ID I3NEY9_ICTTR Unreviewed; 998 AA.
AC I3NEY9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=KIF19 {ECO:0000313|Ensembl:ENSSTOP00000022936.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000022936.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000022936.2}
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,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; AGTP01087338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01087339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01087340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01087341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01087342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005336033.1; XM_005335976.1.
DR AlphaFoldDB; I3NEY9; -.
DR STRING; 43179.ENSSTOP00000022936; -.
DR Ensembl; ENSSTOT00000020241.2; ENSSTOP00000022936.2; ENSSTOG00000025305.2.
DR GeneID; 101968075; -.
DR CTD; 124602; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000160989; -.
DR HOGENOM; CLU_001485_15_0_1; -.
DR InParanoid; I3NEY9; -.
DR OrthoDB; 239968at2759; -.
DR TreeFam; TF331721; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005930; C:axoneme; IEA:GOC.
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:0008574; F:plus-end-directed microtubule motor activity; IEA:Ensembl.
DR GO; GO:0060404; P:axonemal microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0070462; P:plus-end specific microtubule depolymerization; IEA:Ensembl.
DR CDD; cd01370; KISc_KIP3_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF52; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 11..346
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 477..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..388
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 522..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 998 AA; 110965 MW; F3F339D6C5A606EB CRC64;
MKDSGDCKDQ QLMVALRVRP ISVAELEEGA TLIAHKVDEQ MVVLMDPMED PDDILRAHRS
REKSYLFDVA FDFTATQEMV YQATTKSLIE GVISGYNATV FAYGPTGCGK TYTMLGTDHE
PGIYVRTLND LFRAIEETSN DVEYEVSMSY LEIYNEMIRD LLNPALGYLE LREDSKGVIQ
VAGITEVSTI NAKEIMQLLM KGNRQRTQEP TAANQTSSRS HAVLQVAVRQ RSRVKNLLQE
VRQGRLFLID LAGSERASQT RNRGQRMKEG AHINRSLLAL GNCINALSDR GSNKYVNYRD
SKLTRLLKDS LGGNSRTVMI AHISPASTAF EESRNTLTYA GRAKNIKTRV KQNLLSVSYH
IAQYTSIIAD LRGEIQRLKC KIDQQAGRGQ AQGQLGRGDI RHIPAEVQLH RGQGEQDEMG
PLREQLISAF QEQMDVRRRL LELENQAMEV QIETSRHLLT IAGWEHENSR RALKWREEQR
KESYTKDDSE KDSDTGDDQL DILEPPEVAS ARESIAALVG KQKQLHKEKL ALEQRCRELR
ARGRRLEETL PRRIGSEEQR EVLSLLCRVH ELEVENTEMQ SHALLRDGAL RHRREALRRL
EQHRSLCDEI IQGQRQIIDD YNLAVPQHLE ELYEVYLREL EEGSLERATI MDRVASRALQ
DSSLPKIAPA GATLTPDSDL ESVKTLNSEA QHLLGSTLPP LGTDSDAHHV FKASSRAWQV
KSSSVPTPPP IQGGSLVTQE ALPPDSLGSH ITSSPDSSEN LSEILLSHKE RKEILTGTKC
ISVKAARRRS RALGTEGRHL LAPAMERSSL SLHSLSEADD ARPPGPLACK RPPSPTLQHA
ASEENLSSST GETPSQAVGH RGGGPGFWLR GQKKSPGKKK EESLEAKRRK RRSRSFEVTG
QGLSRPKTHL LGPRPSESTS DHKTPVGGHP SPGVRHLGKV TLPLAKVKLP TGQNTGPGDP
SALTVPPNPA GVSRRVTRGP HLPHGSSTHG KDGRFRHN
//
