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Database: UniProt
Entry: D8SPP7_SELML
LinkDB: D8SPP7_SELML
Original site: D8SPP7_SELML 
ID   D8SPP7_SELML            Unreviewed;      3461 AA.
AC   D8SPP7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Dynein heavy chain {ECO:0000313|EMBL:EFJ13707.1};
DE   Flags: Fragment;
GN   Name=DHC2-2 {ECO:0000313|EMBL:EFJ13707.1};
GN   ORFNames=SELMODRAFT_449697 {ECO:0000313|EMBL:EFJ13707.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ13707.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000256|ARBA:ARBA00004611}.
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DR   EMBL; GL377631; EFJ13707.1; -; Genomic_DNA.
DR   RefSeq; XP_002985213.1; XM_002985167.1.
DR   STRING; 88036.D8SPP7; -.
DR   EnsemblPlants; EFJ13707; EFJ13707; SELMODRAFT_449697.
DR   Gramene; EFJ13707; EFJ13707; SELMODRAFT_449697.
DR   KEGG; smo:SELMODRAFT_449697; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   HOGENOM; CLU_000038_0_0_1; -.
DR   InParanoid; D8SPP7; -.
DR   OMA; GRDIPCS; -.
DR   Proteomes; UP000001514; 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-SubCell.
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:0030030; P:cell projection organization; IEA:UniProtKB-KW.
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; 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:SF1; DYNEIN 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   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
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:0000256|ARBA:ARBA00022846};
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:UP000001514}.
FT   DOMAIN          199..597
FT                   /note="Dynein heavy chain linker"
FT                   /evidence="ECO:0000259|Pfam:PF08393"
FT   DOMAIN          726..1052
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          1218..1361
FT                   /note="Dynein heavy chain AAA 5 extension"
FT                   /evidence="ECO:0000259|Pfam:PF17852"
FT   DOMAIN          1582..1680
FT                   /note="Dynein heavy chain 3 AAA+ lid"
FT                   /evidence="ECO:0000259|Pfam:PF17857"
FT   DOMAIN          1744..2004
FT                   /note="Dynein heavy chain AAA module D4"
FT                   /evidence="ECO:0000259|Pfam:PF12780"
FT   DOMAIN          2018..2361
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          2391..2612
FT                   /note="Dynein heavy chain ATP-binding dynein motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12781"
FT   DOMAIN          2857..2970
FT                   /note="Dynein heavy chain region D6 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF03028"
FT   DOMAIN          3005..3145
FT                   /note="Dynein heavy chain AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF18198"
FT   DOMAIN          3152..3457
FT                   /note="Dynein heavy chain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18199"
FT   COILED          2261..2309
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EFJ13707.1"
SQ   SEQUENCE   3461 AA;  391489 MW;  56D1DD1EDBB5CCA2 CRC64;
     IGVLHIDSKS LRNSLLPVTT RTLDAIKGLL LIAAREETIK VLAHFQEKVK ALEVRPTMEK
     KKASLAEATI VDEMYSLLAG YEVKVPTDDQ IKLDDLHEIV QKYGDSIEAA TIYIEENRTD
     MMADLDSKAN SLNEELVAIL GMLHQERFLR SESDPFEIVT EMEQIWDRMV EIRDTLEIYK
     DYQKLFQMDM EDMSNFLMTE KEYNLRYGVW KALRDWLVMV KQWREGPVAS LKAPEVQGKT
     DEYAKEAYKM GKANKEDTVV FRLKDAIDDF KQLLPLIEEL ANPALKDRHW TQIFKQVGQE
     YKDGLVFSIN DMLDYKIMDK IEEVRVIGGV ASKEFSFQRT LDKMEKDWEG VEFIVLPYKD
     SGTFILGGLD DIQTILDDQL VKIMSMCASP FIKIFEGRAV RWKTLMINMQ DLLDNWVECQ
     ATWQYLGPIF GSKDIMRQMP EEGEKFQTVD ATWRDVMKRT VATPGCIETA VDVERLEKLK
     EANRLLEIIN KGLASYLEVK RVAFPRFFFL SNDEMLEILS ETKDPLRVQP HLKKCFEGID
     TLRFEHNMDV TGMISAEGEV VPLVEKFNPK AAQGAVEKWL LQVEEGMLQS LQEQCSSSVI
     AYAETVREKW VLEWPGQIVL VVSAIYWTTM VTESILAGGN AVRECEKACT EQLGRIVNLV
     RGNLTRLNRA TLSALVVMDV HARDVVTILA NAKVEKETDF LWQSQLRIYW EKDTCFVRMM
     NAGVEYGYEY LGNSSRLVIT PLTDRCYRTL MGAIHLNMGG APEGPAGTGK TETTKDLAKA
     LARQCVVFNC SDSLDYLAMA KFFKGLAAAG AWACFDEFNR IDLEVLSVVA QQVLEVQLAV
     QNKVKTFVFE GTELTLKPTC NVFITMNPGY AGRSELPDNL KALFRTVAMM VPDYAMISEI
     MLYSSGYLLA RDCARKIVAT YRLCSEQLSS QDHYDYGMRA VMAVLRAASN LKQRYPDEEE
     FILMLRSIID VNLCKFLSQD VPLFNGIVSD LFPGVVLPEP DYTNLDKVIR DNCKKFNLQP
     TPYFKIKIIQ LYEMIIVRHG LMLVGLSFSG KTCALRVLQA ALTDLAEQGL DNERRVQIAT
     VNPKSVTMGQ LYGQADPMTQ EWLDGVLAVR FREQASDPSN DRKWLVLDGP VDAIWIENMN
     TVLDDNKKLC LPNSEIIQMS SSMNMIFEVG DLAVASPATV SRCGMVYLEP HQMGWQPLML
     SWLDTLPASL QGPLRTHLQG LFEWMVTACL RFVRKSVKEL SPTSDANIVV SLMRNFYGLI
     DELKPEEAGK AFGKEKLGIW VDSIFLFSLV WSIGATGDNE ARQGFDAFLR HLAAGEVPEG
     YELWVPSTHV DLFTKIMPDD DGATVYDFLF DKENAAWLLW TATIVPLEIP QGAIFSEIII
     PTKDMVRYTF LLDKGIQANY PVLLVGSTGT GKSVYINRHL SLGLPKEFFT TIFVCFSART
     SANMTQNQID GQLDRRKRGI YGPVLGKRCI IFVDDLNMPQ PEVYGAQPPI ELLRQYMDHD
     GWYGRDNVFK KIVDVLFVAG MGPPGGGRNF VTQRFLRHFN VVGVAQVAED SLRLIFNTIL
     NWHLTINNEF PKDVIYLQPA VINATMDVFN ESKAQLLPTP TKSHYTFNLR DYAKVIQGMM
     LQDSSKVPVG REGARQHVRL WVHEVLRVFY DRLVDDQDRD WLLKYLKELV QTRFKQQFDE
     LFGHLLGENE LEIGQNEMRR CFFGVYMNED VESRVYEEIT DVPEIISLME NYLTDYNGVS
     KRPMNLAIFL FAVEHVSRIC RVLRQPGGHM LLVGVGGSGR QSLTRLGASV SAMEVFQVEI
     SKSYTKVEWR EDLISFLKKA GAAPGLPSVF LFSDTQITDE GFVEDLNNLL NSGEVPNMFP
     SDEKAQVLEA TKEKAAKLGK ELDSPMEQWR YFVEQCRQKL HVIFCMSPVG QAFRDRLRQF
     PSLVNCCTID WFQEWPVDAL EAVAYKFLKD MPLEDKARAS IVKICKAFHE NVREYSLQYK
     LKQGRHNYVT PTSYLELIST FQTLLQTKQE EKLKQKRRYE VGLEKLQSSA EQVAVMQQEL
     QDLMPKLIVT VKEVEKLMAK VEREKKEVVE PKKAIVMKDE AEASKQAAEA KGIKDECEAV
     LAVAMPVLEE ALAALDTLSA NDINYVKKLS NPPAAVKLVM EAVCVILDVK PAKIPDGKGG
     TLMDYWKPSV VLLNNKDFLQ NLKDYDKDNI EAKIIAKIRS QYTSNPEFTP AKAANASAAA
     EGLCKWIIAM DKYDTVAKFV APKKAKLREA EGKYEVVMVG LRAKQTELKG LLDKLGQLEE
     ELDANMLKKE NLQHEVKMCT VKLERAEQLI GGLGGEKTRW IAAAKQLGIE YVNLTGDVLV
     ASGIIAYLGA FTAGYRIEIV DLWTKLVRSE NIPRSTSFSF FDILGNPVHV REWMIAGLPN
     DSFSIENGII VANSRRWPLM IDPQGQANKW IRNMERERNL QIIKLLGGGD YMRILENAIQ
     FGLPVLLENV GEELDPSLEP LLLRQIFKSG GMMCIKLGDT VIEYNNDFRF YITTKYRNPH
     YLPETAVKVT LLNFMITKDG LSDQLLGVVV AKERPDLEQQ KNELVVQGAE NKRRLKELED
     KILEVLSSSE GNILEDETAV KIISEAKVVG NDITVKQTLA EQTEKNIDEA RKGYQSCGEY
     AAILFFCITD LANIDPMYQY SLPWFSSLFV ISIASSEKNP DLIKRLEIIQ DFFLYVLYNN
     VCRSLFEKDK LLFSCLLASR ILEMKGEISV PEWMFFLTGG VASSPDRPNP APEWLLDKAW
     GELCRVSKFP AFADLSDHVI ANTAAWKAMF SSPEPHMERI PGKYNDVTSF QKLLVLRCIR
     PDKVIPGIQR FVTEKLGEEF VQPPQFNLAS CYKDSSATCP LIFVLSPGSD PTAALLKFAG
     DMEMGDRLAP ISLGQGQGPK AATMITDAMA TAGSWVLLQN CHLAPSWMPE LERICENVPA
     EVHQDFRLWM TSYPSPKFPI TVLQNGVKMT NEPPKGLRAN MRRSYGLDPI SNEEFFESSN
     QPEVFKGLLF GLAFFHAVVQ ERRNFGPLGW NIPYGFDDGD LRISVRQLHM FINESTPGQL
     PLEALRYVTG ECNYGGRVTD DKDRLLLNTI LRTVYCPEMP QPGYKLSESG IYQTPEPGNW
     ESYAKTIDTF PIIPGPEVFG LHTNADITKD MNATALILSS LLATSAAMVS AGGGGGGGGG
     GGGEGGVAVV VREILRILSP NFDIEACERK YPVLYEESMN TVLSQEMTRF NKLLDRIRGS
     LINMEKAIRG VVVMSAELET AYKSMMINQV PALWQKVSYP SLKPLSSYIT DLMERLHYLQ
     DWYDHGVPAV HWVSGFFFAQ SFLTAAMQNY ARKHRYAIDT LGFDYFVVDG EPTQAPREGV
     YIKGLYLEGC AWDPVNKCLC ESQPKVIFVP APIIWLKPVL QSDMRDFNHY NCPVYRTMER
     RGVLATTGHS TNFLMYLKMP SKEPADHWIR RGVAMLCSLS D
//
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