MYO5_CANGA
ID MYO5_CANGA Reviewed; 1217 AA.
AC Q6FN18;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Myosin-5;
DE AltName: Full=Class I unconventional myosin MYO5;
DE AltName: Full=Type I myosin MYO5;
GN Name=MYO5; OrderedLocusNames=CAGL0K03487g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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-358) 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; CR380957; CAG61337.1; -; Genomic_DNA.
DR RefSeq; XP_448376.1; XM_448376.1.
DR AlphaFoldDB; Q6FN18; -.
DR SMR; Q6FN18; -.
DR STRING; 5478.XP_448376.1; -.
DR EnsemblFungi; CAG61337; CAG61337; CAGL0K03487g.
DR GeneID; 2890177; -.
DR KEGG; cgr:CAGL0K03487g; -.
DR CGD; CAL0134571; CAGL0K03487g.
DR VEuPathDB; FungiDB:CAGL0K03487g; -.
DR eggNOG; KOG0162; Eukaryota.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; Q6FN18; -.
DR OMA; MESKWGT; -.
DR Proteomes; UP000002428; Chromosome K.
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..1217
FT /note="Myosin-5"
FT /id="PRO_0000338545"
FT DOMAIN 37..716
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 720..740
FT /note="IQ 1"
FT DOMAIN 741..766
FT /note="IQ 2"
FT DOMAIN 772..962
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1083..1145
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 405..487
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 956..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1046
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1084
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1174
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 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1217 AA; 135835 MW; DF5566948B4E9626 CRC64;
MAILKRGARN KTHQEPAKRG GNNIKKAAFE TSKKKEVGVS DLTLLTSISD ESINDNLKKR
FLNGTIYTYI GHVLISVNPF RDLGIYTDAI MKSYQGKNRL EVPPHVYAIS EAMYYNLKAY
NENQCVIISG ESGAGKTEAA KKIMEYIAAT SSTHSESIGK IKDMVLATNP LLESFGCAKT
LRNNNSSRHG KYLEIRFNSQ FEPCAGNITN YLLEKQRVVG QITNERNFHI FYQFTKGASD
NYRQTFGVQL PEQYVYTSAS KCTSVDTIDD VKDFEATIKA MQVIGLAQEE QDQIFRMLAA
ILWIGNISFI ENEEGNAQVR DTSVTDFVAY LLQVDSQSLI KALVERIVET NHGSRRGSVY
HVPLNIVQAT AVRDALAKAI YNNLFEWIVD RVNKSLHAYP GADKSIGILD IYGFEIFEHN
SFEQICINYV NEKLQQIFIQ LTLKSEQDTY AREKIQWTPI KYFDNKVVCD LIEAKRPPGI
FAAMNDSVAT AHADSSAADQ AFAQRLSLFS SNPHFEQRQN KFVIKHYAGD VTYDVLGMTD
KNKDQLQKDL VELVGTTTNA FLTTLFPNQV DKDNKRRPPT AGDKIIKSAN ELVETLSKAQ
PSYIRTIKPN QTKSPNDYDD HQVLHQVKYL GLQENVRIRR AGFAYRQGFE KFVERFYLLS
PRCSYAGDYT WTGDILEAVR LILQDALIPE KEYQLGVTQV FIKTPETLFA LENMRDKFWH
NMAARIQRAW RRYLQRRIDA AVKIQRTIKE RKEGNKFEKL RDYGTSLLGN KKERRSMSLL
GYRAFMGDYL SCNESKSNGS YIKRQAGISE KVVFSFHGEA LHSKFGRSAQ RLKKTFILSP
TTLYIIGQVR VQNAMQYTAD YKINVNSILQ LNMTNLQDDW VGIVLANSSM PDPLINLSFK
TELITHLKTL NSKIQVKVGP TLEYQKKPGK MHSVKCQVSD TAPKYGDVYK SSTIFVRRGN
PANSKSKKKP RKKSSGMSAP TTQSSKTLAP PRMSSNNQNT TVSQSLNGGM NVKPQTPASR
SAKKPAPPPP GSKKPAPQPM AKKPAPHPTP QAQMQTQTQI PASQSSATQS SIPPPPPPPP
SKTSEPQFEA AYDFPGSGNP SELPLMKGDI VYITKEEPSG WSLAKTLDGS KSGWVPTAYM
VKHEGAKAPP PAPAVTASQP AIQNQSQPAS AQTVAATSQV PASFGDGLVS ALAARANKMR
VESDEEAAAS SDNDDDW
