Reviewed, UniProtKB/Swiss-Prot Q2GJV5 (PNP_ANAPZ)

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:	APH_0767

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	838 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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: UniProtKB-KW 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 – 838	838	Polyribonucleotide nucleotidyltransferase HAMAP MF_01595		PRO_0000329501
Regions
	Domain	561 – 620	60	KH
	Domain	630 – 697	68	S1 motif

Sequences

	Sequence		Length	Mass (Da)
	Q2GJV5-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 27ABDC2FF220C83B	FASTA	838	89,762
	10 20 30 40 50 60 MFDITRKCVE WGDRSLTIES GKIARQAGGA VVVDYGGTSV LATVVSQKSK EAVDFLPLTV 70 80 90 100 110 120 QFLAKSYAVG KIPGGFFKRE GKPSDRETLI SRIIDRSIRP LFPSGFSDEV AVVCNLLSYD 130 140 150 160 170 180 ASSPPETVAL IGASAALAIS GIPFHCPVAG ARIGYIRGEG RYILNPSADE LSVSALDMFY 190 200 210 220 230 240 ARTDTSILMV ESEAHELTEA EMLGALQFGH EHCEEIIKVI GEFAEEARKC APAEFVPCDL 250 260 270 280 290 300 STIIDSIGSD YKERFLVAYS EKEKKARVAK LDAVRASLTE DLRVKFLSES EGGSKYIAQD 310 320 330 340 350 360 IVYAMKTFER SLVRERVLES KSRIDGRAYD QIRNIEIEVD LISKAHGSAL FTRGDTQALV 370 380 390 400 410 420 ITALGTPQDE QIVDGFDGDK RERFLLHYNF PPYAVGEASA LRPPGRREIG HGKLAWRAIH 430 440 450 460 470 480 PVLPSKADFP YTIRVVSEIT ESDGSSSMAT VCGASLALMD TGVPLKSSVA GIAMGLIKEG 490 500 510 520 530 540 DRYAILSDIL GDEDYLGDMD FKVAGTREGI TALQMDMKVK GIDFAVLGTA LDQAKEGRFF 550 560 570 580 590 600 IIEKMDRVIK ESRGAVREHV PRMESMLIDK GKIKNVIGAG GKNVREICEK TGAKIEISQD 610 620 630 640 650 660 GTVMIYAVGR EAIESAKDMI TGIVSEPEVG KIYSGEVCEL AKYGAFVTFL GARKGLVHIS 670 680 690 700 710 720 EIRNEHINAV ADVLAVGDKV KVLVIDMDKD HIQLSMRRID QETGDQVDCE LYAPQRRNGV 730 740 750 760 770 780 AAGNTVGDSS VNGGGAGSVY VPRGDYGGAS AGRNGRGGGK RDGAAKSSSS AGNGGGRSSS 790 800 810 820 830 STRRRHSAGS SGYSSDSSSG NTKSSSSESS GGTGGRGRNG ANGDVQNGPA APKKPRFF

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000235 Genomic DNA. Translation: ABD44311.1.
RefSeq	YP_505346.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3930955.
GenomeReviews	Gene locus APH_0767 in contig CP000235_GR.
KEGG	aph:APH_0767.
NMPDR	fig|212042.5.peg.742.
TIGR	APH_0767.
Phylogenomic databases
HOGENOM	Q2GJV5.
OMA	Q2GJV5. GHGNLAK.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0767-MON.
Family and domain databases
HAMAP	MF_01595. [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. IPR012162. PNPase. IPR015848. PNPase_PH_RNA-bd_bac/org-type. IPR003029. Rbsml_prot_S1_RNA-bd_dom. [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.
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]
SMART	SM00322. KH. 1 hit. [Graphical view]
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_ANAPZ

Accession

Primary (citable) accession number: Q2GJV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	March 21, 2006
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)