UniProt: B8NTQ4

Database: UniProt
Entry: B8NTQ4_ASPFN

LinkDB:  B8NTQ4_ASPFN 
Original site:  B8NTQ4_ASPFN

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Ontology (5)   
   GO (5)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (21)   

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ID   B8NTQ4_ASPFN            Unreviewed;      2402 AA.
AC   B8NTQ4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Myosin type II heavy chain, putative {ECO:0000313|EMBL:EED46321.1};
GN   ORFNames=AFLA_099850 {ECO:0000313|EMBL:EED46321.1}, G4B84_009201
GN   {ECO:0000313|EMBL:QMW33735.1};
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:EED46321.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED46321.1, 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:EED46321.1};
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:QMW33735.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW33735.1,
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   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; EQ963484; EED46321.1; -; Genomic_DNA.
DR   EMBL; CP059871; QMW33735.1; -; Genomic_DNA.
DR   RefSeq; XP_002383857.1; XM_002383816.1.
DR   STRING; 332952.B8NTQ4; -.
DR   EnsemblFungi; EED46321; EED46321; AFLA_099850.
DR   VEuPathDB; FungiDB:AFLA_010228; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_5_0_1; -.
DR   OMA; QRAMDIE; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 6.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}.
FT   DOMAIN          116..166
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          170..864
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          743..765
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          2374..2402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          942..1274
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1314..1578
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1614..1648
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1724..1792
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1836..1905
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1955..2067
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2124..2186
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2215..2362
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2376..2402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         263..270
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2402 AA;  276974 MW;  65C2410B9B60A0BC CRC64;
     MLPSQLNGSP KRANPFSRAS PSPSPSPSPA PRAARPKSAL ITQSSKFEEA RGHFRNSSSL
     AQSTQAPFSR ITSRQRSNSL RNDVTSGTFA PEFIKSEELQ RGADQIRGLE GDNDFSGNKY
     VWLRDPEKAF IRGLILEERA NGKLLVQSDD GEQREVDADQ IDKVNPAKFD KADDMAELTH
     LNEGSVVHNL HTRYQADMIY TYSGLFLVTV NPYCPLPIYS NEYVKMYKGR SREETRPHIF
     AMADEAFRNL VEEGENQSIL VTGESGAGKT ENTKKVIQYL AAVATSDTPH ARSGTKQLSI
     LSQQILRANP ILEAFGNAQT VRNNNSSRFG KFIRIEFTRS GQISGAWIDW YLLEKSRVVK
     PNSQERNYHI FYQLLRGADP ALRESLLLSG LGIGDFAYTR DGNDSIIGVS DDEEWNALLE
     AFHIMDFSED EQMHILRTIS AVLHLGNVAI VKESLRADQA ALGPDALRSV EKACQLLGIP
     SKPFVKGLLH PRVKAGREWV EKVQTPEQVR LALDALAKGI YERSFGNLVN RINQRLDRSA
     TTSDDSYFIG VLDIAGFEIF QNNSFEQLCI NYTNEKLQQF FNHHMFVLEQ EEYAKEQIEW
     QFIDFGKDLQ PTIDLIELTN PIGIFSCLDE DCVMPKATDK SFTEKLHSLW DRKSPKYRAS
     RLSQGFILTH YASEVEYDTN GWLEKNKDPL NDNVTRLLAA STDRHVANLF SDCGDPDDEA
     DYSKSRVKKG LFRTVAQRHK EQLSSLMSSL NSTHPHFVRC IIPNHKKRPK MFNAPLVLDQ
     LRCNGVLEGI RIARTGFPNR LSFAEFRQRY EVLCRNVSKG YLDGQSIAQM MLDKLGLDPT
     WYRVGRTKVF FRAGVLAELE EKRDELIRSI MTRFQSMARG FVQRRISNKR LYRAEATRII
     QQNFGVYLKL KANPWWRLFS RMKPLLGETR TANEVKKRDE KIQQLETKAK QDLADRQKLD
     EERRRTEIEI QKIQQTLESE RALALDKEEI FKRLQMREVE LSEKLAGAIA DQESLEDQLD
     ELIAAKKRCD EELHTRITQL EQAGEIIQRF EAEKHEMQAH LEEIDRRLLE AEQISAQKDG
     NIKELDQELK MLQSHLTLKD RKVQELEAKL LKVDQDLDIK LANTSKELDQ SKKQVKDLID
     ENRSIRQQIS DLSVTSTGYE EMLRRKESEM AVLRNDVRRH EEDKQQLETE RTSLSTRHDN
     MQKRLRELQA ETDAMRSEKA HLERELTDVK KLLDEKISED AEAVESRKLL EQQIHDLKEQ
     LFQAQADLSR ERQSRDDVQM LAEHNLTELR DKYTSLNDSK IIIEKEMYIQ QDTLRRATEA
     RLAAEQSRKE LQTELIKLRD RFTSVENARL NAEAEIERNI KNQANERLDS VRKDLDEKSR
     QVDEIEAERE RLSIRVQELT NAIAESDNFR IRHDQHKERL ERELVTLKGR LTASENDNRA
     LLTKIQQKNL DIARSNSKAS ENSRLRVTTL QREKAKLEED SKKLSRQLGD LQLTITSLEK
     QKEKLSLSLE DLNHEANRER KACRNAEKAA STANLQLAEA NRNLETERQL RTQAQANTRK
     LQTSLDTANK EIEGLHRQLM LLHKVVDPDS DRSPESWEEV QPDLSQKVDL AQLLDTTRAQ
     LQVTEEKYNR AESQLAEMRR RHGDEMRELD ARYSSSKRAL LEEIDQNQVA GNRTPTHLRK
     DSENGIAKKY NTPTTPNRRF NFNENANDSA RSDRTVDTVG YQKRMDMAAE LEELQNKLQM
     SEMQNKHLQS QIQLANPLGD MRQDESPSVR RMQLLERENG RLHDQLDDSA KKVSALERSI
     HLGDLSLRDV QAKSHEELYD LINSQEQSRR SLLKVHNEAI AEFSDMKAQL EKLKRSKATL
     EVELRDSRSE AQELQLAKDQ DAASRNQLLQ EFADLQIRLD AETSKSADLA ASQSLYKTRA
     DEYFSKLEQA EVTVLKATRA EQFAKAQAQE AEDTCARIMS ERKEMDSLVE DLQRQTQALE
     ARMEDQAAEL EGALQSKQRL QNELEDYRNQ RAIDIEDKET SMEQTRQKYQ REFSTLNNEL
     EMEREKILKV RGENSRLREE LEDLRSKWDN EVLNSSTWAK EKSRMEVMLQ DVTTSRDEAV
     NAHNEAQSRV VTLLSQVRDL RTSVDDVTAE RDMLLKEKKM LEVRLTEAGE RLEELAKGES
     PSMRNAASMN RELLELKSKL AQQEDVSAAA VGKMRRADAL VTEIQKEITA EREANAQLFK
     DKATLEKQLK ESQLRCVDLE TKSYSSGSQD VKFLHKRIKD LEAHLEEQEA KHSSEQRSLR
     NVDRTVKDLQ SQIERREKIN AQLTDDVNKA RDKIDRLLRN IEELQHNDTD TQLQVRRAER
     ELREEKEKSL RLERELQGWR ALRLERGRGH VTFSDVGSRR GSNGFSSSDI PQRMPSNTKG
     FL
//

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