ID   TSP1L_DANRE             Reviewed;         316 AA.
AC   Q4KM14;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=tRNA selenocysteine 1-associated protein 1-like;
DE   AltName: Full=tRNA selenocysteine 1-associated protein 1;
DE   AltName: Full=tRNA selenocysteine-associated protein 1;
GN   Name=trnau1apl; Synonyms=secp43, trnau1ap, trspap1;
GN   ORFNames=zgc:113964, zgc:77884;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the early steps of selenocysteine biosynthesis
CC       and tRNA(Sec) charging to the later steps resulting in the
CC       cotranslational incorporation of selenocysteine into selenoproteins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRM TRSPAP family. {ECO:0000305}.
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DR   EMBL; BC098884; AAH98884.1; -; mRNA.
DR   AlphaFoldDB; Q4KM14; -.
DR   SMR; Q4KM14; -.
DR   STRING; 7955.ENSDARP00000073432; -.
DR   PaxDb; Q4KM14; -.
DR   ZFIN; ZDB-GENE-040426-2386; trnau1apb.
DR   eggNOG; KOG0118; Eukaryota.
DR   InParanoid; Q4KM14; -.
DR   PhylomeDB; Q4KM14; -.
DR   PRO; PR:Q4KM14; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   CDD; cd12612; RRM2_SECp43; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034510; SECp43_RRM2.
DR   InterPro; IPR040434; TSAP1.
DR   InterPro; IPR041085; TSAP1_C.
DR   PANTHER; PTHR37457; PTHR37457; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   Pfam; PF17654; Trnau1ap; 1.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Protein biosynthesis; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..316
FT                   /note="tRNA selenocysteine 1-associated protein 1-like"
FT                   /id="PRO_0000304921"
FT   DOMAIN          6..89
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          99..178
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          239..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..273
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   316 AA;  35853 MW;  DDE467B505257372 CRC64;
     MFNRMTSLWM GDLDPYMDEN FIKQAFSTMG ETAFGVKIIT HRVTGGSAGY CFVEMADEAS
     VDRCVQRLNG KLVPGSNPPR KFKLNYATYG KRPEPGPEFS VFVGDLTSEV DDYQLHQFFL
     KKFPSCKGAK VVTDPYGNSR GYGFVKFSDE NEQKKALEEF QNASGLGGKP IRISIAVNKG
     NKASTYHNQN NTYNTNYQQQ YYRQPYNSYY PQWGYDQYSG YNYGYNPYAA PPPMMGPPPP
     MGMPPMPPDM QGSTEAHDGT EEVEEDPSED PNPQVDVEEL NRQYMERSEE LYDSLMECHW
     LPMDTITSDI SMMNGS