ID   TF3A_XENBO              Reviewed;         339 AA.
AC   P17842;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Transcription factor IIIA;
DE            Short=TFIIIA;
GN   Name=gtf3a;
OS   Xenopus borealis (Kenyan clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=2110661; DOI=10.1093/nar/18.8.2117;
RA   Gaskins C.J., Hanas J.S.;
RT   "Sequence variation in transcription factor IIIA.";
RL   Nucleic Acids Res. 18:2117-2123(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=2331751; DOI=10.1016/0092-8674(90)90809-s;
RA   Joho K.E., Darby M.K., Crawford E.T., Brown D.D.;
RT   "A finger protein structurally similar to TFIIIA that binds exclusively to
RT   5S RNA in Xenopus.";
RL   Cell 61:293-300(1990).
CC   -!- FUNCTION: Involved in ribosomal large subunit biogenesis (By
CC       similarity). Interacts with the internal control region (ICR) of
CC       approximately 50 bases within the 5S RNA genes, is required for correct
CC       transcription of these genes by RNA polymerase III (By similarity).
CC       Also binds the transcribed 5S RNA's (PubMed:2331751).
CC       {ECO:0000250|UniProtKB:P03001, ECO:0000250|UniProtKB:Q92664,
CC       ECO:0000269|PubMed:2331751}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Synthesized in oocytes and, in much lower levels,
CC       in somatic cells.
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DR   EMBL; X17695; CAA35689.1; -; mRNA.
DR   EMBL; M32472; AAA49713.1; -; mRNA.
DR   PIR; B34895; B34895.
DR   AlphaFoldDB; P17842; -.
DR   SMR; P17842; -.
DR   PRIDE; P17842; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 6.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Ribosome biogenesis;
KW   RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..339
FT                   /note="Transcription factor IIIA"
FT                   /id="PRO_0000047084"
FT   ZN_FING         13..37
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         43..67
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         73..98
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         105..129
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         135..159
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         162..188
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         192..214
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         221..246
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         252..276
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          275..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        222
FT                   /note="C -> R (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="E -> A (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="R -> K (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="S -> N (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="A -> G (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="G -> D (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="V -> A (in Ref. 2; AAA49713)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   339 AA;  39202 MW;  A4D006C537961599 CRC64;
     MGEKALPVVY KRYICSFADC GASYNKNWKL RAHLCKHTGE KPFPCKEEGC DKGFTSLHHL
     TRHSITHTGE KNFKCDSDKC DLTFTTKANM KKHFNRFHNL QLCVYVCHFE GCDKAFKKHN
     QLKVHQFTHT QQLPYKCPHE GCDKSFSVPS CLKRHEKVHA GYPCKKDDSC LFVGKTWTLY
     LKHVKECHQE PVMCDECKRT FKHKDYLRNH KKTHKKERTV YCCPRDGCER SYTTEFNLQS
     HMQSFHEEQR PFACEHAECG KSFAMKKSLE RHSVVHDPEK RKLKEKCPRP KRSLASRLSG
     CAPPKSKEKS AAKATEKTGS VVKNKPSGTE TKGSLVIEK