ID A0A1R3JPS2_COCAP Unreviewed; 1068 AA.
AC A0A1R3JPS2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CCACVL1_04826 {ECO:0000313|EMBL:OMO96697.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO96697.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO96697.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO96697.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO96697.1}.
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DR EMBL; AWWV01007377; OMO96697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JPS2; -.
DR STRING; 210143.A0A1R3JPS2; -.
DR EnsemblPlants; OMO96697; OMO96697; CCACVL1_04826.
DR Gramene; OMO96697; OMO96697; CCACVL1_04826.
DR OMA; REMVNPS; -.
DR OrthoDB; 54358at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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; cd21203; CH_AtKIN14-like; 1.
DR CDD; cd01366; KISc_C_terminal; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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; PTHR47972:SF12; KINESIN-LIKE PROTEIN KIN-14H; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50021; CH; 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 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:UP000188268}.
FT DOMAIN 32..154
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 468..788
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 259..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 551..558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1068 AA; 118483 MW; D8C670E4F1334295 CRC64;
MEAESILQVS VMSVLEDVLQ QQGNRTSNIV PALLRYEAAG WLRKTVGVVG GKDLPAEPSE
EEFRLGLRSG IILCNVLNKV QPGAVPKVVE GACDSVIIPD GAALSAYQYF ENIRNFLVAV
EEMGIPTFEA SDFEQGGKSS RIVHCVLALK SYSEWKQNGA IGTWKYSANA KPSNFGTAKP
FARKNSEPFT NPISRTVSLG EKSVESFCSE QSELSEAGSV RSLQKLVRAA LSDKRQEEIP
VIVESMLNKL TEEFERRLTS QKEQIRITSK DMEESVPDDS ASQTTSCEDK DEVEAPTEAP
INEVVEAPTE EMVEDEALRK ETIESPTEEV IDNEPSKELQ KSESYKEKCK ADEEESIRRR
KAAEESLRRR KADEEESLRR RKADEEESMR RLLKQQALVE QQKRDIMELK HSLHATKSGM
QCLQKVYQEE FIILGKQFHR LSHAALGYQK VLEENRKLYN QVQDLKGNIR VYCRVRPFLN
GQQNNMTSVD HVDHSSITIV TPSKYGKEGK KLFTFNRAFG SNATQAEVFA DTQPLIRSVL
DGYNVCIFAY GQTGSGKTYT MTGPKELTEE ELGVNYRALG DLFFLQQQRK ETISYEISVQ
MLEIYNEQVR DLLSSEEIRN SSQNGINVPD ANLVRVTSTA DVINLMNLGH KNRAFSATAM
NDRSSRSHSC LTVHVQGKEL TSGNILRGSM HLVDLAGSER VDKSEVTGDR LKEAQHINKS
LAALGDVISS LASKNAHVPY RNSKLTQLLQ DSLGGQAKTL MFVHIAPEYE ALVETISTLK
FAERVATIEL GAAKVNKDSG GEVRELKEQI ASLKAALARK EGEPESMQMQ MQRSQSLSSS
SETNSMSKTG SSPSPSLPKW NSLSDLSSSN INTENESSST SRRDSLEIQE MLANPSLWPP
LGSPALSVKE DDKDSVPGDW VDKVMVNKQE KLDNNTSKNQ NPSPASKEVS KEVINGQLPG
KFYQTYIRTP TKVHPESNLT KPTAIKKGNQ DDDSDATSDC SESEVWQSST PKTTNGAKPK
KQQLRTVKST ETRSSIPSLI PSPSARKSPN AGSNQTLQKG KRKTGLTK
//
