ID A0A0K0FYC5_STRVS Unreviewed; 1631 AA.
AC A0A0K0FYC5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Kinesin-73 (inferred by orthology to a D. melanogaster protein) {ECO:0000313|WBParaSite:SVE_1745100.2};
OS Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_1745100.2};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_1745100.2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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 STRING; 75913.A0A0K0FYC5; -.
DR WBParaSite; SVE_1745100.2; SVE_1745100.2; SVE_1745100.
DR Proteomes; UP000035680; 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; 1.
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:UP000035680}.
FT DOMAIN 13..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 369..413
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1631 AA; 184096 MW; BBDC04151756046E CRC64;
MLNHPMTVDG VERVKVAIRT RPLNKREIDL GTKCCVNFSS TSQIILSQPL EEGKSPKVFS
FDHCFNSTDP HSATFINQED VFENLGKDVV DNAFAGYNAC IFAYGQTGSG KSYTMMGTST
NPGIIPRLCN NIFERIDIEN KENVSCKVEV SYMEIYNEKV RDLLDPKNST KRPLKVREHK
ILGPTVDGLS VLAVSSFEQI NQLIDEGNKS RTVAATNMNA QSSRSHAVFT ISLTQTIKQK
DKDFSGEKVA KISLVDLAGS ERAQKTGAVG KRLEEGGNIN KSLTTLGMVI SALAEKSGKK
DKFVPYRDSV LTWLLKDNLG GNSKTIMIAT ISPSSDNYDE TLSTLRYADR AKSIENHAII
NEDPNAKIIR ELREEVENLR QQISQTMEQK SETQELRERL AESERIVSQM NKSWEERLKE
TDIIYAERQK DLAEIGIALT GSGIKVQKDR FYLVNLNADP SMNELLVYYI NQKAYVGCSE
SLENGIKNDF LLQGLGVQPY HAKLEVCDDE ITGQQKLFIE PLAENARICV NGRLINQKTP
LRNGFRLLIG NNHFFKVNCP KDDKSNLAST NSMIASIMEE SFFDYDKAWS EVNTSDLGCN
SGIEAVDDYI EHLTLKHHED KQAALEKQYE EFERYIQTLS TSITAPSTPM TPGSGFILTS
PIAGTPSCNL PSVSFPSNPK VADKTKFFKW AQKREELFKE SLEKLKKEIM RAHALVREAN
MISEEINGKR RGMIRYDVTL QIPAANLRPS KIKVGNSVSE PVIVVKRDGM SGYQLWSLEQ
LENKLIDMRE MYNERFNINI DSSVSSDTST PSSDEAIESD VDCFEEIHDI GGYRRNYVFD
SQEKHSLIGV ANIFLEVLFH EMKLNYKVPI ISQQGEVCGK LHIEVYRLPD NNCSKMIDSM
SESTDSTDSV DSGSWRVHGY GDSNTFIGKT ITCRVRIKKA SNLPIVLSNF VFCQYSFFNI
SEMLVVAPKY EPNATANNGN FEFDHEKDFQ VVVNEEFLEY IQEDALSIEV WGHRSSGFGP
DTTINKEEEF DLAQKQKSLQ ERWIEVTRRL ELSVSIKELN DNGEYKNVEV STNNDIACGG
IYQLKQGQQR RIDVSISERN DHGNLPLMIS EITSVSIGSI FVANCDKNEN FDSYQEEDLD
MIKDLWATAL KERHKYLSKQ ISMINEKGSK KTGKDTEREK SLITQWMILT EERNAVSVPA
TNSSIPGAPS DISVPLGCER HVPVVFLNID TEEMNAFNDY SSNHDHNNPT KIIGLSSQLP
RENFMTMLQL HIIEKNDAEL RVSCPWDSSI HGESCLNCVS NSNEKIFGIV KVSVRITQPV
PMEIVLRKRI CMSIYKKPSL TEMLIKKIVR NENVYSTKVF YDVVAQIPKS SLEMENRESL
ALLAASTDDE EFHKNKVSSG LLYNSSNEED IISLEKQMKY IESYTKTIQD VECMLKLDRL
RQEAAMFNMI PRNERAQRLS FGNPTNSFRM KRTISLPNSI SNSLPPIASK YSANGISDIL
ESSFCDRSNM DTSMVSSSGV SSMSRPTFLN LKSTINNNHH KLSSLVSPIL ELNTKLHGID
EEEKILEYSN ILNENNYTST VVTTIDVING NESVPSFSII NNYDNLTRTN KLFKDDSMKN
NNKNFLNGAF Y
//
