ID B4LP34_DROVI Unreviewed; 1936 AA.
AC B4LP34;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Uncharacterized protein, isoform C {ECO:0000313|EMBL:EDW62228.2};
GN Name=Dvir\GJ19868 {ECO:0000313|EMBL:EDW62228.2};
GN ORFNames=Dvir_GJ19868 {ECO:0000313|EMBL:EDW62228.2};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW62228.2, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:EDW62228.2, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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; CH940648; EDW62228.2; -; Genomic_DNA.
DR RefSeq; XP_002051035.2; XM_002050999.2.
DR STRING; 7244.B4LP34; -.
DR EnsemblMetazoa; FBtr0437696; FBpp0394504; FBgn0207010.
DR eggNOG; KOG0241; Eukaryota.
DR HOGENOM; CLU_001485_29_0_1; -.
DR InParanoid; B4LP34; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0000235; C:astral microtubule; IEA:EnsemblMetazoa.
DR GO; GO:0005769; C:early endosome; IEA:EnsemblMetazoa.
DR GO; GO:0035371; C:microtubule plus-end; IEA:EnsemblMetazoa.
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:EnsemblMetazoa.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0051294; P:establishment of spindle orientation; IEA:EnsemblMetazoa.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IEA:EnsemblMetazoa.
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:UP000008792}.
FT DOMAIN 5..352
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1845..1887
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1598..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1904..1936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..622
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1657..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1748..1782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1936 AA; 216431 MW; 8E072BB885C7EAC1 CRC64;
MSSDKIKVAV RVRPFNRREI ELGTKCIVEM EKQQTILQNP PTLEKMERKQ PKTFAFDHCF
YSLNPEDDSF ASQETVFDCV GRDILDNAFQ GYNACIFAYG QTGSGKSYTM MGSQENKGII
PRLCDKLFLA IANKSTPELM YKVEVSYMEI YNEKVHDLLD PKPNKHSLKV REHNVLGPYV
DGLSQLAVAS YQDIDNLMTE GNKSRTVAAT NMNAESSRSH AVFSVVLTQI LTDQATGVSG
EKVSRMSLVD LAGSERAVKT GAVGDRLKEG SNINKSLTTL GLVISKLADQ SNGKKGGNEK
FVPYRDSVLT WLLKDNLGGN SRTVMVATIS PSADNYEETL STLRYADRAK RIVNHAVVNE
DPNARIIREL RHEVETLRSM LKHATGSPVG DVQDKLAESE NLMKQISQTW EEKLVKTERI
QNERQQALEQ MGISVQASGI KVEKNKYYLV NLNADPSLNE LLVYYLKERT LIGGRSISGQ
QPDIQLSGLG IQPEHCVITI EDTGLFMEPV QGARCFVNGS AVLEKTPLQN GDRILWGNHH
FFRVNSPRIG NNATLCASEP QTPAQLIDYN FARDEIMQNE LSNDPIQTAI ARLERQHEED
KQVALEKQRQ EYERQFQQLR NILSPSTPYA PYAPYDPLRM GKVTPNTPTS QMRVEKWAQE
RDEMFRRSLG QLKTDIMRAN SLVQEANFLA EEMEKKTKFS VTLQIPPANL SPNRRRGAFV
SEPAILVKRT NSGSQIWSME KLENKLIDMR EMYQEHKERI LNGLPLIETF SDDEFDDKDE
DNGKPQDPFY ESQENHNLIG VANVFLEVLF HDVKLDYHTP IISQQGEVAG RLQVEIQRVA
GQMPQDRMCE SVSETSSADS RDEYDDPVDP MANQITCRVT IKCASGLPLS LSNFVFCQYT
FWGHQEMVVP VINAESTALD QNMVFKFEHT QDFTVTINEE FLEHCIEGAL SIEVWGHRSA
GFSKSKGWEV EQQQAKARSL VDRWAELSRK IELWVEIHEL NDNGEYSPVE VTNRNEVLTG
GIYQLRQGQQ RRVNVRVKPV QNSGTLPIIC QSIVNVAIGS VTVRSRLQRP LDSYQEEDLT
VLREKWSEAL GRRRQYLDQQ IQMLIKKEEK NEQERERELS LVHQWVSLTE ERNAVLVPAP
GSGIPGAPAS WDPPAGMEPH VPVLFLNLNG DDLSAQNTND ELSISGINSI LSKEHGHRFY
TLQILQHLDK DVCCVASWDS SMHDSQALNR VTEANERIYL ILRTTVRLSH PAPMDLVLRK
RLSINIKKGQ TLTDRLKKFR LVRGENAIWQ SGVTYEVVSN IPKASEELED RESLAQLAAS
GDDCSACDGE TYIEKYTRGV SAVESILILD RLRQNVAVKE LETAHGQPLS MRKTVSVPNF
SQTVKETTNT GSIMRFDASM ESLLNVGRSE SFADLNNTAL GNKFTPAHSG AGAGGGNGGV
IRNRHSFGGK GSSDDSPGKA FGIASPATSK LLGMRMTTLH EEPLGGHRSL DEEPEDSYSD
SEYAAEYEQE RQQNKNLATR SRLTASKTMD SFMDVSSHSN QSYLSYTSSA NTNMKHLTGL
ATLSMSSSTS SGYGSQAVSC NNLSNEDITS MRSMSIDETP DFDRINSHSP PKSQTRVNPF
LKDMPKAKTQ DAEAKKLQQT LTHPLEQPKE NAQSDEECEQ QQSNNNESVK LPVPEMPQEQ
QQQREVVQQE QQPDAPELVQ ATDNQNGNKM LEHAADTSET VESVEQQLEG NGIVKEQLPP
GKVMRRKKSA TQPTNNGDSS NNNNNNSSSN SNNTSQVTRN NQRASVAKME GLGAYLDVNA
SIMSSSTEVE DDGKDLDVTL PEWIVVGESV LIRPYNTSGV ISFVGTTHFQ PGAWIGVALD
TPTGKNDGTV QGIQYFQCKP KHGIFVRADK LLLDKRGKAM RAYKATEKSN SINKEMSSSM
TRSKSRGESL NVSARK
//
