ID A0A317WKW2_9EURO Unreviewed; 1572 AA.
AC A0A317WKW2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Class V myosin {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO94DRAFT_467586 {ECO:0000313|EMBL:PWY85658.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY85658.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY85658.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY85658.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWY85658.1}.
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DR EMBL; MSFK01000016; PWY85658.1; -; Genomic_DNA.
DR STRING; 1450535.A0A317WKW2; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
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; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 3.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT DOMAIN 6..59
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..780
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1232..1501
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1081..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 915..1078
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1082..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1572 AA; 179448 MW; 85A1CCB277D88811 CRC64;
MVHNYEVGTR AWQPDPTEGW VASEVKEKLV EGDKVQLVFL MENGETKTLE TTQAELQVDN
NPKLPPLMNP AMLEASEDLT SLSHLNEPAV LQAIKLRYAQ KEIYTYSGIV LIATNPFARV
DSLYVPQMVQ VYAGKHRASQ APHLFAIAEE AFADMLRDGK NQTIVVSGES GAGKTVSAKY
IMRYFATRES SDQPGKYTTS RADAISETEE QILATNPVME AFGNAKTTRN DNSSRFGKYI
EIMFDDRTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGATESER QELGLASIED
FDYLNQGGTP TIDGVDDRAE FNATKKSLGT IGVPEKTQAE IFRVLAALLH LGNVRITATR
TDSSLSPSEP SLVQACEMLG IDANEFAKWI VKKQLITRGE KITSNLTQQQ ATVVRDSVAK
FIYSSLFDWL VDKINRGLAT DSVLSKFKSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
QEFNQHVFKL EQEEYVREQI DWTFIDFSDN QPCIDLIEAK LGILSLLDEE SRLPMGSDEQ
FVTKLHHNFA ADKQKFYKKP RFGKSAFTIC HYAVDVTYES DGFIEKNRDT VPDEHMEILR
GSSNDFVKEI LDTAAAVREK DSASISSKPV AAPGRKIGVA VNRKPTLGGI FKSSLIELMN
TINSTDVHYI RCIKPNEAKE SWKFEGPMVL SQLRACGVLE TVRISTAGYP TRWTYEEFAI
RYYMLCHSSQ WTSEIRNMCH AILQKALGDG TQQKQDKYQL GLTKIFFRAG MLAFLENLRT
SRLNECAVMI QKNLRCKYYR RRYLEARASI LTTQALVRGF LARQRAAEIR QVKAATTIQR
VWRGQKERRK YNRIRANFVL FQSVAKGFLC RQSILDTIHG NAAIVIQRSF RSWRQLRAWR
QYRRKVIIVQ SLWRGKEARK EYKKLREDAR DLKQISYKLE NKVVELTQYL ESLKRENKSL
NSQLENYETQ LKSWRSRHNV LENRSKELQA EANQAGITAA RLTAMEEEMN RLQQNHNDAQ
ATIKRLQEEE KVSRESIRSA NQELERLQQL NTEAENEKAS LRQQIVDLEE QLELAKRVVP
ANGTNGDQQN GGPIQPPASG LINLVSSKKP KPKRRSAGAE RIDIDRFSAA YNPRPVSMAI
PSSAMGRQHF SGNAFAPGLD SVEVELENLL SEEDELNEEV TMGLIRNLKI PLPSSTPPPT
EKEVLFPAYL INLVTSEMWN NGFVKESERF LANVMQSIQQ EVMQHDGDDA INPGAFWLSN
VHEMLSFVFL AEDWYEAQKT DNFEYDRLLE IVKHDLESLE FNIYHTWMKV LKKKLYKMIV
PAIIESQSLP GFVTSETNRF LGKLLPSNNN PAYSMDNLLS LLNNVYKAMK AFYLEESIIT
QTVTELLRLV GVTAFNDLLM RRNFLSWKRG LQINYNITRI EEWCKSHDMP EGTLQLEHLM
QATKLLQLKK ATLNDIEIIQ DICWMLSPNQ IQKLLNQYLV ADYEQPINGE IMKAVASRVT
EKSDVLLLTP VDMEDSGPYE IAEPRVITAL ETYTPSWLQT PRLKRLAEIV SAQAMAQQER
LEINEGGATP MN
//
