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Database: UniProt
Entry: A0A2V1E070_9PLEO
LinkDB: A0A2V1E070_9PLEO
Original site: A0A2V1E070_9PLEO 
ID   A0A2V1E070_9PLEO        Unreviewed;      1209 AA.
AC   A0A2V1E070;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=DM02DRAFT_587214 {ECO:0000313|EMBL:PVI03676.1};
OS   Periconia macrospinosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX   NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI03676.1, ECO:0000313|Proteomes:UP000244855};
RN   [1] {ECO:0000313|EMBL:PVI03676.1, ECO:0000313|Proteomes:UP000244855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE2036 {ECO:0000313|EMBL:PVI03676.1,
RC   ECO:0000313|Proteomes:UP000244855};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
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; KZ805328; PVI03676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1E070; -.
DR   STRING; 97972.A0A2V1E070; -.
DR   Proteomes; UP000244855; 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:UP000244855};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          37..716
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          774..963
FT                   /note="TH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51757"
FT   DOMAIN          1058..1119
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..611
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          929..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1024..1040
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1059
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         130..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1209 AA;  133278 MW;  C06CD5322D82ACED CRC64;
     MKAVSKRAGR KKEGGGGAPK QQFAKKAVFE STKKKEVGVS DLTLISKISN EAINENLKKR
     FENAEIYTYI GHVLVSVNPF RDLGIYTDQV LESYKGKNRL EMPPHVFAIA ESAYYNMNAY
     KDNQCVIISG ESGAGKTEAA KRIMQYIANV SGGSNTSIQE IKDMVLATNP LLESFGNAKT
     LRNNNSSRFG KYLEIQFNAQ GEPVGANINN YLLEKSRVVG QITNERNFHI FYQFAKAASE
     SHRQTFGIQQ PQSYVYTSRS KCYDVPGIDD HAEFKDTLNA MKVIGLSQAE QDNIFRMLAA
     ILWLGNVSFQ EDDSGNAAIV DQSVVDFVAY LLEVESAHVN KALSTRVMET SRGGRRGSVY
     DVPLNPAQAM AVRDALAKGI YFNLFDWIVQ RVNVSLQARG AMSHSIGILD IYGFEIFEKN
     SFEQLCINYV NEKLQQIFIQ LTLKAEQEEY AREQIKWTPI KYFDNKVVCE LIEEKRPPGV
     FSFLNDACAI ANADPAAADQ TFAQRLGALS TNPNFEPRQG RFVIKHYAGD VAYAVDGMTD
     KNKDQLLKDL LLLLGNSSNS FVHTLFPDQV NTDDRRRPPT AGDKIKASAN DLVSTLMKAQ
     PSYIRTIKPN ENKSPSEFNE PNVLHQIKYL GLQENVRIRR AGFASRQTFE KFVERFFLLS
     PKTGYAGEYT WSGDYQSGAK QILRDTNIPA EEFQMGTTKV FIKTPETLFA LETMRDRYWH
     NMAIRIQRAW RNYLRYRAEC ATRIQRFWRR VNGGMEFIQV RDEGHKILGG QKERRRFSLI
     GSRRFMGDYL GIGNKGGPGE VIANAIGISG EEVVFSSRAE VLVSKLGRSS KPEARQLALT
     KKNVYLIKQV LANRQIQIQA ERTIPVGAIK YISCSKLKDD WFSIGVGSPQ EPDPLVSCVF
     KTEFFTHLKH VLRGSLNLKI GDTIEYNKKP GKPAQIKTMK DPAVPRDDTY KSGTIHTGPG
     EPPNSVSKPT PKGKQVAAKP ITKGKLLRPG GPGGGPSKLA SRPAQSRPTP AAVPQPKPVP
     QPVAALSNGS SHARSSSASS NRAPPPPPPA PPAAPPAPKE PTYRAMYDFA GQSAGELSIK
     KDEIILVTQK EGNGWWLAQR LDKSASGWAP SAYLEEFVSK PAPPPAPPRP AAGSNGVRGK
     PAPPAPPAKR PAAKNRPPVG GAARDSGYSG SNSDAGARDS GGSIAGGLAE ALRQRQAAMQ
     GKKADDDDW
//
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