ID M1AB64_SOLTU Unreviewed; 1005 AA.
AC M1AB64;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Kinesin heavy chain {ECO:0000313|EnsemblPlants:PGSC0003DMT400018808};
GN Name=102597887 {ECO:0000313|EnsemblPlants:PGSC0003DMT400018808};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400018808, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400018808}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400018808};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
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DR RefSeq; XP_006355844.1; XM_006355782.2.
DR AlphaFoldDB; M1AB64; -.
DR STRING; 4113.M1AB64; -.
DR PaxDb; 4113-PGSC0003DMT400018808; -.
DR EnsemblPlants; PGSC0003DMT400018808; PGSC0003DMT400018808; PGSC0003DMG400007291.
DR GeneID; 102597887; -.
DR Gramene; PGSC0003DMT400018808; PGSC0003DMT400018808; PGSC0003DMG400007291.
DR KEGG; sot:102597887; -.
DR eggNOG; KOG0239; Eukaryota.
DR InParanoid; M1AB64; -.
DR OMA; HNNSIMT; -.
DR OrthoDB; 54358at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1AB64; baseline and differential.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR CDD; cd21203; CH_AtKIN14-like; 1.
DR CDD; cd01366; KISc_C_terminal; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972:SF61; KINESIN-4-LIKE; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT DOMAIN 40..162
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 395..719
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 754..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 726..753
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 756..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1005 AA; 110685 MW; 22DAD957F2182008 CRC64;
MAADGALSFS VASVVEDVLQ QHGSRSRNLD LDARRAEEAA TRRYEAAAWL RKVVGFVGAK
DLPAEPSEED FRLGLRSGII LCNVLNKMQP GAVSKVVESP VDSALIPDGA ALSAYQYFEN
VRNFLVAAQE LGIPSFEASD LEQGGKSSRV VSCVLGLKAY SEWKQTGGTG VWKFGGNVKS
TTSAKQFVRK NSEPFSSSLS RSMSMNEKST NGVCTEAESN KMSSSSLSNL VRAILIDKKP
EEVPNLVESV LNKVVEEFEQ RITSQIQLNK AITPKDSAVS CGNKFLQKHS SASTKTDQRT
VTLMKEENRI VNGELQRRHM MQNTFVDQQQ RDIKDLKQTL LTTKAGMQFM QMKFHEEMQN
IGMHVHGLAH AASGYHRVLE ENRRLYNQVQ DLKGSIRVYC RVRPFLPGQS SYISNVDHID
DGSITIGVPS KNGKGRKSFN FNKVFGPSVT QGEVFSDTQQ LIRSVLDGYN VCIFAYGQTG
SGKTYTMTGP KDLTEQSQGV NYRALGDLFL LAEQRKDTFL YDVSVQMIEI YNEQVRDLLV
SDGVHKRLEI RSASQGLTVP DASLVRVAST SDVIDLMNLG QRNRAVSATA LNDRSSRSHS
CLTVHVQGRD LTSGAILRGC MHLVDLAGSE RVDKSEVTGD RLKEAQHINK SLSALGDVIS
ALAQKNAHVP YRNSKLTQLL QDSLGGQAKT LMFVHISPEP DAIGETISTL KFAERVSTVE
LGAARVHKDT TDVKELKEQI ASLKAALARK ETEPVSMSYK VTSSPGGLQS SPFQSNLQGR
EMLGNSNIQR RPVEDVGNRE VSSNSASRQR RQSFDLDELL GNSSPWPPVS SPSENYVEDD
INMSSGEWVD KVMVNKQEAA RGVGNLFGCW ESEKGNGSDV LYEKYLSDSS KVYQEKTSNL
FQMSNHFDIT ATEDLDEFDA TTSDSSEPDL LWQFNNSKVN TFPSSGNGSK IQKPNTKPGK
IPESRNVVHK VGPPLSRQTS GISHNQRNGR QAMTAEMKRK AGSRK
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