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
//