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Database: UniProt
Entry: B8NLP2_ASPFN
LinkDB: B8NLP2_ASPFN
Original site: B8NLP2_ASPFN 
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
//
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