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Database: UniProt
Entry: A0A1A8VVZ0_PLAMA
LinkDB: A0A1A8VVZ0_PLAMA
Original site: A0A1A8VVZ0_PLAMA 
ID   A0A1A8VVZ0_PLAMA        Unreviewed;      1590 AA.
AC   A0A1A8VVZ0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   SubName: Full=Kinesin-8, putative {ECO:0000313|EMBL:SBS84666.1};
GN   ORFNames=PMALA_010440 {ECO:0000313|EMBL:SBS84666.1};
OS   Plasmodium malariae.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5858 {ECO:0000313|EMBL:SBS84666.1, ECO:0000313|Proteomes:UP000078597};
RN   [1] {ECO:0000313|Proteomes:UP000078597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Naeem Raeece;
RL   Submitted (MAY-2016) 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; FLQW01000570; SBS84666.1; -; Genomic_DNA.
DR   VEuPathDB; PlasmoDB:PmUG01_08036700; -.
DR   Proteomes; UP000078597; 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; cd00106; KISc; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
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   PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF15; KINESIN-LIKE PROTEIN KIN-4A; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|PROSITE-ProRule:PRU00283};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT   DOMAIN          508..838
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1570..1590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         595..602
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1590 AA;  178269 MW;  E19D8D10F60C1354 CRC64;
     MSRKLTNVSK RNNNNEKSNK SLNEIYIYNK KFKHLNGSST NGQNTNGQNT NGQNTNGQNT
     NEQNTNGQNT NGQNTNGQNT NGQNTNGQNT NGKNTNGKTS NGTNRTKGTT NSTCKKKNTI
     FFSAQNEIEE EKKKKKKGIL ILHTNTECKA ILKKKKINDA KFVENVDAEI ANVNNCSSCV
     IKNNFYQNKK KILRITPEYC DTKKKIAHHV KNKNTLHANK CVNEDILFNN NISSAFKINI
     NSDSGSSVHG NSVNVSNVSG STISGSTISG SIISSSNVNG NTISKRNITN SKGEKRKHPL
     IIWSSDEKEG VKKKYSTNHN TNSIINYNDR TLKIFCNLSE DNSKNITCAS GYISNDRISN
     IYNGAVNSAR NSVHNDNVLG TNSKDSNRKK KNSQNDVQNQ LFIPNNDLKK IKNYTMERTN
     KNKLSVTSSP NKKVIENINE YPITSKNIYD SIYIPQINIK NLINSDQINN IGVPSPTHAC
     NNNSNGLNNV LRKSESSNLI NALNAYSNVK VAVRIKPITE SEENIVSIFN KNYVLIEKEN
     EKECYLLSQK KKQATYVFDV VFDVNATQEE VFFDTAKPLI PHVFKGINCT VFAYGATGSG
     KTYTMLDDKN HNGIVQLSLL ELFTIIKEKK CRNIKIVMSF LEVYNETIRD LLAKEKNKTL
     DVQEDVAEVK VSNLCEMEIQ SYEQAMFLIN EGVKNRKMSP TRANKVSSRS HAILQIYVFN
     EILDSNMNTI NYKAKLCFVD LAGSERASAT SNKGERFKEG SYINQSLLAL ANCINSLASN
     RNISKVRVKY RDSKLTHLLK NSLEGNCLVV MIANINPSRK SFQESNNTLK YAFRARNIKL
     CATVQTNDNK ESDIEKILKK NNILQKEYDI VLAKYNNIKD FYSPLKVLFQ LYKLVHSCYK
     RMQSASENFS ILELKQDISI YEQLIKVKSD AIRKRMDLLN CGADEKHFID IFDSFEDKNL
     DYFIHSDKNG GNDSNIDCND SNICCNDSNI CCNDSNIGCN DSNIGCNDSN IGCNDSNICG
     NDSNICGNDS NIGGNDSNIG GNDSNIGGND SNIGGNDNNI GGNDNNIGGN DNNIGCNDNN
     DSYNNNNNGY DDNSTGYGNN NNGYTDNSKG YNNNSTSYDN NNNGYGNNST GKNIGFSVLN
     GEGVENRTVL EEKLLKKKDL QFCDNSTTLR SDYIFFKNDM SKIKLDDDLS SDELSVYDVK
     NVDALVNCSI KGKRGQLINV FESKKNVRIN GNDTSHYGVV RQGHTGNSAK NGHMDLGAIQ
     YDDYTTNTNK HNALKDVYIL KNERNNINVN FDISKSNHIV NFLKEPLIDD ITSENNYMSL
     IKEQNGKMKI HTNENMPIKL NRNEKKEQLQ TLHNNLTDMQ NSILFNTINK QIGESPHSPI
     IKKNVKELLL HNNLNKKSFL LNGKISKNMT TEQVNSDLIG NYNISADGNK NLYGSDNNEI
     NDNSGNNDNN NKSGNNDNNN NSENNVRGND SVSEEDLTSG TPAGEETNIL KESNTWKGTI
     EHFHDAYEGG NINVKVFNKE KNSAITNIEW DKLMIKNNYD DRTIDNNDEI RERNKRKFVI
     LGENIKHEHE HTNERSMSVK KKKLSIKSKK
//
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