ID F4LN47_TREBD Unreviewed; 426 AA.
AC F4LN47;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Poly(A) polymerase {ECO:0000313|EMBL:AEE16812.1};
DE EC=2.7.7.19 {ECO:0000313|EMBL:AEE16812.1};
GN OrderedLocusNames=Trebr_1388 {ECO:0000313|EMBL:AEE16812.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE16812.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|RuleBase:RU003953}.
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DR EMBL; CP002696; AEE16812.1; -; Genomic_DNA.
DR RefSeq; WP_013758517.1; NC_015500.1.
DR AlphaFoldDB; F4LN47; -.
DR STRING; 906968.Trebr_1388; -.
DR KEGG; tbe:Trebr_1388; -.
DR eggNOG; COG0617; Bacteria.
DR HOGENOM; CLU_015961_0_1_12; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000006546; Chromosome.
DR GO; GO:0000166; F:nucleotide 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:UniProtKB-KW.
DR GO; GO:0043633; P:polyadenylation-dependent RNA catabolic process; IEA:InterPro.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR InterPro; IPR010206; PolA_pol_I.
DR InterPro; IPR032828; PolyA_RNA-bd.
DR NCBIfam; TIGR01942; pcnB; 1.
DR PANTHER; PTHR43051; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43051:SF1; POLYNUCLEOTIDE ADENYLYLTRANSFERASE FAMILY PROTEIN; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AEE16812.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW RNA-binding {ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953}.
FT DOMAIN 50..165
FT /note="Poly A polymerase head"
FT /evidence="ECO:0000259|Pfam:PF01743"
FT DOMAIN 201..253
FT /note="tRNA nucleotidyltransferase/poly(A) polymerase RNA
FT and SrmB- binding"
FT /evidence="ECO:0000259|Pfam:PF12627"
FT REGION 363..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47822 MW; D37CD01F889A4764 CRC64;
MLIRYTADAK GKPVKKAVIY TKEEHSIPRE KIDADALRVI SMLREYGFDA YVVGGAVRDL
LVDKDPKDFD IVTDAPPPRI KKIFRNSRII GRRFRLVHVF FGPKIFEVST FRSITDGSVG
NSFGSMDEDV QRRDFTLNAL YYDPVREQIV DYVGGVKDIR KGVIRPVIPI ERIFEEDPVR
MLRAVKYAAT TGCKLPGYLK RKIRKSAHLL SPVSPSRLTE ELMKIINSGH AYDIVKFSLE
VDLYMYLQPA ATAMMYADPK YEHDYFVHLK ELDALHVVDP SARLGQKLAY LIYDFTAGLT
DWTEEAESRS AAGELYMKTW AQCRNFVLPM NPQRTELEFA IRTVLKKLGI SVHIPKKVFG
SGSTRTLNES GTGKNGNAAG SAKRRRKRHA PAKDTAAVPS KDAAAAPAVF SRPCETVSES
PKSAVL
//
