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Database: UniProt
Entry: A0A061D507_BABBI
LinkDB: A0A061D507_BABBI
Original site: A0A061D507_BABBI 
ID   A0A061D507_BABBI        Unreviewed;       536 AA.
AC   A0A061D507;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Actin-related, putative {ECO:0000313|EMBL:CDR95771.1};
GN   ORFNames=BBBOND_0209240 {ECO:0000313|EMBL:CDR95771.1};
OS   Babesia bigemina.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR95771.1, ECO:0000313|Proteomes:UP000033188};
RN   [1] {ECO:0000313|Proteomes:UP000033188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RA   Aslett M., De Silva N.;
RL   Submitted (JUN-2014) 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; LK391708; CDR95771.1; -; Genomic_DNA.
DR   RefSeq; XP_012767957.1; XM_012912503.1.
DR   AlphaFoldDB; A0A061D507; -.
DR   STRING; 5866.A0A061D507; -.
DR   EnsemblProtists; CDR95771; CDR95771; BBBOND_0209240.
DR   GeneID; 24564312; -.
DR   KEGG; bbig:BBBOND_0209240; -.
DR   VEuPathDB; PiroplasmaDB:BBBOND_0209240; -.
DR   OMA; DICAPPR; -.
DR   OrthoDB; 227162at2759; -.
DR   Proteomes; UP000033188; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 4.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033188}.
FT   REGION          361..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  58731 MW;  05D81A2C0F46F046 CRC64;
     MDAVAYAALP RVVLDNGSGN LKFSLASSKK PPTVMPNCIG QPKRKFTSQS FSADTSHSSP
     SDPLSYAEHG ESIGDACYTL WEYFCLRPWA DGLLYEPNRQ RTIWNKIMGR PHIKINGVPA
     NMLAIAPANA ALCITEPNMA PGMCRQTLAE LIFEDLGFSL AAIMSSQAAS NWYYSVAKNP
     ASGAASDAKL TAYPSASAAP ASLPPDTACC LVVDCGFGSS HCVPFANGKP IQRAALRNGL
     AGSHLNAYLK NVSAIRTINL EFNELLVQHM KEEACYVSAD FNLEMRAARQ LRRIKGSSWL
     THDYVLPTYG GKSKSHLHRH FNNHSVSAPP LLTDERRPVV ERLARGATLT PEDLEAIVPQ
     QSADHANGDQ TAENNRADGQ TNGDMQNTLE AANIIAEETA KEDKKANNHV VGLFNERFAI
     PELLFSPQDL RLNECGIAEL ALRSIALAPT CLQRYLAENV LLTGGSTKFP GFTERFYSEL
     RAMLPADWNL QIYSAEDRAL TAFYGARLYA RDDTAFLETA VTRNFYLEHG GIYPHR
//
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