CN6LB_XENLA
ID CN6LB_XENLA Reviewed; 550 AA.
AC Q5XH73;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=CCR4-NOT transcription complex subunit 6-like-B;
DE EC=3.1.13.4 {ECO:0000250|UniProtKB:Q96LI5};
GN Name=cnot6l-b;
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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Poly(A) nuclease with 3'-5' RNase activity. Catalytic
CC component of the CCR4-NOT complex which is one of the major cellular
CC mRNA deadenylases and is linked to various cellular processes including
CC bulk mRNA degradation, miRNA-mediated repression, translational
CC repression during translational initiation and general transcription
CC regulation. Additional complex functions may be a consequence of its
CC influence on mRNA expression (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000250|UniProtKB:Q96LI5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96LI5};
CC Note=Binds 2 magnesium ions, but the ions interact each with only 1 or
CC 2 residues. {ECO:0000250|UniProtKB:Q96LI5};
CC -!- SUBUNIT: Component of the CCR4-NOT complex.
CC {ECO:0000250|UniProtKB:Q96LI5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96LI5}. Nucleus
CC {ECO:0000250|UniProtKB:Q96LI5}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q96LI5}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; BC084200; AAH84200.1; -; mRNA.
DR RefSeq; NP_001088222.1; NM_001094753.1.
DR AlphaFoldDB; Q5XH73; -.
DR SMR; Q5XH73; -.
DR DNASU; 495050; -.
DR GeneID; 495050; -.
DR KEGG; xla:495050; -.
DR CTD; 495050; -.
DR Xenbase; XB-GENE-977554; cnot6l.S.
DR OMA; DHFLMLT; -.
DR OrthoDB; 724242at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 495050; Expressed in egg cell and 19 other tissues.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd10312; Deadenylase_CCR4b; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR034967; Deadenylase_CCR4b.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS51450; LRR; 4.
PE 2: Evidence at transcript level;
KW Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat; Magnesium;
KW Metal-binding; mRNA processing; Nuclease; Nucleus; Reference proteome;
KW Repeat; RNA-mediated gene silencing; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..550
FT /note="CCR4-NOT transcription complex subunit 6-like-B"
FT /id="PRO_0000314590"
FT REPEAT 52..73
FT /note="LRR 1"
FT REPEAT 75..96
FT /note="LRR 2"
FT REPEAT 98..120
FT /note="LRR 3"
FT REPEAT 121..143
FT /note="LRR 4"
FT REGION 1..148
FT /note="Required for interaction with cnot1, cnot3 and
FT cnot7"
FT /evidence="ECO:0000250"
FT REGION 153..550
FT /note="Nuclease domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 405
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 405
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
SQ SEQUENCE 550 AA; 62625 MW; 58213E8057FB6951 CRC64;
MPKEKYDPPD PRRIYTIMSA EEVANGKKSR WDELEISGRV RSLSMSLWSL THLTVLHLSD
NNLSRIPPDI AKLHNLVYLD LSSNKLRSLP AELGNVVSLR ELLLNNNLLR VLPFELGRLF
RLQTLGLKGN PLSQDILGLY QEPDGMRKLL NYMLDNLSVH PEQLPQRPWI TLKERDQILP
SVPFTVMCFN VLCDKYATRQ LYGYCPSWAL NWEYRKKGIM EEIVSCDADI ISLQEVETEQ
YYTLFMPALK ERGYDGFFSP KSRAKIMSDQ EKKHVDGCAI FFRTEKFSLV QKHTVEFNQI
AMANSEGSEA MLNRVMTKDN IGVSVLLEVH TDFSGAGMKP HHSSEKQLLM VANAHMHWDP
EYSDVKLIQT MMFVSELKSI IEKAASRPGS PTPDSNSIPF VLCADLNSLP DSGVVEYLTN
GGVADNHKDF KELRYNECLT NFSCNGKNGT PDGRITHGFQ LRSAYENNLM PYTNYTFDFK
GVIDYIFYSK THIDVLGVLG PLDPQWMMDN NIAGCPHPHI PSDHFSLLTQ LELHPPFLPV
INGVHLPSRR
