ID A0A0N4YB34_NIPBR Unreviewed; 1588 AA.
AC A0A0N4YB34;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Kinesin-like protein {ECO:0000313|WBParaSite:NBR_0001364701-mRNA-1};
GN ORFNames=NBR_LOCUS13648 {ECO:0000313|EMBL:VDL77237.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001364701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001364701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL77237.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UYSL01021105; VDL77237.1; -; Genomic_DNA.
DR STRING; 27835.A0A0N4YB34; -.
DR WBParaSite; NBR_0001364701-mRNA-1; NBR_0001364701-mRNA-1; NBR_0001364701.
DR OMA; MAIQTEH; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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; IPR035892; C2_domain_sf.
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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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:UP000271162}.
FT DOMAIN 9..369
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 858..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 397..441
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 862..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 111..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1588 AA; 179081 MW; 274F4AE0F0739DED CRC64;
MTAVDDCEKV KVAVRVRPFN KRELDLNTKT VVRMCNGQTI LDHVSDEVTE TCPKFPFFSK
QPKTFAFDHS FYSTDANDPN FASQEEVFNS LGSGVLENAF SGYNACIFAY GQTGSGKSYS
MMGTSEQPGI IPRLCNEVFR RIQETTCESL QYKVEVSYME IYNERVRDLL DPKKRAQFYY
FLSNKHHLKV REHKILGPMV DGLSVLAVNS FEQIASLIEE GNKSRTVAAT NMNAESSRSH
AVFNITLTQI LKDVEKNFTG EKVAKISLVD LAGSERAGKT GAMGKRLEEG GNINKSLTTL
GMVISALAER SNGKKEKFIP YRDSVLTWLL KDNLGGNSRT VMIATISPAA DNYEETLSTL
RYADRAKRIV NHAVVNEQTH EMERRRIRFQ DPNARVIREL REEVETLRMQ ISQTLKEHSE
TAELRERLAE SERLVAQMNK SWEERLKETD TLNKERQRDL AEIGISIESS GIKVEKDRFY
LVNLNADPSL NELLVYYINT TAIIGNLDEN ETSLDSGLGN SVEDLNPKDA TERTSIVLRG
LGVMRRHARL SVVEERGRSR LYVEPLSPEG RVCVNGREIS DRTPLRHGNR LLIGMNHFFR
VNCPKDVDMT QSIMDESVLF DYNDAWHEVA TFIYHPPSIV HFPPFIFLCD NERDSSPLSF
MNSYKMASPN TIQKVPLMFQ EDKQAALERQ YEAFERYIQN LTAGGFTPST PMTPGYGFGT
PLGTPGTALP PFPFPANPKQ MVRSKFFYWA QRKEEMFAES LKRLKSDVIR ANALTREANM
ISRELGNTRR QTTYDVTLQI PAANLRPSKI KAGTFVCEPV IVVRRTGMSG SQLWTVAQLE
NKLIDMREMY SDKLNGVLRE PSCASSPESS PSRSLPQSSM DEVMIDPFFE SQEHHNLIGV
ANVFLEVLFH DMKLDYQVNT SELSLVPIIS HQGEVSGRLH VQIYRVPGES DGIQSPEREY
NDGLERAEGL LGKVITCRVR IKKASSLPES LSHFVFCQYS FFNLSEMLVV APVFDPTQAS
ETQTQATTFV FDHEKDFKVV VTEEFLEYVQ DDALSIEVWG HRNGGIMEDG QPKLDAEEKS
KSLQVPDGPR SQSSSPKHGS LKDFKVVVTE EFLEYVQDDA LSIEVWGHRN GGIMEDGQPK
LDAEEKSKSL QARWSEVSRR LELWTEFREL NETGHWIPVE VRQQDDVATG GVHQLKQGQQ
RRLVVGLSLP QHGAGLPLGI DTITSVSIGC VCLSESGDQK TYDSYQEEDL DRIRAQWTLA
LQTRQKYLEQ QLDSLCSKSN KSESELEREH SLMGQWVSLT EERTAVSIPA PNSDIPGAPC
DWIPPPGVEE HVPVLFLDLN SDDMTGELTS DENTPRIAGL HSFLPKEDSG GPLVMLPIVH
FDDKELIATC SWDSSIHDHP ALNVPSSSNE KVYAIVKVGV RLSHPCSMEL VLRKRVCLNI
YKKASLTDRI RKRIVGSESL HRTAVYYDVV AHLPKSSHDM EERSSLALMA ARHTTSSDDD
GSSDEGRHSS RQLSYIEAYT KSIQAVESML KLDRLRQEVA ITNMLSRRER QQRLSHLCMP
SQSFRMKRAV SLPNAISLVS PEIVGGHL
//
