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Database: UniProt
Entry: A0A199VIQ3_ANACO
LinkDB: A0A199VIQ3_ANACO
Original site: A0A199VIQ3_ANACO 
ID   A0A199VIQ3_ANACO        Unreviewed;      1283 AA.
AC   A0A199VIQ3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-MAY-2023, entry version 30.
DE   SubName: Full=Kinesin KP1 {ECO:0000313|EMBL:OAY76625.1};
GN   ORFNames=ACMD2_07340 {ECO:0000313|EMBL:OAY76625.1};
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:OAY76625.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY76625.1, 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:OAY76625.1};
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-14 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010899}.
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:OAY76625.1}.
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DR   EMBL; LSRQ01001765; OAY76625.1; -; Genomic_DNA.
DR   STRING; 4615.A0A199VIQ3; -.
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; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
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   InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR   PANTHER; PTHR47972:SF49; KINESIN-LIKE PROTEIN KIN-14M; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16796; Microtub_bd; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50021; CH; 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}; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000092600}.
FT   DOMAIN          26..130
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          735..1043
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1106..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          518..647
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1107..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         819..826
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1283 AA;  144759 MW;  7E1B38081A598D7A CRC64;
     MASASSDAEM GTQFLDQIEF NLIQSAKRRS EVVEWLNGLF SDFKLSPNAS EEELRARLID
     GAVLCAILRR LFPRYVEEKN PSQARGVDNV KKFLSAIERM GLHGFKSSDL EQGPISAVVI
     CLLSLRDRSS SHVGEDRFPN SSAKGESEAM RRWKLLENSR LEAVDVLRME NSRGAQNGEG
     LGEERKQSMM ESKLQRVLRS PVMSEPSTPL SRYAGHKFHE VFQLKQGGYS DLPAAKISEM
     MKSNSLDNAP TQSLLSVVNG ILDESIERKS GEIPYRVACL LRKVIQEIER RISTQAEHIR
     NQNNLIKARE EKYQSRIRVL ETLASGTSEQ TQTETNKVDE KKRVGEEEMT RLIKEKGNSD
     LIISNLKKEL ESLKTGEEQV TRLMKEKEDC DLIISNLKKE LEALKTGEEQ ISRWMKEKGD
     CDLIISNLKK ELEALKTGEE HVTRLMKEKG DSDLIISNLK KELEALKIRE EQVTRLMKGK
     GDSDLIISKL KQELETSKNG EEQVTRLTKE KKDSDLIISK LKQELETLKN GEEQVTRLMK
     GKEECDLIIL KLKQELENLK KSYEEQGQLL ETKKEDVIRL SKEKENSDNI ISKLKREIEV
     AKKLHEQQCQ QLEIKAKETK VELEKRIKEV EHLLEESRRR TKELELSSES KFKKYIEKES
     LVRKFTGVQL QNVQELRLSS VSIRHEVLNT QNRWSEEINN LGQRLKVMID AAQNYHATLA
     ENRKLYNEIQ ELKGNIRVYC RIRPFLPGEN RKSTTIEYIG QNGDLLLANP SKQGKDGHKM
     FTFNKVFGPV VTQEEVFVDI QPLIRSVLDG YNVCIFAYGQ TGSGKTYTMT GPNNLTEKEW
     GVNYRALNDL FHISRNRGDT IMYEVGVQMV EIYNEQVRDL LINDGSQKKY PFVLTISIYH
     PVSQSYAGLQ IELSEPLLSM IEVADLTVHV RGLDLKTGAT LRGSLHLVDL AGSERVDRSE
     VTGDRLKEAQ HINKSLSALG DVIFALSQKN AHVPYRNSKL TQVLQSSLGG HAKTLMFVQI
     NPDASSYSES LSTLKFAERV SGVELGVARS QKEGKDVREL MEQVSFLKDT IAKKDEEIEH
     LQLLKDVKTH SPRLKVEKHG AALLKHSSSS PGVSLLSGST APQNQKSSIG RTVTNNRAAP
     DTDVFSDNSD RHSEAGSLQS IDDFKHQKEI VIGQSKLSGG ETGQSSIELD FVSLGDADYE
     ERLSDISDSG LSMGTETDGS ISSVVEFTLF PESEQSSDAT REKAFEEKYN HPSSGIFTPD
     SKKMAIDQNR KAGANLLPVL RNG
//
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