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Database: UniProt
Entry: A0A0V1H0W5_9BILA
LinkDB: A0A0V1H0W5_9BILA
Original site: A0A0V1H0W5_9BILA 
ID   A0A0V1H0W5_9BILA        Unreviewed;       741 AA.
AC   A0A0V1H0W5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=osm-3 {ECO:0000313|EMBL:KRZ04295.1};
GN   ORFNames=T11_1761 {ECO:0000313|EMBL:KRZ04295.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ04295.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ04295.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ04295.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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:KRZ04295.1}.
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DR   EMBL; JYDP01000167; KRZ04295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1H0W5; -.
DR   STRING; 268475.A0A0V1H0W5; -.
DR   Proteomes; UP000055024; 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   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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF32; KINESIN-LIKE PROTEIN; 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|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   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          6..335
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          718..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          343..430
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          478..551
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         92..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   741 AA;  84222 MW;  F1969708C9D71F15 CRC64;
     MSPSECVKVV VRSRPLGQRE LKIGCSVVVE MDPKRAQCSI RNPADKTGTT KLFTFDGAYD
     MNATTENIYN DIVYPLVESV LEGYNGTVFA YGQTGSGKSF TMQGPHNWPC QRGVVPRAFE
     HIFEAIATTE NVKFLVCASY LEIYIEDVRD LLGKDTKQKL EIKEHPEKGV YVAGLSMHPV
     HNINEVEQLL ARGMRNRATA ATLMNTDSSR SHSIFTLHLE MIEMATDGQH IKMAKLHLVD
     LAGSERQSKT GTTGERLKEA TKINLSLSAL GNVISALVDG KSTHVPYRDS KLTRLLQDSL
     GGNTKTIMIA CISPADNNYD ESLSTLRYAN RAKNIKNKPR INEDAKDALL RQYQEEIARL
     KQLLDKAQMQ NTISSVNGTG DKDEIEKIRE NYEQKMSCLE QKYLDEQMNK AKLENELSQM
     QDNYRQTLSR LSQDNTNVTS NNAKPLMRVA DAEAALEKLK LIERQMIGGE QTSNTALVEK
     RKLKKHEAER RRKELLATAK NGQSDEMEDF HADKDRLESI RNKLENAQKV NVNLQREIED
     LQSEFERDRV DYLETIRRQN QQMKLYQQLL AKVKPCIRKD SNYADLESIK RAAVWDGDAQ
     KWNLPEFLFI KTKLPKAESV NNLKSAAENN QIDNYNTDSD DSGEELLRQR FAKSEEENIA
     GTYFKPLRPV SVINKTREDK MRNIDQPGTY FPYKHNTTWK HLQSGILYTD DLYDGRASQA
     SNASRLTPTN IFKPPSSRTT P
//
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