ID A0A445EQN6_ARAHY Unreviewed; 231 AA.
AC A0A445EQN6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|ARBA:ARBA00031517};
GN ORFNames=Ahy_A01g002415 {ECO:0000313|EMBL:RYR77794.1};
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:RYR77794.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR77794.1, 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:RYR77794.1};
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 -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|RuleBase:RU003330}.
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:RYR77794.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SDMP01000001; RYR77794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445EQN6; -.
DR Proteomes; UP000289738; Chromosome a01.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359:SF191; ADENYLATE KINASE 4; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 2.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 144..179
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
SQ SEQUENCE 231 AA; 25572 MW; 0727FE43164D7F1B CRC64;
MGSSSAAPNL EDVPSMDLMT ELLRRFKCSA KPDKRLILIG PPGSGKGTQS PIIKDEYCLC
HLATGDMLRA AVAAKTPLGI KAKEAMEKVR LSIYFFLQID VLLSAFHEEI DNLDQMLEKQ
GLKVDKVLNF AIDDSILEER ITGRWIHPSS GRSYHTKFAP PKVSGVDDVT GEPLIQRKDD
TAAVLKSRLD AFHKQTEPVI DYYTKKGIVA NLHAEKPPKE VTVEVEKVLS S
//
