ID   MB211_XENLA             Reviewed;         359 AA.
AC   Q6GQD9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Putative nucleotidyltransferase MAB21L1;
DE            EC=2.7.7.- {ECO:0000305};
DE   AltName: Full=Protein mab-21-like 1;
GN   Name=mab21l1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Putative nucleotidyltransferase required for several aspects
CC       of embryonic development including normal development of the eye (By
CC       similarity). It is unclear whether it displays nucleotidyltransferase
CC       activity in vivo. Binds single-stranded RNA (ssRNA) (By similarity).
CC       {ECO:0000250|UniProtKB:O70299, ECO:0000250|UniProtKB:Q13394}.
CC   -!- SUBUNIT: Monomer. Homodecamer; composed of 2 back to back
CC       homopentamers. The protein may exist as monomer in solution and
CC       oiligomerizes upon ligand binding. {ECO:0000250|UniProtKB:Q13394}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O70299}.
CC   -!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
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DR   EMBL; BC072806; AAH72806.1; -; mRNA.
DR   RefSeq; NP_001085465.1; NM_001091996.1.
DR   AlphaFoldDB; Q6GQD9; -.
DR   SMR; Q6GQD9; -.
DR   DNASU; 443891; -.
DR   GeneID; 443891; -.
DR   KEGG; xla:443891; -.
DR   CTD; 443891; -.
DR   Xenbase; XB-GENE-1001182; mab21l1.L.
DR   OMA; AVDKCKY; -.
DR   OrthoDB; 771781at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 443891; Expressed in camera-type eye and 13 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR024810; Mab-21_dom.
DR   Pfam; PF03281; Mab-21; 1.
DR   SMART; SM01265; Mab-21; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT   CHAIN           1..359
FT                   /note="Putative nucleotidyltransferase MAB21L1"
FT                   /id="PRO_0000312785"
FT   BINDING         23..24
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   BINDING         63..66
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   BINDING         73
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N884"
FT   BINDING         75
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N884"
FT   BINDING         248
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
FT   BINDING         252..255
FT                   /ligand="a ribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61557"
FT                   /evidence="ECO:0000250|UniProtKB:Q13394"
SQ   SEQUENCE   359 AA;  40954 MW;  4DD852BF6792F336 CRC64;
     MVAAQAKLVY HLNKYYNEKC QARKAAISKS IREVCKVVSD VLKEVEVQEP RFISSLNEMD
     NRYEGLEVIS PTEFEVVLYL NQMGVFNFVD DGSLPGCAVL KLSDGRKRSM SLWVEFITAS
     GYLSARKIRS RFQTLVAQAV DKCSYRDVVK MVADTSEVKL RIRERYVVQI TPAFKCTGIW
     PRSAAHWPLP HIPWPGPNRV AEVKAEGFNL LSKECHTLAG KQSSAESDAW VLQFAEAENR
     LQLGGCRKKC LSLLKTLRDR HLELPGQPLN NYHMKTLVSY ECEKHPRESD WDESCLGDRL
     NGILLQLISC LQCRRCPHYF LPNLDLFQGK PHSALENAAK QTWRLAREIL TNPKSLEKL