ID A0A0D1YSA5_9EURO Unreviewed; 564 AA.
AC A0A0D1YSA5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=PV11_00113 {ECO:0000313|EMBL:KIV84329.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV84329.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV84329.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV84329.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000256|ARBA:ARBA00008593}.
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DR EMBL; KN846951; KIV84329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YSA5; -.
DR HOGENOM; CLU_013572_2_1_1; -.
DR OrthoDB; 21395at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:InterPro.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
DR CDD; cd05402; NT_PAP_TUTase; 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:UP000053599}.
FT DOMAIN 333..433
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 503..539
FT /note="PAP-associated"
FT /evidence="ECO:0000259|Pfam:PF03828"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 63506 MW; A2281E60E005EB78 CRC64;
MDSYRPGGGD RRANGDKDSY RPPRRDDDFR PPWPPREADN GMYYFRGSRD EDARRDYSYR
PRPRYPDPRD GPRRRDPYRR PYNPARIAER PLLRLNNQVE DSSLLDPNAD LKFRNLDEIT
DSEEEVMAVS EDEGQERGAK RARVIANDSD IAQTAPKWSN PDPYTSLPPV GDVDTTAKRT
DVLKLIRKAR LDAQNQSDIV SNADDFISFD VDVSDAEESV EESVSQPMGA TISVAEAPAP
AAEMKQERVL GKRKRGDATG RHNLETQSDP LVYSDKYVRG EWQAIPGKDP APWLVATVST
DLPGIALHKE IIDFYEWVKP KDYERAVRNE VFRRLRDAFT RLWPGGELKA FGSYAAGLYL
PTADMDLVYL RRGFRPGVPL IQREAKNLLF SCSRYLRDNR IAKPASITVI SGAKVPIIKF
VDRASGLKVD LSFDNDSGVV AIDTFQRWKE SYPAMPIIVA IVKQYLMIRG LNDVATGGLG
GFSTICLVTN LLQLLPASSQ PINLGEALVE FFNLYGNLFD RNSVAIRMDP PAYLDKVTFS
PLISILLTRS AEGIHAPCFQ RQGR
//
