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Database: UniProt
Entry: A2QN88_ASPNC
LinkDB: A2QN88_ASPNC
Original site: A2QN88_ASPNC 
ID   A2QN88_ASPNC            Unreviewed;      2406 AA.
AC   A2QN88;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 100.
DE   SubName: Full=Contig An07c0130, genomic contig {ECO:0000313|EMBL:CAK39397.1};
DE            EC=3.6.4.1 {ECO:0000313|EMBL:CAK39397.1};
GN   ORFNames=An07g04780 {ECO:0000313|EMBL:CAK39397.1};
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK39397.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK39397.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC   {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270131; CAK39397.1; -; Genomic_DNA.
DR   EnsemblFungi; CAK39397; CAK39397; An07g04780.
DR   VEuPathDB; FungiDB:An07g04780; -.
DR   HOGENOM; CLU_000192_5_1_1; -.
DR   Proteomes; UP000006706; Chromosome 4L.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; -; 1.
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; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 2.
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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000313|EMBL:CAK39397.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000006706}.
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..91
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          2264..2284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2379..2406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          942..1585
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1613..1647
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1723..1798
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1835..1876
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1954..2066
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..86
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   2406 AA;  277202 MW;  084E9C744797D25D CRC64;
     MLPSQLNGSP KRANPFSRAS PSPTPSPTQQ TRGIRPKSAV VTSPSKFEEA RGHFRNSASI
     SQSPSPLVAR TTHRPRSSSI RNDVSSGTFA PEFIKSEELR RGADQIRGQE GDNDFSGNKY
     VWLRDTEKAF VRGLVLEEQE GGRMLVQTDN GEQREVDADQ VDKVNPAKFD KADDMAELTH
     LNEASVVHNL HTRYQADLIY TYSGLFLVTV NPYCPLPIYT NEYVKMYKGR NREESRPHIF
     AMADEAFRNL VEEGENQSIL VTGESGAGKT ENTKKVIQYL AAVATTDTPY ARSGTKQLSA
     LSQQILRANP ILEAFGNAQT VRNNNSSRFG KFIRIEFTRA GQISGASIDW YLLEKSRVVK
     PNSHERNYHI FYQLLRGADR KLREALLLSD LQIEDFAYTR DGNDTIAGVS DEDEWKMLIE
     AFHVMDFSEE DQMCILRTIA AVLHLGNITI VKESLRADQA ALGPDSLNSV ERACHLLGIE
     PELFVKGLLH PKVKAGREWV EKVQTPEQVR LALDALAKGI YERGFSNLVD RINNQLDRST
     VAGDDSFFIG VLDIAGFEIF KNNSFEQLCI NYTNEKLQQF FNHHMFVLEQ EEYAREQIEW
     QFIDFGKDLQ PTIDLIELTN PIGIFSCLDE DSVMPKATDK SFTEKLHSLW DRKSPKYRAS
     RLSQGFVLTH YAAEVEYGTE GWLEKNKDPL NDNITRLLAR SGEKHVATLF SDCGDADDDS
     DYPKSRVKKG LFRTVAQRHK EQLSSLMNQL NSTHPHFVRC IIPNHKKRPK MFNAPLVLDQ
     LRCNGVLEGI RIARTGFPNR LSFSEFRQRY EVLCPAMPKG YLDGRNAAHV MLQKLGLDPA
     WYRVGRTKVF FRAGVLAELE EKRDQLIRTI MTRFQSVARG FVQRRISNKR LYRAEATRII
     QDNFKTYLQL KANPWWRLYS RMRPLLGETR TANEVKRRDE KIKSLEAKMN QDIADRQKLE
     EERRRTEIEI QKIQQTLESE RALALDKEEI FKRLQVREVE LSEKLAGAIA DQESLEDQLD
     DLIAAKKRTD DELELRITQL EQAGEIIQRF ENEKHEMQAR LEELEKKLAE AESSSLEKEA
     KIKELGQELK MLQSHLSLKE RKLQDLETKL LKTDQDLEVK LSKTSRDLEE SKKHIKELIE
     ENRVIRQQIT DLSSTSTGYE EMLRRKESEM AVLRNDAKKH EEEKRYLESE KVSLTTRHDS
     MQERLRELQA EVDAMRSEKV QLEREAADVK KLLEAKISED AEAGESRKLL EQQIQELKNQ
     LFKAQADLSR ERQSRDDVQM LAEHNLAELK DKYTSLNESK IIIEKEMYIQ QDTLRRATEA
     RVAAEQSRKE LQTELIQLRD RFTKVEDARL NAEADIERNI MKQANERLES VRKDLDDKTR
     QLEEVEAERS RLSTRIQELT HAIAESDNFR IRHDQHKERL ERELVTLKGR LTASENDNRA
     LLTKIQQKNL DIARSTSRAS DNSRLRITAL QKEKTKLEED NKKITRQLGD LQVNITSLEK
     QKEKLSLSLE DLNHEVAREH KASRNAEKAA STANIQLAEA NRNLETERQL RTQAQANTRK
     LQGSLDTANK EIEDLHRQLM LLHKVVEPES DESESWEKVQ PSLAKKVDLA QLLQTTQSRL
     QVTEEKYSRA EAQLAEMRRR HGDEMKELDA RYASSKRALL EEIDQNQVAS PRTPTHLRKN
     SDNVLAKKFG TPTTPNRRLN FNETANDSAR SDRTVDTVGY QKRMDLAAEI EELQNKLQMS
     EMQNKHLQNQ LSQAAPGRDM WQEESPSLRR MQLLERENGR LHEQLDDSSK KVSALEKNIR
     SGDLSLRDVQ AKSHEELYDL INSQEQSRRS LLKVHNEAIA EFSDAKAQFE KLKRAKATLE
     VELRDARSEF QELQVARDQD AVSRNQLLQE FSDLQIRLDA ETSKSADLAS SMSLYKTRAD
     EYFSKLEQAE IAVLKATRAE QFAKSQAQEA EDTCAQIMSE RKQMDALVED LQRQTQSLEA
     RMEDQAAELQ GALQAKQRLQ NELEDYRNQR AIDIEDKETS MEQTRQKYQR EFTTLNNELE
     MEREKVLNVR GENSRLREEL EDLRSKWDNE VLNSSTWAKE KARMDIMLQD VTTSRDEAVN
     AHNEAQSRVV SLLSQVRTLR TSVDDVTAER DMLLKEKKML ETRLAEAGER LEDLAKGESP
     SMRNAASMDR ELLELKSKLA QQEDVSAAAV GKMRRAEALA TEMQKEVTAE RETNAQLFKD
     KAALEKQLKE SQLRCVDLET KSYSSGSQDV RFLHKRIKEL ETHLEDQEAK HSSEQRSLRN
     VDRTVKDLQS QIERRDKMNS QLNDDVSKAR DKIERLLRNI EELQHTDSET QLQVRRAERE
     LREEREKSLR LERELEGWRA LRVERGSVLG RSHVGAFSDA GSRRGSSVYG GDIPQRMPSN
     TKGFLA
//
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