ID B7K2Z3_RIPO1 Unreviewed; 903 AA.
AC B7K2Z3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Polynucleotide adenylyltransferase region {ECO:0000313|EMBL:ACK67694.1};
GN OrderedLocusNames=PCC8801_3742 {ECO:0000313|EMBL:ACK67694.1};
OS Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC
OS 8801)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK67694.1, ECO:0000313|Proteomes:UP000008204};
RN [1] {ECO:0000313|Proteomes:UP000008204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001287; ACK67694.1; -; Genomic_DNA.
DR RefSeq; WP_012596952.1; NC_011726.1.
DR AlphaFoldDB; B7K2Z3; -.
DR STRING; 41431.PCC8801_3742; -.
DR KEGG; cyp:PCC8801_3742; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0617; Bacteria.
DR eggNOG; COG0618; Bacteria.
DR HOGENOM; CLU_015961_5_0_3; -.
DR OrthoDB; 9805698at2; -.
DR Proteomes; UP000008204; 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; 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; 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; 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 ECO:0000313|EMBL:ACK67694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008204};
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 903 AA; 102280 MW; 93B7B1D805FF46A9 CRC64;
MDLILCHQTV DFDALGAAVG LSCLKRGSRI VLTGGAHPAV KDFLALHRDE LALIELRSVN
PKKIRTLMVV DNQQRDRLGK ASPWFDFPQI TSVELYDHHL NSVSDIPATF SQIEPLGATT
TLMVEKMQRE GIDPNPIEAT VMALGIHVDT GSLTFPQSTP RDAHGLAWLM EKGANVKTIA
EYCDPGFSIQ LQELLIEALD NLKKTSVRGY VIASVLLTTE TFIPGLSNLA ERLIELTESD
ALLFGHYYDK RRPDKPYSQG RLTVIGRTKI EGTNLNQLFS AYGGGGHAQA ASLMLREIEP
EATLDKLLQE FIAQIPHPLT ARDLMSSPVR TIRPETTIEQ AQRVLFRYGH SGLSVVNEND
ILVGIISRRD LDLALHHGFS HAPVKGYMTR HLKTITPETL LPEIESIMVT YDIGRLPVVE
GDKLLGIVTR TDLLRQIHQN RGENRDENGH KIPLVSCLLP SISQRLSPSI WKLLQFAAKE
AEKRGWHLYI VGGAVRDLLL SEEQEFLLLQ DIDLVVDGFH RSADVGAGVE LASTLQENFP
NARLSIHGEF QTAALLWHKD PQLGSLWVDI ATSRTEFYPY PAANPEVEAS SIRQDLYRRD
FTINALAVRL TPPRKGELLD FFGGMLDLRS RQIRVLHANS FIEDPTRIYR AVRFAVRLGF
EIDPQTETYI NYAIESGIYE RLRIENHPAP ALTTRLKAEL KYILESYYWK PALKLLADLD
ALKCLHSQLI LDDILWWQIR YVSRCLRYLD PENQLEHWLL RLEVLITQLD PTERSKIAVN
LQLPKESLER LKKLSQIELE IKQNLLKCTQ LSEIVNVLRP YRLPNLILVS VRSSCEIRRT
IWEYLTKWSK IQAPLTGNDL KVMGYKPGPQ YKTILDRLLN ATLDGEISSR DDAEVFLKKI
TNH
//
