ID A0A0P8Y3R4_DROAN Unreviewed; 1947 AA.
AC A0A0P8Y3R4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KPU76315.1};
GN Name=Dana\GF11865 {ECO:0000313|EMBL:KPU76315.1};
GN Synonyms=dana_GLEANR_11887 {ECO:0000313|EMBL:KPU76315.1};
GN ORFNames=GF11865 {ECO:0000313|EMBL:KPU76315.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:KPU76315.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:KPU76315.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CH902619; KPU76315.1; -; Genomic_DNA.
DR RefSeq; XP_014762930.1; XM_014907444.1.
DR SMR; A0A0P8Y3R4; -.
DR EnsemblMetazoa; FBtr0381227; FBpp0341544; FBgn0088905.
DR GeneID; 6494727; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22706; FHA_KIF13; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12473; DUF3694; 2.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000007801}.
FT DOMAIN 21..368
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1856..1898
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 784..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 605..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 867..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1947 AA; 217617 MW; 2CB32CEFD14F5C15 CRC64;
MNHSPARIEN HPEASAMSSD KIKVAVRVRP FNRREIELGT KCIVEMEKQQ TILQNPPTLE
KIERKQPKTF AFDHCFYSLN AEDDNFASQE TVFDCVGRDI LDNAFQGYNA CIFAYGQTGS
GKSYTMMGSQ ESKGIIPRLC DKLFSAIANK STPELMYKVE VSYMEIYNEK VHDLLDPKPN
KQSLKVREHN VLGPYVDGLS QLAVTSYQDI DNLMTEGNKS RTVAATNMNA ESSRSHAVFS
VVLTQILTDQ ATGVSGEKVS RMSLVDLAGS ERAVKTGAVG DRLKEGSNIN KSLTTLGLVI
SKLADQTNGR KGGNDKFVPY RDSVLTWLLK DNLGGNSRTV MVATISPSAD NYEETLSTLR
YADRAKRIVN HAVVNEDPNA RIIRELRHEV ETLRSMLKHA TGSPVGDVQD KLAESENLMK
QISQTWEEKL VKTERIQNER QQALEKMGIS VQASGIKVEK NKYYLVNLNA DPSLNELLVY
YLKDRTLIGG RSISGQQPDI QLSGLGIQPE HCVITIEDSG LYMEPVQGAR CFVNGSAAVE
KTPLQNGDRI LWGNHHFFRV NSPKSNNTSM CASEPQTPAQ LIDYNFARDE IMQNELSNDP
IQTAIARLER QHEEDKQVAL EKQRQEYERQ FQQLRNILSP STPYAPYAPY DPLRMGKITP
NTPTSQMRVE KWAQERDEMF RRSLGQLKTD IMRANSLVQE ANFLAEEMEK KTKFSVTLQI
PPANLSPNRR RGAFVSEPAI LVKRTNSGSQ IWTMEKLENK LIDMREMYQE HKDRVMNGLP
LVEPFSDEEY DDKDEENKPQ DPFYESQENH NLIGVANIFL EVLFHDVKLD YHTPIISQQG
EVAGRLQVEI ERIAGQMPQD RMCESVSESS GDSRDEYDDP VDPTANQITC RVTIKCASGL
PLSLSNFVFC QYTFWGHQEM VVPVINAEST AHDQNMVFKF EHTKDFTVSI NEEFLEHCIE
GALSIEVWGH RSAGFSKSKG WEVEQQQAKA RSLVDRWAEL SRKIELWVEI HELNDNGEYS
PVEVTNRNEV LTGGIYQLRQ GQQRRVNVRV KPVQNSGTLP IICQSIVNVA IGSVTVRSRL
QRPLDSYQEE DLTVLREKWS EALGRRRQYL DQQIQMLIKK EEKNEQERER ELSLVHQWVS
LTEERNAVLV PAPGSGIPGA PASWEPPSGM EPHVPVLFLN LNGDDLSAQN TNDELSIAGI
NSILSKEHGH KFYTLQILQH LDKDVCCVAS WDSSMHDSQA LNRVTEANER VYLILRTTVR
LSHPAPMDLV LRKRLSINIK KGQTLTDRLK KFRLVRGENA IWQSGVTYEV VSNIPKASEE
LEDRESLAQL AASGDDCSAS DGETYIEKYT RGVSAVESIL TLDRLRQNVA VKELETAHGQ
PLSMRKTVSV PNFSQIMRFD ASMESLLNVG RSESFADLNN SALGNKFSPA GHGAGGAGSG
VIRNRHSFGG KGSSDDSPGK AFGIGTIALL SARPTFLNLN LNLNTLRNAP TKPSPATTKL
LGMRMTTLHE EPLGGHRSLD EEPEDSYSDS EYAAEYEQER QQNRSFAGGR SRLTASKTMD
SFMDVSNHSN QSYLSYTSSA NSNMKHLTGL ATLSMSSSTS SGYGSQAVSC NNLSNEDIAS
MRSMSIDETP DFDRINSNSP PNRQTRVNPF LKDMPKAKAQ DQPEPQAKKL QETFTHPLEL
PKENAQSDED EPEQLPKNNN NNNVESVKPA EPMIVAEMEQ EAADPEIESQ PELATDNQNG
NKSAEEEVLE GDGIVTEELP AGKVVRRKKS NTQPPNNLNN NNTSNSTSQA PRVNHRASVA
KMEGLAALMD SSIMTSSTEI DDESKDVEIT VPDWIVVGES VLIRPYNTSG VIRFVGVTEF
QPGAWIGVEL DTPTGKNDGS VKGIQYFQCK PKHGMFVRSD KLMLDKRGKA MRAYKAAEKS
NSISKEMSSS MTRSKSRGES LNVAARK
//
