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Database: UniProt
Entry: A0A210QMB2_MIZYE
LinkDB: A0A210QMB2_MIZYE
Original site: A0A210QMB2_MIZYE 
ID   A0A210QMB2_MIZYE        Unreviewed;      1208 AA.
AC   A0A210QMB2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Adenylate kinase isoenzyme 5 {ECO:0000313|EMBL:OWF49868.1};
GN   ORFNames=KP79_PYT03819 {ECO:0000313|EMBL:OWF49868.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF49868.1, ECO:0000313|Proteomes:UP000242188};
RN   [1] {ECO:0000313|Proteomes:UP000242188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX   PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA   Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA   Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA   Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA   Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA   Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA   Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA   Chourrout D., Li R., Bao Z.;
RT   "Scallop genome provides insights into evolution of bilaterian karyotype
RT   and development.";
RL   Nat. Ecol. Evol. 1:120-120(2017).
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWF49868.1}.
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DR   EMBL; NEDP02002907; OWF49868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A210QMB2; -.
DR   STRING; 6573.A0A210QMB2; -.
DR   Proteomes; UP000242188; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
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; 5.
DR   CDD; cd22978; DD_AK5; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 5.
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; 5.
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; 5.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 3.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWF49868.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242188};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          65..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1208 AA;  133882 MW;  0B5667FEE8B3D5DB CRC64;
     MTTDDAKSYL SKREIPRLFE SLMTGLMYHR PTDHIKYLID CLHKVQDKGS NNITWSAFVD
     IRRTKTPLPP ITPPDGKKRR SRPSSRQKEP SKIEEDKKNL DDKKASPLPP ITKSEDGVPD
     VPVILIVGGP GSGKLTQVKL LQKTYPGWVH LSMGDLLRSE IADKGSAEDK WEMIGDLVNR
     GEMAPEDITA DLILKSLKSH PKAEGFILEG YPRTVTQMKE FDKIVGRLDM AFMLDCDEHC
     CTQRLLQRGK QEGRVHDNIN AVQRRLTAFK NNTLPAAKVL DDRGKLFVIN ADRDIKEIAF
     ELGQCFQKSI FGDKKGKKLV PPRCTVPNPP EEGSVPVAAT YERPAEAIAR TKSQLEDSMA
     LAKDAPEIVN KDEGRKPELP TCPIIVLAGG PGSGKGTQAK MIIERYPGTV HVSMGDILRT
     EISQKGTADQ KWGMISSLVQ QGEMAPEEVT VDLLKDNLAK HKDASAIILE GYPRDKTQVE
     EFNKYIGGLN FVLLIDSEEY YMQKRLVDRG KETERIDDNL SAISSRINFF RNKTLPVLKH
     YDDNGKLVAL YGDRDIQEVF FDVTQVLDKA FFGDKAQQQP APPSEDAALD TSVLKDTKIV
     FVVGGPGSGK GTQCERIVQQ FGFTHLSTGD LLRAEVASGS ARGKELTSIM ESGQLVPLDV
     VLQLLKEKMM AAAATSSGFL IDGYPREMEQ GTRFENEVAP CTCVLYFEAS DETMTQRLLG
     RALTSGRVDD NEETIKKRLT TFHDITTPVI DYFTQHDKVK KVSAERHVDE VYGDVKTIFD
     ELVPGSTVPK KGAPTTPPPE VPTQETTPVD TSILKDTKVV FVVGGPGSGK GTQCERIVQQ
     FGFTHLSTGD LLRAEVASGS ARGKELTSIM ESGQLVPLDV VLQLLKEKMV AAAATSSGFL
     IDGYPREMEQ GTRFENEVTP CTCVLYFEAS DETMTQRLLG RALTSGRVDD NEETIKKRLT
     TFHDITTPVI DHFSQQEKLK KVSAERDVAD VFTDVQEIFN NITGAKAKKE STDAAPSLKD
     AKVIFVVGGP GSGKGTQCAK IVEKYGFCHL SSGDLLREEV SSGSDRGKRL NEIMEKGELV
     TLDEVLALLR NAMEAKISTS KCFLIDGYPR ELEQGTRFEN EIVECTSVVY FEVPDEVMTE
     RLLERGKTSG RVDDNEETIK KRLETFHNQT KPVVDHYASK DKAVKIVATG TVDEIFAEVQ
     KFMDSKTW
//
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