Q1LSL2 (PNP_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyribonucleotide nucleotidyltransferase
EC=2.7.7.8

Alternative name(s):
Polynucleotide phosphorylase
Short name=PNPase

Gene names

Name:	pnp
Ordered Locus Names:	BCI_0627

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	697 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity. HAMAP MF_01595
Catalytic activity	RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. HAMAP MF_01595
Subunit structure	Homotrimer. Organized into a structure (processome or RNA degradosome) containing a number of RNA-processing enzymes By similarity.
Subcellular location	Cytoplasm By similarity HAMAP MF_01595.
Sequence similarities	Belongs to the polyribonucleotide nucleotidyltransferase family. Contains 1 KH domain. Contains 1 S1 motif domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro mRNA catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'-5'-exoribonuclease activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW polyribonucleotide nucleotidyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 697	697	Polyribonucleotide nucleotidyltransferase HAMAP MF_01595		PRO_0000329529
Regions
	Domain	553 – 612	60	KH
	Domain	622 – 690	69	S1 motif

Sequences

	Sequence		Length	Mass (Da)
	Q1LSL2 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 7420BCBEF594D25F	FASTA	697	76,711
	10 20 30 40 50 60 MLNPIVHRFQ YGKHIVILET GIVARQATAA VMVNMADTIV LVTVVGVKQV KPGQKFFPLM 70 80 90 100 110 120 VNYQERTYAA GRFPGGFFRR EGRPSEGEIL ISRMIDRPLR PLFPDGFLNE VQVIATVVSI 130 140 150 160 170 180 NPQVSPDIVA MIGVSAALSI SGIPFNCPFG AARVGYINNQ YVLNPTIAEL VDSSLDLVVA 190 200 210 220 230 240 STANAVLMVE SEAKQLSEEQ MLSAIIFGHE QQQLVIQNIN HMVTIVGKPK WSWQAQVIDT 250 260 270 280 290 300 NLQLCVTELA ESRLNEAFCI SDKQERDVCI ETIKSDVLSA LQQKNETIEE ETISNIFANL 310 320 330 340 350 360 EKQIARNRIL GGKLRIDGRN HKMIRSLDMR TSILPRTHGS ALFVRGETQA LVTVTLGTER 370 380 390 400 410 420 NAQNIDELIG ERTDRFLLHY NFPPYCVGEI GLVGSPKRRE IGHGRLAKRG ILAVMPTANE 430 440 450 460 470 480 FPYTVRVVSE ITESNGSSSM ASVCGTSLAL MDAGVPIKAA VAGVAMGLIK EDNNFVILSD 490 500 510 520 530 540 ILSNEDYIGD MDFKVAGSKN GITALQMDIK TKGITNNIIQ LALNQAKDAR MHILNMMEQV 550 560 570 580 590 600 ISMSRTDISP FAPRIHTIKI HPDKIKDVIG KCGSVIRALT EETKTIIDIE DDGTVTVAAT 610 620 630 640 650 660 DSIKAQQAIC RIKDITAEIE VGSIYHGKVT RIVDFGAFIA ISSNKEGLVH ISQITNKRVE 670 680 690 KVADYLSIDQ IVLVKVLEVD RQGRIRLSMK DTNLTNK

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF13852.1.
RefSeq	YP_589052.1. NC_007984.1.
3D structure databases
ProteinModelPortal	Q1LSL2.
SMR	Q1LSL2. Positions 617-691.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LSL2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056300.
GenomeReviews	Gene locus BCI_0627 in contig CP000238_GR.
KEGG	bci:BCI_0627.
PATRIC	21074761. VBIBauCic75062_0594.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1185.
HOGENOM	HBG382411.
OMA	YGETVVL.
PhylomeDB	Q1LSL2.
ProtClustDB	PRK11824.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0627-MONOMER.
Family and domain databases
HAMAP	MF_01595. PNPase. [Tree]
InterPro	IPR001247. ExoRNase_PH_dom1. IPR015847. ExoRNase_PH_dom2. IPR004087. KH. IPR004088. KH_type_1. IPR018111. KH_type_1_subgr. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR012162. PNPase. IPR015848. PNPase_PH_RNA-bd_bac/org-type. IPR003029. Rbsml_prot_S1_RNA-bd_dom. IPR020568. Ribosomal_S5_D2-typ_fold. IPR022967. RNA-binding_domain_S1. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit.
KO	K00962.
PANTHER	PTHR11252. PNPase. 1 hit.
Pfam	PF00013. KH_1. 1 hit. PF03726. PNPase. 1 hit. PF01138. RNase_PH. 2 hits. PF03725. RNase_PH_C. 2 hits. PF00575. S1. 1 hit. [Graphical view]
PIRSF	PIRSF005499. PNPase. 1 hit.
SMART	SM00322. KH. 1 hit. SM00316. S1. 1 hit. [Graphical view]
SUPFAM	SSF46915. 3_ExoRNase. 1 hit. SSF55666. 3_ExoRNase. 2 hits. SSF50249. Nucleic_acid_OB. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.
TIGRFAMs	TIGR03591. Polynuc_phos. 1 hit.
PROSITE	PS50084. KH_TYPE_1. 1 hit. PS50126. S1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PNP_BAUCH

Accession

Primary (citable) accession number: Q1LSL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program