MBLC1_XENLA
ID MBLC1_XENLA Reviewed; 233 AA.
AC Q498J9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Metallo-beta-lactamase domain-containing protein 1;
DE EC=3.1.27.- {ECO:0000250|UniProtKB:A4D2B0};
DE AltName: Full=Endoribonuclease MBLAC1 {ECO:0000250|UniProtKB:A4D2B0};
GN Name=mblac1;
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 (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that catalyzes the hydrolysis of histone-
CC coding pre-mRNA 3'-end. Involved in histone pre-mRNA processing during
CC the S-phase of the cell cycle, which is required for
CC entering/progressing through S-phase. Cleaves histone pre-mRNA at a
CC major and a minor cleavage site after the 5'-ACCCA-3' and the 5'-
CC ACCCACA-3' sequence, respectively, and located downstream of the stem-
CC loop. May require the presence of the HDE element located at the
CC histone pre-RNA 3'-end to avoid non-specific cleavage.
CC {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end
CC ribonucleotide-RNA + a 5'-end (5'-phospho)-ribonucleoside-RNA + H(+);
CC Xref=Rhea:RHEA:68096, Rhea:RHEA-COMP:15179, Rhea:RHEA-COMP:17355,
CC Rhea:RHEA-COMP:17428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:138282, ChEBI:CHEBI:173118;
CC Evidence={ECO:0000250|UniProtKB:A4D2B0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68097;
CC Evidence={ECO:0000250|UniProtKB:A4D2B0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:A4D2B0};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:A4D2B0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A4D2B0}. Nucleus {ECO:0000250|UniProtKB:A4D2B0}.
CC Note=Localizes in the nucleus during early S-phase of the cell cycle.
CC {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- DOMAIN: Contains four of the five characteristic MBL-fold metal-binding
CC motifs, with two waters completing metal coordination.
CC {ECO:0000250|UniProtKB:A4D2B0}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00189.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC100188; AAI00189.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q498J9; -.
DR SMR; Q498J9; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0008334; P:histone mRNA metabolic process; ISS:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR039344; MBLAC1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR23200; PTHR23200; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..233
FT /note="Metallo-beta-lactamase domain-containing protein 1"
FT /id="PRO_0000337030"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
SQ SEQUENCE 233 AA; 24765 MW; 78E8CE374FDB1E79 CRC64;
MASLQANATS SLQYQTAPLE SSHIPGSPHS VHVLLEGYSK DVGGDLFQAD GSVTLIQGPL
TVLVDTAGPW SRDSLLQSLQ NQGVAPADVT HVICTHGHSD HVGNLNLFSH AEILVSYDLW
RNGYYVAHDF RAGVPYVLPG GEGLEVVATP GHTGSDISLL VPGTSLGTVV VAGDLFEREG
DGDSWQPLSE DPERQEDSRA AILKVADVII PGHGPPFRVI KHGQLAQQET KNN
