ID   TXND3_HELCR             Reviewed;         837 AA.
AC   P90666;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Thioredoxin domain-containing protein 3 homolog;
DE   AltName: Full=Intermediate chain 1;
DE   AltName: Full=NME/NM23 family member 8;
GN   Name=NME8; Synonyms=IC1;
OS   Heliocidaris crassispina (Sea urchin) (Anthocidaris crassispina).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae;
OC   Heliocidaris.
OX   NCBI_TaxID=1043166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 390-403; 561-570 AND
RP   576-590, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=8970153; DOI=10.1091/mbc.7.12.1895;
RA   Ogawa K., Takai H., Ogiwara A., Yokota E., Shimizu T., Inaba K., Mohri H.;
RT   "Is outer arm dynein intermediate chain 1 multifunctional?";
RL   Mol. Biol. Cell 7:1895-1907(1996).
CC   -!- FUNCTION: May be required during the final stages of sperm tail
CC       maturation. May act by reducing disulfide bonds within the sperm
CC       components (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. In sperm, it is a component of the
CC       arm dynein of sperm axoneme. {ECO:0000269|PubMed:8970153}.
CC   -!- DOMAIN: Contains 3 inactive NDK domains that each lack the active His
CC       residue, suggesting that they have no NDP kinase activity.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NDK family.
CC       {ECO:0000305}.
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; D63884; BAA09934.1; -; mRNA.
DR   PIR; T02761; T02761.
DR   AlphaFoldDB; P90666; -.
DR   SMR; P90666; -.
DR   PRIDE; P90666; -.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; IPR023005; Nucleoside_diP_kinase_AS.
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; PS00469; NDP_KINASES; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; Redox-active center; Spermatogenesis.
FT   CHAIN           1..837
FT                   /note="Thioredoxin domain-containing protein 3 homolog"
FT                   /id="PRO_0000120159"
FT   DOMAIN          6..115
FT                   /note="Thioredoxin"
FT   REGION          201..345
FT                   /note="NDK 1"
FT   REGION          355..491
FT                   /note="NDK 2"
FT   REGION          493..629
FT                   /note="NDK 3"
FT   REGION          633..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..799
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..837
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        39..42
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   837 AA;  91624 MW;  20F56ACDC0F19BAE CRC64;
     MPAKKEQIQL QKEILNQEMW DELLSLEGLT VIDVYQKWCG PCAAVLSLFK RLRNEIGDDL
     LRFAVAEADS IETLERYRGK CEPCFLRYGS GQLVNVVRGV NAPALLKNVE RELKQEHKVL
     EEGVERVVIK DPLLAAFEAE EQQAAQAEEL EKKRLEEEAR IKEIKELGDA GEVSVRPVSQ
     GTVDTLMHGR QDGPQTEPVP KEVTVVLIKP DAVANGHVDS IIAKIEEHGF EILTTEDKTL
     TEDEAREFYK QHEEEEHFEV LVTFMASGPS KILVLTRGDT GEGVVSEVRN LLGPKDIEVA
     KEEAPDSLRA QFGTDKKMNA MHGADSKETA AREMAFLLPN FSVPIVPGTG PPPTIEKTLA
     LIRPSALKDH KDEMLQKIQE AGFEVCLQKM VQLTEDQAKE FYKEQEGTPH FEDLIREMTS
     GEVLALGLAK ESAIQSWREF IGPTTIDEAK EKAPDSLRAQ YSIPDTQVNV VHGSDSVDTA
     EKELGFFFPK QTTLAVIKPD AAGEHKEAII EKIKEAGFNI SLQRDVELNK ELASKLYLEH
     EGKEFYENLI DHMSSGLSMV MVLSREDAVD GWRTLMGPTD PDYAREHAPE SLRALLGKDV
     LQNAVHGSSN PEEAKTRIER LFPDVEVLPG GEVKDSVASI SMEQSQVKGE GEEGGEEQTE
     QPAGEGEEQQ AEQPAAESGE QQAEGGEPAT ETATEGGEQQ AEQPPAEGGE KPAEEETQQT
     QEGETPAADE AQAEQTQEGE TPAADEAQAE QTQEGEEQKP AEEEAAPATE ETAAEQAPAA
     EETQQTQEGE EKKEETEQTQ DAPAAGGGEE AVATEGGGEG DAKPEGGEEK TEEQTAS