ID A0A3S4BER3_9PEZI Unreviewed; 1169 AA.
AC A0A3S4BER3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=TT172_LOCUS419 {ECO:0000313|EMBL:SPQ18000.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ18000.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ18000.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) 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; OUUZ01000001; SPQ18000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4BER3; -.
DR Proteomes; UP000289323; 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 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; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 42..716
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 774..964
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1017..1077
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..37
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 951..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1169 AA; 129888 MW; 2C7349C9DE8456E3 CRC64;
MGITRRAKDK AARADRSAAG TGQAGPSKPK KATFDTTKKK EIGVSDLTLL RTVSNEAINE
NLKKRFEGGE IYTYIGHVLV SVNPFRDLGI YTEQVLNSYR GKNRLEMPPH VFAIAESAYY
NMKAYKDNQC VIISGESGAG KTEAAKRIMQ YIANVSGGET GDIQQIKDMV LATNPLLESF
GNAKTLRNNN SSRFGKYLQI HFNAQGEPVG ADITNYLLEK SRVVGQITNE RNFHIFYQFT
KGASQHYREI FGVQKPETYI YTSRSKCFNV DGIDDLADFQ DTLNAMKVIG LSQAEQDSIF
RMLAAILWTG NLVFREDDSG YAAVSDQSVV DFLAYLLEVD PARLVHAITI RILTPRNGEV
IESPANVAQA MATRDALAKA IYNNLFDWIV ERINQSLRAR QATANSIGIL DIYGFEIFEK
NSFEQLCINY VNEKLQQIFI QLTLKAEQEE YAREQIKWTP ISYFDNKIVC DLIESIRPPG
IFSAMKDATK TAHADPAACD RTFMQSINGM SNPHLTPRQG SFIVKHYAGD VTYTVDGITD
KNKDQLLKGL LNLFQISQNR FIHTLFPDQV DQDNRKQPPS AGDRIRASAN ALVDTLMKCQ
PSYIRTIKPN ENKSPSEYNV PNVLHQIKYL GLQENVRIRR AGFAYRQSFE KFVDRFFLLS
PATSYAGEYT WQGSYEAAVK QILKDTSIPQ EEWQLGVTKA FIKSPETLFA LEHMRDRYWH
NMATRIQRMW RAYLAYRAEA ATRIQRFWRK KRVGAEYLQL REEGHRVLQG RKERRRMSLL
GSRRFLGDYL GINASTGPGA QVRNAIQLGS NEKAVFSCRG EILEAKFGRS SKPSPRILIV
TNSKYYIVAQ VLGQNHQVQI VVERALPLGA IKFIGTSTCR DDWFSLGVGS QQEADPLLNC
VLKTEMFTQM KRVMPGGFNL KIGDTIEYAK KPGKMQVVKV LKDAPTPHDF YKSGAVHTQQ
GEPANSVSRP TPKGKPVPPR PITRAPAVSS HIYIGCCNRV VTARPSTPCG GGGGGGGGIG
HHSLTHSTAI QLRDNELSIK AGELIEIVQK ENNGWWLAKN AAGQAWVPAA YVEEQEAAPV
VAPRPPPPPP AANGAVAKAK PAAPQPPAKR PAAGKKPAAL QARDSGMSLN GSDSSRSNTP
TPSLAGSLAD ALLARKNAMA KKDDDDDEW
//
