位置:首页 > 蛋白库 > MBLC1_RAT
MBLC1_RAT
ID   MBLC1_RAT               Reviewed;         251 AA.
AC   Q6AYD1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC079097; AAH79097.1; -; mRNA.
DR   RefSeq; NP_001020167.1; NM_001024996.1.
DR   AlphaFoldDB; Q6AYD1; -.
DR   SMR; Q6AYD1; -.
DR   STRING; 10116.ENSRNOP00000001831; -.
DR   jPOST; Q6AYD1; -.
DR   PaxDb; Q6AYD1; -.
DR   GeneID; 304346; -.
DR   KEGG; rno:304346; -.
DR   UCSC; RGD:1306932; rat.
DR   CTD; 255374; -.
DR   RGD; 1306932; Mblac1.
DR   eggNOG; KOG4736; Eukaryota.
DR   HOGENOM; CLU_030571_2_6_1; -.
DR   InParanoid; Q6AYD1; -.
DR   OMA; FPGQPYS; -.
DR   OrthoDB; 1139836at2759; -.
DR   PhylomeDB; Q6AYD1; -.
DR   TreeFam; TF316508; -.
DR   PRO; PR:Q6AYD1; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001357; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6AYD1; RN.
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:0031124; P:mRNA 3'-end processing; ISO:RGD.
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..251
FT                   /note="Metallo-beta-lactamase domain-containing protein 1"
FT                   /id="PRO_0000337029"
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="1"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:A4D2B0"
SQ   SEQUENCE   251 AA;  26137 MW;  49FDECF42EE41C02 CRC64;
     MSGPVRTEPL HGETPLLASS GSYSVVVLLR GYAEPQGVGD AVRADGTVTL VLPRGWVSDT
     SRRLAPSADG GAKTALEEAV RGPILVDTGG PWTRDALLEA LATQGVAPGD VTLVVGTHGH
     SDHIGNLGLF PQAALLVSHD FCLPGGLYLP HGLCETQPLI LGSGLQVWAT PGHGGQRDVS
     VVVEGTSLGT VVVVGDVFER LGDEDSWQDL SEDPVAQQRS RERILSVADV VVPGHGAPFR
     VVREAVKSSE D
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024