ID A0A179UXY3_BLAGS Unreviewed; 1266 AA.
AC A0A179UXY3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=polynucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012388};
DE EC=2.7.7.19 {ECO:0000256|ARBA:ARBA00012388};
GN ORFNames=BDBG_07470 {ECO:0000313|EMBL:OAT12079.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT12079.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC {ECO:0000256|ARBA:ARBA00010912}.
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DR EMBL; GG657466; OAT12079.1; -; Genomic_DNA.
DR RefSeq; XP_002622068.1; XM_002622022.1.
DR AlphaFoldDB; A0A179UXY3; -.
DR STRING; 559298.A0A179UXY3; -.
DR GeneID; 8502443; -.
DR KEGG; bgh:BDBG_07470; -.
DR VEuPathDB; FungiDB:BDBG_07470; -.
DR OrthoDB; 5479694at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
DR Gene3D; 1.10.1410.10; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR040459; MJ1316.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR PANTHER; PTHR10682:SF23; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF13563; 2_5_RNA_ligase2; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF04457; MJ1316; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF55144; LigT-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..588
FT /note="Endonuclease/exonuclease/phosphatase"
FT /evidence="ECO:0000259|Pfam:PF03372"
FT DOMAIN 678..730
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 805..941
FT /note="Poly(A) polymerase central"
FT /evidence="ECO:0000259|Pfam:PF04928"
FT DOMAIN 1179..1248
FT /note="MJ1316 RNA cyclic group end recognition"
FT /evidence="ECO:0000259|Pfam:PF04457"
FT REGION 212..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 141687 MW; 1B13F9FD5DA6F046 CRC64;
MADLTEPPRT TSLTLNAYQT ALCIIPPTPF VEDTNRLRAL YDQAFEKWPA HVNLIYPFVS
TDRLPAAVDL IRSNLFSWLT EVEDTCFHVR LNKPGNFTQR HGNIVYLAPD ESDGFLNLND
FRNVILKGFK QPANEQQRGY QPHLTIGQSK ANDDNARDHL LSKAKLLPPI EWRVGQLAIM
VREKAGNTRR MKLWGTIDLD GAATFNQIVD TPQDMEQGRD GSKISTSPTS SEFSSQYLHS
ISERGGSGAE SRITYMFAAD AGIWTPAEAS GGSEDEEQIQ SALKVSSYNV LVDSIYPPAT
DRHQILLQTL LSKASTADVL VLQEVSDSFL TYILGHDAIR TTYPFATHGP PEQKGIGPLP
SIRNVVALSR SNFTWSWLPL GTNHKGAVIL ALSDIGKIDE SGYVPAIIAG IHLSSGLFDY
AVAARKQQLQ KLSNFLSANY TNNPKVIAGD FNMTTSTITH EEASGRKSIS SRSIETLPVL
ETMLQYAGYW DSWSVAHTKI RDMMSPARLE RDFTQLYDGE QGATFDPLEN SLAAISSDST
ANPRPQRYDR ILFSKDDLRV TGFNMFGFPV EIIDEATGNI ERQFPSDHWG IRASLEFDPN
GGEDVDPFKS MPLYAKLAHS NFDNPAGLKV CLADKSIVPS SEDAEKRKAA FSLLKNLIQH
GSLPESGKGK EIDQPRLSIV VTTVGSYGLG VWTDSSDVDC LCVGSISSKV FFELTLQRLK
KGAEWDVKIL RKVKAATGTM LELEINSVKF DLQYCPAAAV AERWLEVPHL PRSSPLFDLA
LLPLMKLQPY RDQAYLQRTV PNPATFRLLH RIIKAWAKHR GIYSSKFGYL GGIHITMMLS
QVMKLLPSPA PVTSAADILC TFFNYYGNFN WKEDVMYDPS FHKKPPRYHR TPQEGMVILT
LHAPVMNVAR SASIPSTRTI VDEMKRADNL ISEGNTNWAE LVGIVANTGK SSLSVSGDEF
LRSYNSYIKI NVQYWGLSLA KGSSLVGWLE SRCLVLLADL HRKFPDIQTR IWPARFTQIE
DHDDSTPAQE EREYQGCYLI GLTKAEHATD PTRTLSKSDR KLAHDTLQAS IDQFASNIHN
DKKYFDSASA WVDVSHVKQG NLGPLNLDDR DWGAYTIQDN DFDDSDSEDD DSDIYIEEGG
DDNADDDEAT TESDLLPSTK KKNTHKSTTK PPVLTAKLRP ASDILSRLRW DPSLHGTEYI
IGYEDRFLGE KEISLDRWKS EQTDEEFIPQ HRILYFKRKD DGRVVWDREA RRDEIFGSGV
GKGKEF
//
