MYO1_CHAGB
ID MYO1_CHAGB Reviewed; 1214 AA.
AC Q2HDI2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=CHGG_01722;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}.
CC -!- DOMAIN: The myosin motor domain displays actin-stimulated ATPase
CC activity and generates a mechanochemical force. {ECO:0000250}.
CC -!- DOMAIN: The tail domain participates in molecular interactions that
CC specify the role of the motor domain (By similarity). It is composed of
CC several tail homology (TH) domains, namely a putative phospholipid-
CC binding myosin tail domain (also named TH1), an Ala- and Pro-rich
CC domain (TH2), followed by an SH3 domain and a C-terminal acidic domain
CC (TH3). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; CH408029; EAQ93487.1; -; Genomic_DNA.
DR RefSeq; XP_001220943.1; XM_001220942.1.
DR AlphaFoldDB; Q2HDI2; -.
DR SMR; Q2HDI2; -.
DR STRING; 38033.XP_001220943.1; -.
DR PRIDE; Q2HDI2; -.
DR EnsemblFungi; EAQ93487; EAQ93487; CHGG_01722.
DR GeneID; 4386911; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q2HDI2; -.
DR OMA; MESKWGT; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000001056; 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-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 3.40.850.10; -; 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 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 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; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..1214
FT /note="Myosin-1"
FT /id="PRO_0000338546"
FT DOMAIN 40..715
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 719..739
FT /note="IQ 1"
FT DOMAIN 740..765
FT /note="IQ 2"
FT DOMAIN 773..963
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1065..1124
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..487
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 948..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1196
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 1004..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1214 AA; 134575 MW; 4C3E10714F9B33FF CRC64;
MGITRRAKDK AARAERSGGG GGGSSKPKKA TFDTTKKKEI GVSDLTLLRT VSNEAINENL
KKRFEGAEIY TYIGHVLVSV NPFRDLGIYT DQVLDSYRGK NRLEMPPHVF AIAESAYYNM
KAYKENQCVI ISGESGAGKT EAAKRIMQYI ANVSGGGETG DIQQIKDMVL ATNPLLESFG
NAKTLRNNNS SRFGKYLQIH FNAQGEPVGA DITNYLLEKS RVVGQIVNER NFHIFYQFTK
GASQHYRETF GIQKPETYIY TSRSKCFNVD GIDDLAEYQD TLNAMKVIGL SQAEQDNIFR
MLAAILWTGN LVFREDDNGY AAVSDQSVVD FLAYLLEVDP ARLVHAITIR VLTPRNGEVI
ESPANVAQAT ATRDALAKAI YYNLFDWIVE RVNQSLRARQ AAANSIGILD IYGFEIFEKN
SFEQLCINYV NEKLQQIFIQ LTLKAEQDEY AREQIKWTPI SYFDNKIVCD LIESVRPPGV
FSAMKDATKT AHADPAACDR TFMQSINGMS NPHLTPRQGN FIIKHYAGDV TYTVDGITDK
NKDQLLKGIL NLVQGSQNKF LHDIFPQQVD QDNRKQPPSA GDRIKTSANA LVETLMKCQP
SYIRTIKPNE NKSPTEYNVP NVLHQIKYLG LQENVRIRRA GFAYRQSFEK FVDRFFLLSP
ATSYAGEYTW QGSYEAAVKQ ILKDTSIPQE EWQLGVTKAF IKSPETLFAL EHMRDRYWHN
MATRIQRMWR AYLAYRAESA TRIQRFWRKK RTGAEYLQLR DDGHRVLQGR KERRRMSILG
SRRFLGDYLG INASTGPGAQ MRNGMQLGNN ERAVFSCRGE VLEAKFGRSS KPSPRTIVVT
NNKFYVVALV MGQNNQPQVI LERSFPLGAI KFISTSTARD DWFSLGVGSQ QEADPLLNCV
LKTEMFTQMK RVMPGGFNLK IGDTIEYAKK PGKMQLVKVL KDAPTPHDFY KSGAVHTQQG
EPPNSVSRPT PKGKPVPPRP ITRGKLIKPG GPGGRPSRVP VNRTPQPRPS GASAATTSRP
VPQPHPAAAA AAAASVSIPS HTRQKSNSSA VRAPPPPPPA APPAKPKIMA KVLYDFAGQR
ENELSIQAGQ VIEIVQKENN GWWLAKLSGG QAWVPAAYVE EQEAAPVPAP RPPPPPPAAA
NGARAKPAAP QPPAKRPAAG RKPAALQGRD SAMSMNGSDS SRSSTPTPSL GGSLADALLA
RKNAMAKKDD DDDW
