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Database: UniProt
Entry: Q4QFM9_LEIMA
LinkDB: Q4QFM9_LEIMA
Original site: Q4QFM9_LEIMA 
ID   Q4QFM9_LEIMA            Unreviewed;      4268 AA.
AC   Q4QFM9;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   SubName: Full=Putative dynein heavy chain {ECO:0000313|EMBL:CAJ03160.1};
GN   ORFNames=LMJF_14_1060 {ECO:0000313|EMBL:CAJ03160.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ03160.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CAJ03160.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=16020728; DOI=10.1126/science.1112680;
RA   Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA   Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA   Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA   Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA   Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA   De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA   Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA   Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA   Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA   Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA   Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA   Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA   Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA   Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA   Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA   Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA   Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA   Barrell B., Myler P.J.;
RT   "The genome of the kinetoplastid parasite, Leishmania major.";
RL   Science 309:436-442(2005).
RN   [2] {ECO:0000313|EMBL:CAJ03160.1, ECO:0000313|Proteomes:UP000000542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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DR   EMBL; FR796410; CAJ03160.1; -; Genomic_DNA.
DR   RefSeq; XP_001687705.1; XM_001687653.1.
DR   STRING; 5664.Q4QFM9; -.
DR   EnsemblProtists; CAJ03160; CAJ03160; LMJF_14_1060.
DR   GeneID; 5650309; -.
DR   KEGG; lma:LMJF_14_1060; -.
DR   VEuPathDB; TriTrypDB:LmjF.14.1060; -.
DR   VEuPathDB; TriTrypDB:LMJFC_140017900; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_140017700; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_140017100; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   HOGENOM; CLU_000038_0_3_1; -.
DR   InParanoid; Q4QFM9; -.
DR   OMA; EKTMNAV; -.
DR   Proteomes; UP000000542; Chromosome 14.
DR   GO; GO:0097729; C:9+2 motile cilium; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; 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; IBA:GO_Central.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
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; 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; DYNEINS 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   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:UP000000542}.
FT   DOMAIN          691..1091
FT                   /note="Dynein heavy chain linker"
FT                   /evidence="ECO:0000259|Pfam:PF08393"
FT   DOMAIN          1243..1584
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          1907..1975
FT                   /note="Dynein heavy chain AAA 5 extension"
FT                   /evidence="ECO:0000259|Pfam:PF17852"
FT   DOMAIN          2201..2289
FT                   /note="Dynein heavy chain 3 AAA+ lid"
FT                   /evidence="ECO:0000259|Pfam:PF17857"
FT   DOMAIN          2362..2623
FT                   /note="Dynein heavy chain AAA module D4"
FT                   /evidence="ECO:0000259|Pfam:PF12780"
FT   DOMAIN          2637..2967
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          2994..3220
FT                   /note="Dynein heavy chain ATP-binding dynein motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12781"
FT   DOMAIN          3558..3671
FT                   /note="Dynein heavy chain region D6 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF03028"
FT   DOMAIN          3732..3834
FT                   /note="Dynein heavy chain AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF18198"
FT   DOMAIN          3935..4264
FT                   /note="Dynein heavy chain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18199"
FT   REGION          1604..1626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3828..3847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3867..3891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3920..3943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2638..2693
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2851..2934
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        3867..3885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3929..3943
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4268 AA;  473184 MW;  C43F5DA402F57053 CRC64;
     MMSTKVIQEL KELPLNTVED AQKFFSIVDD VKEQGVALPP ITHMFFARVD SGLHFEPYHI
     RTICRDNRPM NYYVVTKGHV IHVDRRNGEY KVVATLEQWL LEAKCFNRIC KIAFFRNYIR
     HKALLRLLES ARRTKLERIR AILSKRLLLA TPTFQKDLIA LRRKAFDFQW TPATEGFKKV
     LSLQISGEKG NIAGFSTDEF VEMQDDYGKL LQRKFASLLL DILSVVVERV ENVTQLLSTM
     RVIEKYPGAT GCVNKDVTAK ELHKRQMEQK RLVVDYEKLP SYIRLVHHFQ LESTFQQACS
     TFFDLEGAVR RRAAILRWRF RVECIVEGRK ELSLFPSKEH VTKTAEAVMD KCIDLLSGAP
     TCVGSEALKP FTTMIQTATV RSALLGDALI SVYKKEVLQF IEADYDEAKS KLSSYEPLVT
     VSQFLAEWQD VSMNWDSTLS HENSLLVSIT ESEIRGYATR AYKAQSEIMK LSNRTYGTVV
     VECDKTLQKL VAQLKGVLVD IEAALGQLIK LNFRYLKAEC DFWVGKLSLP DIALAQFINW
     YLGLQDSGSI FDEFSNHVVD IQNLHRLLCE LREKSNAGVI NDEVDYSSVL RAPFQCAVTE
     ARKYYLSNSS RIKEMLLAEH TRIIASVTST TKRLASEYSN ENANEIGAPV TQKLEDVRDE
     LVQANSEARQ LDMYARVLEM QTFNWSEIAV AEDELQKYVE LWNVHKEATD LRHRLEAKTV
     EEIDGQELKD TIVSLFQRAF KAQKNTPGCT ANYLVKSLAV EKANVPMYVE LCNPALKEAH
     WLQLFQHTSI QLIPSAKRTL RSLEAAGLMT NEHSAAVREV VSSAVGVYEL EQQLKKLQDY
     WANHLFVVVP YGGRSNAFVV DAVDATLEEL EEQQIVVQTC LTSKYLAPVQ TEMKEWEAKL
     SLIHSVLMEW VGVQKAWMYL EFIFTSDDIK RQLPDESLLF SSADRFFGSL MKRCSEDPHM
     APLCLEGNGD TLKKLQKCTY QLECIQKKID EYLETKRVAF PRFYFLSNDE LLSILSDSRN
     PLAVQPHLQK CFDNIKALVF ADDKTIVAMR SSEGEEVLFT HPVKVIGNVE SWLNDVERAM
     RATLFDCLAA CLRAYTTEHR TKWFFEHPAQ CVTTVDQIMW TREVEEVITA TGSGDSSAWS
     SYQDRFGEQL LQTVELVKLS LTALQRTVVS NLIVVDVHCR DVCAELAADS ASAAPHPCSS
     LLDFGWQKQL RFYYGPPTSA HGSGGVAEMA DCFVRHGAAE LPYGYEYLGN QPRLVITPLT
     ERAFLTCTAA LHMQKGAAPQ GPAGTGKTES VKDLGKALAR TVVVFNCSDG LDYRMMSQMF
     AGLAQAGAWA CFDEFNRIEL EVLSVVAQQM LDITTAITQR QTFMKFEGHH IKLHTNFGVF
     ITMNPGYAGR TELPDNLKAL FRPVCMMIPN YALIAEIMFY AEGYGKAQSL AAKMIRLYSL
     ASQQLSKQDH YDFGMRAVKS ILVLAGRLKR ADPDSDEELL LVRAIREANL PKFLVDDRHL
     FMALLHDFFP TIVEVAPASV SEVILSEAKC FLTEELVHTS LSSPEAQMRL QPTEGLLFKT
     QQLFDTLMTR HGLMLVGHTM TGKTTVRDTL ASVLTRLGRV LDTTPVPGAA GGDSGNGNPG
     AKGGLAGTRR HTLAASMRAL DARCQSYFTT THATVCNPKA ISMTELYGDV NPLTREWQDG
     VFSAIVRDLV KQSAAQHGRA ATRHWVIFDG PVDAVWVENL NTVLDDSKML CLVNGERIRI
     PDTISLLFEV QDLRVASPAT VSRCGMVYVD EECVDGGWSP LLHSLSQAAA QELRAQWHHD
     RFLQLCGSLV PPLLQVVREE CTEYIATCNA QLTLNLFYLM KAAVQHLQGV IDEDRQEQQK
     QLRDDAAALV LDSGVSRPSI DSTFRRFSRR RSSRVTRTAV LVRGDAIFDA LFLQSCAWGL
     GGNLTETTRA RFAAAMLPLV RKGALNFPAD AEAEGCGVFD YGVDYEIGDW RRWSEMVPEF
     HYNASVPYFD LLVPTEQTAA LQYLLRSATT THHHMLLNGL TGTGKSSTVN SFLLQTLHTE
     DAASSTAAFR FTLSAQTSAQ ALQNTIEMKL TRRKGDREFG APSGKTMMIA VIDDCNVPQL
     EEYGAAPPVE LLRQMITQGG FYDRKRLFFK EVVQTMLIAC CGEPGGGKNE MTPRFTSKLL
     CFCAPQLTET SMRSIFSAIL KGFFYARGFA TEVAALADAV VDSTLEAYRR IAVECLPTPD
     KTHCTFNLRD VSKVFQGILQ IKPAHCASPQ ALIDLWSHEA SRVFHDRLID DTDRGWWWRC
     CAEVIEKHFC GDVTAANADA ADTDAAQPVP SPLPAPDPAQ LATIFYGAWV NRDYQRIGQD
     TSLQVVAQQH LAEYNTQSTT PMNLVFFDQA VQHLSRICRI VSQPRGHALL VGVGGSGRSS
     LCRLAAFMMN MDVQTVHIAR NYGIEEFRDE VRKVLLDSGA RGKEVVFVIS DSQLVHSEML
     EDINNLLNTG EVPGMMGLED METVVRCCRE ASLASGRPDT RASVYEYFVS QSRERFHLCL
     CMSPMSGVFR DRLRMFPALV NCTTIDWFSE WPQEALRAVA QSTLSSAARD GAAGPGTDQL
     SALMVLLQST VKDAAERLYA QHRRRTHVTP TSYLAVLTLY NTMGRRLRRD LQASANRYRN
     GLKKLDTAKS TIAQLQQQIR EMQPGLAAAA KQVEEQKQTL AVEQLEANQM KEAQSKEEAT
     ALQLMNEAES IRRECEEGLQ QALPALEAAK QALETLSAKD IQEIKTFTTP PSNVEKTMNA
     VLVLLGEKDG WASAKACLGK LDFISRLTGY PRDSITPACI RKLAVFVQDP DFVPDIIEKT
     SLPCRSMCMW VHAMYKYYFV AKEIAPKRAR LAGAEEKVEV ARKELQAKQV ALQKVLDHIS
     DLQAAAAAAQ EKADHFQRQI ETAMARLVRA DQLISGLASE RVRWKEALAK LETQLGCVEG
     TAALAAGCVG YLGPFPLDYR EVLVERWRSE CTALHIPFDA TYSLEGFETE ATVQQWALQS
     LPRDTYSIQN ATILHRTTQC CYMIDPQGQA NAFVRKLERS RSSGAAGLLQ LKLNSPNFMR
     QIENAVQKGQ AVLLEDVGET LDAALDPILL KQVRRVAGRD VVTLGDREVT YDDRFHLYIT
     TKLANPVLTP ELQVKLTVID FTVTREGLEE QLLADIVGSE RASLQQRGDR CVISIAANRE
     EIAALEAQVL QQLSDATGDV LDNAELIQAL QTSKVTSEKI GVELAAVEET NKTINATRDV
     YRPLAVRGSL LYGAITQMAK VDPMYDYSLP FFKNLVVSVL ASTRRQRPQL QQPHRPSSIP
     ASSMMLGNGS LHEREAQNCH VSLAPTDSSH GLPGASAEEE EEAAAAMSEA EVEARVVMLV
     EEVTWMSYRV LCRGLFGPHK LLFSFVLATT LLRSTGQITK EEWELFLCGG AGRALPPAFA
     AAGGEGSDGA TVQRPGYVSS GTWVDFGAIC GLEAFAEVYE SFIASLADTS DLGDADLSGD
     RPLPWTAWFT ETYGAEVLTR LPASLAHLSL WHRVLAVKIL RPNKFHYMAA QLVADTLGQR
     YTIAPPFDLE EAFLDSTKMT PIIFILSPGA DPTSLFLSFA EERGFSGRKH MLSLGQDQDV
     RATQMIREGQ REGAWVYLQN CHVYASWMPQ LQALVESMNP SEIHADFRLW LTSNPSPSFP
     PLVLQAGLKL TQEPPMGLRG KVLSTLRSTV VADVWAATAS AADVGNADSN DASVSASSPA
     VLRGGHPSIE LQRLVWTLAF YHGTVMERRR YRPLGWNISY DWGMADFEAG LATLQTALDR
     CKDGGAGLPT EELCYMLGTI DFGGRVTDEW DTLCLQVLTR RFFDTDAPGT TLQQKSPQDA
     ITPPPFPKDG VSYAALLQLA EAAFTVGRES RKDGDGEDES GESPARFGLH DNATLSVEQQ
     LSLGLVDALV LMNASGAVTG ATSAQRRSAS GDHGEEDAKA SGDEAMENPV AAVARNLLAQ
     LPPLLPRQEA VLGSMTSPNH STTTTTAVSA VADPAPLQTL LSHETDLYNC LLSTMQSSLA
     ELIRALKGEV VVTSRLELMM QRLAFNQVPE VWAQVGYLTL KPLGSFMEDL LRRVHFMRRW
     GEAGPPPSFW LSGVFFPQGF VTALLQARSR ALQVPIDSLQ LRFRALAPSE AAEVSALTAS
     HEAGTGSKAP TLVGAYVNGL YLEGCGWDAA RGGLVEAAPG ALTVELPIIH FEPVMGSESV
     AKGPSASAAE AAAAYVCPLY KVRTRAGTLS TTGVSTNYVT SLTLPSLDGV PGDHWTLRGV
     AALCALDN
//
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