ID   TXND6_XENLA             Reviewed;         625 AA.
AC   Q6IRC5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Thioredoxin domain-containing protein 6 {ECO:0000305};
DE   AltName: Full=Thioredoxin-like protein 2;
DE            Short=Txl-2;
GN   Name=nme9 {ECO:0000312|Xenbase:XB-GENE-5862245};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH70973.1};
RN   [1] {ECO:0000312|EMBL:AAH70973.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH70973.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=33263282; DOI=10.7554/elife.58662;
RA   Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA   Marcotte E.M., Wallingford J.B.;
RT   "Functional partitioning of a liquid-like organelle during assembly of
RT   axonemal dyneins.";
RL   Elife 9:0-0(2020).
CC   -!- FUNCTION: May be a regulator of microtubule physiology.
CC       {ECO:0000250|UniProtKB:Q86XW9}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:Q86XW9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:33263282}. Dynein axonemal particle
CC       {ECO:0000269|PubMed:33263282}. Note=Associated with microtubules.
CC       Detected in cilia of lung epithelium, and associated with the spermatid
CC       tail and manchette (By similarity). {ECO:0000250|UniProtKB:A0A1L1SUL6}.
CC   -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR   EMBL; BC070973; AAH70973.1; -; mRNA.
DR   RefSeq; NP_001085047.1; NM_001091578.1.
DR   AlphaFoldDB; Q6IRC5; -.
DR   SMR; Q6IRC5; -.
DR   GeneID; 432114; -.
DR   KEGG; xla:432114; -.
DR   CTD; 432114; -.
DR   Xenbase; XB-GENE-5862245; nme9.L.
DR   OrthoDB; 971216at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 432114; Expressed in testis and 14 other tissues.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB.
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:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.70.141; -; 3.
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   Pfam; PF00334; NDK; 3.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 3.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54919; SSF54919; 3.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..625
FT                   /note="Thioredoxin domain-containing protein 6"
FT                   /id="PRO_0000452447"
FT   REGION          158..302
FT                   /note="NDK"
FT   REGION          594..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  70243 MW;  1C0947344FDF3DAB CRC64;
     MAGKKRESSL QIALSNQEQW EEALSTKGLQ VVDVYQAWCG PCKPTVSLFR KIKNELGDDL
     LHFAVAESDT IDSLVKYRGK CEPTFLFLAG GELVAVVRGA NGPLLQKTII EQLAAEKKVL
     NQGSERHVIK DEVLLEEEDE IAPVQAQTED EELVPSGKSY TVAIIKPDAV AHGKTDEIIM
     KIQESGFEIL ANEERTMTES EAREFYQHRA GEEKFQELIQ FMSSGPCHIL IISKSEEDED
     VIPAWREFIG PTDVEIAKKE KPESLRAQYG TEVLYNAVHG SNDREQASRE LAFFFPNFKI
     SNESLKELTS VKPERTLALI RPEILKERKD EILQSIKDAG FSIAMQKEVM LTEHQVQEFY
     KEHINEDYYP ALLKQMTSGP VLALALVKDN AVGHWRNMLG PASLSQALSE APDSLRAQFA
     PSDSETNQLH GSSTTEEAKK EINFFFPVEH TLATIKPDAL EEHRDEILEQ IQGAGFTISQ
     IKEANLNREM AEEFYKEHKG KPFFEQLVNY MCRGPCLMMI LSKENAVHEW RSLMGPTDPA
     EAQKVLPDSL RGKFAKSILQ NAVHGSSNSD HAMEKIKFIF GDIDLDRIVH ESFGETPETS
     ASDISRNAAA QGDDPEQDES KEMEE