A3DCH7 (PNP_CLOTH) 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:	Cthe_0418

Organism

Clostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]

Taxonomic identifier

203119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium thermocellum

Protein attributes

Sequence length	700 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-Rule MF_01595
Catalytic activity	RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate. HAMAP-Rule 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.
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: HAMAP
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: HAMAP polyribonucleotide nucleotidyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 700	700	Polyribonucleotide nucleotidyltransferase HAMAP-Rule MF_01595		PRO_0000329605
Regions
	Domain	554 – 613	60	KH
	Domain	623 – 691	69	S1 motif

Sequences

	Sequence		Length	Mass (Da)
	A3DCH7 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 4DAC5DD2A1704F59	FASTA	700	77,318
	10 20 30 40 50 60 MYKTFSMELA GRTLTIETGK LAQLANGSVL VRYGDTVVLS TATASATPRE GVDFFPLSVD 70 80 90 100 110 120 YEERLYAVGK IPGGFIKREG KPSEKAILTA RVIDRPLRPL FPKDLRNDVA IVNTVLSVDQ 130 140 150 160 170 180 DNSPELAALL GSSIAVSISD IPFNGPVGAV ILGLIDGEVI INPTEKQKEI SQMYVTLAGT 190 200 210 220 230 240 RNKIVMIEAG ANEVPDEVML DAIKKGHEEI KKIVDFIDGI VKEVGKPKFE YESAEVPEEI 250 260 270 280 290 300 FNAVREYAYD KMREAVLAVD KQVRDKNIDD LTKEITEHFA EVFPEMEPAI KEAIYKLEKK 310 320 330 340 350 360 VVREYILEEG RRVDGRRLDE IRPLSAEVGL LPRVHGSGLF TRGQTQVLSS VTLGAMGDVQ 370 380 390 400 410 420 ILDGIDTEET KRYMHHYNFP GFSVGEAKSS RGPGRREIGH GALAERALEP VIPSEEEFPY 430 440 450 460 470 480 TIRVVSEVLM SNGSTSQGSV CGSTLALMDA GVPIKKPVAG ISAGLVVDEN NPDRFVTFMD 490 500 510 520 530 540 IQGIEDFFGD MDFKVAGTKD GITAIQVDIK IDGLTEEIIK QAFELTRKGR LYIIDNVLLK 550 560 570 580 590 600 AIPEPRKQMS KYAPKIISTT INPDKIREVI GPGGKMINKI IDETGVKIDI NDDGRVYIFS 610 620 630 640 650 660 SDIQAGKRAR SMIEAIAKDI EPGQVFLGRV IRVTSFGAFV EFLPGKEGLV HISKLDKKRV 670 680 690 700 ERVEDIVRVG DQILVKVIEI DKQGRVNLSR KDAMEDEWDK

References

[1]

"Complete sequence of Clostridium thermocellum ATCC 27405." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000568 Genomic DNA. Translation: ABN51656.1.
RefSeq	YP_001036849.1. NC_009012.1.
3D structure databases
ProteinModelPortal	A3DCH7.
ModBase	Search...
Protein-protein interaction databases
STRING	203119.Cthe_0418.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN51656; ABN51656; Cthe_0418.
GeneID	4808421.
KEGG	cth:Cthe_0418.
PATRIC	19514497. VBICloThe47081_0443.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1185.
HOGENOM	HOG000218327.
KO	K00962.
OMA	YTMRVVS.
ProtClustDB	PRK11824.
Enzyme and pathway databases
BioCyc	CTHE203119:GIW8-435-MONOMER.
Family and domain databases
Gene3D	1.10.10.400. 1 hit. 2.40.50.140. 1 hit.
HAMAP	MF_01595. PNPase.
InterPro	IPR001247. ExoRNase_PH_dom1. IPR015847. ExoRNase_PH_dom2. IPR004087. KH_dom. IPR004088. KH_dom_type_1. IPR012340. NA-bd_OB-fold. 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]
PANTHER	PTHR11252. PTHR11252. 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_CLOTH

Accession

Primary (citable) accession number: A3DCH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	March 20, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program