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
//