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Database: UniProt
Entry: A0A2I0J4M8_PUNGR
LinkDB: A0A2I0J4M8_PUNGR
Original site: A0A2I0J4M8_PUNGR 
ID   A0A2I0J4M8_PUNGR        Unreviewed;       559 AA.
AC   A0A2I0J4M8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=CRG98_028767 {ECO:0000313|EMBL:PKI50860.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI50860.1, ECO:0000313|Proteomes:UP000233551};
RN   [1] {ECO:0000313|EMBL:PKI50860.1, ECO:0000313|Proteomes:UP000233551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PKI50860.1};
RA   Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA   Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA   Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA   Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT   "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL   Submitted (NOV-2017) 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,
CC       ECO:0000256|RuleBase:RU000394}.
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:PKI50860.1}.
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DR   EMBL; PGOL01002078; PKI50860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0J4M8; -.
DR   STRING; 22663.A0A2I0J4M8; -.
DR   Proteomes; UP000233551; 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   CDD; cd01374; KISc_CENP_E; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF51; KINESIN-LIKE PROTEIN KIN-7O; 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   ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233551}.
FT   DOMAIN          3..329
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          335..416
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         78..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   559 AA;  62892 MW;  A860487BDEA7031D CRC64;
     MERIHVSVRA RPLSPEDAKT SPWRISGNSI FIPNHSSKFE FDRIFGEDCP TQEVYQARTK
     DIVAAAVRGF NGTVFAYGQT NSGKTHTMRG SAAEPGVIPL SVYDLFDTIE KEKDREFLLR
     MSYMEIYNEE INDLLVPEHL RLQIHENLER GIHVAGLQEE IVASPEQVLE LMESGESHRH
     IGETNMNVYS SRSHTIFRMQ KRKTESGDKH EDEGGHTSCD AVRVSVLNLV DLAGSERAAK
     TGAEGVRLKE GSHINKSLMT LGTVIKKLSE GAESQGGHVP YRDSKLTRIL QPALGGNSNT
     AIICNITLAQ VHADETKSSL QFASRALRVT NHAHVNEILT DAALLKRQKK EIEELRAKLQ
     GSHSEYLEEE ILNLRNTLLQ TELERERIAL ELEEEKKAHA ERERRLQEQA KKIENLSTMV
     LYSSRDENRD NIKKGKRRDT WCPGALSRET LGEARPTIDV KGSAGKTASS RHEMGPLLPF
     DELVNEIEVG LDNSCKIEED HDHGAQEDSI IPNPQSLMHV TSRRKASTRN KTVAEVNINP
     VEIHAAYDDL LIKFENQIW
//
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