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Database: UniProt
Entry: G3XPS1_ASPNA
LinkDB: G3XPS1_ASPNA
Original site: G3XPS1_ASPNA 
ID   G3XPS1_ASPNA            Unreviewed;       682 AA.
AC   G3XPS1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE            EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN   ORFNames=ASPNIDRAFT_44704 {ECO:0000313|EMBL:EHA27270.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA27270.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA27270.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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:EHA27270.1}.
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DR   EMBL; ACJE01000003; EHA27270.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3XPS1; -.
DR   STRING; 380704.G3XPS1; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1181500; -.
DR   HOGENOM; CLU_013572_2_1_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
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;
FT   DOMAIN          289..387
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          457..513
FT                   /note="PAP-associated"
FT                   /evidence="ECO:0000259|Pfam:PF03828"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..616
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  75706 MW;  FF5F0F52C6DE20AF CRC64;
     MPPAFEFRGN DRRSGHHPRH EFTFRYARPG TSERPLLRSK RETTPEQLLP SGAADSKPAL
     KFAPVANLSD SEEADMDVSS EDEDEAAHPR KKRAVDPNNS GTATAAPAPA PPAPKWSNPD
     PYTVLPPPDE TQSKRVDVVK LIRKARIAAT AAQPTQEDAV KTNEDFISLS GLVDEDEGGG
     NAPEGAPTGP RRQLEGKDSA FGSRKRTYDD EIKGVSKKTG KPLSKYYDDG SIIDEWRARS
     SENATPWASS MAPSLHVGAR LHNEILSFYH WVKPVRYEQI VREDLVARLQ AAFQSRYYGV
     QLRPFGSFAS GLYLPTADID LVLLSTNFMR NGIKTFGERK GQIYAFSAFL KNLNIAVPNS
     IETIAHARVP ILKFVDKLTG LRVDLSFDND SGLVANETFQ QWKAEYPAMP VIVSVIKQFL
     LLRGLNEVPT GGLGGFSITC LVTSLLQHLP HGHGTPNLGS VLMDFFEFYG NGFDYDSVGI
     RFNPPGYFNK RVYKLSFNNS PRLSIEDPNN ADNDVSGGTR EIALIFRAFS EAYQRLKERM
     ISTATAGQTQ ASILEAIIAA NYEEYTEQRW QLKQVFDTDE RFARYRRAST PPPPPPDSPP
     ADAAPPLPPN PPPAAPKSQK DKMTKLQKKQ QAARERSARL KRLRPDIPSI PYSISNEQAI
     SLGGYKSQSD MDRDLLMREK GM
//
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