ID A0A1S3CQK5_CUCME Unreviewed; 1278 AA.
AC A0A1S3CQK5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Kinesin-like protein KIN-4C {ECO:0000313|RefSeq:XP_008466163.1};
GN Name=LOC103503659 {ECO:0000313|RefSeq:XP_008466163.1};
GN Synonyms=103503659 {ECO:0000313|EnsemblPlants:MELO3C003524.2.1};
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_008466163.1};
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|EnsemblPlants:MELO3C003524.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008466163.1}
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_008466163.1; XM_008467941.2.
DR EnsemblPlants; MELO3C003524.2.1; MELO3C003524.2.1; MELO3C003524.2.
DR Gramene; MELO3C003524.2.1; MELO3C003524.2.1; MELO3C003524.2.
DR eggNOG; KOG0244; Eukaryota.
DR InParanoid; A0A1S3CQK5; -.
DR OrthoDB; 602895at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; 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 CDD; cd01372; KISc_KIF4; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 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 PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 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 14..365
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1011..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 556..701
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 741..768
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 795..822
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1020..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1278 AA; 143115 MW; 010544CBE6EECBB3 CRC64;
MENLDGKSSD SSQCVRVAVN IRPLITPELM VGCTDCITVV PGEPQVQIGS HIFTYDNVYG
SAGSPSYALY DDCVAPLVEA LFQGYNATVL AYGQTGSGKT YTMGTNYSGE GTNDGVIPKV
MEKIFKKVEA MKDSTEFLIR VSFIEIFKEE VFDLLDASTC VNNTKGEGTK PFAPPRVPIQ
IRETVNGGIT LVGVTEAEVR TTEEMTSYLS RGSLARATGS TNMNSQSSRS HAIFTITMEQ
KKKLGQGTSH DDTCDDILCA KLHLVDLAGS ERAKRTGADG MRFKEGVHIN KGLLALGNVI
SALGDEKKRR EGCHVPYRDS KLTRLLQDSL GGNSRTVMIA CVSPADSNAE ETLNTLKYAN
RARNIQNKAV INRDPVGAQI QKMRSQIEQL QAELLFYRGD AGLPYEELQI LKHKISLLEA
SNGELLRELQ ERRVTCDHLS QRAIDAQVEK DKFAMIIESV RNGKSLDEIE SNYDKDCELI
KSYVSKIQEL EGEVLRLQSF KSSKHSQYAD LAESDDDRPQ SGNILFPCSN EYSSEYDPKA
GDIPDGIEDH EKELEHSTMQ ERLDRELKEL DKKLEQKEAE MKRFAGTDTS VLKQHYEKKV
HELEQEKRAL QKEIEELRCN LSNISSTSDD GAQKLKQEYL QKLNFLETQV SELKKKQDAQ
AQLLRQKQKS DEAAKRLQDE IHRIKTQKVQ LQHKIKQESE QFRSWKASRE KEVLQLKKEG
RRNEYEMHKL LALNQRQKMV LQRKTEEAAQ ATKRLKELLE SRKAARETSS GGSNGPGIQA
LMQNIEHELE VTVRVHEVRS EYERQMEERS KMAKELAKLK EEELNRGSNL SDCTQTMSPG
ARNSRIFALE NMLATSSSSL VSMASHLSEA EERERILGGR GRWHQVRSLA DAKNIMNFLM
NLASSSRCLL WDKEFASREK DSEIRELKQK IVNLSGMLKK SEAQKAELIH ENSALKRYSQ
GHNYDLRKQE HRNSVIIQAD MDTSESDYAN YSSDGDDDNY DWERSMKRRL NRKKTSKTKG
RVSMAVSNGT DSREFNLDSS GDGGIIRGNE STATSVVCCT CSKFSSCKTS KCQCRANGGA
CGASCGCIPS KCSNRGSKSD RDASMQPDSF KDVRNGTENE ETDEENQDLV SRGARLLQNA
LAERPSDAPP PPTAEDGGAK RKPLSDIGNT LVKSKANKPN QRKKWRKSTI QLIPTPQQAS
SEPEKPSATE KTENDPNEVV NIPLKLPRAM RSAAVVNGGN NNLLRERNAD QPEDSIGGNK
GHELVVPKRV DEKENCNR
//
