ID A0A0A1U8G1_ENTIV Unreviewed; 1230 AA.
AC A0A0A1U8G1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Actin, putative {ECO:0000313|EMBL:ELP91225.1};
GN ORFNames=EIN_151120 {ECO:0000313|EMBL:ELP91225.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP91225.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP91225.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP91225.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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; KB206474; ELP91225.1; -; Genomic_DNA.
DR RefSeq; XP_004257996.1; XM_004257948.1.
DR AlphaFoldDB; A0A0A1U8G1; -.
DR EnsemblProtists; ELP91225; ELP91225; EIN_151120.
DR GeneID; 14890172; -.
DR KEGG; eiv:EIN_151120; -.
DR VEuPathDB; AmoebaDB:EIN_151120; -.
DR Proteomes; UP000014680; Unassembled WGS sequence.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF387; ACTIN; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000014680}.
FT REGION 1..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1230 AA; 133286 MW; 0DEBCFF9322F5533 CRC64;
MSTKAEKLKL KEEEKKKKEE EKRKKEEAKK KAEEEKKHKK EEEKRKKEEE KEKKKLEKEK
KEQEKHHKGG HETEKQKVEK EKPKDEIKEK EKTEKDEKAK KEEEEKKQKE AAEAKAKKEE
EEKVAKEKEA AEQKAKEEAA EKEKLEKEKA EKDAEEAKKK EEEAAKEKEA KEKAEKEEQE
KAKEAAEQKA KTEVVENDKL NKEIIEKANE DVEAAKKKEE QEKQEADKKK AEEEAAKKKE
EEEAAAKKAE EERVEKEKAE IEKANKEAAE KEKKEAEEAK ANEERIAKEK AEQEAKLEAE
RVEKERLEKE KLEQDRLAKE KEEAEKLEKE RLEKEAAQKA EEERILKERA EAERIEKERL
EREAAEKLEK ERLEQERVAK EKEEEERKAK ELAEKLAREE AEKLEKERIE KEVAAKLEQE
RVAKEKAEAE RILKEKEESE RLEKERLEQE KIAKEKAEKE EQEKAVAEQK KKEEEEKAKK
AAEEAQKKSQ PIPTLGNQPG LGMGMGLGAS QPGLGAKPPG LGQPGLGGMG LGAQPTPQPS
LGMGMGAPGL GQPGLGMGAP QPGLGAKPPV LGQPGLGGMG QPGLGMGAPQ GGLGGMGQPG
LGAKPPGLGL GAQPAGLGSQ STQQPGLGMG MGAPQPGLGG IGAAQPGLGV KPPGLGQPGL
GGMGLGAQPT PQPSLGMGMG APGLGQPGLG MGAAQPGLGG MGQPGLGAKP PGLGLGAQPA
GLGLGAQPSG LGLGAPSGGL GLGGAPTGLG LGGGQPTGLG LGGGQPAGLG LGGGLGMPGL
GMGGGLGIGG MPAMGGMPGL GGMGGLPGMG MPAMGGMPDM GEIEKPEETA GGEQPKKRKR
QKKKIMISQS AFFTHENEEK ANETLSRIPD DAVIVFDCGS SFIKVGTGGG EQPKKVIPNC
YCKIDDEEAE NGVRYEFGYK AIDEDEGLVW PLDPRKETDW DGFFSVIQNI YQNELNGCDP
AAHPVVMTEL PSMNEAATER LKVMMFNDLN VPFLKIVNPA LMALYAEGKE TGIVVEIGNR
MQIVPAVDGY VIDSAIEKIK GNVSGLTEYM SRLLRACGYI YTTSAQMELV RAIKESVCYV
ALDYDSEMKR KAKEVMKEFV VPGNEQASKF FQERFQCPEA LFQPEKVGLD TLGVPEMVFN
TIKKCPLTSR RPLLQHIVLA GGSTLFEGLP ERLEKELKRL CTENKMNPRD VKIISLQNRK
YLAWVGASLL AGMSTLQDDE TCTKDHYSNQ
//