ID A0A0C2PZT7_9CYAN Unreviewed; 916 AA.
AC A0A0C2PZT7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Poly(A) polymerase {ECO:0000313|EMBL:KIJ77074.1};
GN ORFNames=SD81_09825 {ECO:0000313|EMBL:KIJ77074.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ77074.1};
RN [1] {ECO:0000313|EMBL:KIJ77074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ77074.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000256|ARBA:ARBA00007265,
CC ECO:0000256|RuleBase:RU003953}.
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:KIJ77074.1}.
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DR EMBL; JXCB01000007; KIJ77074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2PZT7; -.
DR OrthoDB; 9805698at2; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031123; P:RNA 3'-end processing; IEA:UniProt.
DR CDD; cd04595; CBS_pair_DHH_polyA_Pol_assoc; 1.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.10.310.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002646; PolA_pol_head_dom.
DR PANTHER; PTHR47788:SF1; A-ADDING TRNA NUCLEOTIDYLTRANSFERASE; 1.
DR PANTHER; PTHR47788; POLYA POLYMERASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF01743; PolyA_pol; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU003953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003953};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 320..379
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 383..438
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 433..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 102565 MW; 619A9739F4987C33 CRC64;
MDLILCHTTA DFDSLGAAVG LSRLLPGSKI VLSGGSHPPV RDFLALHRDE YQLIERRSVN
PKEIRSLIVV DTQQRDRLGK AAEWLDLPHI KEIIIYDHHQ EQLGDIPATK VHISPVGATT
TLIVEQLQKQ QISLTSAEAT VMALGIHVDT GSLTFDYATP QDALALAWLM QQGASLSVVS
QYVDPGLSPQ LQQLLKVALE KLQTICVGGY KIAWVTLKTD NFVPGLSSLA SQLVELTEID
ALLLLNEYPL SEGESRLIVI GRAQIQSINL NELFQPFGGG GHSQAAALNL RGVNTEEILN
QLLEGMKATI PHPPTARDLM SSPVRTIRPE TTIAEAQRTL LRYGHSGLCV VDAEGELVGI
ISRRDLDIAL HHGFSHAPVK GYMTVNMRTI TPDTTLPEIE SLMVTYDIGR LPVLEHGQLV
GFVTRTDVLR ELHQKEERGN GREKGAGEKN IKSPTLNELH SRLAPQLWQL LTKASLEAEK
RGWHLYLVGG AVRDLLLAEE ATGTLLIKDI DLVVDGFHKS ADVGAGVELA KALQQIYASA
RLEIHGAFQT AALLWHKDPE LDSLWVDIAT ARTEFYPYPA ANPEVEASSI RQDLYRRDFT
INAMALRLTP PRAGELLDFF GGLVDLQAKQ IRVLHANSFI EDPTRIYRGV RFAMRLGFHL
EAQTEEYIRY AINSGVYDRT TRENSRTPAL QTRLKAELKH ILEAAYWKPA LQLLADLGAL
QCIHPTLKLD EELLRQLRLL ERCLRRFDSQ QTLIHWQMRL EALIAHLAPK YRGKVARNLQ
LPDDSITRLD KLAQVQEKVN KMTSTPFVEA HRGGGVAFEE TIRPSQVVQL LRQYDVPMLI
LIAVQSPRVI RRKIWQYLTI WRNVQPILNG NDLQQIGYKP GPQYRQMLDD LLAATLDKVI
CNKTQAEEFL AQHYPR
//
