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Database: UniProt
Entry: A0A199UWB6_ANACO
LinkDB: A0A199UWB6_ANACO
Original site: A0A199UWB6_ANACO 
ID   A0A199UWB6_ANACO        Unreviewed;       848 AA.
AC   A0A199UWB6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Kinesin-like protein NACK1 {ECO:0000313|EMBL:OAY68916.1};
GN   ORFNames=ACMD2_12039 {ECO:0000313|EMBL:OAY68916.1};
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY68916.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY68916.1, ECO:0000313|Proteomes:UP000092600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY68916.1};
RX   PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA   Redwan R.M., Saidin A., Kumar S.V.;
RT   "The draft genome of MD-2 pineapple using hybrid error correction of long
RT   reads.";
RL   DNA Res. 0:0-0(2016).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-7 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007310}.
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:OAY68916.1}.
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DR   EMBL; LSRQ01004666; OAY68916.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199UWB6; -.
DR   STRING; 4615.A0A199UWB6; -.
DR   Proteomes; UP000092600; Unassembled WGS sequence.
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   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR021881; NACK_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF64; KINESIN-LIKE PROTEIN KIN-7A; 1.
DR   Pfam; PF11995; DUF3490; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092600}.
FT   DOMAIN          32..258
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          254..322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          369..396
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          450..477
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        478..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..571
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         118..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   848 AA;  95441 MW;  19BA2DDF8E985E13 CRC64;
     MGVPARIPGT PASKIERTPF STPGGSRVKE EKIFVTVRVR PLSKKEEALK DQITWECIDN
     QTVLYKTPSQ DRASSPASYC FDRVFGPTCL TETVYQEGAK EVALSALKGI NATIFAYGQT
     SSGKTYTMRG ITESAVNDIY KHIENTPERE FVIKISAMEI YNEIVKDLLK PDSGPLRLLD
     DPEKGTIVEK LEEETAKDGQ HLRHLIGICE AQRQVGETAL NDTSSRSHQI IRLMVESSLR
     ENSGCVKSFV ASLVVSDKQL VKHLQKEVAR LEAELRTPES SSCSEALLME KEMKIKKMEM
     EMEELKRERD VAQSKLDELR KKMGDDLSRW NPFDSSPHCV AKCLTFSGPS PQAQPKNPMR
     QSSTAPFMLM HEIRKLEQLQ EQLGEEANRA LEVLQKEVAC HRLGNQDAAE TIAKLQAEIK
     EMCTVRSVNK KVEVENAVDG ANLKEEITKL HSQGNTIANL EAQLENVQKS IDKLVMSLPN
     NRSSECNSEM NTPKSSKSHS KKKKMLPLAL SSSSNRPNFI KAPCSPLSSA REILESEVEN
     RAPKSENIIS HEDLPSSEKA TPTKSEDGGE VSSREGTPSG YRRSSSVNMR KMQKMFQNAA
     EENVRSIRAY VTELKERVAK LQYQKQLLVC QVLELEGNEA AGNGAQGREA DISAHQSSPE
     SWQAMFKEQM QQIMQLWDVC HVSIIHRTQF HMLFRGDPAD QIYIEVELRR LIWLQEHFAE
     VGDASPVPTG DDSAVSLSSS IKALRHEREF LARRMSARLT KEEREQLFHK WQVPLDGKQR
     KLQLVNKLWM DPNDPANVEE SANIVARLVG FCEGGNITKE MFELNFSLPA SKKPWLLGWQ
     PISNLLRL
//
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