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Database: UniProt
Entry: A0A061H862_9BASI
LinkDB: A0A061H862_9BASI
Original site: A0A061H862_9BASI 
ID   A0A061H862_9BASI        Unreviewed;       790 AA.
AC   A0A061H862;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN   ORFNames=PFL1_04038 {ECO:0000313|EMBL:EPQ28210.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ28210.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ28210.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ28210.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000256|ARBA:ARBA00008593}.
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DR   EMBL; KE361635; EPQ28210.1; -; Genomic_DNA.
DR   RefSeq; XP_007879753.1; XM_007881562.1.
DR   AlphaFoldDB; A0A061H862; -.
DR   GeneID; 19318145; -.
DR   KEGG; pfp:PFL1_04038; -.
DR   eggNOG; KOG1906; Eukaryota.
DR   HOGENOM; CLU_013572_4_0_1; -.
DR   OrthoDB; 21395at2759; -.
DR   Proteomes; UP000053664; 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:UP000053664}.
FT   DOMAIN          158..254
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          325..383
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          36..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..689
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  85779 MW;  0C42AF90872682F2 CRC64;
     MQGNAHASTS ASAVEQPPTA AATAFGSQDF IAFDFNDDDD AAAASTSTDL QQQQQQPSQP
     TTRKERNAKG RASDVVASSS QAAGKKRKID DRRDDGKTKQ ERIQERKELR SKYTPWSADV
     DWDRCRNGAE MLHRELMAFD MWLAPTYAEH ETRVMVIDLI RRAIKGRWSD AEVYSFGSQE
     TKLYLPQGDI DLVVVSDMMD YQARETVLRA MASTLRQHNL ATQVQVIARA KVPIVKFVCT
     YAKLHVDISV NQTNGLSAAK YVNSWLRKTP SMRPLVMAVK HLLVQRGMSE VFSGGLGSYS
     VILMVISFLQ LHPKLQRAEI DPARNLGVLF LEFLELYGKN FGYDTCGISI RGKGGYFSKA
     RRGWRDERKP FMLCIEDPHD PSNDISRGSY GILNIRAVFS GAFDIVTAAI CHRGRGAAER
     ATAKQPTHRK FGDGDDDDDD DSENEDAAAR RVLLEEARGV VHNPDDKDPK SLLGCIVGVS
     KAMMKQRSDM EDLYHSGSLQ NRLGRPPPLP SPPPAERYMR ADASASASAS APKGPKGKAA
     QQQQQQQQQQ QQQQQGPSPK KIKGQAQRLA ASAASSQRRG NASDPISISS SPDRDLEPST
     TLSIRGAANK QHQNGRANGS AAATADGASR SSSPDIVDEA ELAASQGFSF SSGSNPSQSR
     GEALMGLPHD SPSQSAVHAH SNGVIEILST SDEEDSRYNA APAKRRKTAH NSSPHVAAGK
     GRNGARGARR GDPAAEMEDL SMTAPSTFVD DSSDDAASAA GGGKLTARAR REYWASKGVV
     SPKEQEGDLD
//
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