MYO1_PICST
ID MYO1_PICST Reviewed; 1256 AA.
AC A3LYL7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Myosin-1;
DE AltName: Full=Class I unconventional myosin;
DE AltName: Full=Type I myosin;
GN Name=MYO1; ORFNames=PICST_79258;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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-360) 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}.
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DR EMBL; CP000501; ABN68192.2; -; Genomic_DNA.
DR RefSeq; XP_001386221.2; XM_001386184.1.
DR AlphaFoldDB; A3LYL7; -.
DR SMR; A3LYL7; -.
DR STRING; 4924.XP_001386221.2; -.
DR EnsemblFungi; ABN68192; ABN68192; PICST_79258.
DR GeneID; 4840534; -.
DR KEGG; pic:PICST_79258; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; A3LYL7; -.
DR OMA; MESKWGT; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000002258; Chromosome 7.
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 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..1256
FT /note="Myosin-1"
FT /id="PRO_0000338560"
FT DOMAIN 37..724
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 728..748
FT /note="IQ 1"
FT DOMAIN 749..774
FT /note="IQ 2"
FT DOMAIN 782..971
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1101..1161
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 407..490
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 965..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1256 AA; 140578 MW; AE9AC7EFF08AD209 CRC64;
MAIVKRGGRT KNKTQQQAPA KSGIKKAEFD LHKSKEVGVS DLTLLSKITD EAINDNLHKR
FMNGTIYTYI GHVLISVNPF QDLGIYGPET LSKYRGRNRL EVPPHVFAIA ESMYYNLKSY
NENQCVIISG ESGAGKTEAA KQIMQYIANV SVDSGNAEIS KIKDMVLATN PLLESFGCAK
TLRNNNSSRH GKYLEIQFSE SNHQPIAAHI TNYLLEKQRV VSQITNERNF HIFYQFTKHC
PTQYQQQFGI QGPETYVYTS SAKCINVDGI DDSKDLDETL SAMKIIGLTE LEQNNIFRMI
ASILWIGNVS FVEDESGNAA IRDDSVTQFV AYLLEVNPEI LKKAIVERVI ETTHGMRRGS
TYHVPLNIVQ ATSVRDALAK GIYNNLFEWI VERVNVSLKG ASQSSKTIGI LDIYGFEIFE
HNSFEQICIN YVNEKLQQIF IQLTLKAEQD EYVKEQIKWT PIDYFNNKVV CDLIEATRPQ
PGLFAALNDS IKTAHADSDA ADQVFAQRLS MVGASNRHFE DRKGKFIIKH YAGDVTYEVA
GMTDKNKDAL LRDLVELLST SANPFVNQVL FPPSLLASIT DSKKRPETAS DKIKRSANDL
VGTLSKCQPS YIRTIKPNQT KRPKEYENQQ VLHQIKYLGL KENVRIRRAG FAFRTTFEKF
VQRFYLLSPA TGYAGDYIWR GDDISAVKEI LKSCFIPATE YQLGTTKVFI KTPETLFGLE
DMRDKYWHNM AARIQRAWRR YVKRKEDAAR TIQSAWRIKK HGNQFEQLRD YGNGLVQGRK
ERRRMSMLGS RAFMGDYLGC SDTSGYGRFI VTQTGINEKV VFSGRGEILL SKFGRSSKRL
PRIFVVTRTT IFIIAEVLIE KRLQLQSEFK IPISGLNYVA LSHLQDNWVA LSLHSPTPST
PDVFISLDFK TEFVTHLKKI NPGLTINIGT TVQYQKKPGK FHTVKFISGN SSDVPEYGDV
YKSGTVTVKP GLPSSSRNPK RPRGKSGKVD YSKYYNRGVK KSFPVPSARP TAASQPSYKS
PVEQSYQPQV LAYQTPRPEE AKPVQRKAPP PAPVVQNQPQ RQPQAIEPVR PVKKTAPSPP
VRKTAPPPPP PPPALSAPAK PKFPTYKAMY DYDGSVAGSI PLVKDVVYYV ESINGKWGLV
KTLDESKEGW SPIDYLSQCE PPSSLFGAAN PPSRPVAPSQ PKVQSRESTV ASAAVSSSTP
ASTVSNGSLS NGLAEALRAK KTEETTLAGS LADALKKRQG ATRDDSDDED DDDDDW
