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Database: UniProt
Entry: M1AB63_SOLTU
LinkDB: M1AB63_SOLTU
Original site: M1AB63_SOLTU 
ID   M1AB63_SOLTU            Unreviewed;       973 AA.
AC   M1AB63;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Kinesin heavy chain {ECO:0000313|EnsemblPlants:PGSC0003DMT400018807};
GN   Name=102597887 {ECO:0000313|EnsemblPlants:PGSC0003DMT400018807};
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:PGSC0003DMT400018807, 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:PGSC0003DMT400018807}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400018807};
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   AlphaFoldDB; M1AB63; -.
DR   EnsemblPlants; PGSC0003DMT400018807; PGSC0003DMT400018807; PGSC0003DMG400007291.
DR   Gramene; PGSC0003DMT400018807; PGSC0003DMT400018807; PGSC0003DMG400007291.
DR   HOGENOM; CLU_001485_8_0_1; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1AB63; baseline and differential.
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; 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   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   BINDING         477..484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   973 AA;  107152 MW;  378BFB201892CC9B 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
     IPESRLVLIP ITL
//
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