ID A0A267FYT8_9PLAT Unreviewed; 861 AA.
AC A0A267FYT8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=BOX15_Mlig032493g3 {ECO:0000313|EMBL:PAA78988.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA78988.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA78988.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA78988.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA78988.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:PAA78988.1}.
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DR EMBL; NIVC01000658; PAA78988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267FYT8; -.
DR STRING; 282301.A0A267FYT8; -.
DR Proteomes; UP000215902; 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; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000215902}.
FT DOMAIN 516..846
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 482..509
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 607..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 861 AA; 94759 MW; BB9763B87995311B CRC64;
MLSTCRMEQK SQGYPMSAVG AAGGTSSSSS SDTGKPAPGG GRGQPGGNRR GRSGDRHLDR
GDRGGGGGSG GGGGGGSGVK RRRWRSAKSA LLTAPSAIGE LTGDSSWPAA DTAAASLVVS
GDACSGSRYS PFPQRAFLAD KDWQQLSARR DNGKLAKCRL SNDKYSRMLY SYHRLYQEYQ
YICACLLPQS AKQQQIEQFE TVGESHNNSD KMQQQQQQQQ QQQQQQQQQQ QQQQQQQPSG
IKEFGELNGN VILPDRNFRL RTCRKRRSVV CNQMLTRSEF GTAVWLSVPI VIELLLPRLQ
KQIQAIVCAC PHISDPLEVL AELRASRYDT ERCIEYLRQT LPLRTVVRDV LSVRSAPGRV
NFSSGTATTV TAEGNANNTT TRAASPRMGG AATAAAPGLP AMAASGDPAE AEAGGRPLLR
GVRRLRADVQ VVRASLSSVS AAMAAGLGKI RCHLSAQQER AKRQLQQLQQ PQQQQQDQSA
ALSRMQKCLD ELRQKCREEE SRRRLAFNAL QEQLGNIRVY CRCTRIEGDQ AVEPITQEQV
RVRSQLQSQQ LSQQSQQQGQ QQPQQEEVFR FDRVFGPDAP QETLFEELRP LITSFLDGYN
VCFITYGGEA SGKTFTLLGS SKQRGLVYRA LLAVLHETAS RAADWSMELD TACLEIYNDA
CFDLLSERQP VSLYKDCSLA SAFSALRLAP IREENDVTQL LRACSARRRV AKTALNPRSS
RSHLVHLVRL QARSRVHGHT TCSYLGMMDL AGAENIIKAD TWREPERAAE AGHINRSLAA
FNRLFLTLRR TPPGAACYRE ARLTQMLKPF LVNHGKCCII VTVRTDSSSA SGSLSTLRFG
RDARQVALGK AQRQLLVASV D
//
