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Database: UniProt
Entry: A0A665T035_ECHNA
LinkDB: A0A665T035_ECHNA
Original site: A0A665T035_ECHNA 
ID   A0A665T035_ECHNA        Unreviewed;       566 AA.
AC   A0A665T035;
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};
GN   Name=parn {ECO:0000313|Ensembl:ENSENLP00000002674.1};
OS   Echeneis naucrates (Live sharksucker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Echeneidae; Echeneis.
OX   NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000002674.1, ECO:0000313|Proteomes:UP000472264};
RN   [1] {ECO:0000313|Ensembl:ENSENLP00000002674.1}
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; A0A665T035; -.
DR   Ensembl; ENSENLT00000002855.1; ENSENLP00000002674.1; ENSENLG00000001311.1.
DR   Proteomes; UP000472264; 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; 3.30.420.10; 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:UP000472264}.
FT   DOMAIN          179..245
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          141..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  64898 MW;  AEDC227BF9B63DC8 CRC64;
     MEVTRKNYKD SLNTVYSAIE EADFLAIDGE FSGISDGPNV SALTNGLDTP EERYTKLKKH
     SMDFLLFQFG LCTFKYDQAK SKYITKPFNF YIFPKPFNRT SPDIKFICQS SSIDFLASQG
     FDFNKVFCHG IPYLNQDEEA QLREQTEERR NQHANGGGTP SYISPSSSKS PANVPEEHKD
     FINRVIEKVE ALFSNSEKTL DLEPCTGFQR KLIYQTLNWK FPKGLHVETV ETEKKERYIQ
     VIKVDEEERK RREQQKLERE QEELNDAVGF SRVIHAISKS GKLVVGHNML LDVMHTIHQF
     YCSLPEDLQD FKEVTMCVFP RLLDTKLMAS TQPFKELITN TSLAELEKQL KDTPFKSPQV
     ETAAGFPSYD TAQEQLHEAG YDAYITGLCF ISMANYLGSF LTPPKAYISA RSKLIEPFFN
     KLFLMRIIDI PYLNITGPDL QPKRDHVLYV TFPKEWKTSD LYQLFSAFGN IQVSWVDDTS
     AFVSLSQTDQ VQIAMNTSRY AESYRIQTYA EYVQGKQLEK EKLGQTVKSW GEDGWVKSHY
     ASSTTSSGFG FYLWPPVPGQ IECIVD
//
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