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Database: UniProt
Entry: A0A183MQD7_9TREM
LinkDB: A0A183MQD7_9TREM
Original site: A0A183MQD7_9TREM 
ID   A0A183MQD7_9TREM        Unreviewed;       239 AA.
AC   A0A183MQD7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=ADK_lid domain-containing protein {ECO:0000313|WBParaSite:SMRG1_13660.1, ECO:0000313|WBParaSite:SMRZ_0001826301-mRNA-1};
GN   ORFNames=SMRZ_LOCUS18262 {ECO:0000313|EMBL:VDP27116.1};
OS   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001826301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0001826301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP27116.1, ECO:0000313|Proteomes:UP000277204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zambia {ECO:0000313|EMBL:VDP27116.1,
RC   ECO:0000313|Proteomes:UP000277204};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR   EMBL; UZAI01017597; VDP27116.1; -; Genomic_DNA.
DR   STRING; 48269.A0A183MQD7; -.
DR   WBParaSite; SMRG1_13660.1; SMRG1_13660.1; SMRG1_13660.
DR   WBParaSite; SMRZ_0001826301-mRNA-1; SMRZ_0001826301-mRNA-1; SMRZ_0001826301.
DR   Proteomes; UP000050790; Unassembled WGS sequence.
DR   Proteomes; UP000277204; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01428; ADK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR036193; ADK_active_lid_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01351; adk; 1.
DR   PANTHER; PTHR23359:SF234; ADENYLATE KINASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN          146..181
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
SQ   SEQUENCE   239 AA;  27197 MW;  435F6C983CA4DE38 CRC64;
     MFHEFASWYR RWRFGEGTRI DLVLIGPPGS GKGTQAVKIA ERYKICHLST GDILRAIIAS
     GSELGQKVQK ITESGGLVSD DIVCDLIAQK INSPECKNGL LFDGFPRTLE QAKKLDNLLR
     DRQIHLSAAL EFKLDPTILE KRICGRLFHL ASGRSYHELF NPPKVPMVDD ITGDRLVHRS
     DDKPEALKKR LYEYEKNATP ILHFYESQNK LLRINANKDV NQVFSDIQEL IRLKLAEGR
//
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