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Database: UniProt
Entry: S7N106_MYOBR
LinkDB: S7N106_MYOBR
Original site: S7N106_MYOBR 
ID   S7N106_MYOBR            Unreviewed;       277 AA.
AC   S7N106;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   20-JUN-2018, entry version 20.
DE   SubName: Full=Deoxyguanosine kinase, mitochondrial {ECO:0000313|EMBL:EPQ09690.1};
GN   ORFNames=D623_10005164 {ECO:0000313|EMBL:EPQ09690.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ09690.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D.,
RA   Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N.,
RA   Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A.,
RA   Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
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DR   EMBL; KE162813; EPQ09690.1; -; Genomic_DNA.
DR   RefSeq; XP_005869481.1; XM_005869419.2.
DR   GeneID; 102255187; -.
DR   KEGG; myb:102255187; -.
DR   CTD; 1716; -.
DR   KO; K00904; -.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019206; F:nucleoside kinase activity; IEA:InterPro.
DR   InterPro; IPR002624; DCK/DGK.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Complete proteome {ECO:0000313|Proteomes:UP000052978};
KW   Kinase {ECO:0000313|EMBL:EPQ09690.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW   Transferase {ECO:0000313|EMBL:EPQ09690.1}.
FT   DOMAIN       41    275       dNK. {ECO:0000259|Pfam:PF01712}.
FT   NP_BIND      45     53       ATP. {ECO:0000256|PIRSR:PIRSR000705-3}.
FT   NP_BIND     202    206       ATP. {ECO:0000256|PIRSR:PIRSR000705-3}.
FT   NP_BIND     254    256       ATP. {ECO:0000256|PIRSR:PIRSR000705-3}.
FT   ACT_SITE    141    141       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000705-1}.
FT   BINDING      70     70       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000705-2}.
FT   BINDING     100    100       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000705-2}.
FT   BINDING     111    111       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000705-2}.
FT   BINDING     142    142       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000705-2}.
FT   BINDING     147    147       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000705-2}.
FT   BINDING     211    211       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000705-2}.
SQ   SEQUENCE   277 AA;  32122 MW;  BB61256699FCA889 CRC64;
     MAAGRRFLRL LRAPSSSMAQ SPLQGVPPSK GLHAGHGPRR LSIEGNIAVG KSSFVKLLTK
     RYPEWHVATE PVASWQNVQA AGPQKAFSTL NPGNLLDLMY REPARWSYTF QTFSFMSRLK
     MQLEPFPEKV LQAKKGVQIF ERSVYSDRYI FAKNLFENGS LNDMEWHIYQ DWHSFLLQEF
     ASRLQLHGFI YLQATPQVCL KRLHRRGREE ERGIELEYLE QLHGQHEAWL VHKTTKLHFE
     TLLNIPVLVL DVSDDFCEDV TKEEEFMEKV NTFVDTL
//
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