ID A0A0D2N084_9CHLO Unreviewed; 782 AA.
AC A0A0D2N084;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=MNEG_1992 {ECO:0000313|EMBL:KIZ05967.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ05967.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ05967.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ05967.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(2013).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; KK100432; KIZ05967.1; -; Genomic_DNA.
DR RefSeq; XP_013904986.1; XM_014049532.1.
DR AlphaFoldDB; A0A0D2N084; -.
DR STRING; 145388.A0A0D2N084; -.
DR GeneID; 25734870; -.
DR KEGG; mng:MNEG_1992; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000054498; 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:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR007263; DCC1-like.
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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF04134; DCC1-like; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51371; CBS; 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 ECO:0000256|RuleBase:RU000394};
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498}.
FT DOMAIN 33..72
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 308..760
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 498..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..775
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 398..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 782 AA; 80981 MW; 286166453A1F3C46 CRC64;
MVACKVVGVI SRKDLIKVRQ QGGSLQQKVK AHMTSPAITI TPDAPVADAG ALMLKEKIRR
LPVVDAEGKP LGKPGCSGAR RAAAAVAAEA GGGSIVSRSD IFAPLMMEKY KAYQDKEVAA
VVTGAGITMT WDIKYLYDGE CSMCLTLKGV LERQDKKKRI RFVDIADLDY DPMANMGVEF
EDAMETIHAI RPDGRVLQGT DALRGLFDEV GLGWVVTVME LPLVGKLVDL LYEFLSKNRI
KIGGMMDALV AAKRVSMSKA GVEVCGDVDG GCEIEWGEMS LDGEDQGPGA AGAAGTSESV
ERVSSASAVK VAVVVRPLLP FEIQAGAKDV VSVAPPSKIS LPQRATNGGA PVDQHDFTFD
RVYRADGPGA SSKLNDEMIT NVLDCFCQGF NGTILAYGQT GSGKTYTMGT AATAKELAAA
AARGGTGGGG GAAVVGVVPR AIARVFEYVQ KAAPLYDCAL TVTYVEIYNE QVLDLLAGTT
TATGAGAVTS AHVTGGGAGT SGGGGAQPPS QGGAGGFGGG GGAVAIREGP EGQIILEGAT
EARVRSREEV ASLLARGNER RAVGSHKLNE ASSRSHAVLA LALEQRARPG AGVPRELRYL
RWAERRLAVV GGSWRQLAAV GGGWDCLVDS RSKLALVDLA GSERAKQTGT TGTRFQEGVA
INSGLLALGN VITALSEQQR GRSGGGKGGG GAAAAAAAAA ARRHVPYRDS KLTRLLQDGL
GGNRYAGRAM LISNSLQLNN ALSPEQEVAF LRSALEAAQA EAAALRVEVA ALQAENVSLR
RG
//
