ID   A0A3Q4HHG2_NEOBR        Unreviewed;       533 AA.
AC   A0A3Q4HHG2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Adenylate kinase isoenzyme 5-like {ECO:0000313|Ensembl:ENSNBRP00000019878.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000019878.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000019878.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR   AlphaFoldDB; A0A3Q4HHG2; -.
DR   Ensembl; ENSNBRT00000020405.1; ENSNBRP00000019878.1; ENSNBRG00000015295.1.
DR   GeneTree; ENSGT00940000155917; -.
DR   OMA; NGLVHIC; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000015295; Expressed in brain and 2 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
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; 2.
DR   CDD; cd22978; DD_AK5; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   PANTHER; PTHR23359:SF79; ADENYLATE KINASE ISOENZYME 5; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 2.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ   SEQUENCE   533 AA;  60261 MW;  E915C43F26B5A8F0 CRC64;
     MNTNDAKEYL ARREIPQLFE SLLTGLMYYR PDDPIEYLEG CLKKARELGG PEKVRWDTFV
     GQEKKSLPPL NGGQSRRSLF RNVLPDSPNF PYRRYDRLPP ISQFSIESDS DLSETAELIE
     EYEVFDPSRP RPKVILVIGG PGSGKGTQSL KIADRYGFQY MSVGELLRKK MIHNATSNRK
     WSLIAKIITN GELAPQETTI TEIKQKIMKI PDANGIVIDG FPRDVGQALS FEDQICTPDL
     VVFLACTNHR LKERLQKRAE QQGRPDDNPK AIERRLTNFK QNTIPLVKYF QERGLIVTLD
     ADRDEEEVFC DIGMTLDNKL FPSKEPAAGK KKICFYKEVI LSDHSTATIW PYFRLFLCVS
     VSGGPGSGKA LQCERMEERF GLRRVTLGDL LCSELQSNSD RGRYLRDALE RGEQLPEVSD
     TLLELLCDAV VSSVRQGKGL VISGFPRDLR QAEEYEAKMG EPSAVLLLNC SADTMSNRLQ
     CRGRSGFQAA PDRESVLHRR VESFCSDTQA VAAHYEHKRL LHTVRLGSKL CKG
//