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Database: UniProt
Entry: A0A1S8BM09_9PEZI
LinkDB: A0A1S8BM09_9PEZI
Original site: A0A1S8BM09_9PEZI 
ID   A0A1S8BM09_9PEZI        Unreviewed;      1150 AA.
AC   A0A1S8BM09;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=PAB-dependent poly(A)-specific ribonuclease subunit PAN2 {ECO:0000313|EMBL:OMP88610.1};
DE   Flags: Fragment;
GN   ORFNames=BK809_0005329 {ECO:0000313|EMBL:OMP88610.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP88610.1, ECO:0000313|Proteomes:UP000190776};
RN   [1] {ECO:0000313|EMBL:OMP88610.1, ECO:0000313|Proteomes:UP000190776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F98.1 {ECO:0000313|EMBL:OMP88610.1,
RC   ECO:0000313|Proteomes:UP000190776};
RA   Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA   Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT   "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT   in grapevine trunk diseases.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMP88610.1}.
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DR   EMBL; MSZU01000074; OMP88610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8BM09; -.
DR   STRING; 420778.A0A1S8BM09; -.
DR   OrthoDB; 9810at2759; -.
DR   Proteomes; UP000190776; Unassembled WGS sequence.
DR   GO; GO:0031251; C:PAN complex; IEA:InterPro.
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:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:InterPro.
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; IPR048841; PAN2_N.
DR   InterPro; IPR028881; PAN2_UCH_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
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   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; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022839};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190776};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          481..825
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          379..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OMP88610.1"
SQ   SEQUENCE   1150 AA;  128094 MW;  ED4D6DACBCD821F5 CRC64;
     LSQIPLPPPG PHAMPTPATT VAFDTHQDLL WSGNDYGRVS SFFGPELQRY TSYRAHPSGE
     GAVKQLLFCD KGVLSISVRS VHLASRRGVT QWHLTNEGFK DLRCMSFTSK GVYEVLVAGC
     QDSMFRIDVE KGTITATLPA ENSYTMMKKG GQYICAATTA GMVQIIDPSS FKIVKSWQAH
     KEWINDMDAK SDFLVTCGFS RRQMNNLILD PFAYVYDLKT LLPLPPIPFH VGAAFVRMHP
     RMSTTSIVAS QSGQLQVVDL MNPNTANVRQ VNLYETYLTC LEMAPSGEAL ALTDALCSVR
     IWGSPTKVRF TDQSQPTEFP DHGIPPPKLD WSMDTPLSTI GMPYYRETLL SVWPSHMIFE
     VGAPPPKLDS QVSTSLKRAE MGQWAPNPRK TRRNQVQATR MLEKDNPLKP PKFLSEKARD
     GNAGKDGERR MSETLEALTD LMLDGSTKKD VPVMYRNVEI KYSKFGVDDF DFKYYNKTEY
     SGLETHIANS YANPLLQLFR FTPLVRNLAL HHAATSCLFE NCLLCELGFL IDMLEKACGQ
     NCQATNFLKT FSGLSNAASL GLLEEHSPNS SLTIMIQNLN RFLLDKLTAD FRQMAQGVGH
     LDHAFTTNAV ANIRCAQCNN ETRRPGASLV HELVYPPKNT MKNPMRASRP TFSQILKASV
     ERQDQNRGWC DRCKRYQQLA ARKTIQNIPP ILMINAAIHS HEAKQLWATP NWLPEKIGII
     VNQGQFFCYE GQDLEHHLRR NFYDIQVYEL IGVVADINSG ENQKSHLVSM INVAPSSRNE
     EEAAEGGSGK WHLFNDFLVR PVSKEEALRF EPNWKLPSVL TYESVKASHH IDDSWKENLD
     TSLLYRTWGP AGEMSDNSDF KPLHPSEHPG PGWPVAIDAE FVSLQREEIE ISASGQRETI
     RPSRLGLARV SVLRGGDSST TSGGDIDSEN GDEIDNNSDE GKPFIDDYIA IAEPIVDYLT
     LFSGISPGDL DRSTSRHALV GLKVAYKKLW LLLNLGCVFV GHGLPKDFRT INIHVPKAQV
     VDTVDLYFIP ARQRKLSLRF LAWVVLEEDI QQDTHDSVED ARTALKLWKH WRDVEAAEGR
     GVCEEMVRDI YKRGWEVGFK VPGSAGVAAG GAGAGGGAAT PTRMTPVRPG TGGWKPPPGG
     VSFGSPSPMK
//
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