ID W2T2D1_NECAM Unreviewed; 1579 AA.
AC W2T2D1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Kinesin motor domain protein {ECO:0000313|EMBL:ETN75724.1};
GN ORFNames=NECAME_03696 {ECO:0000313|EMBL:ETN75724.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN75724.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; KI660278; ETN75724.1; -; Genomic_DNA.
DR RefSeq; XP_013297951.1; XM_013442497.1.
DR STRING; 51031.W2T2D1; -.
DR EnsemblMetazoa; NECAME_03696; NECAME_03696; NECAME_03696.
DR GeneID; 25343730; -.
DR KEGG; nai:NECAME_03696; -.
DR CTD; 25343730; -.
DR OMA; MAIQTEH; -.
DR OrthoDB; 126886at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF5; -; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 2.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
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:UP000053676}.
FT DOMAIN 8..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1465..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..407
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1579 AA; 177388 MW; 08DECFB97991098B CRC64;
MTAEDSEKVK VAVRVRPFNK RELDLGTKAV VRMCNGQTIL DHISDDKQPK TFAFDHSFYS
TDPNDPSFAS QEEVFNSLGS GVLENAFAGY NACIFAYGQT GSGKSYSMMG TSEQPGIIPR
LCNEVFRRIR ETTCDTLHYK VEVSYMEIYN ERVRDLLDPK KSNKHHLKVR EHKILGPLVD
GLSVLAVDSF QQIASLIEEG NKSRTVAATN MNAESSRSHA VFNITLTQIL KDVEKDFTGE
KVAKISLVDL AGSERAGKTG AIGKRLEEGG NINKSLTTLG MVISALAERS NGKKEKFIPY
RDSVLTWLLK DNLGGNSRTV MIATISPAAD NYEETLSTLR YADRAKRIVN HAVVNEDPNA
RVIRELREEV ETLRMQISQT LKEHSETEEL RERLAESERL VAQMNKSWEE RLKETDTLNK
ERQRDLAEIG ISIESSGIKV EKDRFYLVNL NADPSLNELL VYYINSTAII GNLDEIETSL
DSGLGNSVED LDKKDGGERT SIVLRGLGVM RRHARLSVVE ERGRQRLYVE PLSCEGRVCV
NGREITDRTL LRHGYRLLIG MNHFFRVNCP KDVDMTQSVM DESVLFDYDD AWHEVNGDGG
GNPISTAVDQ YMEQVTLKHQ EDKQAALERQ YEAFERYIQN LTAGGFTPST PMTPGYGFST
PLGTPGTALP PFPFPANPKQ MVRSKFFYWA QRKEEMFAES LKRLKSDVIR ANALTREANM
ISRELGNTRR QTTYDVTLQI PAANLRPSKI KAGTFVCEPV IVVRRSGMSG SQLWTVAQLE
NKLIDMREMY NDKLNGVIRE PSCTSSPEGS PAHSVPQSSL DEVMIDPFFE SQEHHNLIGV
ANVFLEVLFH DMKLDYQVPI ISHQGEVAGR LHVQIYRVPN CESDGIQSPE REYCDGLERA
ESLLGKVITC RVRIKRASSL PESLSHFVFC QYSFFNLSEM LVVAPVFDPS QASESQTQAA
TFVFDHEKVS LSYQFRRSKR QHYMPLQDFK VVVTEEFLEY VQDDALSIEV WGHRSGGVTD
MSEPKLDAEE KSKSLQARWS EVSRRLELWT EFRELSETGQ WIPVEVRQQD DVATGGVHQL
KQGQQRRLLV GLSLPQHGAG LPLGIDTITS VSIGCVCVCD AGQQRVLDSY QEEDLERIRA
QWTLALQSRQ KYLEQQLDSL SSISNKSEAE LEREHSLMGQ WVSLTEERTA VSIPAPNSDI
PGAPCDWIPP PGVEEHVPVL FLDLNSDDMT GEMTSDENTP RVAGFHSFLP KEESGGPLVM
LPIVHFDEKE LIATCSWDSS IHDQPALNVP SSSNERVYAI VKVGVRLSHP CSMELVLRKR
VCLNIYKKAS LTDRIRKRIV GTDPLHRTAV YYDVVAHLPK SSHDMEERSS LALMAARHTA
STEEEHMGGN DDGHRPNKQL SYIEAYTKSI QAVESMLKLD RLRQEVAITN MLSRRERQQR
LSHLGLPSQS FRMKRAPLNQ LPATSRHSEL TAESQHKPPQ PPDTPMSMST TSMVTSLISP
LNEKLCGIDE EISAKNEMYS ADVRNGNMSA ASVLTTSSIL TSSTDDENRP DMDILQLNNN
QQLGKEKLYL KGICAKNGC
//
