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Database: UniProt
Entry: A0A1S4AM81_TOBAC
LinkDB: A0A1S4AM81_TOBAC
Original site: A0A1S4AM81_TOBAC 
ID   A0A1S4AM81_TOBAC        Unreviewed;       632 AA.
AC   A0A1S4AM81;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Kinesin-like protein KIFC3 {ECO:0000313|RefSeq:XP_016477832.1};
GN   Name=LOC107799255 {ECO:0000313|RefSeq:XP_016477832.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016477832.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016477832.1}
RP   IDENTIFICATION.
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_016477832.1; XM_016622346.1.
DR   AlphaFoldDB; A0A1S4AM81; -.
DR   SMR; A0A1S4AM81; -.
DR   STRING; 4097.A0A1S4AM81; -.
DR   PaxDb; 4097-A0A1S4AM81; -.
DR   GeneID; 107799255; -.
DR   KEGG; nta:107799255; -.
DR   OMA; MDHTHLV; -.
DR   OrthoDB; 54358at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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:UP000084051}.
FT   DOMAIN          97..421
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          19..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          49..83
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          417..466
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        531..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   632 AA;  71392 MW;  4E8071F6371DA001 CRC64;
     MFVSTEEEHI SLPLANGKVL ENSSPIGSNP DSNEDEVSQE IPSNFMDVNV VQEDEKFQLE
     QRILNLEGEI GSLRNKERSL DERRREALNK ILDIKGCIRV FSRVRPFLPT DKRRTHQPIS
     VESEKIVVRS GGSRKEFEFD KVFTQEAIQE DVFAEVEPIL RSAIDGHNVC ILAYGQTGTG
     KTYTMEGTTE SPGIIPRVLQ ELFHLSSLDS STSFTFSISM LEVYLGSLRD LLAPRPSSRT
     YTASRCNLNI QTDSKGSVEI DGLTEVEISN FTKATWWYNK GRRVRSTSWT NVNETSSRSH
     CLTRISIYRY GDALGGKAEV SKLWMVDLGG SERLLKTGAI GQTLDEGRAI NLSLSALGDV
     IAALRRKRGH VPYRNSKLTQ VLKDSLGDRS KVLMLVHVSP YEEDVGETTC SFTFAKRARA
     AECNRELSQE SKKLREKRIS ELEEQMKEAE EGCQEIRTQI QKAEFLLNEN KRLFMKKYQP
     LEDEETFPIT PKENVAEIIT VTPRNSEKGV KTKVTSSVPR FMSATVASRQ RETTAEREIR
     SRPKSLRSWA RSSTQLSGSQ SNSFSDRRFK AQLRTSNKRS RYSETNTIAG DIKCEDSDIK
     PSVLPQSKTI ASSDPKPRGT VPHHRRRMSD LL
//
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