ID M1KI21_ENCCN Unreviewed; 493 AA. AC M1KI21; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 03-MAY-2023, entry version 35. DE RecName: Full=poly(A)-specific ribonuclease {ECO:0000256|ARBA:ARBA00012161}; DE EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161}; DE AltName: Full=Carbon catabolite repressor protein 4 {ECO:0000256|ARBA:ARBA00030493}; DE AltName: Full=Cytoplasmic deadenylase {ECO:0000256|ARBA:ARBA00031469}; DE AltName: Full=Glucose-repressible alcohol dehydrogenase transcriptional effector {ECO:0000256|ARBA:ARBA00033317}; GN ORFNames=ECU11_0770 {ECO:0000313|EMBL:AGE94876.1}; OS Encephalitozoon cuniculi (Microsporidian parasite). OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae; OC Encephalitozoon. OX NCBI_TaxID=6035 {ECO:0000313|EMBL:AGE94876.1}; RN [1] {ECO:0000313|EMBL:AGE94876.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23376943; DOI=10.1128/EC.00307-12; RA Selman M., Sak B., Kvac M., Farinelli L., Weiss L.M., Corradi N.; RT "Extremely Reduced Levels of Heterozygosity in the Vertebrate Pathogen RT Encephalitozoon cuniculi."; RL Eukaryot. Cell 12:496-502(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; CC Evidence={ECO:0000256|ARBA:ARBA00001663}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. CC {ECO:0000256|ARBA:ARBA00010774}. 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; KC513604; AGE94876.1; -; Genomic_DNA. DR AlphaFoldDB; M1KI21; -. DR SMR; M1KI21; -. DR VEuPathDB; MicrosporidiaDB:AEWD_110760; -. DR VEuPathDB; MicrosporidiaDB:AEWQ_110760; -. DR VEuPathDB; MicrosporidiaDB:AEWR_110760; -. DR VEuPathDB; MicrosporidiaDB:ECU11_0770; -. DR VEuPathDB; MicrosporidiaDB:M970_110760; -. DR OMA; NIDGCAM; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. 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 PANTHER; PTHR12121; CARBON CATABOLITE REPRESSOR PROTEIN 4; 1. DR PANTHER; PTHR12121:SF34; POLY(A)-SPECIFIC RIBONUCLEASE; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR Pfam; PF13855; LRR_8; 1. DR SMART; SM00369; LRR_TYP; 3. DR SUPFAM; SSF56219; DNase I-like; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR PROSITE; PS51450; LRR; 2. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022839}; KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}. FT DOMAIN 175..448 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" SQ SEQUENCE 493 AA; 56489 MW; C8C4E4A040A1D52D CRC64; MAEECLVSRK KFGGKAMEVR SEMWTGLDLC SQGIKNISKS LFDMRFIRTL NLANNEIEVI PREICNLRHL EVLNLSKNKI RSIPPEIGKI VSLRELNLSD NLISNIPMEM GTLYNLEVFE IANNPLIVPF NTLIRDKKLL QFCREHNTGY PPPNDRLWIE CTGKNVFYGD TVSVGTFNIL SNIYATRMTY APSWVINSEF RREGVLQEIV LYNVDILCLQ EIELYSFFDF YKEQLEMRCN YDSIIYPRGR VKSVPDKKNV DGCAIFWRRS KFRLIAQFPI DFHQKVIQDT RFNTNQELLD RYGKKDNIAI GALLERPNGQ QVLVMNTHIF WDPDYPDIKL LQVLLLVEEI KRVSSRHPNA CLLLQGDFNS LRSSSVYKSI TTPVIDFADF GDTMQHLSNQ QFGDGLGLND AYSNQDLGFT NFTPGFKGVI DYIFYGGGIS LASVLSPVED EYTENVAGLP NMHFPSDHIF LGAKFAFPNK NISQNAFGRN SRQ //