ID   L5M4D6_MYODS            Unreviewed;       351 AA.
AC   L5M4D6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Thioredoxin domain-containing protein 6 {ECO:0000313|EMBL:ELK33192.1};
GN   ORFNames=MDA_GLEAN10020944 {ECO:0000313|EMBL:ELK33192.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK33192.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142,
CC       ECO:0000256|RuleBase:RU004011}.
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DR   EMBL; KB104502; ELK33192.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5M4D6; -.
DR   eggNOG; KOG0888; Eukaryota.
DR   eggNOG; KOG0907; Eukaryota.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   CDD; cd04416; NDPk_TX; 1.
DR   CDD; cd02948; TRX_NDPK; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR   InterPro; IPR034907; NDK-like_dom.
DR   InterPro; IPR036850; NDK-like_dom_sf.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46135; NME/NM23 FAMILY MEMBER 8; 1.
DR   PANTHER; PTHR46135:SF1; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 6; 1.
DR   Pfam; PF00334; NDK; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT   DOMAIN          158..302
FT                   /note="Nucleoside diphosphate kinase-like"
FT                   /evidence="ECO:0000259|SMART:SM00562"
FT   REGION          133..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  39061 MW;  12F9FE651577B516 CRC64;
     MGSKKKEIAL QVNISTQELW EEMLSSKGLT VIDVYQGWCG PCKPVVSLFQ KMRIEVGLDL
     LHFALAEADC LDVLEKYRGR CEPTFLFYAG GKLVAVVRGA NAPLLQKTIL DQLEAERKVL
     AEGRERKVIK DEALSEEEER FPHEKDGGED ADVASSEKTC TLAIIKPDAV GHGKTDEIIM
     KIQEAGFDII TSEERTMTEA EMRLFYQHRS GEEAFEKLVH HMCSGPSHLL ILTRTEDTED
     VATAWRALMG PCDPHVARRE QPDSLRAQYG TEVPFNAVHG SRDAEAARRE LALLFPSFTF
     ADHVREAALV CGTEDWDGAV SGIPQSVCRP TEREEGVVGP TEVLPFPEDV H
//