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Database: UniProt
Entry: A0A1S4E1Y2_CUCME
LinkDB: A0A1S4E1Y2_CUCME
Original site: A0A1S4E1Y2_CUCME 
ID   A0A1S4E1Y2_CUCME        Unreviewed;      2217 AA.
AC   A0A1S4E1Y2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Phragmoplast orienting kinesin-1 isoform X2 {ECO:0000313|RefSeq:XP_016902233.1};
GN   Name=LOC103497757 {ECO:0000313|RefSeq:XP_016902233.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_016902233.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|RefSeq:XP_016902233.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-12 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034488}.
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DR   RefSeq; XP_016902233.1; XM_017046744.1.
DR   OrthoDB; 472090at2759; -.
DR   Proteomes; UP000089565; Unplaced.
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; cd01373; KISc_KLP2_like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR044986; KIF15/KIN-12.
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   PANTHER; PTHR37739:SF18; KINESIN-LIKE PROTEIN KIN-12C; 1.
DR   PANTHER; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 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; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000089565}.
FT   DOMAIN          175..512
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2195..2217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          834..888
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1167..1245
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1685..1768
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1804..1866
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1894..1921
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2066..2191
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         256..263
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   2217 AA;  252456 MW;  3A073C507CDAFE14 CRC64;
     MSKHLPVSKN SQPEYNENEL GVSPSGLHFP PPRTPFNIIA DPAQFQKEFH DSGFDSNLKL
     QSTKADLFSD RKSEVSLKIN GNACTSNGTP RFSAQGRRVN SEPSSTHSTP AKSSSRVSLG
     GAIVATGSKA PQLADGRAGS SYRFSRRISM PNTECPVDVS HIDLEEDPSF WKDHNVQVMI
     RIRPLSTMER DSQGYGRCLR QESAKTLVWL GHPETRFTFD HIACEKISQE NLFKVAGQPM
     VENCLSGYNS CMFAYGQTGS GKTYTMMGGI YELEGKLNED CGLTLRIFEH LFTRIGMEEK
     SKRDVKLKYS CKCSFLEIYN EQITDLLEPS STNLQLREDS KKGVYVENLT EHSVSTINDV
     VKLLLQGAAN RKMAATYMNS ESSRSHSVFT CIIESHWEKD SRTHLRFARL NLVDLAGSER
     QKSSGAEGDR LKEAANINKS LSTLGLVIMS LVDLAHGKHR HIPYRDSRLT FLLQDSLGGN
     SKTTVIANVS PSFCSANETL STLKFAQRAK QIQNNAKVNE CASELMHFGN SQGQLSFLLK
     HSNFPRSILS SVPRLEEFGV SAPFDDYGAL GNRMQTENHK MKLMEASLIG ASRREEVANT
     TIKKLEFEIE HMKRLAFQQE EDGQRTKMLL KFREEKIRQL ELFLGGMVSA DQYLLDENKA
     LAVEIKMLQA KIDRNPELTR VSLENSKLTE QLQVYHNFYE LGEREALLTE VAELRNELLV
     ALGKNSTISE RDKYQNETMS IKSYIQDDTL SYIAGSEENF ENTLGQGSDD ELGAKPIFSR
     KDLTDAKMLA ESMDSDNHMQ AENHGCKQFK CCMVENFIKQ SDGTKCQNDG NLMNQHEDVD
     NKTLQVKLEN LTRELEEVRL SNIHYQENQN QQNQIEDVRQ QVEMETASTI LQLQEEVETL
     QLELNDRLHG LAQENTLLKD LLSAKNEEMR MLCIDWETAM VELTSFLLDS SRSIRDAHGQ
     IEGIANLFPE VNVGISEQVQ QAIKVCIEKE ETILFLHKNL EDARLMVKEM ELKLDSLKEA
     TLAFNESEQM HDNISAAGAK PLSPQMTDEN IMGEFLDKRL GVKNSPLIEA EKSADAAVTA
     VEWLSQPQEL GCCNSIERQM PISKLDVSSQ RSSHIFDNLM ANTNELLLEE SDTVSNMIWL
     GLTELKNITI GHYADMEMHI SALHIYIQDL YSEYQELIQD MAREIHELRL KAETSNESYK
     SLQFFKDKDQ SAQKYWNIEN QNSILDQIKA KIYEAKNRLN ILEDSIDRNT AGCGERYLDQ
     YPVKEDGWSS DCSTSSSEIS TESDTSRGKF LDYMNGGEGT TISLRKELYM TYNAIRKLCM
     QIDTVLMHDI GGNSLSEEMD QGKTLFKLRM EKAEAGCSNT SKVISIEEIK QDGGFLTRFE
     EAQEAIKEAD IMLNALLRAN ANAKQLTDIF KQAGEQLQIE RDNLVDEVGQ LKSSMHLKDA
     ENKLLHDQVC FNLEEVANSV SSLEGCISQT QRDVDEKFGI ISCDIISLRD EMLKSVSNWK
     SLLEDIFLEI MGREFASFVI HQCYSKEICW QFAAQFKADP NFLPLKWQRC LESTNASGST
     CLTDKEDIML INKIEKGRTE LITGLEEVDG GFSYDDILYE KLALKKELRR KEVLLEGLLF
     DFRLLQESTS KTKDMKDETD YSLSQLQHEL EIKANQLDSV LVQQRKLEGL LTDTEKALFL
     SNSKLDKAKE TMTSISEHNA QLKKQVEDLY LQKFEAEKQL AEQQDVINKL ENEILHLTSL
     EKRSVLSVED IENDLSRVIN ERDQLHEQVC FLTDKLDIAY AMADEKEAVA TEARQESEAS
     KLYAEEKEEE VKILEHSVEE LESTINMLET KVHEMDEEVE KNRTLRESLE LEKKILRQRL
     LAVENLSEDM DCGAEIVEHA QDQPRQPGNI LLELLETKSR IKLLEQERVE QDKEVKRLKE
     YISELVLHAD AQAMKYQQKY TSLEVMVRDA SKDHSNPMTA PALDKVEKNS ARPRGSSSPF
     RCISNLVHQM NLEKEHELST ARLRIEELEL LATSRQKEIC ILNARLAAAE SMTHDVIRDL
     LGVKLDLTKY ANFIDQYQVQ KMVTEAHLQS QQFQEKEREV QDLRTQINDL HEERECYKSV
     LSKKEAEALH MQIACEKLRE RDHLLSSQNG ILKTENKNLK KKIVELDDRG NTLHQTQSSQ
     RDLRHSFLTK NDELTKRLAN SKMLLSRVND EMARYRIPRG SSSHHRSGGS GKEISHE
//
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