ID A0A287CZC7_ICTTR Unreviewed; 772 AA.
AC A0A287CZC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
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:ENSSTOP00000026662.1, 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:ENSSTOP00000026662.1}
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,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; AGTP01057026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287CZC7; -.
DR STRING; 43179.ENSSTOP00000026662; -.
DR Ensembl; ENSSTOT00000021020.2; ENSSTOP00000026662.1; ENSSTOG00000021156.2.
DR GeneTree; ENSGT00940000158533; -.
DR InParanoid; A0A287CZC7; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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; cd01375; KISc_KIF9_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:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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 6..324
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 466..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 333..360
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 504..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 772 AA; 87476 MW; 70CB482400BAC77F CRC64;
MGTRKKVHAF VRVKPTDDFA HEMIRYGDDN KSIDIHLKKD IRKGVVNNQQ TDWSFKLDGV
LHDASQDLVY ETVAKDVVSQ ALDGYNGTIM CYGQTGAGKT YTMTGQVFKM IEERPTHAIT
VRVSYLEIYN ESLFDLLSTL PYVGPSVTPM TIVENPQGVF IKGLSVHLTS QEEDAFSLLF
EGETNRIIAS HMMNKNSSRS HCIFTIYMEA HSRTLSDEKY VTSKINLVDL AGSERLGKSG
SEGRVLKEAT YINKSLSFLE QAIIVLGDHK RDHIPFRQWK LTHALKDSLG GNCNMVLVTN
IYGEAAQLEE TLSLLRFASR MKLVTTEPAI NEKYNAERMV KNLEKELVLL KQELAIHDSL
ANRNIVTYDP MDEIQIAEIN SQVRRYLEGT LDEIDIINLR QIQEVFNQFW VVLSQQEQEV
EAALRRKYTL IDKNDFATIS AVQKAGIIDV NGHLVGEPDG QGFGLGVAPF STKPAKKSKS
KKTVKDPPSS SARKEGASSP VSGKDLDMIS TSKTQLVPSS KDGDVKDVLS RDRETSSIEP
LPSDSPKEES RPLRPTTPPS KLMAFEDFKN ERGSEINRIF KENKSILNER RKRASETTQH
INVIKREIDV TKEALNSQKS LREKQGEYEN KGLMIIDEEE FLLILKLKDL KKQYRSEYQD
LRDLRAEIQY CQHLVDQCRH RLLMEFDIWY NESFVIPEDM QVALKLGSSI GPGMVPVSRI
VSLGEDDQDN FAQLQQTVLP EGPDAISFYN AKIKTEQKHN YLKTIMGLQQ TH
//