ID R9P1L9_PSEHS Unreviewed; 422 AA.
AC R9P1L9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Actin {ECO:0000313|EMBL:GAC95089.1};
GN ORFNames=PHSY_002664 {ECO:0000313|EMBL:GAC95089.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC95089.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells. {ECO:0000256|ARBA:ARBA00003520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the actin family.
CC {ECO:0000256|ARBA:ARBA00006752, ECO:0000256|RuleBase:RU000487}.
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DR EMBL; DF238790; GAC95089.1; -; Genomic_DNA.
DR RefSeq; XP_012188676.1; XM_012333286.1.
DR AlphaFoldDB; R9P1L9; -.
DR STRING; 1305764.R9P1L9; -.
DR GeneID; 24107955; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR OrthoDB; 10at2759; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF387; ACTIN; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..422
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004477912"
SQ SEQUENCE 422 AA; 46894 MW; 9D5D83FC347BC758 CRC64;
MLLLSVVIIV NALREATPVR FADITCLPPP PPLRLSNVSP FVLPLTSLIT TTTTVTKPCS
NVIMEAGFAG DDAPRAVFPS VVGRPRHQGV MVGMGQKDSY VGDEAQSKRG ILTLKYPIEH
GIVTNWDDME KIWHHTFYNE LRVAPEEHPV LLTEAPLNPK ANREKMTQIL FETFNAPAFY
VAIQAVLSLY ASGRTTGIVL DSGDGVTHTV PIYEGYSLPH SILRLDLAGR DLTEYLARIL
TERGYPFTTT AEREIVRDIK EKLCYVALDF EQEMLTATQS SALEKSYELP DGQVITIGNE
RFRTPEVLFQ PAFLGLEAAG IHETTYNSIM KCDLDIRKDL YGNIVMSGGT TMYAGISDRM
QKEITALAPS SMKVKIVAPP ERKYSVWIGG SILASLSTFQ QMWISKQEYD ESGPSIVHRK
CF
//
