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Database: UniProt
Entry: A0A177CNJ5_9PLEO
LinkDB: A0A177CNJ5_9PLEO
Original site: A0A177CNJ5_9PLEO 
ID   A0A177CNJ5_9PLEO        Unreviewed;       717 AA.
AC   A0A177CNJ5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=PAP/OAS1 substrate-binding domain-containing protein {ECO:0000313|EMBL:OAG08327.1};
GN   ORFNames=CC84DRAFT_1162297 {ECO:0000313|EMBL:OAG08327.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG08327.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG08327.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG08327.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000256|ARBA:ARBA00008593}.
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DR   EMBL; KV441550; OAG08327.1; -; Genomic_DNA.
DR   RefSeq; XP_018038692.1; XM_018177957.1.
DR   AlphaFoldDB; A0A177CNJ5; -.
DR   STRING; 1460663.A0A177CNJ5; -.
DR   GeneID; 28761443; -.
DR   InParanoid; A0A177CNJ5; -.
DR   OrthoDB; 170176at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF40; POLY(A) RNA POLYMERASE GLD2; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          193..226
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          542..622
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          23..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   717 AA;  79122 MW;  BBA6A627C096A013 CRC64;
     MAEQQAQSSL EDQLRSMILT NVTIGSTPDS SNAHMSNHHQ QNWRSRGRGR GRGRPYAPRG
     GNYWAGTEHQ HRGFPAAPPE QNMAPQSTPR TLQRPYDNGN TLNLAHSAGP SRPYGPHGHP
     PRRGQTMRSS YANGGFQQHQ VSDLTLQAAY LDHLASLEIP KAEISKEEYE EKETFRQQLE
     AVCQKEFTNK YSGDIASIKL VTFGSIASGF ATPGSDMDLA IVPQWKDPTK SQDSSIDRDI
     PRLLERAVLD AKMGGRLLTR TRVPILKVCQ KPTEDLYNAL FEERQKWDQL PEEEQYAAPA
     VPGAAVQNPS EPQEQVNSPQ VNDSQSFPTL AEAKAVKGIA RSAPSAKVIE HDDEGKAEVL
     QAPVFDSFKE NNGPKDIADA ADPSKNQQPR GPKKWLRERK SGPLDFPKVG VGIQCDVNFE
     NPLAIHNTQL LRCYSLTDPR VRPMVLFIKA WAKRRKINSA YSGTLSSYGW VLMVLHYLVN
     MANPPVCPNL QSSWRPTTTK AEDLQQILEQ TTVGGYAVRF WHDEPAIVQL ASAGQLSRNT
     QSIGELLRGF FHYYASIPQP NHYGQKHWSF FWATEVLSLR TPGGIRQKTE KGWTKATTTI
     SNGKEVRQRY LFAIEDPFEL DHNVARTVTH DGIVAIRDEL RRAGRILNSV GRGQAPEGGL
     FDEVVEQAPP VMPNKTEDGS ETAAPVAEGA AGETDGGADK STTPAATNYA APGCGTG
//
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