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Database: UniProt
Entry: K2ND09_TRYCR
LinkDB: K2ND09_TRYCR
Original site: K2ND09_TRYCR 
ID   K2ND09_TRYCR            Unreviewed;       266 AA.
AC   K2ND09;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Adenylate kinase, putative {ECO:0000313|EMBL:EKF32776.1};
GN   ORFNames=MOQ_003370 {ECO:0000313|EMBL:EKF32776.1};
OS   Trypanosoma cruzi marinkellei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF32776.1, ECO:0000313|Proteomes:UP000007350};
RN   [1] {ECO:0000313|EMBL:EKF32776.1, ECO:0000313|Proteomes:UP000007350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:EKF32776.1,
RC   ECO:0000313|Proteomes:UP000007350};
RX   PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA   Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA   Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA   Andersson B.;
RT   "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT   with the bat-restricted subspecies T. cruzi marinkellei.";
RL   BMC Genomics 13:531-531(2012).
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:EKF32776.1}.
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DR   EMBL; AHKC01009609; EKF32776.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2ND09; -.
DR   EnsemblProtists; EKF32776; EKF32776; MOQ_003370.
DR   OrthoDB; 141498at2759; -.
DR   Proteomes; UP000007350; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043227; C: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; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR036193; ADK_active_lid_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF253; KINASE, PUTATIVE-RELATED; 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.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007350};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT   DOMAIN          123..157
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
SQ   SEQUENCE   266 AA;  30436 MW;  D3BF8562CB3DB6D1 CRC64;
     MHLFVLGPPG SGKTSISTVL KERYGVCHVT PSDAVSHAVE YVGSAFGDQL RLLEEGKPIP
     DWLLTRVVAE ATRGPDCSNG FLLDDFPKTA EQARLLNEEG VKPDAIVLLN FADHLLIERF
     CGRWVHPVSG RMYHTLYDPP KVKGRDDVTG QPLVQRPEDS EDTVRERLAN FHQNLKALRL
     VYSDERLWHT VDGYAAVDTV HRSICRILDP ILASRKRRWW SFFFHIRMNQ TAGSPLLLFF
     FLNGDDVKYA FFLKLLLYPF CWVRHS
//
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