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Database: UniProt
Entry: A0A2I2GFZ7_9EURO
LinkDB: A0A2I2GFZ7_9EURO
Original site: A0A2I2GFZ7_9EURO 
ID   A0A2I2GFZ7_9EURO        Unreviewed;      1571 AA.
AC   A0A2I2GFZ7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Myosin class V heavy chain {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P170DRAFT_433649 {ECO:0000313|EMBL:PLB51780.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB51780.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB51780.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB51780.1,
RC   ECO:0000313|Proteomes:UP000234275};
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:PLB51780.1}.
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DR   EMBL; MSFO01000002; PLB51780.1; -; Genomic_DNA.
DR   STRING; 1392250.A0A2I2GFZ7; -.
DR   VEuPathDB; FungiDB:P170DRAFT_433649; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000234275; 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   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:UP000234275}.
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          1231..1500
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   COILED          915..1078
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1571 AA;  179551 MW;  1EB868F1E02413B1 CRC64;
     MAHNYEVGTR AWQPDPTEGW IASEVKEKSV DGDKVQLVFL MENGESKTVE TTQAELQLDN
     NSRLPPLMNP AMLEASEDLT NLSHLNEPAV LQAIKLRYAQ KEIYTYSGIV LIATNPFARV
     DSLYVPQMVQ VYAGKHRASQ APHLFAIAEE AFADMLRDGK NQTIVVSGES GAGKTVSAKY
     IMRYFATRES SDQPGKYTTS RAEAISETEE QILATNPVME AFGNAKTTRN DNSSRFGKYI
     EIMFDDRTNI IGAKIRTYLL ERSRLVFQPL KERNYHVFYQ LVAGATDDEK QELGLGSVED
     FDYLNQGGTP TIDGVDDKTE FNATRKSLST IGVSDKTQSE IFRILAALLH LGNVKITATR
     TDSTLSPSEP GLVKACDLFG IDANEFAKWI VKKQLITRGE KITSNLTQQQ ATVVRDSVAK
     FIYSSLFDWL VDKINRGLAT DQVMSQFKAF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
     QEFNQHVFKL EQEEYVREQI DWTFIDFSDN QPCIDLIEAK LGILSLLDEE SRLPMGSDEQ
     FVTKLHHNFA ADKQKFYKKP RFGKSAFTIC HYAVDVTYES DGFIEKNRDT VPDEHMEILR
     NSSNEFVKEI LDTAAAVREK DSASISSKPV AAPGRKIGVA VNRKPTLGGI FKSSLIELMN
     TINSTDVHYI RCIKPNEAKE AWKFEGPMVL SQLRACGVLE TVRISTAGYP TRWTYEEFAI
     RYYMLCHSSQ WTSEIREMCH AILQKALGDG SHKKQDKYQL GLTKIFFRAG MLAFLENLRT
     SRLNECAIMI QKNLRCKYYR RRYLEARASI LTTQALIRGF LARQHAAEVR QVKAATTIQR
     VWRGQKERKR YNRIRENFVL FQSVAKGFLC RRNIMDTIHG NAAKVIQRSF RSWRQLRAWR
     QYRRNVVIIQ SLWRGREART EYKRLREDAR DLKQISYKLE NKVVELTQYL ESLKRENRSL
     NSQLENYETQ VKSWRSRHNA LENRTRELQA EANQAGITAA RLTAMEEEMS LLRQNHHEAQ
     ATIKRLQEEE KVSRESILAA NQELEGLRHL NNEAESEKVS LRQQVADLEE QLELAKRTMP
     VNGLNGEQQN GGSVQPPASG LINLVSSKKP KPKRRSAGAE KIETDRFSGA YNPRPVSMAI
     PSTLARQNFS NTTFSPGLDS VEVELENLLS EEDELNEEVT MGLIRNLKIP LPSSTPPPTE
     KEVLFPAYLI NLVTSEMWNN GFVKESERFL ANVMQSIQQE VMQHDGDDAV NPGAFWLSNV
     HEMLSFVFLA EDWYEAQKTD NYEYDRLLEI VKHDLESLEF NIYHTWMKVL KKKLFKMIVP
     AIIESQSLPG FVTSETNRFL GKLLPSNNNP AYSMDNLLSL LNNVYKAMKA FYLEDSIIIQ
     TVTELLRLVG VTAFNDLLMR RNFLSWKRGL QINYNITRIE EWCKSHDMPE GTLQLEHLMQ
     ATKLLQLKKA TLNDIEIIQD ICWMLSPNQI QKLLNQYLVA DYEQPINGEI MKAVASRVTE
     KSDVLLLTPV DMEDSGPYEI ADPRVITALE TYTPSWLQTP RLKRLAEIVS AQAMAQQERL
     EMAENGSMAA E
//
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