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
//