GenomeNet

Database: UniProt
Entry: A0A0A0LPD7_CUCSA
LinkDB: A0A0A0LPD7_CUCSA
Original site: A0A0A0LPD7_CUCSA 
ID   A0A0A0LPD7_CUCSA        Unreviewed;      1083 AA.
AC   A0A0A0LPD7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Csa_2G250930 {ECO:0000313|EMBL:KGN61841.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN61841.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN61841.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX   PubMed=19881527; DOI=10.1038/ng.475;
RA   Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA   Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA   Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA   Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA   Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA   Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA   Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA   Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA   Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA   Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA   Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA   Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT   "The genome of the cucumber, Cucumis sativus L.";
RL   Nat. Genet. 41:1275-1281(2009).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; CM002923; KGN61841.1; -; Genomic_DNA.
DR   RefSeq; XP_011649254.1; XM_011650952.1.
DR   AlphaFoldDB; A0A0A0LPD7; -.
DR   STRING; 3659.A0A0A0LPD7; -.
DR   EnsemblPlants; KGN61841; KGN61841; Csa_2G250930.
DR   GeneID; 101206475; -.
DR   Gramene; KGN61841; KGN61841; Csa_2G250930.
DR   KEGG; csv:101206475; -.
DR   eggNOG; KOG0242; Eukaryota.
DR   OMA; NDKCSEN; -.
DR   OrthoDB; 5476186at2759; -.
DR   Proteomes; UP000029981; Chromosome 2.
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   CDD; cd01374; KISc_CENP_E; 1.
DR   CDD; cd16649; mRING-HC-C3HC5_CGRF1-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF35; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
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:UP000029981};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          103..420
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   DOMAIN          1036..1071
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          429..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          641..668
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          696..779
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          808..835
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          895..933
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        544..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         183..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1083 AA;  120221 MW;  87E9C52D52D15A30 CRC64;
     MASSSRARSS SPFSYRKSSS PYSSTSSSSS FTNGKLIPRS CSTSASSYFN SGGGLGSRSM
     TPNRGRSDSM YHSPHGSSSR TPVGFASEEL ISEPVDASRC GESISVTIRF RPLSEREFQR
     GDEIAWYADG DKIVRNEYNP ATAYAFDRVF GSQTSTPEVY EVAAKPVIKA AMEGVNGTVF
     AYGVTSSGKT HTMHGDQSSP GIIPLAIRDV FSIIQDTPGR EFLLRVSYIE IYNEVINDLL
     DPTGQNLRVR EDAQGTYVEG IKEEVVLSPG HALSFIAAGE EHRHVGSNNF NLFSSRSHTI
     FTLMIESSAH GDEYDGVIFS QLNLIDLAGS ESSKTETTGL RRKEGSYINK SLLTLGTVIG
     KLSEGKASHV PYRDSKLTRL LQSSLSGRGH VSLICTVTPA SSNLEETHNT LKFANRAKRV
     EIYASRNKII DEKSLIKKYQ REISSLKQEL DLLKKGMLVG VNHEEIMNLR QQLEEGQVKM
     QSRLEEEEEA KVALTSRIQR LTKLILVSSK NSIPLSDIPS QARNRSLGDN DNFHVLRDVS
     LPTESENLKG SPSSLSEAQS NPSYDFKQRS SSSKWNANEE LSSASSTVTE SNQGGMTMSD
     QMDLLVEQVK MLSGEIAFST STLKRLVEQS VTDPESSKTQ IQSLEHEIQE KKKQMRILEQ
     RITESREASI ANASVAEMQQ TVTRLMAQCN EKGFELEIKS ADNRILQEQL QNKSAENKEL
     QDKLRLLEQQ LTSFTGDRSS LIFEQHAPGE SVDELKKKIQ SQEFENEKLK VEQVQLSEEN
     SGLRVQNQKL AEEASYAKEL ASAAAVELKN LAGEVTKLSV LNAKLEKELS SAREMIHSRS
     MQNANGVNRK YNESLRPARK GRHSGRLNER AGAINDEFDT WSLDSDDLKF ELHARKQREA
     ALEAALAEKE FVEDQYRKKI EEGKKKEEAL ENDLANMWVL VAKLKKEGGG VVPELPSDTR
     HNGEVAVECF VDEKKIKTRT DSSITDRGMV DILKPAGVEV PKEEPLVLRL KAKMQEMKEK
     ELKSMTNGDV NSSNTCKVCF ESPTAAILLP CRHFCLCKSC SLACSECPIC RTNIADRLFA
     FTS
//
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