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B5RMZ9 (PNP_BORDL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyribonucleotide nucleotidyltransferase

EC=2.7.7.8
Alternative name(s):
Polynucleotide phosphorylase
Short name=PNPase
Gene names
Name:pnp
Ordered Locus Names:BDU_813
OrganismBorrelia duttonii (strain Ly) [Complete proteome] [HAMAP]
Taxonomic identifier412419 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorrelia

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in mRNA degradation. Catalyzes the phosphorolysis of 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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01595

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01595.

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Polyribonucleotide nucleotidyltransferase HAMAP-Rule MF_01595
PRO_1000147890

Regions

Domain553 – 61260KH
Domain622 – 71594S1 motif

Sites

Metal binding4861Magnesium By similarity
Metal binding4921Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
B5RMZ9 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 751BCFA38546ECF6

FASTA71780,239
        10         20         30         40         50         60 
MRKILKLKIG REDLILETGL LAKQANGAVL ATYGGSTVLA TVCCSDSIRE NLDFVPLSVE 

        70         80         90        100        110        120 
YNEKYYAAGK IPGGFIKREG KPKDKEVLVS RLIDRPMRPL FDKRFGREIQ VVPTTLSTDQ 

       130        140        150        160        170        180 
MNPPDIVGMN AAFTAVFLSD IPFNGPIAAV RIAYLNDEFI VNPSFDEIQD SVLDIVVAGS 

       190        200        210        220        230        240 
LDGITMVEGG ANEVSEEILL DAIDKAYAYI KQICDLQKEF IYLIGEREKL PLAYEEKVFE 

       250        260        270        280        290        300 
FKDDLRSLIY SELKDACFVR GKLNRDKAIK LVKQKAYEHF SSLEQINDEN EILFYKACDD 

       310        320        330        340        350        360 
FEQEIVRKSI LEDNLRTDGR TPTQIRDIIA EVDLLKRTHG SALFTRGETQ ALAVTTLGTS 

       370        380        390        400        410        420 
IDEQVMDDID GDKRLNFMLH YNFPPFSVGE TGRLMTGRRE IGHGHLAQRS LEAMLPKKDD 

       430        440        450        460        470        480 
FPYTIRVVSE VLESNGSSSM ATVCSGSMSL MAAGVPVKEQ VAGIAMGLIS NDDKYVILSD 

       490        500        510        520        530        540 
ILGEEDHLGD MDFKVAGTKN GITGFQMDIK ISNVTKQLMR DALEQARIGR MHILSIMDSV 

       550        560        570        580        590        600 
ISSSRGDISV NAPKIVQLQI DIDKISLVIG STGKTVKAIT DEFEVRVQIE QDGRITLFGT 

       610        620        630        640        650        660 
DNLKMQKAKA KIESIVREPK VGEIYDGIVK KINSFGAFIE LTPTKEGFLS NRSRSRDDRY 

       670        680        690        700        710 
GSDIRHSRYS NRNSRYGRDN RSSFSMRFPR LEEGQIVKVR ISDIDKFGKI ELELARD 

« Hide

References

[1]"The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii."
Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 4:E1000185-E1000185(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ly.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000976 Genomic DNA. Translation: ACH93735.1.
RefSeqYP_002222441.1. NC_011229.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412419.BDU_813.

Proteomic databases

PRIDEB5RMZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH93735; ACH93735; BDU_813.
GeneID6918039.
KEGGbdu:BDU_813.
PATRIC20563748. VBIBorDut9941_0818.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1185.
HOGENOMHOG000218326.
KOK00962.
OMALDFFPLT.
OrthoDBEOG6WT8CC.
ProtClustDBPRK11824.

Enzyme and pathway databases

BioCycBDUT412419:GJ78-813-MONOMER.

Family and domain databases

Gene3D1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.230.70. 2 hits.
HAMAPMF_01595. PNPase.
InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR027408. PNPase/RNase_PH_dom.
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]
PANTHERPTHR11252. PTHR11252. 1 hit.
PfamPF00013. 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]
PIRSFPIRSF005499. PNPase. 1 hit.
SMARTSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMSSF46915. SSF46915. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF55666. SSF55666. 2 hits.
TIGRFAMsTIGR03591. polynuc_phos. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNP_BORDL
AccessionPrimary (citable) accession number: B5RMZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 4, 2008
Last modified: February 19, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families