ID A0A059CLF9_EUCGR Unreviewed; 561 AA.
AC A0A059CLF9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=EUGRSUZ_C00416 {ECO:0000313|EMBL:KCW78991.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW78991.1};
RN [1] {ECO:0000313|EMBL:KCW78991.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW78991.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000582};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR EMBL; KK198755; KCW78991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CLF9; -.
DR EnsemblPlants; KCW78991; KCW78991; EUGRSUZ_C00416.
DR Gramene; KCW78991; KCW78991; EUGRSUZ_C00416.
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; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR018962; DUF1995.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359:SF167; ADENYLATE KINASE 5, CHLOROPLASTIC; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF09353; DUF1995; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 354..522
FT /note="DUF1995"
FT /evidence="ECO:0000259|Pfam:PF09353"
FT REGION 36..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 61241 MW; 084A1E0379800AD9 CRC64;
MQVGSPSHAL IPPFTSLSLS PTSATMLHAS LSSLHCSSAS PSPSPPRLSS PSLYPSSPSS
ARPTCLRSRH VLSFSVPAKT HLRAKSKSMG LKVNCLAGEP LKVMISGAPA SGKGTQCELI
VKKFGLVHIS TGDLLRAEVS AGTEIGNKAK EFMNAGKLVP DEIVTAMVTA RLSLPDAQEK
GWLLDGYPRS YAQAQSLEER KIRPDIYIVL EVPDEILIDR CVGRRLDPLT GKIYHIKNFP
PETEEIKARL VTRPDDTEEK VKSRLEIYKQ NAQAILSTYL SVMNKIDGNR PKDVVFGEVD
SLLSRVQKDK AKTTKLGNPV SGISLPSNQA TKKEGKWRGI PTRLNNIPHS REIRTYFYDD
VLQATQRAIY DGKTRLKVEI NIPELNPEMD VYRIGTLTEL VRVIALSFAD DGKRVKVCVQ
GSMGEGALAG MPLQLAGTRK ILEFMDWGDD GALGTFIQIG SIGAKEVDEQ DDIFILVAPQ
NAVGNCIIDD LRGMTESAGM RPVILINPRL KDLPGSSGIM QVSTMLICGN KMDIDLNWFS
YLETCFEDHG TGQEIGVCGI I
//
