ID A0A0S3S0A0_PHAAN Unreviewed; 1021 AA.
AC A0A0S3S0A0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.04G391300 {ECO:0000313|EMBL:BAT86277.1};
GN ORFNames=VIGAN_04391300 {ECO:0000313|EMBL:BAT86277.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT86277.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT86277.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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 EMBL; AP015037; BAT86277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3S0A0; -.
DR Proteomes; UP000291084; Chromosome 4.
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:SF39; KINESIN-LIKE PROTEIN KIN-14I; 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:UP000291084}.
FT DOMAIN 40..162
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 411..736
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 956..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 743..770
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 956..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1021 AA; 112402 MW; 4882142CA4E0256B CRC64;
MAAEAALFFS VASVVEDVLQ QHGPRLKDLD LESRKAEEAA SRRYEAAGWL RKMVGVVAAK
DLPAEPSEEE FRLGLRSGII LCNVINKVQS GAVPKVVESP IDSASIPDGA PLTAYQYFEN
VRNFLVAVQE IGLPTFEASD LEQGGKSSRI VNCVLALKSY SEWKTSGANG VWKFGGNLKP
TVSAKSFVRK NSDPFTNSLS RTSSINDKHL TVLSSDVESD KMSGSHSLSS LVRAILLDKK
PEEVPKLVES VLCKVVEEFE QRIASQGEKA KVTSIDPVSQ SNGSVVADKK GEKKIHVVTK
KEDGIHKSPV NAMVSKKEDR IHKNLVADEE SQRQFLKQKM LFDQQQREIK ELRHTLHTTK
SGMQFMQMKF REEFSNLGMH VHGLAHAASG YHRVLEENRK LYNQVQDLKG SIRVYCRVRP
FFPGQSNHLS AVENINDGTI TVNIPSKNGK GRRSFNFNKI FGPSATQAEV FLDMQPLVRS
VLDGYNVCIF AYGQTGSGKT YTMTGPKEIT EKSQGVNYRA LSDLFLIADQ RKDTFQYDVS
VQMIEIYNEQ VRDLLVTDGT NKRLEIRSSS QKGLSVPDAS LVPVSSTIDV IELMNLGQRN
RAVGATALND RSSRSHSCLT VHVQGRDLTS GAILRGCMHL VDLAGSERVD KSEATGDRLK
EAQHINKSLS ALGDVIASLA QKNSHVPYRN SKLTQLLQDS LGGQAKTLMF VHISPESDAI
GETISTLKFA ERVATVELGA ARVNKDSSDV KELKEQIASL KAALARKEGE SEHSLCSSSE
KYRTKGIELS PYQIPDTGDQ LGCRRPMVEV GNIELQSNTT VRHKTQSFDF DEISGNSPPW
PPVNNSLGQN YAEDDKESGS GEWVDKVMVN NKQDVNKTEN LLGCWQTSNG NLSESFYQKY
LKDSCKMYSE QSYNMFIGGN QFNIVGSDDT DEPDAATSDS SEPDLLWQFN HSKLSSMTSG
IGSKTTRSIS KSAKSPELSK NAVHSSPLGP SPSLKQSNGV SHRTGRHPAP VDVKRRSGGR
K
//
