ID B8NLP2_ASPFN Unreviewed; 1009 AA.
AC B8NLP2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 03-MAY-2023, entry version 83.
DE SubName: Full=Kinesin family protein {ECO:0000313|EMBL:EED49177.1};
GN ORFNames=AFLA_092580 {ECO:0000313|EMBL:EED49177.1}, G4B84_008549
GN {ECO:0000313|EMBL:QMW33118.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED49177.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED49177.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED49177.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW33118.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW33118.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; EQ963480; EED49177.1; -; Genomic_DNA.
DR EMBL; CP059870; QMW33118.1; -; Genomic_DNA.
DR RefSeq; XP_002381078.1; XM_002381037.1.
DR AlphaFoldDB; B8NLP2; -.
DR STRING; 332952.B8NLP2; -.
DR EnsemblFungi; EED49177; EED49177; AFLA_092580.
DR VEuPathDB; FungiDB:AFLA_009494; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_1_1; -.
DR OMA; VYNVNRH; -.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 5.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; cd01370; KISc_KIP3_like; 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:SF13; KINESIN-LIKE PROTEIN; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT DOMAIN 9..379
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 632..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 717..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1009 AA; 110275 MW; CA5DEB94854FE2BA CRC64;
MAIPSDASSI TVAVRVRPFT IREAAQISKC EDGPLFLGDG SLAGAPTPKL NQKGIRSIIK
VIDDRCLVFD PPEDSPVQKF SKSVVPNGKR VKDQTFAFDR IFDQNASQGE VYEATTRTLL
DSVLDGYNAT VFAYGATGCG KTHTITGTAQ QPGIIFMTMQ ELFERIDERS GEKATEISLS
YLEIYNETIR DLLVPGGSKG GLMLREDSNK SVSVSGLSSH HPQNVQQVMD MIMKGNECRT
MSPTEANATS SRSHAVLQIN IAQKDRNADV NEPHTMATLS IIDLAGSERA SATKNRGERL
FEGANINKSL LALGSCINAL CDPRKRNHVP YRNSKLTRLL KFSLGGNCKT VMIVCVSPSS
QHFDETQNTL RYANRAKNIQ TKVTRNVFNV NRHVKDFLVK IDEQMNLINE LKAQQKDYER
IAFAKFKKQT EKKDAVVREG ISRIRNAYEH SLPERQERTA NMLKSRQISR RIGILSSWIA
AFDSVCANSE NEVPLANLQA IRKTAQGVLL ELESSRQHYH QRLARSTWDR GINSAVEHAV
RQLHDFGIND NGDLANLHRE AELLKSNTER DAFSAVAEQE KAGEAETVQL LLQAQFEAIS
AIEDIMQMSE EEAVEAGKSI LSKMLDSCST ATSSLVKPDG SLPAAQPFSP SKAMSPKPKK
RVSLAALPAG KTLAAPISLA STAPASPGKG SPRRRRLGGG RKSVTFSPKK PQAKSTKRSV
RWKDDEQDGS LAEFQKTPQK PRAQLFPEGP QGSPSEPPMP RTSPVPRGIP VPSRNISPSY
GFSPVPAPPE PTLHVPKNNR FKAGFLSKKI SGSPIAPPPS TSLPASDGEH SPLRNIENSS
FLNRASVDRP SRIAVRTSSG SYTSSPASDN KESWKANKDD AIRISSAMRR ISGGHFGAGA
SANSLRVHRR RSPGSATYGS SSPENTMFTA QARRMAKGEK EHEAKPGVLG PRTLPIMKNT
GRRTTFGGEI RPRDISLTSR DAIRLSAMAT PNLQRPSESL YSNSGAGWR
//