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Database: UniProt
Entry: A0A1S3C724_CUCME
LinkDB: A0A1S3C724_CUCME
Original site: A0A1S3C724_CUCME 
ID   A0A1S3C724_CUCME        Unreviewed;      2222 AA.
AC   A0A1S3C724;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Phragmoplast orienting kinesin-1 isoform X1 {ECO:0000313|RefSeq:XP_008458297.1};
GN   Name=LOC103497757 {ECO:0000313|RefSeq:XP_008458297.1};
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_008458297.1};
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_008458297.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-12 subfamily.
CC       {ECO:0000256|ARBA:ARBA00034488}.
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DR   RefSeq; XP_008458297.1; XM_008460075.1.
DR   GeneID; 103497757; -.
DR   KEGG; cmo:103497757; -.
DR   eggNOG; ENOG502QR1R; Eukaryota.
DR   InParanoid; A0A1S3C724; -.
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|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: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          2200..2222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          839..893
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1172..1250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1690..1773
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1809..1871
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1899..1926
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2071..2196
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   2222 AA;  253016 MW;  3CD8D84F35715063 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 CASGDETALQ RQILHLKGQL
     SFLLKHSNFP RSILSSVPRL EEFGVSAPFD DYGALGNRMQ TENHKMKLME ASLIGASRRE
     EVANTTIKKL EFEIEHMKRL AFQQEEDGQR TKMLLKFREE KIRQLELFLG GMVSADQYLL
     DENKALAVEI KMLQAKIDRN PELTRVSLEN SKLTEQLQVY HNFYELGERE ALLTEVAELR
     NELLVALGKN STISERDKYQ NETMSIKSYI QDDTLSYIAG SEENFENTLG QGSDDELGAK
     PIFSRKDLTD AKMLAESMDS DNHMQAENHG CKQFKCCMVE NFIKQSDGTK CQNDGNLMNQ
     HEDVDNKTLQ VKLENLTREL EEVRLSNIHY QENQNQQNQI EDVRQQVEME TASTILQLQE
     EVETLQLELN DRLHGLAQEN TLLKDLLSAK NEEMRMLCID WETAMVELTS FLLDSSRSIR
     DAHGQIEGIA NLFPEVNVGI SEQVQQAIKV CIEKEETILF LHKNLEDARL MVKEMELKLD
     SLKEATLAFN ESEQMHDNIS AAGAKPLSPQ MTDENIMGEF LDKRLGVKNS PLIEAEKSAD
     AAVTAVEWLS QPQELGCCNS IERQMPISKL DVSSQRSSHI FDNLMANTNE LLLEESDTVS
     NMIWLGLTEL KNITIGHYAD MEMHISALHI YIQDLYSEYQ ELIQDMAREI HELRLKAETS
     NESYKSLQFF KDKDQSAQKY WNIENQNSIL DQIKAKIYEA KNRLNILEDS IDRNTAGCGE
     RYLDQYPVKE DGWSSDCSTS SSEISTESDT SRGKFLDYMN GGEGTTISLR KELYMTYNAI
     RKLCMQIDTV LMHDIGGNSL SEEMDQGKTL FKLRMEKAEA GCSNTSKVIS IEEIKQDGGF
     LTRFEEAQEA IKEADIMLNA LLRANANAKQ LTDIFKQAGE QLQIERDNLV DEVGQLKSSM
     HLKDAENKLL HDQVCFNLEE VANSVSSLEG CISQTQRDVD EKFGIISCDI ISLRDEMLKS
     VSNWKSLLED IFLEIMGREF ASFVIHQCYS KEICWQFAAQ FKADPNFLPL KWQRCLESTN
     ASGSTCLTDK EDIMLINKIE KGRTELITGL EEVDGGFSYD DILYEKLALK KELRRKEVLL
     EGLLFDFRLL QESTSKTKDM KDETDYSLSQ LQHELEIKAN QLDSVLVQQR KLEGLLTDTE
     KALFLSNSKL DKAKETMTSI SEHNAQLKKQ VEDLYLQKFE AEKQLAEQQD VINKLENEIL
     HLTSLEKRSV LSVEDIENDL SRVINERDQL HEQVCFLTDK LDIAYAMADE KEAVATEARQ
     ESEASKLYAE EKEEEVKILE HSVEELESTI NMLETKVHEM DEEVEKNRTL RESLELEKKI
     LRQRLLAVEN LSEDMDCGAE IVEHAQDQPR QPGNILLELL ETKSRIKLLE QERVEQDKEV
     KRLKEYISEL VLHADAQAMK YQQKYTSLEV MVRDASKDHS NPMTAPALDK VEKNSARPRG
     SSSPFRCISN LVHQMNLEKE HELSTARLRI EELELLATSR QKEICILNAR LAAAESMTHD
     VIRDLLGVKL DLTKYANFID QYQVQKMVTE AHLQSQQFQE KEREVQDLRT QINDLHEERE
     CYKSVLSKKE AEALHMQIAC EKLRERDHLL SSQNGILKTE NKNLKKKIVE LDDRGNTLHQ
     TQSSQRDLRH SFLTKNDELT KRLANSKMLL SRVNDEMARY RIPRGSSSHH RSGGSGKEIS
     HE
//
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