ID D8TUB8_VOLCA Unreviewed; 1334 AA.
AC D8TUB8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Kinesin-like protein {ECO:0000313|EMBL:EFJ49115.1};
GN ORFNames=VOLCADRAFT_127415 {ECO:0000313|EMBL:EFJ49115.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ49115.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC {ECO:0000256|ARBA:ARBA00025673}.
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; GL378337; EFJ49115.1; -; Genomic_DNA.
DR RefSeq; XP_002950012.1; XM_002949966.1.
DR STRING; 3068.D8TUB8; -.
DR GeneID; 9619332; -.
DR KEGG; vcn:VOLCADRAFT_127415; -.
DR eggNOG; KOG0243; Eukaryota.
DR InParanoid; D8TUB8; -.
DR OrthoDB; 5688491at2759; -.
DR Proteomes; UP000001058; 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; cd00106; KISc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1470.10; Photosystem I PsaD, reaction center subunit II; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
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:UP000001058}.
FT DOMAIN 40..74
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 133..166
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 474..844
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 217..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1171..1198
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1262..1296
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 217..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 561..568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1334 AA; 140559 MW; D033FA9678E16871 CRC64;
MAFMQAGMSA EALAAAAELD VPPGKYQVIK AVISDMIEPD SLPPGWEARY DAAMVRREYV
NKDTGEVQYK HPLLSYYRGA AFMELGGSQQ LQGNEEEQPP APQEILDMCA YLGINPSQDD
PYILEVARLA ISAPLPAHWV EAEDDDGNPM FTNQQTGESQ PSHPLDPYFV EMIKRRRREL
LVRSDGVGIR SALAAKRLHE IGVPGITVPP ELLEDVAGSR RQEEEEEEEA SGAGRNFGPL
VTIEETEEEG HDDEDHTHKP GKQPQQPPQQ QMQKPLQLQP QVQQKQKQKQ ESQRSLMLED
FEGEEEDGDE EEEEKARAAA EYDDEDAALA ALRAQAAEAA RRAAAAVAEF DAKFPPLPVL
LNDSSGGGGD LRRSRSYTEV ETGRLMKQIS AIEAARSALT TAAASDVPTA AAASAAGSIY
AVARLPSGRL DLLRSRVYGS SGVASAAAAA AVAAAAADSA PPSRNPAREP SRERIRVAVR
ARPVPKPGEP DAWLIDPVSR TVRLKENAAS ATHRHISADR VYCFDLVLSP DSSTKQLWAS
HVVPLMDASL GGINTTVFAY GQTGSGKTYT MFGSDGRLED GAIAMSLSYL FKALKVAGWG
GSLGGGGAGD GGGGGPIVVS RALRKLKGGA EEYTVKISML ELYNEQLRDL LAPGGGPFDR
LGRPSGAPLA LQDDPRVGVR VSGLDEHAVA DVPAAMALVA RGAMSRSVGS TAMNEVSSRS
HTIVRLALET REATTRELVH TSLVSFVDLA GSERLAKTGS SGTRFVEGTN INISLLMLGT
VVSKLAEGRT GEFIPYRNSK LTRLLQPCLG GNSKTAIIAT INPSVDHVEE TFNTLAFATR
AMDVVNQVSV NSYIRGSGAV GGALSGAAAA ALQKQVATLK AELAALKKEA GGAGGLGSGT
ALLLGPDGGG ANAAALMAER LARLEIDKAR LLDRLEALTG RAQGDVYDDL PPTPPDLHLP
PPRPPGRSGS SGSLAAAGTT PSLALRSIAR LACVGRAGGG GGAVGGSPSK SLIPRPNEQI
PPEEVVVAVR GMRDERDELR RRDLKLRRNL EEAHERLAEV EPYRVLAEQV KEVVGMLENI
LGPSPVAVAG ADRDLDSDPA TAACNQAARL AENVQAVAMM HNELLALQQQ LATSEAVAAA
AARRAGSAET ALQRAAVTAA EDWMATGDGG DARLKNMVEQ LNSQLTAVRR ELDVTKSELA
KWRGLAAEAP EVGEPGAADG GDGDVDDVYG DDDGEGEASR QPAKRLASAA SLNVGSFAIR
KAREAMVQAS SLEARCNAAE AERDELRERL QALEEAVAAG GVGGRGLLQP PGGGRGGGYG
STAVRQCFRK GGLR
//
