ID   D0A6H7_TRYB9            Unreviewed;      1017 AA.
AC   D0A6H7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Adenylate kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TbgDal_XI3960 {ECO:0000313|EMBL:CBH17278.1};
OS   Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=679716 {ECO:0000313|EMBL:CBH17278.1, ECO:0000313|Proteomes:UP000002316};
RN   [1] {ECO:0000313|Proteomes:UP000002316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/CI/86/DAL972 {ECO:0000313|Proteomes:UP000002316};
RX   PubMed=20404998; DOI=10.1371/journal.pntd.0000658;
RA   Jackson A.P., Sanders M., Berry A., McQuillan J., Aslett M.A., Quail M.A.,
RA   Chukualim B., Capewell P., MacLeod A., Melville S.E., Gibson W.,
RA   Barry J.D., Berriman M., Hertz-Fowler C.;
RT   "The genome sequence of Trypanosoma brucei gambiense, causative agent of
RT   chronic human african trypanosomiasis.";
RL   PLoS Negl. Trop. Dis. 4:E658-E658(2010).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN554974; CBH17278.1; -; Genomic_DNA.
DR   RefSeq; XP_011779542.1; XM_011781240.1.
DR   AlphaFoldDB; D0A6H7; -.
DR   GeneID; 23867381; -.
DR   KEGG; tbg:TbgDal_XI3960; -.
DR   VEuPathDB; TriTrypDB:Tbg972.11.3960; -.
DR   OrthoDB; 5483389at2759; -.
DR   Proteomes; UP000002316; Chromosome 11.
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; cd22967; DD_AK7; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like 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; IPR036291; NAD(P)-bd_dom_sf.
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; SSF51735; NAD(P)-binding Rossmann-fold domains; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          189..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          913..967
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        196..212
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1017 AA;  115206 MW;  4C17C70483729E8A CRC64;
     MSVEEVSCLS EDFASRTTTS VLILYADTYF GRRMFQQFYG RKSKTGTCYR INACMWSESS
     VENFIDYCDT LPFQMGHSFR SRQSLPTVID LGTQAEKANL GSTIDGGATQ GPDNADGTSH
     QLNVFWRRNG PKLHQAVLAS DLIVVELRSA QDVFDIVHLL TTKILRKTKR LILVSSLLTW
     YATPPLQRES VEEVNGETDS VENEEEGEHH EEEQEEVQQP MKPDEVEALL GPLEVAEDDY
     ENSPLEGEAE GELELLTEDQ YNRRIPHAKY FNWREAERVV ASANSDDRHL QTCVVFAGLT
     YGEGEDVMES FFRQVWSREE HGLPIYGSGS QIVPCVHIRD LVTFAQRLLE AAAPPTSRYV
     FATDNSNVSW RRMVLALNRA FGGEKTFHVP PSEYLLHKNV ELFTMNLRVE NSTMNEMMDE
     SDWAARGGFV DSIDKVAHEF IESHNLQPIR ILILGPPLSG KTALSGAVAK RHYHVPTFTI
     EQVREEYKEH IEILKSRLAK FRQCLHEREK TRREEAKKRA FLRPRNKPEV KEEEEDDQNA
     MGETQQQPTA SPDSGRQGNM ESTRLVDCST TVAEDDVDGK AVDFSLNEEE MQNVEALVDD
     WYQGNERAIQ IRDTIASMER VLSMRIRVQP PSSNDPLGSS NPKKRKEGTK QKRVAKVVNK
     KPVAEEEEHN PVQQESAPFQ DKALACMVRW RLSRPDCRNQ GYVLDGFPET VEQARLVFGQ
     TPLELPENNE DTVISLPSAP AGSGGYARTA VVRHSASLSA NAPPESTELC DEDRLPDFVF
     VLTAPDNYLL DRLTAVSKIS GETGSTEEKC LRRFEAAMAN YQQQYTNAEY TLPNFFETAS
     TVAKVLTPGG RTPTVLAVDV SGQPLLPPPP PESDFAVPEP GQLEKLLCAY VGPSHTLGLS
     PKQLFDEEIR ARNLEMEERK KEMRAITEQY ERELRECMME SEQRSVVEDA RRAIDLADRE
     ALEERKRPLR MYLNHNIMPL LSKGLVEVCK RRPVDPVDFL AEWLMLHNPH DDSCFEL
//