ID A0A445B5C1_ARAHY Unreviewed; 458 AA.
AC A0A445B5C1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Actin {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ahy_A10g048551 {ECO:0000313|EMBL:RYR33885.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR33885.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR33885.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR33885.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYR33885.1}.
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DR EMBL; SDMP01000010; RYR33885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445B5C1; -.
DR Proteomes; UP000289738; Chromosome a10.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF555; ACTIN-3; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51246 MW; A387E6A2DE509A9C CRC64;
MSEMKRKEKK RKEKDREELK KCGVRERGHR HPLLLLLLGR LFSSLKMADG EDIQPLVCDN
GTGMVKAGFA GDDAPRAVFP SIVGRPRHTG VMVGMGQKDA YVGDEAQSKR GILTLKYPIE
HGIVSNWDDM EKIWHHTFYN ELRVAPEEHP VLLTEAPLNP KANREKMTQI MFETFNVPAM
YVAIQAVLSL YASGRTTGIV LDSGDGVSHT VPIYEGYALP HAILRLDLAG RDLTDSLMKI
LTERGYMFTT SAEREIVRDI KEKLAYVALD YEQELETAKS SSAVEKNYEL PDGQVITIGA
ERFRCPEVLF QPSMIGMEAA GIHETTYNSI MKCDVDIRKD LYGNIVLSGG STMFPGIADR
MSKEITALAP SSMKIKVVAP PERKYSVWIG GSILASLSTF QQMWISKGEY DESGPSIVHR
KLCEPCCVVR IVGGLRCKPD VSYFYLRPSA RYGVYYDN
//