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Database: UniProt
Entry: A0A0B0NAJ1_GOSAR
LinkDB: A0A0B0NAJ1_GOSAR
Original site: A0A0B0NAJ1_GOSAR 
ID   A0A0B0NAJ1_GOSAR        Unreviewed;      1052 AA.
AC   A0A0B0NAJ1;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Kinesin-related protein {ECO:0000313|EMBL:KHG11578.1};
GN   ORFNames=F383_15119 {ECO:0000313|EMBL:KHG11578.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG11578.1, ECO:0000313|Proteomes:UP000032142};
RN   [1] {ECO:0000313|Proteomes:UP000032142}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. AKA8401 {ECO:0000313|Proteomes:UP000032142};
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-5/BimC subfamily.
CC       {ECO:0000256|ARBA:ARBA00034704}.
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DR   EMBL; KN396126; KHG11578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0NAJ1; -.
DR   SMR; A0A0B0NAJ1; -.
DR   Proteomes; UP000032142; Unassembled WGS sequence.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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   GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR   CDD; cd01364; KISc_BimC_Eg5; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR047149; KIF11-like.
DR   InterPro; IPR047241; KIF11-like_kin_motor_dom.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR   PANTHER; PTHR47970:SF29; KINESIN-LIKE PROTEIN KIN-5B; 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:UP000032142}.
FT   DOMAIN          52..394
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          410..509
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         138..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1052 AA;  119069 MW;  E5C7AC1CA2A205EA CRC64;
     MSLTPDQFRK GAMGGLVPSP SPFLTPRPER RRADSRGPDW FSNRQDRDKE VNVQVLLRCR
     PLSEDEQKMN VSRVISCNEL KREVTVLQNV ANKQVDRVFT FDKVFGPKAQ QRTIYDQAIA
     PIVNEVLDGF NCTVFAYGQT GTGKTYTMEG GMRNKGGDLP AEAGVIPRAV RQIFDTLEAQ
     NADYSMKVTF LELYNEEITD LLAPEESSRY AEDRQRKPIS LMEDGKGCVI VRGLEEEAVY
     SANEIYTLLE RGAAKRRTAD TLLNKRSSRS HSVFSITVHI KESAVGDEEL IKCGKLNLVD
     LAGSENISRS GAREGRAREA GEINKSLLTL GRVISALVEH SAHIPYRDSK LTRLLRDSLG
     GKTKTCIIAT ISPSAHSLEE TLSTLDYAYR AKNIKNRPEA NQKMSKAVLL KDLYLEIERM
     KEDVRAARDK NGVYIPHERF VQEEAEKKAR MEKIEQLEND LNLSEKQSNK YHELYLTEQE
     QRLDLESVLK DCKLNLEKTR AELLDLQENH RAAILTLKEK EFIISKLLCS ENFLIERAKE
     LRSDLQHASE DINSLFAKLD DKDKMEAENR SIVLTFGSRL DQRLKDLHKT ILGSVSQQHQ
     QLRCMEEQAH SFLASKCDAT KALESRIKNM TETYASGVTT MKELANKIQR STSSDLEEMS
     FAFSSQIEAI EQFLVTAVLE AKKVIEDLLS SLNEQKELLV FSARQQEEGL HRNLISAQEI
     SKATFHFLTD INNQASKFMT VLEEMEAKKS QQLTNFENRF KAKAAREEKQ AIEKIAAILV
     TLTSNRSAMV SEASGCMKDM DIQDNRTLQQ QMSMMQQVSA DVGKEMCKYI EKVESHFVKD
     TFSAAESRGI MEDGLQECSK IVNVSRQQWE NAKTYINELN KSSLAEIKST VRENIKRNHT
     VHEELLSALS STGAEVGART GDITAAINDS LLRDRECKKE IDSLTNCCLD QLKTVQEKHG
     ESISNIRSEA EKCITRDYLV DNHTKPKKRD IVVPSLASIE EMRTSAFEDI EKEGNNLENN
     NRSKWGYNEG KIQQQITSLS PNRTPFADVN SL
//
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