ID A0A2V0P015_9CHLO Unreviewed; 1792 AA.
AC A0A2V0P015;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Kinesin {ECO:0000313|EMBL:GBF92919.1};
GN ORFNames=Rsub_05755 {ECO:0000313|EMBL:GBF92919.1};
OS Raphidocelis subcapitata.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF92919.1, ECO:0000313|Proteomes:UP000247498};
RN [1] {ECO:0000313|EMBL:GBF92919.1, ECO:0000313|Proteomes:UP000247498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-35 {ECO:0000313|EMBL:GBF92919.1,
RC ECO:0000313|Proteomes:UP000247498};
RX PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT insight into genome evolution and environmental adaptations in the
RT Sphaeropleales.";
RL Sci. Rep. 8:8058-8058(2018).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000256|ARBA:ARBA00034488}.
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:GBF92919.1}.
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DR EMBL; BDRX01000036; GBF92919.1; -; Genomic_DNA.
DR STRING; 307507.A0A2V0P015; -.
DR InParanoid; A0A2V0P015; -.
DR Proteomes; UP000247498; Unassembled WGS sequence.
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 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; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR PANTHER; PTHR37739:SF8; KINESIN-LIKE PROTEIN KIN-12D; 1.
DR Pfam; PF00225; Kinesin; 2.
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:UP000247498}.
FT DOMAIN 96..498
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1671..1709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1736..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 505..582
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 607..934
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 984..1148
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1184..1243
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1269..1472
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 50..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1792 AA; 186950 MW; C6BB0AEA62FD70F5 CRC64;
MEGAFRPRVG TSRMVLEQAA GGREPPPTAG LRTTPRRHVP PLTARAAAGA ARQGSSSSLP
RGELAEPSET FSGTGSDELS SLMGDEDGAW ASEGDNVRVI IRMRPPNATE LADGSHYVCA
ETPNTREVLI TLPGRDPYHF AFDDVLQEET GQGEVFETVG APVVDNCLSG YNSSIFAYGQ
TGAGKTFTMT GRLGGGDAAA REQRGLAPRV FEYLFERIEA VQDAQGRNSL KFCCRCSMLE
IYNEVITDLL NPAATNLQIR EDIKRGCYVE GLSEEIVQNV EDAMRVLRRG AENRHVGETR
LNRESSRSHS VFTCVIERHS RERVDDGEGE GAPAGAAAAS SAAGGKAAVA AGSGSRSSGG
GKAGRGGAGK VEGELTKVVF SRLNLIDLAG SERIRGGAHG GSGAQGEHFK EACHINKSLT
TLGRVINELV RSQQTERRGK PPGPPVHVPY RDSRLTFLLQ DSLGGNAKTM IVANVSPSSV
CAQETLSTLY FARRAKHIRN RATVNVDVRG DAALLQREIQ RLNTELDNLR KGVTDPVVQE
CKRLRQQLKS EAAAREELAA RLEVASNDNA QLRRERKRLD EKLAHVHGMA GDLTGLLMRL
SGRMARYEAA DEAVSEARER AAEAELRVEA AQLADARASA AQQAAGGAAA ANELADLKAE
LAAALERARA SQCDAQDAEG AAAALRQQMA VARAAARDAE ARAQQAEERL EEVEQALAEE
AGAREGVDDA LSRARDEAEQ LGAWLDQARG EADALRQQLA DAEARSGEAM QVVEQSFQER
LRAEAQARGE LARRLAEAEG RADDGEAAAA DLRARLAEAE ASAEGAQSTA AELERRLAAE
QSRIEAGGAA AADLERRLAD AEARLAEGAA EAEDLRCQLA DADEQLEEGA AVAEDLHRRL
ADAEGRADDA AAAAAELRAR LAEAEARAQE GADAAADLGA RLAEAEARIE AGGATAGSLQ
ARLADTEARI KAGTAAAAAL EGRLAEATAR AEASAGEAAE LRRLLDSGTA EAQATAAQLL
QRAEGAEARA AGAEEEAADL ARRLEDSESA AAVAEAAAAE EAERAGKAER EVEELAAALA
AAEEAASDAR EAGEALRAVN ADLAGQVHEL EDQLAEVRGE LEQVASKLAS TTSRAEDAEA
ALEAAVEDGG RLRAELEREG AARRGAEGQL LAAGEEIAVQ AAAIDGLRTE LEATRAELAS
ERDAAACHAR DAVASQHDLT SRLIEADAEL HNAHEAIAAS EERARHLDAQ LSAAADARES
SDAAHRQAQH ALRDEVARLS ERAAALSRER DTLSARLASD AALAQQRLDA AGRDNECARA
SLAEAREEGA EAARRLAATG EALAAAQALA EERERDLAAA RRAAEAEAAR HDEAAREAAG
QLSALQLELV QAKEALAARA FELDRALKEA AATAERLDRR RAELATAREE LASARQQLAR
QESVTRDREA LVEDLKRANG AAMQELDGMR RQMSHQMTEL QSRLSEAIGR NSDLEMGSKE
SMMATARHAR ALTEIKRLVE WAADDPRNSC AFATGRLAQA MRAAAAAAAG AGSGSQCSGG
SASLSASASA SASAGAWGRR GGRPLAGGSD DEGDDDDGAV DSARGRSSSP LASGRSSSHS
GARRASGRDA ERSGSPSPRA GLRRAAAGKQ LLQRAGSGSA GAVSAATAAP GVLRRGGPGH
HPDGRQQQHP QPSPSPRLPG GAGAGAGAGE VRAARGHWGQ YGRGYCVGGR GAGGEDDLED
DARSGNHSGG AHAGGGGSGS AAKLWAPHGA AVADEALRGS DQSMGAGPYA GV
//
