MBLC1_BOVIN
ID MBLC1_BOVIN Reviewed; 263 AA.
AC Q2HJB0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) 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}.
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DR EMBL; BC113225; AAI13226.1; -; mRNA.
DR RefSeq; NP_001068680.1; NM_001075212.1.
DR AlphaFoldDB; Q2HJB0; -.
DR SMR; Q2HJB0; -.
DR STRING; 9913.ENSBTAP00000050586; -.
DR PaxDb; Q2HJB0; -.
DR GeneID; 505636; -.
DR KEGG; bta:505636; -.
DR CTD; 255374; -.
DR eggNOG; KOG4736; Eukaryota.
DR InParanoid; Q2HJB0; -.
DR OrthoDB; 1139836at2759; -.
DR Proteomes; UP000009136; Unplaced.
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..263
FT /note="Metallo-beta-lactamase domain-containing protein 1"
FT /id="PRO_0000337026"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4D2B0"
SQ SEQUENCE 263 AA; 27287 MW; 9FEDD3463185A772 CRC64;
MSGLVRTEPL PGETPLLVPG DPYSVVVLLQ GYAEPEGVGD AVRADGSVTL VLPQAWGPAS
SHREPQPYEA KTALEEAARG PILVDTAGPW AREALLGALA GQGVAPGDVT LVVGTHGHSD
HIGNLGLFPG AALLVSHDFC LPGGRYLPHG LGEERPLRLG PGLEVWATPG HGGQRDVSVL
VAGTALGTVM VVGDVFERDG DEGSWQALSE DPVAQKHSRK RILGTADVVV PGHGAPFRVI
REASAPETEP ARSRDGEEPT VHG
