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Database: UniProt
Entry: A0A1Y1V8W1_9FUNG
LinkDB: A0A1Y1V8W1_9FUNG
Original site: A0A1Y1V8W1_9FUNG 
ID   A0A1Y1V8W1_9FUNG        Unreviewed;       692 AA.
AC   A0A1Y1V8W1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN   ORFNames=BCR36DRAFT_412511 {ECO:0000313|EMBL:ORX50017.1};
OS   Piromyces finnis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX50017.1, ECO:0000313|Proteomes:UP000193719};
RN   [1] {ECO:0000313|EMBL:ORX50017.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT   biomass hydrolysis.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORX50017.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000256|ARBA:ARBA00008593}.
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:ORX50017.1}.
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DR   EMBL; MCFH01000022; ORX50017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1V8W1; -.
DR   STRING; 1754191.A0A1Y1V8W1; -.
DR   EnsemblFungi; ORX50017; ORX50017; BCR36DRAFT_412511.
DR   OrthoDB; 21395at2759; -.
DR   Proteomes; UP000193719; Unassembled WGS sequence.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
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   InterPro; IPR045862; Trf4-like.
DR   PANTHER; PTHR23092:SF15; INACTIVE NON-CANONICAL POLY(A) RNA POLYMERASE PROTEIN TRF4-2-RELATED; 1.
DR   PANTHER; PTHR23092; POLY(A) RNA POLYMERASE; 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:UP000193719}.
FT   DOMAIN          203..322
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          385..441
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..110
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..630
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   692 AA;  80670 MW;  B91B3E136D5F6FA7 CRC64;
     MASKVGGKFK KRKQVDDLLN NKKNIEKKYG STKTNGSEKS SKNKKRKLSN SSNNSNNYTI
     LYENGNSNKR KRKNSNNDDF IPLKSKKQKE PKIDYRKKKL HKKAREQKRK EKERQKREIY
     ENDLSNDIDL YELDNDFLLR NENNNNKSNK SKKNKNNNGS GPLWAPFKRY SGTFEERLHE
     EILDFVKYIT PNTSEINTRL YTIDKLREKL HHRFPDSKIE CFGSFSTGLF LPTSDLDIVV
     YRPGGDKNSA SYAANPTQGN QSKNLNKIAR HIRSNGFFIN KVIRHSRIPI IKAEDDLTHY
     SIDISYNQES GVPAIKYIKQ NIKKYPALKP LVYILKHFLY INDMNEVFTG GLGSFSVVCL
     VLSFLKFYTK IFYEKEEGDC ELPENLGTLL INFLYLFGGG FDYENIGISV NDGTFYKKMD
     KGFYNFKQRS LLSLEDPIMP GNDLTKGSHR ILEISRAWKH ALDLLRRGEE KDINKIKKNQ
     PSLLAKILYF DNEEIRRRKQ IREYIYPKVI QRTGNKYSTT PESSENEEED SQMDNDELNS
     NENSASSNND SQASIHNSKK RKLDELDDDE KEDEEEEEED DDDDDDDDIS VPSDKDDDEY
     IPVDSEEDDD DDDDANSDEL TNPPLNDDDE IYEYVSDNDE ENSDINDDEY DEYITKQEDD
     EVDEEFDKEL YDKLGETFLD EDNINIDDIL YK
//
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