ID F0WY73_9STRA Unreviewed; 429 AA.
AC F0WY73;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
GN Name=AlNc14C373G11133 {ECO:0000313|EMBL:CCA26425.1};
GN ORFNames=ALNC14_125690 {ECO:0000313|EMBL:CCA26425.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA26425.1};
RN [1] {ECO:0000313|EMBL:CCA26425.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA26425.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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; FR824417; CCA26425.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WY73; -.
DR EnsemblProtists; CCA26425; CCA26425; ALNC14_125690.
DR HOGENOM; CLU_527353_0_0_1; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; 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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT REGION 213..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 48703 MW; B28A38FE798172B1 CRC64;
MLQVFINGPP GAGKSSLAER LCENYNLAHI ATGTLLRDNI VKNTKVGSEA SNCIRRKELI
PDAVVIDMVA DAVSQCAKIG KEGWILDGFP RTAEQCTAMR NKQIVPSLVI ILELEESECI
KRITGRMFDT VTKRIYHEKY HIPSSLDVSK RLCRRKDDAL ERILPRMEAY RVHGASISEK
CALEAFRMDA KEDLETVFRS ACHLIKQSQC NTENSDNQME ELQRSNSKSK RTQNPTEHHS
TDNPLHLISS ESNSFVSSNN INTQRLENEC VSLKSEANQA VTSLVEAVQR VQTAKKESAD
REIQWIAPFK VMLEDGFNVK KHGRRGRPHI RTVYTDLDHS RVFWQNSSEK RTENGSYLKR
PTIDQSLALC EVLRVVRGQE TNVLKRSGKK ELSHLYVSLI TEKRSLDLEF ETEEMAIFVA
NGFRTLLAL
//
