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Database: UniProt
Entry: A0A672Z446_9TELE
LinkDB: A0A672Z446_9TELE
Original site: A0A672Z446_9TELE 
ID   A0A672Z446_9TELE        Unreviewed;       545 AA.
AC   A0A672Z446;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 20.
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};
OS   Sphaeramia orbicularis (orbiculate cardinalfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX   NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005011590.1, ECO:0000313|Proteomes:UP000472271};
RN   [1] {ECO:0000313|Ensembl:ENSSORP00005011590.1}
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; A0A672Z446; -.
DR   Ensembl; ENSSORT00005011975.1; ENSSORP00005011590.1; ENSSORG00005002752.1.
DR   Proteomes; UP000472271; Unplaced.
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; 3.30.1370.50; R3H-like domain; 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:UP000472271}.
FT   DOMAIN          179..245
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          143..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  62867 MW;  D5DAD730EB6E8333 CRC64;
     MEVTRKNYKD CLNTVYSAIE EADFLAIDGE FSGISDGPNV SALTNGLDTP EERYTKLKKH
     SMDFLLFQFG LCTFKYDQTQ SKYITKPFNF YVFPKPFNRT SPDIKFICQS SSIDFLASQG
     FDFNKVFCHG IPYLNKEEEA QLREQTEERR NQHANGVGTP SYISPSSSKS PAHVPDEHKV
     FINKVVEKVE ALFTNSDKTL DLEPCTGFQR KLIYQTLNWK FPKGLHVETM ETEKKERYIQ
     VSKVDEEERK RREQQKLERE QEELNDAVGF SRVIHAISKS GKLVVGHNML LDVMHTIHQF
     YCPLPELLFY LFVFQELITN TSLYTVISRK TAEGFPSYDT AQEQLHEAGY DAYITGLCFI
     SMANYLGSFL TPPKAYISAR SKLIEPFFNK LFLMRIIDIP YLNITGPDLQ PKRDHVLYVT
     FPKEWKTSDL YQLFSAFGNI QVSWIDDTSA FVSLSQTDQV QIAMNTSRYA ESYRIQTYAE
     YVQGKQQDKE KLGQPAKSWG EGSWVKPHYT AGGISNYYHK RTDNHVKHIG SGWLLPKSES
     CNWIN
//
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