ID A0A2A4JUJ3_HELVI Unreviewed; 1136 AA.
AC A0A2A4JUJ3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=B5V51_11150 {ECO:0000313|EMBL:PCG75695.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG75695.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG75695.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG75695.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG75695.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-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 -!- 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:PCG75695.1}.
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DR EMBL; NWSH01000553; PCG75695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4JUJ3; -.
DR STRING; 7102.A0A2A4JUJ3; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
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; cd01372; KISc_KIF4; 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 InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM01114; CXC; 1.
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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000218220}.
FT DOMAIN 12..340
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1079..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..489
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 561..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 630..657
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 701..728
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 778..814
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 923..964
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1136 AA; 129262 MW; CEA5DEFD31AD751E CRC64;
MVEGDNKGTI DTVQVALRIR PLMQLETDRG CEECIDVVTG QPQVQIKDLA FTYNYVFPQH
ITQQEFYDTA VKGLIGRLFQ GYNVTILAYG QTGSGKTYTM GTNYSGSDGD STKLGVIPQA
VADIFDFIEA HEDKFIFKVN VSFMELYQEQ CYDLLSGKER GHSIIEIRED INKGVILPGI
TELPVTSTME TMMVLERGSS GRVTGSTAMN QASSRSHAVF TIVICKESRT DKNLATTSKF
HLVDLAGSER IKKTKASGER LREGVKINQG LLALGNVISA LGDGTNRSFI SYRDSKLTRL
LQDSLGGNSL TLMVACVSPA DYNLDETVST LRYADRARRI RNKPIINQDA KAAEIVRLNN
LVNELRLQLL GKMPTISEQN NEQLQEELDR EKARYAELLK KHKQVTEHLS NMLIENTNLC
EKALLAEAAK DKIERKLNEL TEQCNQTIEN LNTTDKDDEH QKTTVVDYLK EIKTRLEDLQ
SVNLKSNEEL IDHEIKLSFV TDGDHEKVDD EMPMNEDQAV LEEEKRAMGQ VALNQELQEL
NRAMAIKASV VQAILANNKD MLESHKNLRE NEEKIAHLEK ERDELLQQLK QTKSKDPSHE
ERRTKVSTLE HQISDLKKTC QQQAHIIKTK EKNEAKIASL NAELQAMKAT KVKIIKQMRE
ESEKFRKWKA DNERAMLRLR NEDRKRATAM AKMESLHAKQ QNVLKRKMEE AVAVNKRLKE
ALERQKSTQM KRNAKGSVKA GAVQLYIEQE LEVHLSIVEA EKSLEELMEY RAWITEQIEN
LRNSTDEESN RKKIAELEDD LALRKAQISD LQQKILTADQ ENKSRTQWDN IQSMLEAKVA
LKCLFELLVD AKRELTNQSE KGYQARYEEV KEAHDRLAMD FENSKAEFER QLQMVKLQSE
QKLSALVALQ RGVVGKGDKS EACKHLQNVI QYQQERLEQV EEENKKLVDE LEQLRSAGKK
AKRKPKKEPE VEAVKKVEYV EPTDEEDDEF EDREKDPDWR ATPLFKRIQA QRSRLTMNFT
QADVSVAETS ARALKRGSDG AAHCTCRGSC STKMCGCVKS GKGCSGTCRC QPELCKNRRV
SSDSEDKENN PSSTELSLDT TPPSYFDKRG HLDATYVKKK KSYFFPHDQG MATSTQ
//
