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Database: UniProt
Entry: A0A3B4YHI9_SERLL
LinkDB: A0A3B4YHI9_SERLL
Original site: A0A3B4YHI9_SERLL 
ID   A0A3B4YHI9_SERLL        Unreviewed;       554 AA.
AC   A0A3B4YHI9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Adenylate kinase 5 {ECO:0000313|Ensembl:ENSSLDP00000030035.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000030035.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000030035.1}
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; A0A3B4YHI9; -.
DR   STRING; 1841481.ENSSLDP00000030035; -.
DR   Ensembl; ENSSLDT00000030906.1; ENSSLDP00000030035.1; ENSSLDG00000023096.1.
DR   GeneTree; ENSGT00940000155917; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   REGION          490..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  62142 MW;  9BAAC9AC17E9F0BF CRC64;
     MNTNDAKEYL ARREIPQLFE SLLTGLMYYR PDDPIDYLEG CLKKVRELGG PDKVRWDTFV
     GQEKKSLPPL NGGQSRRSLF RNVLPDSPNF PYRRYDRLPP ISQFSIESDS DLSETAELIE
     EYEVFDPSRP RPKVILVIGG PGSGKGTQCL KIAERYSFQY VSVGELLRKK MIHNATSNRK
     WSLIAKIITN GELAPQETTI TEIKQKIMKI PDANGIVIDG FPRDVGQALS FEDQICTPDL
     VLFLACTNHR LKERLQKRAE QQGRPDDNPK AIDRRLTNFK QNTIPLVKYF QERGLIVTLD
     ADRDEEEVFC DISMTLDNKL FPSKEPAAGP SELDLSLLGE TSSLADAACK YDEVRVPFII
     TYSCTNVCLC LLAGGPGSGK ALQCERMEDR FGLRRVTLGD LLCNELQSHS DRGRHLRDIL
     ERGEQLPEDT LLELLCDAVA SSVRQGKGLV ISSFPRDLRQ AEEYEAKMGE PSAVLLLNCS
     PDTMCSRLQC RGRSSSSSSS GSGFHPGTDR DGAVHRRAEI FCNNSQAVAA HYELTIHLDS
     ILQHLCIILC YCLK
//
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