MYO1_DEBHA
ID MYO1_DEBHA Reviewed; 1304 AA.
AC Q6BUQ2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; OrderedLocusNames=DEHA2C08976g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- PTM: Phosphorylation of the TEDS site (Ser-364) is required for the
CC polarization of the actin cytoskeleton. Phosphorylation probably
CC activates the myosin-I ATPase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382135; CAG86138.2; -; Genomic_DNA.
DR RefSeq; XP_458067.2; XM_458067.1.
DR AlphaFoldDB; Q6BUQ2; -.
DR SMR; Q6BUQ2; -.
DR STRING; 4959.XP_458067.2; -.
DR EnsemblFungi; CAG86138; CAG86138; DEHA2C08976g.
DR GeneID; 2900469; -.
DR KEGG; dha:DEHA2C08976g; -.
DR VEuPathDB; FungiDB:DEHA2C08976g; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q6BUQ2; -.
DR OMA; NGWWLCK; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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 GO; GO:0051641; P:cellular localization; IEA:UniProt.
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; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1304
FT /note="Myosin-1"
FT /id="PRO_0000338550"
FT DOMAIN 36..730
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..754
FT /note="IQ 1"
FT DOMAIN 755..780
FT /note="IQ 2"
FT DOMAIN 788..978
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1155..1217
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..496
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 963..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1304 AA; 145342 MW; 2231DE5CBB3C6621 CRC64;
MAIVKRGVRT KNKQSQQPSK SGIKKAEFDL HKKKEVGVSD LTLLSKIADD AINDNLYKRF
MNSTIYTYIG HVLISVNPFE DLGIYTPEHL NKYKGKNRLE VPPHVFAIAE SMYYNLKSYG
DNQCVIISGE SGAGKTEAAK QIMQYIANVS VDDQVSAGGD GGISKIKDMV LATNPLLESF
GCAKTLRNNN SSRHGKYLEI YFNPSNYQPV SAHITNYLLE KQRVVSQITN ERNFHIFYQF
TKHCPPQYQQ SFGIQGPETY VYTSAAKCIN VDGVDDSKDL QDTLRAMQVI GLSQDEQDNI
FRMLASILWV GNVSFVEDDN GNAAVRDESV TAFIAYLLDV DAETLKTSLI QRVMQTSHGM
RRGSTYHVPL NIVQATSVRD ALAKGIYNNL FDWIVERVNL SLQGSGAVQE KKSIGILDIY
GFEIFEHNSF EQICINYVNE KLQQTFIQLT LKAEQDEYVQ EQIKWTPIDY FNNKVVCDLI
EALRPQPGLF AALNDSVKTA HADSDAADQV FAQRLSMVGA NNAHFEDRRG KFIIKHYAGD
VTYDVAGMTD KNKDSMLRDL VEVLSTSSNS FVSQVLFPPD LLAALTDSKK RPETASDKIK
KSANLLVDTL SQCQPSYIRT IKPNQTKRPK EYDNNQVLHQ IKYLGLKENV RIRRAGFAYR
TTFDKFVQRF YLLSPKTGYA GDYIWQGDDV TAVHEILRSC HIPDSEYQMG TTKVFIKTPE
TLFALEDMRD KYWHNMAARI QRAWRRYIKR KDDAARLIQS AWKNKTHGNQ FEQLRDYGNG
LLHGRKERRR MSMLGSRAFM GDYLGCKYSS GFGRFIMSQA GISDSVIFSA KGDILLSKFG
RSSKRLSRIF ILTKNSLYVI AQTLVQNRLQ VQKEFTIPVS GINYVGLSIY QDNWVAVSLH
SPTPTTPDIF INLDFKTELV THLKKCNPGL NIKIGQTIEY QKKPGKFHTI KFIVGNTAPV
NGDSYKSGTV TVRQGLPGNS QNPKRPRGAA GKVDYSKYYN RGSNMRSTSS YQPPAVSKAP
QSSRPSYIQP PVQQTQQRVV PPVQSQPKPQ AQRYAPPDTQ PQTQRHAPPD TQPHAHPEQA
AQAAQAAFHH TAPQAQNTTQ RKVPPSAPGS YGQQAPTQKP SAPSRPARKT APAPPAKKNV
APPPPPAAAS PPPKPKFPTY KAAYDFQGTG SASELPISKE TIVFITRKED NGWWLAKTLD
ETKEGWVPAA YVVECDPPAN SPAGNAKSPP PPPPQLNSAS QAQQSQQQAQ APNGAGLSNG
LADALKAKKS EETNLAGSLA DALKKRKGAT GDSDEEDEED DDDW
