ID   A0A183JF50_9TREM        Unreviewed;       498 AA.
AC   A0A183JF50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Adenylate kinase 7 {ECO:0000313|WBParaSite:SCUD_0000131401-mRNA-1};
GN   ORFNames=SCUD_LOCUS1315 {ECO:0000313|EMBL:VDO66907.1};
OS   Schistosoma curassoni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000131401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SCUD_0000131401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO66907.1, ECO:0000313|Proteomes:UP000279833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dakar {ECO:0000313|EMBL:VDO66907.1}, and Dakar, Senegal
RC   {ECO:0000313|Proteomes:UP000279833};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UZAK01001037; VDO66907.1; -; Genomic_DNA.
DR   STRING; 6186.A0A183JF50; -.
DR   WBParaSite; SCUD_0000131401-mRNA-1; SCUD_0000131401-mRNA-1; SCUD_0000131401.
DR   Proteomes; UP000050789; Unplaced.
DR   Proteomes; UP000279833; 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   CDD; cd22967; DD_AK7; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR047499; DD_AK7.
DR   InterPro; IPR007858; Dpy-30_motif.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF105; ADENYLATE KINASE 7; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF05186; Dpy-30; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279833};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          176..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          401..461
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        194..212
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  57316 MW;  64841D3968ECBC07 CRC64;
     MDQLLVSIRM NASYVKENFQ IKWHCETGLV DHINLITKEY KLSRQLIPIR LCILGPPASG
     KTTLAKKLCE YYKLPHIHIK QVIDEAIANL KKRVQMIDEA QSDQNQMVNE NEYPGSEDSE
     FLEAIQQNMT ENNGRLGLEY VTTSENNFPP STVIDHESYY PKFPTIYYNY YVDPSTSSLS
     QTSKLRTSGG SGDGEEDEGE QENEEEEEEG IKAIDTSDFT QSANELFKSQ YLQSEKEADD
     VTKELGLLST QPIPMQLPKG LLPAYVFELQ ATDKFLRDRI MNMPEYKVHG THYTESGFWR
     RLNEYRTNQI GINPALSPTL NIPGSPGSEP EVGQVDLNSL SPLASASIYE NSVRAYFDSK
     GILQIPVNIM TDESEELEQT FRKLVYFIGP PRNYGLSDEE IEKQRLIVEK QRIEFERAEE
     ERLKQEIETA EAERNQRIKE WKEKQEALEK EEKDLLNKES EPLRAYLRKH IMPVLAKGLT
     ECVRKRPDDP LDFLVSIY
//