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Database: UniProt
Entry: A0A2K5VR62_MACFA
LinkDB: A0A2K5VR62_MACFA
Original site: A0A2K5VR62_MACFA 
ID   A0A2K5VR62_MACFA        Unreviewed;       578 AA.
AC   A0A2K5VR62;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Poly(A)-specific ribonuclease PARN {ECO:0000256|ARBA:ARBA00015918};
DE            EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
DE   AltName: Full=Polyadenylate-specific ribonuclease {ECO:0000256|ARBA:ARBA00031923};
GN   Name=PARN {ECO:0000313|Ensembl:ENSMFAP00000027221.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000027221.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000027221.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000027221.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the CAF1 family.
CC       {ECO:0000256|ARBA:ARBA00008372}.
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DR   AlphaFoldDB; A0A2K5VR62; -.
DR   STRING; 9541.ENSMFAP00000027221; -.
DR   Ensembl; ENSMFAT00000001405.2; ENSMFAP00000027221.2; ENSMFAG00000044852.2.
DR   VEuPathDB; HostDB:ENSMFAG00000044852; -.
DR   GeneTree; ENSGT00940000153167; -.
DR   Proteomes; UP000233100; Chromosome 20.
DR   Bgee; ENSMFAG00000044852; Expressed in lymph node and 13 other cell types or tissues.
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:InterPro.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   CDD; cd02637; R3H_PARN; 1.
DR   CDD; cd12428; RRM_PARN; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR034042; PARN_R3H.
DR   InterPro; IPR014789; PolyA-riboNase_RNA-binding.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR006941; RNase_CAF1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR15092; POLY A -SPECIFIC RIBONUCLEASE/TARGET OF EGR1, MEMBER 1; 1.
DR   PANTHER; PTHR15092:SF44; POLY(A)-SPECIFIC RIBONUCLEASE PARN; 1.
DR   Pfam; PF04857; CAF1; 1.
DR   Pfam; PF08675; RNA_bind; 1.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT   DOMAIN          117..184
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          499..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  66405 MW;  DAEEBD6D39F7396E CRC64;
     MDFLLFQFGL CTFKYDYTDS KYITKSFNFY VFPKPFNRSS PDVKFVCQSS SIDFLASQGF
     DFNKVFRNGI PYLNQEEERQ LREQYDEKRS QANGAGALSY VSPNTSKCPV TIPEDQKKFI
     DQVVEKIEDL LQSEENKNLD LEPCTGFQRK LIYQTLSWKY PKGIHVETLE TEKKERYIVI
     SKVDEEERKR REQQKHAKEQ EELNDAVGFS RVIHAIANSG KLVIGHNMLL DVMHTVHQFY
     CPLPADLSEF KEMTTCVFPR LLDTKLMAST QPFKDIINNT SLAELEKRLK ETPFSPPKVE
     SAEGFPSYDT ASEQLHEAGY DAYITGLCFI SMANYLGSFL SPPKIHVSAR SKLIEPFFNK
     LFLMRVMDIP YLNLEGPDLQ PKRDHVLHVT FPKEWKTSDL YQLFSAFGNI QISWIDDTSA
     FVSLSQPEQV KIAVNTSKYA ESYRIQTYAE YMGKKQEEKQ IKRKWTEDGW KEADSKRLNP
     QCIPYALQNH YYRSNSFTAP STVGKRNLSP SQEEAGLEDG VSGEISDAEL EQTDSCAEPL
     SEGRKKAKKL KRMKKELSPA GSISMNSPAT LFEVPDTW
//
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