ID G0W8P3_NAUDC Unreviewed; 219 AA.
AC G0W8P3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Adenylate kinase active site lid domain-containing protein {ECO:0000259|Pfam:PF05191};
GN Name=NDAI0C04950 {ECO:0000313|EMBL:CCD24154.1};
GN OrderedLocusNames=NDAI_0C04950 {ECO:0000313|EMBL:CCD24154.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24154.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD24154.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR EMBL; HE580269; CCD24154.1; -; Genomic_DNA.
DR RefSeq; XP_003669397.1; XM_003669349.1.
DR AlphaFoldDB; G0W8P3; -.
DR STRING; 1071378.G0W8P3; -.
DR GeneID; 11496288; -.
DR KEGG; ndi:NDAI_0C04950; -.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_1_0_1; -.
DR OMA; EPIIDYY; -.
DR OrthoDB; 167111at2759; -.
DR Proteomes; UP000000689; Chromosome 3.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
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; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359:SF234; ADENYLATE KINASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 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 Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 133..168
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
SQ SEQUENCE 219 AA; 23930 MW; 8D4EE5A4AFC3B4B9 CRC64;
MSTSSLRIVL IGPPGAGKGT QAPKLVEKYN AAHLSTGDML RSQIAKGSEL GLEAKKIMDK
GGLVSDEIMV NMIKDELTNN PACKNGFILD GFPRTIPQAE KLDQMLAEQG TPLQRAVELK
VDDDLLVSRI TGRLIHPASG RSYHKLFNPP KVDMIDDITG EPLIQRSDDN EDALKKRLAG
YHAQTEPIVD FYKKSGIWSG VDASQPPATV WDEILKALN
//