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Database: UniProt
Entry: A0A1I8I3I7_9PLAT
LinkDB: A0A1I8I3I7_9PLAT
Original site: A0A1I8I3I7_9PLAT 
ID   A0A1I8I3I7_9PLAT        Unreviewed;       453 AA.
AC   A0A1I8I3I7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Actin {ECO:0000313|WBParaSite:maker-uti_cns_0009786-snap-gene-0.7-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0009786-snap-gene-0.7-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0009786-snap-gene-0.7-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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   AlphaFoldDB; A0A1I8I3I7; -.
DR   WBParaSite; maker-uti_cns_0009786-snap-gene-0.7-mRNA-1; maker-uti_cns_0009786-snap-gene-0.7-mRNA-1; maker-uti_cns_0009786-snap-gene-0.7.
DR   Proteomes; UP000095280; Unplaced.
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; 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}.
SQ   SEQUENCE   453 AA;  50023 MW;  55C5B161A629B48D CRC64;
     QWGAVQTIWK STKEESAIEL STNSSTQLEF QQFNRNPQSQ HSAMASEEIA ALVVENGSGM
     CKAGFAGDDA PRAVFPSIVG RPKHSSVMIG MGEKDSYIGD EAQSRRGVLA LKYPIEHGVV
     TNWDDMEKIW HHTFYNELRV APEEHPVLLT EAPLNPKANR EKMTQIMFET FNTPAMYVAI
     QAVLSLYASG RTTGIVLDSG DGGYALPHAI FRLDLAGRDL TDHLVRILTE RGYDFKTSAE
     REIVRDMKEK LCYSALDFEQ EMSTAASSSA LEKRYELPDG QVVTVGSERF RCPEALFQPA
     ILGMESAGIH ETVFNSVMKC DMDIRKDLYC NIVLSGGTSM FPGIADQGDL LPSASVVVVV
     VVSSSSNVFD LHPHRQLQVI SLAQNSLTSL HLVPRVLPLL LHRCQAVRQE AAALLSCQLF
     NGNSSAQQSL LSCLRASRRE ETALFLDIKL TIR
//
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