ID A0A0T6BFU7_9SCAR Unreviewed; 1826 AA.
AC A0A0T6BFU7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:KRT86208.1};
GN ORFNames=AMK59_207 {ECO:0000313|EMBL:KRT86208.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT86208.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT86208.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT86208.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT86208.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT86208.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJIG01000732; KRT86208.1; -; Genomic_DNA.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000051574; 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; 2.
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; 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:UP000051574}.
FT DOMAIN 8..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1750..1792
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 833..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 594..626
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 840..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1826 AA; 204876 MW; ACB691D89A7A75CB CRC64;
MSSSTSDKIK VAVRVRPFSR RELELATLCI VEMEKQQTIL QYPSSLDKIE RKQPKSFAFD
HCFYSADPNR EDYASQEVVF DCLGRDILDN AFQGYNACIF AYGQTGSGKS YTMMGTQENN
GIIPRLCDSL FDLIAKQQSS ELTYKVEVSY MEIYNEKVHD LLDPKTNKQS LKVREHNVLG
PYVDGLSHLA VTSFQDIEIL MAEGNKSRTV ASTNMNSESS RSHAVFTVIL TQTLTDSKTG
VSGEKQSRLS LVDLAGSERA VKTGAVGERL KEGSNINKSL TTLGIVISKL ADQSSGAKNK
DKFVPYRDSV LTWLLKDNLG GNSKTVMVAT ISPAADNYEE TLSTLRYADR AKRIVNHAVV
NEDPNARIIR ELQEEVAALK EMLKHATGSP VGDIQRVDIH QKLSESEKLY KEMSQTWEEK
LMKTERIQNE RQQTLEKMGI SIQDSGIKVE KNKFYLVNLN ADPSLNELLV YYLKEKTVVG
ATGNGQDGEP DIQLSGLGIQ PEHCIITIED GSIFLEPLAN ARSYINGSQV TKKTQLRHGD
RIVWGNHHFF RVNCPKSISS ASEPQTPAQN IDYNFARDEL MLNELSNDPI QAAISRLEKQ
HEEDKQVALE KQRQEYERQF QQLKNTMSPS TPYPPYSYDP FRFGKNTPCT PTTQMRVEKW
AQERDEMFKR SISQLKSGIL KANALVQEAN FFAEEMGKQT KFSVTLQIPP ANLSPNRKKG
AFVSEPAILV KRKSESQVWT MEKLENKLVD MREMYEERKE CGLSLRESPS DPFYESQENH
NLIGVANIFL ESLFHDVILD YHTPIISQQG EVAGRLQVEL SRVSGVLPQD RICEAASDTS
DNSSHDEDDD SGGTSEITVR VHIKQASGLP PSLSNFVFCQ YTFWNHPDPI VVPPFEPESH
NTTFPSQKDS MTFKFDDVRN FPIVTTEEFL EHCAEGALSI EVWGHRSAGF SRLKDGWEVE
QQTRTIARSL IDRWSEVTRK IELWVEIQEL NEFGEYGPVE VTNKTCMLTG GVYQLRQGQQ
RRIQVRVKPV QNSGTLPIIC QSILEIEVGS VTVRNRLQKP LDSYQEEDLT VLRDKWCDLL
KRRREYLDQQ IKKLIDKPDK TEQDIEREQN LVDQWINLTE ERNVVTVPAP GSGIPGAPAI
WEPPAGMEPY VPVLFLDLNA DDLSTHQSGE AVPVTGLNSI LPKEIGSKFY SLHILQHLEK
DVCAVASWDS SIHDNLHLNK VTDANDRVYL ILRTTIRLSH PAPMDLVLRK RLALNIYKRQ
SIADRIKRKI VRTDILTQSG VTYEVVSNIP KACEELEDRE SLAKLACSGE DTSLVDGETY
IEKYTRGVCA VENILSLDRL RQSVAVKELL QAKGQPMMRK TASVPNFSQF MRLDMSTESL
NISRSESVSE LSGDMHSNPT PLRPRTSGLA RPTFLNLNLN LNSLRLQQPT GTTKLFTGIV
SPANQKMGLR MTTLHEEQVP LPRKHSLDLI TDETLQEEKS ESKIYNKSEF TQPTKTGYHP
RRPISSSRTL DSLVELAPKT GTPSASSSGY GSQAVSSTNL TSEDSMSLRS ISIDETPDME
VRSTVVNDLQ PVSESIYDVS NSENEAGEGQ VNVLDQTQSV IEDNSDDSAI NGMSTSNTST
ETSEKIESDP PLEGTSIVKT NLSPGRVVRR VKKTNKSQGT FTSQRASFPQ VRPHLSESKI
ASTMESFHIS SEDGLDSSVD KIEAEESDNN FGSRPDLTKL VDVPVPDWVV LGESVLIRPY
NCSGVVAYMG GTEFAAGTWV GIELDAPKGK NDGMVQGVRY FTCRPKHGMF VRADKLILDR
RGRAMRAYKA EALLNTNHKY SKGMEF
//
