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Database: UniProt
Entry: A0A0M4EQS2_DROBS
LinkDB: A0A0M4EQS2_DROBS
Original site: A0A0M4EQS2_DROBS 
ID   A0A0M4EQS2_DROBS        Unreviewed;       196 AA.
AC   A0A0M4EQS2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Dak1 {ECO:0000313|EMBL:ALC46735.1};
DE   Flags: Fragment;
GN   ORFNames=Dbus_chr3Rg1485 {ECO:0000313|EMBL:ALC46735.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC46735.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC46735.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC46735.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00001331};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR   EMBL; CP012526; ALC46735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4EQS2; -.
DR   SMR; A0A0M4EQS2; -.
DR   STRING; 30019.A0A0M4EQS2; -.
DR   OMA; DVCVQRC; -.
DR   Proteomes; UP000494163; Chromosome 3r sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009041; F:UMP/dUMP kinase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; 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   HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006266; UMP_CMP_kinase.
DR   NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR   Pfam; PF00406; ADK; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   NON_TER         196
FT                   /evidence="ECO:0000313|EMBL:ALC46735.1"
SQ   SEQUENCE   196 AA;  21767 MW;  491FA14C7A404ABA CRC64;
     MSVAMPKVVF VLGGPGAGKG TQCSKIVDRF QFTHLSAGDL LREERAREGS EFGQLIDDYI
     RNGKIVPVEV TCSLLENAMK NSGKSLFLID GFPRNQDNLD GWNRQMSDKT EMQFVLFFDC
     AEDVCVTRCL GRGQGGSGRS DDNMDSLKKR IQTYNNDSLP IIKHFDQAGQ VKKIDASPDA
     DEVFQQVERV FLASGF
//
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