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Database: UniProt
Entry: A0A1W2TBT3_ROSNE
LinkDB: A0A1W2TBT3_ROSNE
Original site: A0A1W2TBT3_ROSNE 
ID   A0A1W2TBT3_ROSNE        Unreviewed;      1212 AA.
AC   A0A1W2TBT3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Myosin-1 {ECO:0000256|ARBA:ARBA00016187};
DE   AltName: Full=Class I unconventional myosin {ECO:0000256|ARBA:ARBA00032645};
DE   AltName: Full=Type I myosin {ECO:0000256|ARBA:ARBA00029665};
GN   ORFNames=SAMD00023353_1001070 {ECO:0000313|EMBL:GAP85408.1};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP85408.1};
RN   [1] {ECO:0000313|EMBL:GAP85408.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP85408.1};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; DF977455; GAP85408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TBT3; -.
DR   STRING; 77044.A0A1W2TBT3; -.
DR   OMA; GCHEHFN; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000054516; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
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   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; PF00018; SH3_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00326; SH3; 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:UP000054516};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          36..710
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          768..957
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1065..1124
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..605
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          947..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1128..1193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..972
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1026
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1051
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1067
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1144
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         129..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1212 AA;  134122 MW;  788810B60D5A40A3 CRC64;
     MGISRRPKDK AGGGGSQVGA AKPKKATFET TKKKEIGVSD LTLLSKVSNE AINENLKKRF
     EGREIYTYIG HVLVSVNPFR DLGIYTDEVL DSYKGKNRLE MPPHVFAIAE ASYYNMKAYK
     ENQCVIISGE SGAGKTEAAK RIMQYIANVS GGESGEIKQI KDMVLATNPL LESFGNAKTL
     RNNNSSRFGK YLQIHFNANG EPVGADITNY LLEKTRVVGQ IANERNFHIF YQFAKGASQD
     YRTRFGVQKP ETYAYLSRSK CFDVDGIDDL AEYRDTLDAM KIIGLSQAEQ DEVFRMLAAI
     LWAGNIQFIE GDDGYAAVAD QSVVDFLAYL LEVSPAALIK GISIRVLTPR NGEVIESPAN
     MAQANATRDA LSMAIYNNLF DWIVGRINQS LQARQATSNN IGILDIYGFE IFEKNSFEQL
     CINYVNEKLQ QIFIQLTLKA EQDEYAREQI QWTPIKYFDN KVVCDLIEQI RPVGIFSALK
     DATKTAHADP AACDRTFMQS INGMSNAHLT PRQGNFIIKH YAGEVSYTVD GITDKNKDQL
     LKGVQNLFQQ SSNRFVHTLF PQQVDQDNRK QPPTAGDRIR SSANALVETL MKCQPSYIRT
     IKPNENKSPT EYNVPNVLHQ IKYLGLQENV RIRRAGFAYR QSYEKFVERF FLLSPATSYA
     GEYTWQGSEE AAVKQILKDT SIPKEEWQLG VTKAFIKSPE TLFALETMRD RYWHNMAIRI
     QRMWRAYLAY RAESATRIQR FWRKKRVGAE YLQLRDQGHT VLQGRKERRR FSLLGSRRFL
     GDYLGVGAST GPGSQVHNAV GIASNEKTLF SCRGEVLEAK FGRSSKPSPR IFIVTNSKFY
     IVAQALVGGQ PQISIERAMT LGSIKFIGTS FCRDDWFSLG VGSPQEADPL LNCVLKTELF
     TQMQRAMPGG FNLKVGETIE YAKKPGKMQV VKVLKDSPQT VDFYKSGAIH TQPGEPPSSV
     SRPMPRANPV PPRPIARGKL IKPGGPGGRP SRLTGARSNA GRSSSAVVPA PRPVPVPTPA
     AAAHTPRPVP TPAAAFANSI PSHTRNKSST SSARPPPPPP PSPPKPKIMA RVLYDFASQR
     ENELSIRAGD IIEVVQKENN GWWLAKSGAG QAWVPAAYVE EQAPASSAIV PRAPPPPPGV
     NGAGRNKPIP PAKRPATARK PGSLQARDSG MSMNGNGSDG SRSNTPTIAG SLADALLARK
     NAMQRKDDED DW
//
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