.
DR STRING; 312017.I7M304; -.
DR GeneID; 7844063; -.
DR KEGG; tet:TTHERM_00565600; -.
DR eggNOG; KOG3595; Eukaryota.
DR InParanoid; I7M304; -.
DR OrthoDB; 166463at2759; -.
DR Proteomes; UP000009168; 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:0016020; C:membrane; 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; 1.10.8.1220; -; 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: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; 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 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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000009168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 4489..4511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1778..1921
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2420..2567
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1593..1620
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3059..3114
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3250..3319
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3570..3626
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..789
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4564 AA; 529589 MW; A0E542A6B058C198 CRC64;
MNRKQLFGDE NPDDDKRISS GDQPVQNIKI ITKTQSQGGF GINNLAGRLY DKGFNLKTMP
SVKRDANSYQ DKVLTANLTN LQNRKTKLVP LIYQPQSVVL HNGKRVHAVV MPGGQLEQDG
FNQSQMGTTS YGGSGALTQF GSTQQPNFFR QTAKSTFNGQ FKLNFGQQND DGAPQSRGMQ
IQSAQKSLRG ESQPPLENEI QPLNKSRTDN MDFKNFMYKT HELFPQNPLE SGQKVQISQS
QNKLPPIDRS QLGSAQQQNN NNINLGSTQV GFKGSFMEAD KAFLKINGFS DVEMDRTKRL
VGRISGKQNI DQRYRNTMGQ TGGFGSFKKK KTDEEELDQN QQHPLPDYKG EFTVVQSEEQ
QNQLGANFEK KGRNPKLDLY IELILKNVVH VHEFQYLIRD DKDKDDDDPY NLIVADYKDI
KAKEKAGTLK EFYTISKKGL THYINGKPVE FIGLAVWMKE REHYDQIKSL KFFTKFRKWK
TLKMWRKNVI KHKTATCAKA LNEKLFILNK TFRDTILQFR SNTYDMMESQ RFISVDNNSY
TGADSTYTLD EFKNLQEQTR KKITDKIQEY SKKCRTIVKS GFDESLNELR RNVYMANNEE
DYQNSRKQNQ NFFRLKESAY ENLGFSDNMN YEQRSELRKV CTKFLRFSYL VDFLAMESLS
NIFKYSVAEL ENKLTCLVDE DFFYEQQKLK NNQNMNNDPL FLVEINPGFE PIPDDATVIE
PIKEFMPKPF GEDTEKQFNI LHHVRLKEPK KKTEEQKAAD AAKKKPKKQN EDGEDEEEEE
DDEDEEGVVP DENRTYNRKI VPTITEKWIR ISPDRETIIS DILRCIAEGT NSIQAFERWS
RHDDMTIYVS VLEEWDDMVG DDWEHPDTNY LNPQDWIDGG SPQDKFQKTF RELISSAFSR
CDSFIKDSFH KYLIEYWENE QIDLNIFRNE KLLNPGESFN WTLRKLTDQK EVYEKEFPDQ
KDLGLLRLDF KTLRKKIINF PNEIIKKFSL FMPEMIRLRN IEVKDWMNNA TNLFKGGGAN
IDEFVKRSNN LKIVQRQLPK YKQKFSDIQH IRNIIIENKF DMKKEDVSAI IDTQNVQKRL
EQTILSAEEL AERNIENYIR DVKEDLIPKL IKEVGELDSQ IQNKKYLSEE LDINVAIKEL
EGLYNDAKKL EDNSKLYNHY EHTLGLPISR FEDLEMLLQD ANLRYLMWKS LKEWKELISG
WVDGKFKDIN TEEIKNKAEY YSKIVARCDK KLPQNAILTE LKKLVTDFRN TMPIVLALRN
ENLKDYHWRD IKKIIGEFEI NDEFTLKKLI DMKVVDFMEE IQEISIQATQ EASLEKQFQE
ISEKWNKQEF TLAPYKHHQP RTKDAYVLDQ LDELFAAIDE YLANLNNILG SRYLKKIREE
VEKFQKNVLY SQECIDDMLA VQKNWIYLEN IFSSNEIKSK LREETQQFEG VDKFFKNQMS
KANKGQGKLI HKFIIQPSKS TAAAAPQPAE AQKDQKEGDK KEVKTQKNDT LSQWRKHKDT
LNSIQKALDD YLEDKRGEFP RFYFLSNDEL IEILAKAGDI EAIQRNLKKC FDGIHRLNID
SNNSIKGMIS PEGETIEFNK FFTAKGEVEK WLLQVQEQMR ESLKKAIKKG KQDIDKDNKE
RKDWVLQHPA QVVATVSNIM WTQSTEIFIQ QQGDADADNP LENWYKINIQ QLQELTALIT
QGLDPLKHKS IVALITQDVH ARDIVYKLWE EGTCSVNDFE WQKQLRYYYY EEPENEVQVK
QVNAKIKYGN EYLGATTRLV ITPLTDRCWI TITGALNIKL GAAPAGPAGT GKTESTKDLA
KALGVFCVVF NCSDQIEYQM MGRLFSGLAQ QGAWACLDEF NRIDIEVLSV IAQQLLTIRQ
ALMKGIKDDE KFLFVDRMIP LKADGYGVFI TMNPGYAGRT ELPDNLKILF RPVSMMIPDY
RLIAEIMLFA EGFVNANPLS KKMVQLYTLS SQQLSQQDHY DFGMRAVKSV LVMAGALKRA
QPDLKEDVVL IRAMRDSNVP KFLKDDLPLF SALIQDLFPN EQIPDPDYGE LPQQIDQSFE
RLNYQKVEEL KHKVIQLFET FNVRFGVMLV GATTSGKTAC FRTLADSMSQ LRKRGSKDNR
FQEVKTHILN PKCITMGELY GQVNPNTQEW QDGLASQIMR EAASDETELR QWVVFDGPVD
ALWIENMNTV LDDNMMLCLA NGQRIKLRTQ MRMLFEVQDL RVASPATVSR CGMVYLMYEN
LGWRPFVQSW IEKKFTTKLD LNDQVEVEEV LSKELRTHLY TLFDEKVDFF IDHIRKMKEP
IATCDLQLVN SLCNLIECFI SEEYGFKKNE RPDFKKRYLD HAFAFAFIWS MCSTVNELNY
DKLDILIRDK FPLCIFPNQG TVYSFFLDVG SQQHNDLTFR HWNDKTPEFV YDKEIPYFNL
LVPTLDTVRY SFFTEWLLSF KKHMYLTGMS GTGKSVILST ILTQISETRN VDHFSLIFSA
QTSSKVTQLT IEGKLEKIKK TLLGAKPNRK TAVFIDDINM PSVEEYGAQP PIELLRFLVD
KGGLYDRKER FWKDIQDTIL CICSAPPGGG RSMLTPRFTR HFNLLCVPQP TRDILFKIFE
SLLTGFFNTG FPDTVKRMAD AIVNGTIDVY QTIAIELKAK PSKFHYTFNL RDVSKVFQGI
MMTTPYGGVR DENSATKLWI HEVQRVFHDR LINDEDRDWF YEYIMQLLGR HFKSRLQKSE
IFGSQQIVFS DILRLDLERK EYEDVTDKMQ KVIRVLDDKQ DEYNSSTTNN KMNLVFFDAC
IYHILRILRV LRSPRGNAML IGVGGSGKQS LTKLATFMLE YKLSLLEITK GFDSEKFRDF
IKELMKDSGG AQGKGTTFIF TDNQIVYESF LEDINNILNS GEVPNLWQQE DKDALISDVR
EINKKLRRAE DPDTIYKTFV ERVRNNLHIV LCMSPVGDAL RVRHRKFPSL VDCCALDWFS
PWPSEALISV ATSILSNDQN FPTPNTITKE ELIEQVAFMC KEVHIQASKQ AEVFEQQLKR
KVYYTPKSYL DLIKLYQKAL SDKRAEFITN QSRLSSGLTK LEQANKSVAQ LQIDLTELKP
QLEEKTIQVN EKLREVEKDS NIAAEKEAVV QEEAEKVQKQ ADRIQLISDE AQAELNKVMP
ELEAAMQAVQ NLDKSALSTL RGMANPPQQA TITFEAVAAL MGEKKTDWAS VKQIFLMDVP
KFIDKMIGFD KDNISEDRLK KLNKVLAKPE FNLEDIKKNL SYAHGLASFC LAMKVYADVN
SKVKPKKIEV ARLNNELNAV KSELYEKESE LKKVKDNVQR LQMETQMMVK QREELETNKE
LTEQRLDRAQ KLIQLTADEQ KRWEKTVVRL GGEIENLFGD VFLSTAQISY NGPFTGVYRK
ELNTNWLTMI REKNIPTSEQ YNLIKTLGDP MLLREWVIQG LPSDQVSQEN SIFAVKGFRW
PLLIDPQLQA NKWIKNMEKQ NKLSIFKFST PKFLDIVKLQ VENGYPILIE DVDSAIDPSI
DSVVNKEFSE VDGRLQLKLG GKDINYHKDF ALYMTTKKPN PQYLPEIFIK VNVINFTATF
EGLEDQLLAD VVKNEKPEVE HQRDENVLKL ATFQKQIIQS EKEILRLLAE AKAEKILDDV
NLIKTLQNAK EMAEEINQQI AKSMEIEKSI DATRSSYKSV SIRGSILFFV IKDLSLIDPM
YQYSLQYISK LFNQAMQSSE QSDDFEQRLK ILIENITKTI YTNVTRGLFE KDKLIFSFLI
ATSINKHANI LNEDIWRILL RGAGLFDKSK QPPNPDKVMI QPLSWDLAYS LELDFPDQFK
GFTKHISQKL SLWKEYQTSE DPLSKKLPEE WHTKLDEFEK IVVLKIFRPE KIMFAISNYV
QYYLGKFYVE QPSVTMERIH ADSDISTPII FVLSQGADPT TSILSFAQQR EMNEKLKIIS
LGQGQGKKAS ILIEEAKREG NWICLLNCHL ARTWMPDLEL IIERIPESEN VSSDFRIFLT
SMPASYFPVS VLQNGIKITT EPPRGFKANL KRSWDNLTDE FLNDCTKADV FHKLTWGLTF
FHAIIQERRK FGPLGWNIRY EFNDSDLETS TTVMRKLLDE QESIPWDALL FVTGEINYGG
RVTDDWDRRC LATILKKFYV KEALEGTYQF SDSPVYKIPR IGNIEQYRAY IESLPLNEDP
SVFGMNENAN IAYQGQESTK MIETILSIQP RMTSASAGKT PDQIVLDLKK SLEEQTPQLL
NKDDGNKELF EKDENDLIPS LSTVLLQEMT KFNLLISTVN RTLADLGKAI DGDIVMSSDL
DQTYNSLLNN QVPKQWEKVS YPSLKPLASW IIDLRERVQF MAKWLKESTP FCYWISGFFF
PQGFLTGVLQ TYARSHKIPI DELQFSFRIL DFDKEQVTTK PTDGVNIYGL YLEGAQWDRR
RKTILDAAPV NQIINYNMYQ FLNITIESNK LLHASALFIK PQLELVFFQQ LVSQQIMYLL
QTFLLLIKIQ ISGFQEELLY FANQINDLRQ SKKNKIIQIN KQILILQKIT ILIFVQFYST
QVYIYFLLFI FSNEAIRDKQ YQISNHYQFY KFINTQKFSI LKLQKQTFYQ FAYIQLTKDN
QSIN
//
