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Database: UniProt
Entry: A0A2H3EA95_ARMGA
LinkDB: A0A2H3EA95_ARMGA
Original site: A0A2H3EA95_ARMGA 
ID   A0A2H3EA95_ARMGA        Unreviewed;      1896 AA.
AC   A0A2H3EA95;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Microfilament motor {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ARMGADRAFT_1042871 {ECO:0000313|EMBL:PBL00633.1};
OS   Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47427 {ECO:0000313|EMBL:PBL00633.1, ECO:0000313|Proteomes:UP000217790};
RN   [1] {ECO:0000313|Proteomes:UP000217790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
CC   -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC       cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC       the cell cortex, assembles in patch-like structures together with
CC       proteins from the actin-polymerizing machinery and promotes actin
CC       assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC       Arp2/3 complex. {ECO:0000256|ARBA:ARBA00025586}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000256|ARBA:ARBA00004134}.
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; KZ293646; PBL00633.1; -; Genomic_DNA.
DR   STRING; 47427.A0A2H3EA95; -.
DR   InParanoid; A0A2H3EA95; -.
DR   OMA; ACGYKPC; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000217790; Unassembled WGS sequence.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
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:0051179; P:localization; IEA:UniProt.
DR   CDD; cd01378; MYSc_Myo1; 1.
DR   CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035535; Fungal_myosin-I_SH3.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR010926; Myosin_TH1.
DR   InterPro; IPR036072; MYSc_Myo1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR024660; UCS_central_dom.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF06017; Myosin_TH1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF11701; UNC45-central; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51757; TH1; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217790};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          652..1331
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1389..1578
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1679..1737
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          304..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1179..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1204..1226
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1567..1681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1737..1878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1656..1681
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1738..1759
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1794..1819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1861
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         745..752
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1896 AA;  207326 MW;  F19075C2441BB3FF CRC64;
     MTSQDKDALG SLDTMLKKTA SSTSTDPLLP DELTYLISAF LPSRPTDDRS KAFLVLSAFC
     QDKGQQMEAA AESLAKVFFP LMLPHLEETV EKDLLIGISF LTSLFQVDWQ SASFIFQQDG
     VLELIMDSVD LNPSAELSLH VAHLLSQACG YKPCRTIFPP QTTKWLEFMS GPSQSTPVRA
     AATIALIKLS RGSASDNADV ARENNTHIHK KDDELAAAMK NMVISGGDHS SIPDSVEGLA
     YLSIDPVVKE ILSQDSDFLK ALLASVPRRR RDYTAETQSS LVYGVVLIIS NLCAYRPHLT
     EEQSQMEKLR RMGKANSQSS GDSPLNDDEK VKGRIRKLMA NGVLDVFPAA LAGSDSQGVR
     LGIGKALLSI VTDKENRGHV LRAGGAKVLL KIIKFSVSLA TSTSQTAALD PAYLESIQAL
     SKLAITASPV QVFGPNDGAI YDIIRPFSLA LQHSSSLLLQ KFEILMALTN LSSHSAEVAS
     RIADSEGLLN RVELLLLEDH VLIRRASMEL ICNLIAGSEK VFERYGGSAS GNSGVKSKVQ
     VLLALSDVED IPTRLAASGA LATVTTELGA CQALLDLQRE RHRAVPILAQ LIDPSTDPEA
     VDSAENHPGL LHRGVAPSKK AGKKVTPAPK KGGGTGKVAK ADWKEGFKKK QVGVSDMTLL
     TTISNESINE NLQKRWTNAE IYTYIGAVLI SVNPFRDLGI YSEDTLQKYK GKNRLEVPPH
     VFGIAESAYY NMNAYHENQC VIISGESGAG KTEAAKRIMQ YIAAVSGGQD SSIQEIKDMV
     LATNPLLESF GCAKTLRNNN SSRHGKYLEI MFNAHGEPIG AQITNYLLEK GRVVGQVENE
     RNFHIFYQFT KAATDEQREA FGLQGPEAYA YTSLSNCLEV QDINDAHDYS ETIKAMDIIG
     LDANEQNEIF RMLAIILWLG NVQFEEKDDG NSQIADTSVT DFVAYLMDVD ASSVVKVLTS
     KIVETQRGGR RGSVYDVPLN PAQASSGRDA LAKAIYNNLF EWIVSRVNVS MKPRSATSQV
     IGILDIFGFE IFEDNSFEQL CINYVNEKLQ QIFIELTLKT EQEEYVREQI KWTPIKYFNN
     KIVCDLIEER RPPGIFAALN DACATAHADP AAADNSFVQR TSMLSSNPHF EARGSQFLVR
     HYAGDVMYNV SGMTDKNKDS LVKDLLDLVA SSTNQFLQTL FPDRPDPNSK KRPPTAGDRI
     KASAGALVDN LMKAKPSYIR TIKPNQNRSS SEYDIKAILH QIKYLGLQEN IRVRRAGFAY
     RNTFEKMVER FYLLSPNTSY AGEYTWQGDS KSGCEQILKD TGIAKDEWQM GVTKAFIKNP
     ETLFALETMR DKYWHNMAAR IQRAFRNYMR YKHECARRIQ RFWKNNKEAL VYAQVRDYGH
     QILGGRKERR RFSLLSYRRF MGDYLGINGK NDLGLEVAAP CNIGNDEVTF SGRIHLLVSK
     FLQSSKPSPR FIVVTQKAVH IVIVQKKEGQ TQQMLERKIP LVTIKSIAMS NLRDDWMCLN
     VNASEEGDPV FSCYFKTELA ANLMQLTHGS ITLNIGPTID YAKKKEKRAQ ITVARDETIK
     KDDVYKSHTI RVPSGEPAGS LSRPPAKRKA GVVRPITQGK LLKAGGPSKP SGNRPKPTVR
     ALPGKVASPV SVATSTPTPK PKPKPAPSSV TSSNGSRPPP APPRNVAPPP PPPPPPAAPA
     VPMYRAKFAF DGQEGEMSLK KDDLVELVEK DDNGWWLVKK DGVEGWAPYN YLEIEAPKAA
     PAPPPPPRAR APPSAPAAKQ APVPATKASL HSVTANASAK PVPVFPGMAA SNGSATPWKK
     QVSTSSSTPD DSPGNSRPSS ALAGRAPPPL AAKPKPPVVA AKPAPKIPGK PPIPTASRPN
     VGAPPPVRSG GISQAPGGQL DLAAALAKRA QRMNED
//
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