ID A0AAE0SBW6_9BIVA Unreviewed; 1284 AA. AC A0AAE0SBW6; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 02-OCT-2024, entry version 3. DE RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2 {ECO:0000256|HAMAP-Rule:MF_03182}; DE EC=3.1.13.4 {ECO:0000256|HAMAP-Rule:MF_03182}; DE AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease {ECO:0000256|HAMAP-Rule:MF_03182}; DE AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2 {ECO:0000256|HAMAP-Rule:MF_03182}; DE Short=PAN deadenylation complex subunit 2 {ECO:0000256|HAMAP-Rule:MF_03182}; GN Name=PAN2 {ECO:0000256|HAMAP-Rule:MF_03182}; GN ORFNames=CHS0354_007971 {ECO:0000313|EMBL:KAK3589026.1}; OS Potamilus streckersoni. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Heteroconchia; Palaeoheterodonta; Unionida; Unionoidea; OC Unionidae; Ambleminae; Lampsilini; Potamilus. OX NCBI_TaxID=2493646 {ECO:0000313|EMBL:KAK3589026.1, ECO:0000313|Proteomes:UP001195483}; RN [1] {ECO:0000313|EMBL:KAK3589026.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CHS0354 {ECO:0000313|EMBL:KAK3589026.1}; RX PubMed=33570560; DOI=10.1093/gbe/evab029; RA Smith C.H.; RT "A High-Quality Reference Genome for a Parasitic Bivalve with Doubly RT Uniparental Inheritance (Bivalvia: Unionida)."; RL Genome Biol. Evol. 13:evab029-evab029(2021). RN [2] {ECO:0000313|EMBL:KAK3589026.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CHS0354 {ECO:0000313|EMBL:KAK3589026.1}; RC TISSUE=Mantle {ECO:0000313|EMBL:KAK3589026.1}; RA Smith C.H.; RT "Developing a high-quality reference genome for a parasitic bivalve with RT doubly uniparental inheritance (Bivalvia: Unionida)."; RL Genome Biol. Evol. 0:0-0(2021). RN [3] {ECO:0000313|EMBL:KAK3589026.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CHS0354 {ECO:0000313|EMBL:KAK3589026.1}; RC TISSUE=Mantle {ECO:0000313|EMBL:KAK3589026.1}; RA Smith C.H.; RL Submitted (MAY-2023) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation CC complex, one of two cytoplasmic mRNA deadenylases involved in general CC and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) CC tails of RNA and the activity is stimulated by poly(A)-binding protein CC (PABP). PAN deadenylation is followed by rapid degradation of the CC shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are CC then degraded by two alternative mechanisms, namely exosome-mediated CC 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA CC decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. CC {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03182}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03182}; CC Note=Binds 2 metal cations per subunit in the catalytic exonuclease CC domain. {ECO:0000256|HAMAP-Rule:MF_03182}; CC -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit CC PAN3. {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the CC regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) CC deadenylation complex. {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000256|HAMAP- CC Rule:MF_03182}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03182}. CC Note=Shuttles between nucleus and cytoplasm. {ECO:0000256|HAMAP- CC Rule:MF_03182}. CC -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal CC hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain CC is predicted to be catalytically inactive because it lacks the active CC site catalytic triad characteristic of thiol proteases, with residues CC at the equivalent structural positions that are incompatible with CC catalysis, and it cannot bind ubiquitin. It functions as a structural CC scaffold for intra- and intermolecular interactions in the complex. CC {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40 CC repeats and the pseudo-UCH domain mediates interaction with PAN3. CC {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03182}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAK3589026.1}. 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; JAEAOA010000537; KAK3589026.1; -; Genomic_DNA. DR Proteomes; UP001195483; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. DR GO; GO:0031251; C:PAN complex; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:UniProtKB-UniRule. DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IEA:UniProtKB-UniRule. DR CDD; cd06143; PAN2_exo; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR HAMAP; MF_03182; PAN2; 1. DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3. DR InterPro; IPR030843; PAN2. DR InterPro; IPR050785; PAN2-PAN3_catalytic_subunit. DR InterPro; IPR048841; PAN2_N. DR InterPro; IPR028881; PAN2_UCH_dom. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR InterPro; IPR028889; USP_dom. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR15728; DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1. DR PANTHER; PTHR15728:SF0; PAN2-PAN3 DEADENYLATION COMPLEX CATALYTIC SUBUNIT PAN2; 1. DR Pfam; PF20770; PAN2_N; 1. DR Pfam; PF00929; RNase_T; 1. DR Pfam; PF13423; UCH_1; 1. DR SMART; SM00479; EXOIII; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50235; USP_3; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03182}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_03182}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_03182}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03182}; KW mRNA processing {ECO:0000256|ARBA:ARBA00022664, ECO:0000256|HAMAP- KW Rule:MF_03182}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03182}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03182}; KW Reference proteome {ECO:0000313|Proteomes:UP001195483}. FT DOMAIN 519..1015 FT /note="USP" FT /evidence="ECO:0000259|PROSITE:PS50235" FT REGION 466..485 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 642..720 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 647..672 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 687..703 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1068 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182" FT BINDING 1070 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182" FT BINDING 1177 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182" FT BINDING 1229 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03182" SQ SEQUENCE 1284 AA; 146263 MW; 722916876BB55E1C CRC64; MQRMNMDFNH MPTSSLNVGF PSGPVEMNPG VGMIPPVMMP EHFQQQAPPG MFPTHPDTVH AGGEYREIHS VLVDGGSHYG VSSVCFDTQE LLWMGNHGGH VTSYCGLDLQ KYTSFQIHAS DEIRQIMPLG EKGVMFLTRG NLRCSNRRGL NVFRYTNAAM HDMQCMIQMN PSSVLIGGHQ TEVLELDLVK LQPKNMFTVA EPGCAIFRET GRYLTVGDTS GKVTLYDCNT MKAEHFLNAH SGTLSDFDIH GNTLITCGYS SRHGTLTADR YLMVYDLRMM RAMTPIQVII EPTFLRFVHT YCPKLAVVSQ VGQFQLIEGT ADMSKFVYSV NVNDGLIMSF DVSKNYQAMA FGDSHGCMHL FATGNQIHFN NHIVSPEYAD PVEPVPPIHI RDELTPLSVI PMTYPRSGRL LSDWPEHLCK KVYRKPKKID PEILRTMKVY QNVGYAPNPG KERRNQIPYI LEDKNAKKKG KKNVPESPVG RGDDPLMQTP QTYRKVILKY SKLGLEDFDF RHYNKTPFAG LETHIPNAYC NCMLQVFFFI EPLRCALLNH LCKREFCLSC ELAFLFHMLD KQKGHSCQAS NFLRAFRTLP EASALSLILG ESEEILLRVN LGHLIQSWQR FIHQQIHSET FTKITVSVEE EKPPQATVPD ITSSSGVTLA DEKSSETTLS SSSSKSKKKK KKSKKKEREE KEKEKKEQRE ESPQNVEVPI PPPVQEEKTV NETEKSIITD LFGLDQVSTL TCRCGQETSR NTKPTLINLR YPDCSPQGPN KAPVHFSFSQ VLEHSLSVEQ NTQAWCNVCE SYQPHNQTKK IESLPDVLAL NCQLENERNQ EFWKIQLMLL KQKEEMEGSF STSSSPIPQS FSPVMCRYGR NCTRKGCRFR HETDMTCEGS DDLFRSKPEI GPVWVPMGLK VTLSADGKPQ IDEISDEEIL PKIHPLRTKY YEIFATVLHV KDAKTGGHLV SHIKVGETYH QRKENVTCTQ WYLMNDFSIT PIEKYEAVQL NLDWKVPCTI YFIRRNIVKY YNLAVKNPIT SDVFFDDSSI LNPKRRKVTF TPLDPKELPK EGTIVGLDAE FVSLNQEESE LRSDGTRSTI KPSHLSVARI TCIRGDGEQA GVPFLDDYIA THEQVVDYLT QYSGIQHGDL NPVISSKHLT TLKSTYIKLR YLIDAGVIFV GHGLKKDFRV INIMVPKDQI IDTVELFYIP RQRMISLKFL AWYFLKLNIQ SATHDSVEDA RTALHLYFKY QEMSKEGMDR VRATINEMYE FGRKNQWKIS EIEEDNVEDT IAVL //