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Database: UniProt
Entry: A0A1Y1ICJ8_KLENI
LinkDB: A0A1Y1ICJ8_KLENI
Original site: A0A1Y1ICJ8_KLENI 
ID   A0A1Y1ICJ8_KLENI        Unreviewed;      1344 AA.
AC   A0A1Y1ICJ8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Kinesin {ECO:0000313|EMBL:GAQ88640.1};
GN   ORFNames=KFL_004470060 {ECO:0000313|EMBL:GAQ88640.1};
OS   Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ88640.1, ECO:0000313|Proteomes:UP000054558};
RN   [1] {ECO:0000313|EMBL:GAQ88640.1, ECO:0000313|Proteomes:UP000054558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ88640.1,
RC   ECO:0000313|Proteomes:UP000054558};
RX   PubMed=24865297; DOI=10.1038/ncomms4978;
RA   Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA   Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA   Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA   Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA   Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA   Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA   Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA   Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA   Tabata S., Ida S., Kurokawa K., Ohta H.;
RT   "Klebsormidium flaccidum genome reveals primary factors for plant
RT   terrestrial adaptation.";
RL   Nat. Commun. 5:3978-3978(2014).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   EMBL; DF237396; GAQ88640.1; -; Genomic_DNA.
DR   STRING; 105231.A0A1Y1ICJ8; -.
DR   OrthoDB; 54358at2759; -.
DR   Proteomes; UP000054558; 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; cd01366; KISc_C_terminal; 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; PTHR47972:SF35; KINESIN-LIKE PROTEIN KIN-14Q; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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:UP000054558}.
FT   DOMAIN          450..774
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          28..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          882..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1076..1131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1147..1175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          317..351
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          842..878
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        28..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..946
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        985..999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1033
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1226..1248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         535..542
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1344 AA;  145831 MW;  30F0DE8B52165C86 CRC64;
     MDVSMSVDGP ANFLSGADKV AAAVDKGGYN FRKRRSPTDF DQKAWGPISP KREKREGGFP
     SGPLTHGTGT EKKQPKSPHK RRPEQTPERI ALRGREQDYE EVDSGGGVLK VDQARQKSPS
     RRYEQQEPPR GGTDAKPRVE KARHGTPQRD DPAQKSPSRR YEDQKPPRSS TPAKGGVEKA
     RQGSPWRERT EAERAKSPGR HVGGPSAFMA SEDKGPEDGG GRAIVKDEVT VLKRQLKDEM
     AASKVLQKKL REFEEERAHD LKDLTRAMDT LKAKEYELEM YVSNHQKNRA SRQGQEQEVR
     SRSQELEGQL AAIADECGAL RDVLERRTRE IDDLRRQLSE RTAEAQRLGE LVDKQAAELA
     NERSRAGDRW RDLHEQICKE IGAVHPASGD APSPDASEAE DAETSERLEN ETKAAVRKLV
     SEYEELKRRF ALESAARKKY YNEVLEMKGN IRVFCRCRPL APSEISSGQS NVVDFDVKGE
     NELLVRSGPR PGDKKAFKFD RVFNPEADQA EVFADTAPVV MSVLDGFNVC IFAYGQTGTG
     KTFTMEGTPA NRGVNYRTID ELFQLARQRH GEARYDVSVS VLEIYNEQIR DLLAAPGSGQ
     KKLEIRQGHQ GNHVPGLTEH PVTCADEAWE LLQSGSRSRS VGATNANEHS SRSHCMLGIS
     VKCENKVTGE TTRSRLWLVD LAGSERVGKS EASGDRLKEA QSINKSLAAL GDVIAALTTK
     SAHVPYRNSK LTHLLQDSLG GDSKALMFVQ ISPAESDAGE SLCSLQFASR VRGIELGPAK
     RQVDGNELFK YKQLVASAKQ EAKAREEALK QLQEGVRAVE GRLQIKDKLC ATLSEKVRIK
     ETREAELEAQ LLAERRALLE ARAAVEAAQN ELHMLRLAGN RAPANPRLET GSRDTGGGLD
     RGPYSQATYH ERQEGGRGNS SSALHGGGDY RASESDRRHE TGHQSGAERP YQEPHSTSDR
     VTAAMAAAQA AIAERKALIE SARQETSPLG KQNPKPSAGD LPTSAAKPPG LPRPDFHREN
     AHSGLRETGF REAGLRETAG MTIGTSGGAE AFGITGRGAI HTGSDSTTVD ASVSLGDWGR
     GDSRGGMGAS VNSRPYNQQP GDRRLPPWSE TAEAHQGGQN DPGRPPPTVN RAPRVVASRF
     NVAVTGPTIG TPLRVRPTSA RPPVSAPNLQ PGLMQNPGFG AAGFEEERRG SVYRTAPTSA
     NPGPVSGAFL EERRGSVYRA LGGDPNQPYG NQSEDSGDDR SGSRGSTVAA KQGDAYDASR
     APLAGLKPNR IDAGPGSAPL AGDAKVKGAR PAFSKGQSGG MAAGAQRVRN GGQVRKQFIA
     TQAAAIAAQT NKPVELVLRE KMWQ
//
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