ID A0A165JDK9_XYLHT Unreviewed; 1263 AA.
AC A0A165JDK9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=L228DRAFT_242504 {ECO:0000313|EMBL:KZF26098.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF26098.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF26098.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF26098.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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; KV407454; KZF26098.1; -; Genomic_DNA.
DR RefSeq; XP_018191653.1; XM_018331448.1.
DR AlphaFoldDB; A0A165JDK9; -.
DR STRING; 1328760.A0A165JDK9; -.
DR GeneID; 28896585; -.
DR InParanoid; A0A165JDK9; -.
DR OMA; MAFHWQS; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000076632; 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:UP000076632};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 43..722
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 780..970
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1091..1152
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..617
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 951..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1092
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1263 AA; 139405 MW; B9EC25D36504F527 CRC64;
MAVTKRAGRK KDAVPAKAAK GAAAGGKPQV KKAAFETSKK KEVGVSDLTL ISKISNEAIN
DNLKKRFENA EIYTYIGHVL VSVNPFRDLG IYTDQVLNSY RGKNRLEMAP HVFAVAESSY
YNMNAYNENQ CVIISGESGA GKTEAAKRIM QYIASVSGGH NSNIQKVKDM VLATNPLLES
FGNAKTLRNN NSSRFGKYLE LQFNAQGEPV GANITNYLLE KSRVVGQITN ERNFHIFYQF
TKSAPQKYRE LFGLQSPESY YYTSQSKCYD VNGIDDHAEF RDTLNAMNVI GLPQAEQDDI
FRMLAAILWL GNIQFVEDDN GNAAIADHSV VDFVAYLLEV DAAHVLKALS IRVMETSRGG
RRGSVYDVPL NPAQAAAVRD ALSKAIYYNL FDWIVDRVNA SLKARGALAH SIGILDIYGF
EIFERNSFEQ LCINYVNEKL QQIFIQLTLK TEQEEYAREQ IQWTPIKYFD NKVVCELIEE
KRPPGVFAAL NDACATAHAD PGAADNTFMQ RLNMLSSNPH FQNRQGQFIV KHYAGDVTYA
VPGMTDKNKD ALLKDLLILM GHSGNSFVHA LFPHQVDTDN KRRPPTAGDK IKASANDLVA
TLSKASPSYI RTIKPNDNKS PTEYNSANVL HQIKYLGLQE NVRIRRAGFA YRQTFEKFVE
RFYLLSPKTS YAGDYIWTGD ALSGTKQILK DTSIPTEEYQ MGVTKAFIKT PETLFALEHM
RDRYWHNMAI RIQRAWRNYL RYRIECAIRI QRFWRKMTGG REFIEWRDYG NKILQGRKER
RRYSLVGSRR FMGDYLGVGN KGGPGEVIRD SIRLGSSERV LFSCRCEILV SKLGRSSKPS
PRILILTNKS VYIVIQSMVN HQLSIHAERT IPLASIKFVG TSTLKDDWFS LGVGSPQEPD
PLISCVFKTE FFTHLKMATP GGLNLKIADV IEYNKKPGKL AVIKTMKDPA IPRDDMYKSG
TIHTSQGEPP SSVSKPTPKG KAIPGKPITS GKLLRPGGPG GGPSKLASRP AAARPVPQPR
AVPQSRPVPQ PVPQPVPQQA PQPTIAQPRP VPQPVAALSA ANHARSASAS STSSGRTPPP
PPPAPPSAPA TPEPTYRVLY DFSGQSENEL SIVKNDLLII VRKENSGWWL AKSSDGSRQG
WAPSAYLQEE TPRPTPPPPP PVAPASTRTP PNGVAANGAA RPPVKAKPAP PAPPAKRPAT
RKPAPPLAPR DSGTNLAEPN GNTSGRNTPN SSSNVSLAGG LAEALRQRQA SMQGKKADDD
DEW
//
