ID A0A0K0F2H4_STRVS Unreviewed; 749 AA.
AC A0A0K0F2H4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
OS Strongyloides venezuelensis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0300300.1};
RN [1] {ECO:0000313|Proteomes:UP000035680}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A, De Silva N.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SVE_0300300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A0K0F2H4; -.
DR STRING; 75913.A0A0K0F2H4; -.
DR WBParaSite; SVE_0300300.1; SVE_0300300.1; SVE_0300300.
DR Proteomes; UP000035680; Unassembled WGS sequence.
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 GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; SM00364; LRR_BAC; 3.
DR SMART; SM00369; LRR_TYP; 2.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF52075; Outer arm dynein light chain 1; 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:ARBA00022801};
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 Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 391..725
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 86875 MW; 2B7F4C8E6BB56DD9 CRC64;
MSESNNDDKD NTKNSQNDDS TNDKNDAVPK ILSLRNLREN DEFKQLCFDN SYNDKRLSSN
LEGPSNRRTP INEGDERLYP FNVSNSLRSK NNSPLIKDSE SKSIYRNAFM SLVTGNLEKN
VNNCYSNDVL NNQCFDGSQK VRRYEYPDDM TTGHKIYSHF PYPEALSDTF QGKLEYPMGN
VTHHYIGIRC IESQQIDKGF NNEVNDCDKD TLIKYLCKNR IPYPNGICQG ISIACGLKVL
PNYVFDNIKT SYITTICLSN NLLTSIPESI GLMRNLKYLD VSYNKLVTLP KSLSKCYNLV
TLDVSNNLIV QFPDNLGLLK KKLEVFSIYN NPLRHDLMHV LTSSDPGKVM LEILQKRFYS
KQVPPPRRDW HFLTQVKTGD NHPNLPFISV MTYNILSYKY LFNNRFNYCP DEELKWEYRK
AVVFEEIFHY SPSIVTMQEV PKGDYESYFH PKLCENGYDG LFFPKSRIKK TKDELTQHVD
GCAIFWQKPL FSYVLHFDIE FKSMVDELFN DDDEMSRRVQ AFDNVALIVV LTIKGEQREG
ESETTAVPNG IYCRPLVVAT THIHWDPDYA DVKLIQSMLL MKSLYDRRRY IANQLRCDIE
EIPIIVTGDF NSRPNSSVLE YIRRKQLPKD DDGLMLFKNC EKLNRISSNP RDFHYYHHGL
KDLEMVDMSR YQFTNFTPEF ADIIDYIFFT SSTISACGII EPPSAEWIKN SEVIGFPHPH
FPSDHIPIVA NFYINNNDNN GIIPNPQQQ
//
