ID A0A2A2LF10_9BILA Unreviewed; 1530 AA.
AC A0A2A2LF10;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=WR25_13706 {ECO:0000313|EMBL:PAV84802.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV84802.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV84802.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV84802.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV84802.1}.
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DR EMBL; LIAE01006817; PAV84802.1; -; Genomic_DNA.
DR STRING; 2018661.A0A2A2LF10; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
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; 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:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 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 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:UP000218231}.
FT DOMAIN 17..357
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1380..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 372..434
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 602..629
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1530 AA; 169948 MW; B4CE06FE9C015B94 CRC64;
MTVAAEMSPV GEAADQKIKV AVRVRPLNKR ELELRTKTVV KMNGNQTILD HPVDENKPKP
FAFDYSFDSS DQNESQFASQ EKVFNEIGYD LMENSFAGYN ACLFAYGQTS SGKSYSMMGT
SDQPGIIPRL CNEIFKRIDQ TTSESLTYKV EVSYMEIYNE RVRDLLDPKK SNKTLKVREH
KILGPIVDGL SNLAVDSYQQ IESLIGEGNK SRTVAATNMN AESSRSHAVF NITLTQTLRD
IENGFSGEKV SKISLVDLAG SERVAKTGAM GKRLEEGGSI NKSLTTLGMV ISALAERSNS
TKKDKFIPYR DSVLTWLLRD NLGGNSRTVM IATVSPAADN YEETLSTLRY ADRAKKIINH
AVVNEDPNAR IIRELREEVE SLRMQISQTK KEQTETLELR ERLAESERLV AQMNKSWEER
LRETETLNKE RQRDLSEIGI SVESSGIKVE KDKFYLVNLN ADPSLNELLV YYVNGTAIVG
NTEEIDASRD SGLGSVEELH LKASSNGDGE KTNIVLRGLG VVHRVFVNGR QISERTLLRN
GFRLLFGVHH FFKVNCPKEA TDGNAMEESC MYDYKDAWDE VNGEGAGGIS AAVDQLMQRV
SIKHEEDKKA ALEQQYEAFE QYIQNLQAGG FTPSTPMTPC WSLATPLGTP ASALPPPFPF
AGGSGGGSSR QTVKSKFFYW AQKKKEMLAE SLKRLKADLI RAHAMTNEAN MISKELAVND
KRVTTYDVTL HIPAANLRPS KIKAGAFICE PVIVVRRVGM SGAQLWSLSQ LENKLIDMRE
LYDDRMNEAA EKGMPRGCGG AVERSEQEAD EESPSVVIDP FFESQVPIIS QQGEVAGRLH
VQIYRVAGPI ESEDDRAVGC ENLIGKVINC RVRIKRVCDL PESLSHFVFC QYSFFNATEM
LVVAPSHDLS HPQPSNHTVV IFEHQRDFPV VVTEEFLEYV QEDALSIEVW GHRSCGSEQK
DAARKLDAEE RNKSLQARWG EVSRRLELWM QINELNENGK WEPVECRQFE DVSTGGVYQL
RQGQQRRICV GVNLPFSEGL PLHIDSIHSV AIGCIWPRKP NVHKTLDSYQ AGIYFLPEQC
LFIILGRRPG SDSLAMDRGL ADEAKLSSCS AKSESDKERE HSLMAQWIAL TEERAAVAIP
APNSKIPGSP CDWTPPLGTE KHVPVVFLDL NPDDMAGEAS ASEVTLRTAG QHSILPLETN
GQFIMLPPLQ FDEKRCCVIC PWDSSVHDND SLNVVTPSNE RIYAILKTTV RLSHPCVMDV
VLRKRICMQV YKKSSFAERI FKRMIGTETA YHTSVLYDLV AHVPKSSCDI EERESLAMLA
AKHAMGSENE AVESMLKLDR LRQEVAITTM LSRKERQERL QHFGLPPHSL KMKRTVSLPN
AISNSTTPLP SSSNCGYDSP MGTSTTTSMT PSCRPPRPTF LSLAHSTSNS SRLTSLMSPA
NERLSGIDEE SKETYPVRSS TVPDALSKNA KDLSNEQMDL RNGNLLLSSS SSKISPLGDC
TSSASGCAGS GALGAMRWAN KPPQGLDLNV
//
