ID A0A218XTQ8_PUNGR Unreviewed; 906 AA.
AC A0A218XTQ8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=CDL15_Pgr003829 {ECO:0000313|EMBL:OWM88417.1};
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:OWM88417.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Ungrouped subfamily.
CC {ECO:0000256|ARBA:ARBA00010103}.
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:OWM88417.1}.
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DR EMBL; MTKT01000797; OWM88417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218XTQ8; -.
DR Proteomes; UP000197138; 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; cd00106; KISc; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR047149; KIF11-like.
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; PTHR47970:SF31; ARMADILLO REPEAT-CONTAINING KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 68..399
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 648..690
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 689..732
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..490
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 529..591
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 906 AA; 98976 MW; DD70A8C5866E0740 CRC64;
MATAFGSNYR NGAPRSSPRV VDSSGRPLSV NHNPKSSLKS KPSGIRKSSP ASLGGGSAGA
AKDDVPGRVR VAVRLRPRNA EELVEDADFG DCVELQPELK RLKLRKNNWD TDTYEFDEVF
TDSASQKRVY EVVAKPVIES VLEGYNGTVM AYGQTGTGKT YTLGNLGEED TAARGIMVRA
MEDILADVSP ESDSICVSYL QLYMETLQDL LDPSNNNISI VEDPKTGDVS VLGAISVEIR
DQQSFLELLS LQKLISTEDA PVMMQAHVRR SIKDSVLSSV NGSNSHVSKA LKPPIVRKGK
LVVVDLAGSE RIDKSGSEGH TLEEAKSINL SLSALGKCIN ALAENNSHVP VRDSKLTRLL
RDSFGGTART SLLITIGPSP RHRGETASTI MFGQRAMKVE NMLKLKEEFD YKSLSRRLEI
QLDKLIAENE RQQKAFKDEI ERISVEAQKR ISEVETKYED ALEAERLKYQ KDYMESIKKL
EEQLVTNQQK LSNGKINTAA NDTSSHINSR EPAALASALE EVANLKKLLG REASLKKAAE
EEINNLKSQL SQSKLLEASA NSEILKLQKM LEDESRQKEK IEGDLAALQS QLLQLSFDAD
ETRRNLDRGG GVNGPSGLES LISQAKNQQV NDPGNGEKAS MAKLFEQVGL HKILSLLEAE
DADIRIHAVK VVANLAAEEA NQQKIVEAGG LKSLLILLRS SDDETVHRVA AGAIANLAMN
ETNQELIMVQ GGIRLLSMTA ANAKDPQTLR MIAGAIANLC GNDKLQTKLR GEGGIKALVG
MVRCGHPDVL AQVARGIANF AKCESKASVQ GMKKGRSLLI EDGALSWIVQ NANNEATPIR
RHIELALCHL AQHEANARDM IGGGALWELV RISRDCSRQD IRTLACQTIS SSPTFQAELR
RLRIEY
//
