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Database: UniProt
Entry: A0A1I8B8A8_MELHA
LinkDB: A0A1I8B8A8_MELHA
Original site: A0A1I8B8A8_MELHA 
ID   A0A1I8B8A8_MELHA        Unreviewed;       598 AA.
AC   A0A1I8B8A8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Kinesin motor domain-containing protein {ECO:0000313|WBParaSite:MhA1_Contig1545.frz3.gene12};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig1545.frz3.gene12};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig1545.frz3.gene12}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   AlphaFoldDB; A0A1I8B8A8; -.
DR   WBParaSite; MhA1_Contig1545.frz3.gene12; MhA1_Contig1545.frz3.gene12; MhA1_Contig1545.frz3.gene12.
DR   Proteomes; UP000095281; Unplaced.
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; PTHR24115:SF802; KINESIN-LIKE PROTEIN UNC-104; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 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; 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   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT   DOMAIN          3..292
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          536..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          434..501
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        549..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   598 AA;  68495 MW;  6E7EA1B7A3AC8994 CRC64;
     MSSLKVAVRV RPFNSREIHI TSSSNQTYSF EFDYSYSSFD KTSVNYASQE MIYDDIGAEM
     LDHAFDGYNV CIFAYGQTGS GKSYTMMGKV NDLEEMGMIP RLCRAIFSRI CENKENQQLK
     YTVEVSYMEI YCEKVKDLLS PKNENLKVRE HPVLGPYVDN LEKMAVCSYE ETVAATNMSD
     TSSRSHTIFT IVLTQRECVN NLETETEGAN INKSLTTLGL VIKKLAEQSN KRKGKQARAA
     VIPYRDSVLT WLLKESLGGN SKTAMIAAIS PAEVNFEETL STLRYADSAK QIVCRAKVNE
     DINAKFFRGY KEEGISKKTF RALDVGNDGG TKTEDYFIPP LTDFSNFTHP RKQWMKWYLE
     LGNRLPSVDS MEIDDPFSSE VPDFKIDGPN DIESFQKIRQ YFTTQIAQRK GFLESVEQNS
     QLFEAKLKQR LCNADLDYQQ LKDSEEEIIR LKQENVSQTG QIRQLQRENN ALRVRLYKYE
     NVQEQERLRG ENQRYLEAER EAALNSNRRT IQKVAELFES PIPTTSNVAR LRKKFVNNTS
     DDTDQETEEG ENGGRKTPKI DASSPKKRRV EGATTVKFYG VKSSPKISGF NNPRYQRR
//
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