ID W5NGD5_LEPOC Unreviewed; 2017 AA.
AC W5NGD5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Kinesin family member 13Bb {ECO:0000313|Ensembl:ENSLOCP00000019694.1};
GN Name=KIF13B {ECO:0000313|Ensembl:ENSLOCP00000019694.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019694.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019694.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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; AHAT01008432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000019694; -.
DR Ensembl; ENSLOCT00000019726.1; ENSLOCP00000019694.1; ENSLOCG00000015976.1.
DR eggNOG; KOG0241; Eukaryota.
DR GeneTree; ENSGT00940000155500; -.
DR HOGENOM; CLU_001485_29_2_1; -.
DR InParanoid; W5NGD5; -.
DR OMA; LVCSIKI; -.
DR Proteomes; UP000018468; Linkage group LG1.
DR Bgee; ENSLOCG00000015976; Expressed in embryo and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd22730; FHA_KIF13B; 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; 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:UP000018468}.
FT DOMAIN 10..361
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1921..1963
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 558..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1375..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..1993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..418
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 622..649
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 570..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2017 AA; 224910 MW; C6078A3D0D03A9C7 CRC64;
MGETNVNDSN VKVAVRVRPM NRREKDLKTK CVVEMEGNQT ILHPATGNLG KGDIRFENEP
SVVFAYDYCF WSMDESEKDK FAGQDVVFQC LGESLLQNAF QGYNACIFAY GQTGSGKSYT
MMGSADQPGL IPRLCSALFE RTLQYQREEE SFTVEVSYME IYNEKVRDLL DPKGSRQALR
VREHKVLGPY VDGLSRLAVT SYKDIESLMS EGNKSRTVAA TNMNEESSRS HAVFNIILTH
TLKDIQSGTC GEKVSKLSLV DLAGSERAAK TGAAGERLKE GSNINKSLTT LGLVISALAD
QGAGKNKNKF VPYRDSVLTW LLKDSLGGNS RTAMVATVSP AADNYDETLS TLRYADRAKS
IVNHAVINED PNARIIRELR EEVEKLREQL TQAESMKAPE LKDRLEESEK LIQEMTVTWE
EKLRKTEAIA QERQKQLESL GISLQSSGIR VGEDKCFLVN LNADPALNEL LVYYLKDHTL
VGAADSQDIQ LCGMGIQAEH CVIDITAEGQ VILTPHRNSR TCVNGSAVSS PVQLYHGDRI
LWGNNHFFRI NLPKRRSRGE REEEEGVIKN SGSSEQLEGD GDTASEVSSE VSFSYELAQT
EVMMKVSLPP DPMQAILMSL ERHHEEEKRS ALERQRLMYE QELEQLRRRL SPDKQQQHYR
SMERLAASPS AQQKLRQWSE EREAVLTRSL RKLREQIVRA NLLVQEASFI AEELEKRTEY
HVTLQIPASN LNANRKRDAV LSEPAVQVRR KGKGKQIWAL EKMENRLVDM RELYQEWNDF
DEDNPVMRSY FKRADPFFDE QENHSLIGVA NVFLSCLFYD VKLQYAVPII NQKGEVAGRL
HVEVVRVSGD FQERLAGGED PESSAEGEVQ DRKLICMVKI LQATGLPQYL SNFVFCQYSF
WDQSEPIIVA PEVDPSASSP ASKDPQCMVV FDHCKELAVT VSEDFIEYLT EGAVAIEVYG
HKQTDPRRNF ALWDLGIIQA KTRTLRDRWS EVTRKVELWV QILELNENGE YVPVEVVAAK
DVRTGGIFQL RQGQSRRIQV EVRSVQDSGT MPLIAESVLA VSVGCVEIRQ ARSAKSGESQ
EVEDDEMDSY QERDLERLRR QWLTALTKRQ EYLDQHLQNL VSKQDKSEDD VDRESQLLEC
RLTLTEERNA VMVPSAGSGI PGAPAEWIPV PGMETHIPVL FLDLSADDFS SQDNLDQPEA
GGWDATLSGE DEDEFFELQI VKHHDGEVNA EASWDSTVHN CPQLSRGAAP DQRVYLTVKT
TVQLSHPADM QLILRKRICV NVTGRQGFAQ SFLRRMSHRS TIPACGVTFE IVSNIPGDAE
GSEDREMLAR LATSVENQQS ADSEAAIEKY LRSVLAVENI LTLDRLRQEV AVKEHLAGKG
KGNRRSLSSP NVHRLSGSRQ DLSPSSQLEN KGRWESQQDI SLTSSQFSRT PPHPSLSKSA
EPEAVKALVP QMPKLLKSLF PVRDDKKDLR PSPLAHQSVP RIMVQSASNE ESPLKPKQVC
FLFSKPFWKQ GAQLSLKLLR TKKSGVLVYC KMTSRIMANY IIICKTDIIH TLFCKLKNER
VFYIGVAMFF ICVKLEIFVY KMKTSKHCNL LQHETDFLFL YLIVEDQSKL LLIFKMYFCE
CILVVPKNDS ISPAAPTIGS ARQYEKYYPT ESISTADGQY EKCSPVKSIT VLEGHDDKHS
IAASLAVVDR PSENHEVPSV PETPDVPQSP ASEVSSGYFS ASISTATLSE ASIIGSDSAS
SPVNQASASN IIVAHLGSPG TDSAATPTNN GKVAEEGLEV AEAGLHLDQS QGSVDKNGEA
SPETIDTTKP PEIKPQMKPE PALLKSSASN PFKIQKVKTS DLKSFTRILA EETTLQEDGN
RALVERSMMS RGSDQEPAET EQLEIGSDPE EAKEAVLPDW LKEGEYVTVG TSKSGVVRYI
GPTDFSDGVW VGVELDVPAG KNDGSVGGKQ YFKCNPGYGV LVRPDRVSRS SGSGKRRGEN
RRTGNFSGSN PNLAALTAMV KGEGAARKGE NRKSWNS
//
