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Database: UniProt
Entry: A0A1U8M4D0_GOSHI
LinkDB: A0A1U8M4D0_GOSHI
Original site: A0A1U8M4D0_GOSHI 
ID   A0A1U8M4D0_GOSHI        Unreviewed;       643 AA.
AC   A0A1U8M4D0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kinesin-like protein klp-3 isoform X2 {ECO:0000313|RefSeq:XP_016721655.1};
GN   Name=LOC107933863 {ECO:0000313|RefSeq:XP_016721655.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016721655.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016721655.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016721655.1};
RG   RefSeq;
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}.
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DR   RefSeq; XP_016721655.1; XM_016866166.1.
DR   AlphaFoldDB; A0A1U8M4D0; -.
DR   GeneID; 107933863; -.
DR   OrthoDB; 54358at2759; -.
DR   Proteomes; UP000189702; Unplaced.
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   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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:SF9; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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; 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:UP000189702}.
FT   DOMAIN          104..429
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          590..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          63..90
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          440..474
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         182..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   643 AA;  72039 MW;  FF00152D6539D76C CRC64;
     MLISSETEEI TLPSTEVKEC STSSPVGSNP DSLNGLPPPP DLPDSPSLST IFCDVNVVPE
     HEKSQLEQSI HKLQGEIAEL RLMLRSIDEK RRETLNKIID IKGSIRVFCR VRPFLWTDKR
     RTPEPILSEL DQVIVTSSGS RKEFGFDKIF HQEANQDDVF VDVEPILRSA LDGHNVSILA
     YGQTGTGKTF TMDGTTVQPG IVPRALKELF QQVSSDKSFS YTFSMSMLEV YMGNLRDLLA
     SKPALRTNET VSRCNLNIQT DPKGSVEIEG LTQVEIPDFA KARWWYTKGR RARSTSWTNV
     NEASSRSHCL TRIVISRRGD TPEAKPKISK LWMVDLGGSE RLLKTGATGQ TLDEGRAINL
     SLSALGDVIA ALRRKKGHVP YRNSKLTQIL KDSLGVGSKV LMLVHISPCQ EDLEETICSL
     SFAKRAKAVD SSRGLPEDLK KLREKRISEL EENMREVEEE CQKLANQISK AEFLLSENRK
     LYSTAYGVPD ESAEKNPENH EEDAKTHVIE TPRVTQKPIQ QSIHRSLPRF MSSTVASRER
     QNAAEKDIVT RARTFRPRAR SSTQLSGFQS LSFSDNRFGS LLRHSVKNSR FKDTNGPAIE
     SPKCNDSSSL KTTSLSRSKV VTSSDPNLRV KLGHHRRRMS DFV
//
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