ID H3BAZ9_LATCH Unreviewed; 437 AA.
AC H3BAZ9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Adenylate kinase 5, like {ECO:0000313|Ensembl:ENSLACP00000019070.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000019070.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000019070.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AFYH01046137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3BAZ9; -.
DR STRING; 7897.ENSLACP00000019070; -.
DR Ensembl; ENSLACT00000019203.1; ENSLACP00000019070.1; ENSLACG00000016782.1.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000155917; -.
DR HOGENOM; CLU_034712_0_0_1; -.
DR InParanoid; H3BAZ9; -.
DR OMA; HTEMADK; -.
DR TreeFam; TF313747; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000016782; Expressed in pectoral fin and 3 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:SF70; ADENYLATE KINASE 1, ISOFORM B; 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:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 49004 MW; CA2A64AA8C56C5FC CRC64;
MNTTEAKDYL SRREIPQLFE SMLTGLMYYR PEDPIEYLEG CLQKVRELGG PEKVRWDTFI
GQERRTLPPI NGGQGKKTLF RTEIVEACAG PYRRFERLPP IQAQFSIESD SDMTEVSGLI
QEYDVFDPLK PRPKIIFVIG GPGSGKGTQS SKIANHYGFI CISVGEILRK QMIHHATSDK
KWELIAQIIA NGELAPPETT IEELKQQFIK QPDAKGFIVD GFPREIGQVF TFEEQIGSPD
LVVLLACSKH QLRQRLEKRG QQQGRPDDNP HAIEKRVDTF KQNITLIMKY YQEKGVIVRF
DADREEEEVF ADIKATVEKR LFPEGRGASG KFSIEGFMVI PAHSSVDTGK AEQRGIDFEI
NLFLSSCVSP AEKLKGSKII FVVGGPGSGK GTQCRKIVAK YGYTHLSTGD ILRAEVQSGS
ERGESISDIM ERGELVP
//
