ID K9T2F3_9CYAN Unreviewed; 908 AA.
AC K9T2F3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=tRNA nucleotidyltransferase/poly(A) polymerase {ECO:0000313|EMBL:AFY76301.1};
GN ORFNames=Ple7327_0874 {ECO:0000313|EMBL:AFY76301.1};
OS Pleurocapsa sp. PCC 7327.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC Pleurocapsa.
OX NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY76301.1, ECO:0000313|Proteomes:UP000010382};
RN [1] {ECO:0000313|EMBL:AFY76301.1, ECO:0000313|Proteomes:UP000010382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY76301.1,
RC ECO:0000313|Proteomes:UP000010382};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished genome of Pleurocapsa sp. PCC 7327.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; CP003590; AFY76301.1; -; Genomic_DNA.
DR RefSeq; WP_015142609.1; NC_019689.1.
DR AlphaFoldDB; K9T2F3; -.
DR STRING; 118163.Ple7327_0874; -.
DR KEGG; plp:Ple7327_0874; -.
DR PATRIC; fig|118163.3.peg.970; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_3; -.
DR Proteomes; UP000010382; Chromosome.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000010382};
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 325..384
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 388..447
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 908 AA; 102468 MW; 96C708B32E91D88F CRC64;
MDLILCHQTA DFDVLGAAVG LSRLKIGSRI VLTGGAHPAV RDFLALHRDE LSLIEMRSVN
PKKIRSLVVV DNQQRDRLGK AAEWFDLPQV KAIAIYDHHL DSSSDIPATQ KQIEAVGATT
TLIVERLQQA KVGLNPVEAT VMALGIHVDT GSLTFPQSTA RDARALAWLM EQGANVKTIA
EYADPGFPPY LQQLLTEAIE RLQMSVVRGY TIASILLTTE TFVPGLSNLA ERLIELTESD
ALLFAHQYSK GRGEEPFKEI RLTIIGRSRI EGTNLHQLFE PLGGGGHAQA ASVILRGVDP
EATLRELVER FKEQIPHPPT ARDLMSSPVR TIRPDTTIEQ AQRILFRYGH SGLSVVDESD
RLVGVISRRD IDLALHHGFS HAPVKGYMTR NLRTIKSDTP LPDIESIMVT YDVGRLPVVE
SGQLIGIVTR TDVLRQIHND RTHKRDEQGK KEPLVSCLLP SLQNRLRPSL WQFLTTAAQE
AQKRGWHLYL VGGAVRDLLL AENHESLLLQ DIDLVVDGFH RSADVGAGVE LASRLREIYP
QARLSVHGEF QTAALLWHKD PEFGSLWVDI ATARTEFYPY PAANPEVEAS SIRQDLYRRD
FTINALAVRL TSPREGELLD FFGGMLDLRS RQIRVLHANS FIEDPTRIYR AVRFAVRLGF
GIEPQTEEYI RYAIESGVYD RLKLENHPAP ALTTRLKAEL HYILEADYWK PALQLLADLG
ALRCLHPTLV LDKKLWWQIR CVSRWLRWLD PENLLHHWLI RLEVLLSAIE SSEGVKIATN
LQLPKDSLER LEQLKTIERE VNSALPKCDR PSEVVNLLRQ YKLASLILVA VRSSKNIRRT
IWQYLARWSQ VRSPLDGKDL KAMGYKPGPQ YREILDELLA ATLDGKIGTR EEAEKFLQDL
KARNRLCC
//
