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Database: UniProt
Entry: A0A2G8JQG9_STIJA
LinkDB: A0A2G8JQG9_STIJA
Original site: A0A2G8JQG9_STIJA 
ID   A0A2G8JQG9_STIJA        Unreviewed;       334 AA.
AC   A0A2G8JQG9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=Sperm adenylate kinase {ECO:0000313|EMBL:PIK37969.1};
GN   ORFNames=BSL78_25192 {ECO:0000313|EMBL:PIK37969.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK37969.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK37969.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK37969.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK37969.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|RuleBase:RU003330}.
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:PIK37969.1}.
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DR   EMBL; MRZV01001423; PIK37969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8JQG9; -.
DR   STRING; 307972.A0A2G8JQG9; -.
DR   Proteomes; UP000230750; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
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; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   REGION          269..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   334 AA;  37573 MW;  4E7775B17729CFC8 CRC64;
     MTPLSPLPLH PPLPIHSQSP ISSLMTGLMY HKPEDHVSYL KQCLQELDGA DAKTSNGTYH
     SVLEMKKTSP LPPIPPALTN GDVKKNLKYI FILVGENLRR QAEQLEGSDE NWKVLSELIK
     VGKLVSEETA FTAVKTDVDN TLEANPENLI GFLVEGFPRT TEQYQMFEKE FGRPDMILSL
     ESEDYRLKFR LDKRKESNLR VDDTEEAVEN RISSFQTSTM SVIDQFQGHS NVLHRVNVDR
     DVEEVFYDMA NIIDGAFFEI RENNTANNAL NAMDPLPPIP KQKTNTEEEL VTQGADSEAG
     GKDEMKQGAT EETDASKVCY KLMNDVIDSY RGDG
//
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