ID A0A0N0DER9_FUSLA Unreviewed; 1212 AA.
AC A0A0N0DER9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=FLAG1_05605 {ECO:0000313|EMBL:KPA41514.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA41514.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA41514.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA41514.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) 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}.
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:KPA41514.1}.
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DR EMBL; JXCE01000094; KPA41514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0DER9; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000037904; 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:UP000037904};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 38..712
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 770..959
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1067..1128
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..607
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 949..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1068
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1212 AA; 133866 MW; 865DB7103FDC3EE3 CRC64;
MGISRRPKNK GAGAAADGAS GGAKPKKATF ETTKKKEIGV SDLTLLSKVS NEAINENLKK
RFEGREIYTY IGHVLVSVNP FRDLGIYTDE VLQSYMGKNR LEMPPHVFAI AEAAYYNMKA
YSDNQCVIIS GESGAGKTEA AKRIMQYIAS VSGGESGDIK QIKDMVLATN PLLESFGNAK
TLRNNNSSRF GKYLQIYFNT QGEPVGADIT NYLLEKSRVV GQITNERNFH IFYQFAKGAS
QQYRETFGVQ KPETYVYTSR SKCLDVDGID DLAEFEDTLN AMKVIGLSQP EQDQIFRMLS
AILWIGNIQF QEDQGGYAEV TDRSVVDFAA YLMEVTPDQL IKGITIRILT PRNGEVIESP
ANPAQAQATR DALAMAIYSN LFDWIVERIN KSLKARQPTT NTIGILDIYG FEIFEKNSFE
QLCINYVNEK LQQIFIQLTL KAEQEEYARE QIQWTPIKYF DNKVVCDLIE QIRPVGIFSA
MKDATKTAHA DPAACDRTFM QSINGMSHAH LTPRQGNFII KHYAGDVTYT VEGITDKNKD
QLLKGLLALF QHSGNDFVHT LFPRPVDTDN RKQPPSAGDR IRASANALVD TLMKCQPSYI
RTIKPNENKS PTEYNGPNVL HQIKYLGLQE NVRIRRAGFA YRQDFDKFVD RFFLLSPATS
YAGEFTWEGT TEAAVKQILK DTSIPKEEWQ MGVTKAFIKA PETLFALEHM RDRYWHNMAT
RIQRMWRAYL AYRAESATRI QRFWRKKRTG AEYLQLRDHG HQVLGGRKER RRMSLLGSRR
FLGDYLGINA STGPGAQIRN AAGIGSNEKA VFSCRGEILE AKFGRSSKAS PRIIVISNSK
FYIIAQMLVN GQPQISVEKS VPLGAIKFIG VSSARDDWFS LGIGSPQEAD PLMNCIFKTE
MFTQMQRVMP GGFNLKIAET IEYAKKPGKL QQVKVLKDSQ VSADYYKSGA VHTQPGEPPS
SVSKPTPKGK PVPPRPITRG KLIKPGGPNG RPSRIQGNRA AKPRPGGGAR AVPQPPAAVS
AAASIPAAAP APTAHNALPS HAKAASAAGR APPPPPPPAA PARPPSPPKV MAKVLYDFAG
QRENELSIAA GQIVEIVQKE SNGWWLAKNP QTAQQAWVPA AYVEEQAPPA PRAPPAPPRS
KPTPPAPPAK RPAAGRKPAE LQQRDSGMSL NTPNGSDSRS STPTPSLGGS LADALLARKN
AMQKEKEDDD DW
//
