ID B0VZW2_CULQU Unreviewed; 1906 AA.
AC B0VZW2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:EDS35204.1, ECO:0000313|EnsemblMetazoa:CPIJ000231-PA};
GN Name=6031153 {ECO:0000313|EnsemblMetazoa:CPIJ000231-PA};
GN ORFNames=CpipJ_CPIJ000231 {ECO:0000313|EMBL:EDS35204.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS35204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS35204.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ000231-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ000231-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) to UniProtKB.
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; DS231815; EDS35204.1; -; Genomic_DNA.
DR RefSeq; XP_001841996.1; XM_001841944.1.
DR STRING; 7176.B0VZW2; -.
DR EnsemblMetazoa; CPIJ000231-RA; CPIJ000231-PA; CPIJ000231.
DR KEGG; cqu:CpipJ_CPIJ000231; -.
DR VEuPathDB; VectorBase:CPIJ000231; -.
DR VEuPathDB; VectorBase:CQUJHB003396; -.
DR eggNOG; KOG0241; Eukaryota.
DR HOGENOM; CLU_001485_29_2_1; -.
DR InParanoid; B0VZW2; -.
DR OMA; GQENHNL; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000002320; 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; 1.
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; 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:UP000002320}.
FT DOMAIN 4..350
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1820..1862
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 837..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1402..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..629
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 845..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1906 AA; 212788 MW; 41CCE528C490D5CD CRC64;
MSDKIKVAVR VRPFNRRELE LATENVIEMN DSQTILKYPA TLDKMERKPP KMFAFDHCFY
STDPVAENFA SQELVFKDVG RDILDNAFQG YNACIFAYGQ TGSGKSYTMM GNQENKGIIP
RLCDELFASI AAKQTDELNY KVEVSYMEIY NEKVHDLLDP KTSKQSLKVR EHNVLGPYVD
GLSQLAVTSF MDIDNLMAEG NKSRTVAATN MNSESSRSHA VFTVVLTQTL IDTLSGVTGE
KVSRVSLVDL AGSERAVKTG AVGERLKEGS NINKSLTTLG LVISKLADQT SGSKNKDKFV
PYRDSVLTWL LKDNLGGNSK TVMLATLSPA ADNYEETLST LRYADRAKRI VNHAVVNEDP
NARIIRELRM EVETLREMLK HATGTSLPGE MKRVDIHDKL AESENLMKQI SQTWEEKLEK
TEQIQSERQQ ALEKMGISVQ DSGIKVEKNK YYLVNLNADP SLNELLVYYL KEVTLIGGHN
NEGTTKQLPD IQLMGLGIQP EHCLITIEDG ELFMAPIDSA RCCVNGSVAT EKTSLNHGDR
ILWGNHHFFR VNCPKSNNNN NNLSSEPQTP AQHLDYYYAQ EELMQNEFSN NPIQAAISRL
EKQHEEDKQV ALEKQRQEYE KQFQQLRNIL SPTTPYAPYA PFDPFRLGKL PPNTPNAQLR
VEKWAQERDE MFKRSLGQLK TDIVRANSLV QEANVLAEEM NKQTKFSVTL QIPPANLSPN
RKRGAFVSEP AILVRRMNSG SQIWSMEKLE NKMIDMRDMY QEYKDNNYTV TDENKNKSDP
FYESQENHNL IGVANIFLEV LFHDVKLDYH TPIISQQGEV AGRLQVEISR VAGQFPQDRV
NESASESSQD SHEDDDMCEP ASNQVTCRIS VKQASGLPLY LSNFVFCQYS FWNHEVAVVP
ATNQEVAAHN QNITFKFDHE SDYIITVNEE FLEHCSDGAL SIEVWGHRSV GFSRAKDWEV
EQQQAKARSL ADRWAELSRK IELWVEIHEL NDNGDWAPVD VQCSKDMLTG GVYQLRQGFQ
RRIMVRVKPV QNSGTLPIIC QSIINVSVGC VTVRSKLQKP MDSYQEEDLT VLRDKWSEAL
GRRRQYLDQQ IQKLINKDDK TEQEKEREQS LVNQWVSLTE ERNAVLVPAP GSGIPGAPAS
WDPPMGMEPH VPVLFLDLNA DDLTTQSVND EVPLAGLNSI LPKEHGNKFY NLQIIQHLDK
DICAVCSWDS SIHDSPSLNR MTEANERVYL ILKTTVRLSH PAPMDLVLRK RLALNIYKRQ
SFTDRLKKLR IGRAECSSLQ SGVTYEVVSN IPKASEELED RESLAQIAAT GEDVSASDGE
TYIEKYTKGV SAVESILTLD RLRQSVAVKE LEQVRGPALS MRKTASVPNF SQMRFFDASL
ESLLGIGRSE SFADLKMGLN SAQSTRETAT SRQKLKGTSP GGGEDSANSS YGLSKYNCLL
SYNLILMMRF FDASLESLLG IGRSESFADL KMGLNSAQST RETATSRQKL KGTSPGGGED
SANYSYGLTS PAASKLAQRM TTLHEEPLIK QICYEEEGED RFSEPEYAEY EDDYEPPKKP
TMSKMKSSYT VESFMDIDKR PGHAGVGGGS DLCKFSAAGK GVKPSGGGQV AQVKSQNIAA
GTPSMSSSTS SGYGSQAVSC SNLTNDDTYS IRSLSVGETP ETMSPSNNVL RSNNPLMKDV
VSFDELNGNR GGDLLEQEAL AYNSNAKRAS EPAVMTGSRD TMIDEEDEGV VNEQEVEEDE
EVIAMDESHV SSTADDDSHL QHEDVVDEEN NSSKLLQDSD VMENSFSTPS KHENIPDWVV
VGESVQIRPY NTSGVISFVG GTHFQGGTWI GVELDTPTGK NDGTVQGIQY FSCRPKHGIF
VRVDKLILDK RGRAMRELKR AEKMKAEFGG QKSGGQKAVS ANGPRK
//
