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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR707 IGR708 IGR704 IGR706 IGR705 IGR702 IGR703 IGR709 rs15, - CT843 CT849 CT848 CT847 CT846 pnp, - CT842 CT849.1 yfhC, - CT844 CT840 ftsH,hflB, - CT841 rs15, - CT843 CT849 CT848 CT847 CT846 pnp, - CT842 CT849.1 yfhC, - CT844 CT840 ftsH,hflB, - CT841 rs15, - CT843 CT849 CT848 CT847 CT846 pnp, - CT842 yfhC, - CT844 CT840 ftsH,hflB, - CT841 CT845 CT845
* Calculated from Protein Sequence

Gene ID: CT842

DNA Molecule Name:
1  

Genbank ID:
843

Gene Name:
pnp  

Definition:
polynucleotide phosphorylase (PNPase)

Gene Start:
995046

Gene Stop:
992962

Gene Length:
2085

Molecular Weight*:
75492

pI*:
5.59

Net Charge*:
-9.23

EC:
2.7.7.8  

Functional Class:
transcription; RNA degradation  

Pathway: pathway table
Nucleotide Metabolism; Purine metabolism
Nucleotide Metabolism; Pyrimidine metabolism

Secondary Evidence:
Luttinger,A., Hahn,J. and Dubnau,D. 1996. Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis. Mol. Microbiol. 19(2): 343-356. Medline: 8825779.

Gribskov M . 1992. Translational initiation factors IF-1 and eIF-2 alpha share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase. Gene 119(1):107-11. Medline: 1383091.

Comment:
In B. subtilis, this enzyme is known to be involved in mRNA degradation, hydrolyzing ss-mRNA in the 3' to 5' direction. It is reported that IF-1, eIF-2, PNPase and ribosomal protein S1 share an RNA-binding motif (see Gribskov, 1992, Medline: 1383091). In Bacillus subtilis, this protein is necessary for competence development (Luttinger et al., 1996, Medline: 8825779).

Blast Summary:  PSI-Blast Search
Hits in gapped BLAST to polynucleotide phosphorylase sequences, e.g., residues 13-695 are 48% similar to the protein from Pisum sativum (AF010578). Residues 13-694 are 44% similar to a polynucleotide nucleotidyltransferase sequence from T. pallidum (TP0886).

CT842 is orthologously related to CPn0999: residues 1-694 of CT842
are 70% similar to residues 1-694 of CPn0999, polyribonucleotide nucleotidyltransferase from C. pneumoniae. This protein is similar to PG690, a predicted polyribonucleotide nucleotidyltransferase from Porphyromonas gingivalis. No similarity to M. genitalium.

COGS Summary:  COGS Search
BeTs to 11 clades of COG1185
COG name: Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase)
Functional Class:  J
The phylogenetic pattern of COG1185 is -----qvcebrhuj--olinx
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 150-167, 462-480, 622-640, 643-664, 635-654 are matched to blocks PR00681A,E,G,H, concerned with
ribosomal protein S1 signatures, e.g. RS1_MYCLE.

ProDom Summary:  Protein Domain Search
Residues 15-586 are 46% similar to a PNPase domain as observed in PNP_BACSU.
Residues 620-688 are 44% similar to an IF2 domain as observed in IF2A_METJA.
Residues 308-469 are 27% similar to a hypothetical domain seen in RNPH_CAEEL.
Residues 340-534 match the RNPH domain of ECOLI.

Paralogs:  Local Blast Search
No strong evidence of paralogs in C.trachomatis. Residues 594-680 are 32% similar to a stretch of CT098, thought to be a ribosomal protein S1 sequence. Residues 603-690 are 37% similar to this sequence.

Pfam Summary:  Pfam Search
Residues 12 to 143 (E-value = 7e-28) place CT842 in the RNase_PH family which is described as 3' exoribonuclease family, domain 1 (PF01138)
Residues 146 to 210 (E-value = 5e-15) place CT842 in the RNase_PH_C family which is described as 3' exoribonuclease family, domain 2 (PF03725)
Residues 323 to 456 (E-value = 3.4e-47) place CT842 in the RNase_PH family which is described as 3' exoribonuclease family, domain 1 (PF01138)
Residues 459 to 529 (E-value = 5e-23) place CT842 in the RNase_PH_C family which is described as 3' exoribonuclease family, domain 2 (PF03725)
Residues 557 to 603 (E-value = 4.3e-10) place CT842 in the KH family which is described as KH domain (PF00013)
Residues 618 to 690 (E-value = 2.8e-16) place CT842 in the S1 family which is described as S1 RNA binding domain (PF00575)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
255  
283

PDB Hit:
gi|2098462|pdb|1SRO| S1 Rna Binding Domain, Nmr, 20 Structures S1 Rna-Binding Domain, Polynucleotide Phosphorylase (Pnpase) Mol_id: 1; Molecule: Pnpase; Chain: Null; Fragment: S1 Rna Binding Domain; Synonym: Polyribonucleotide Nucleotidyltransferase, Pol

Gene Protein Sequence:
MAFETFSVALDKDKTLIFETGKIARQASGAVLVKMNETWVFSSACAASLS
EAVDFLPFRVDYQEKFSSAGRTSGGFLKREGRPSEREILVSRLMDRSLRP
SFPNRLMQDIQVLSYVWSYDGKTLPDPLAICGASAALAISEVPQNCIVAG
VRVGLVGGKWVINPTRDELSASKLDLVMAGTASAVLMIEGHCDFLTEEQV
LEAIAFGQTYIAKICDAIEAWQKAIGKQKNFSAVLDMPEDVQNVVSDFIR
EKFEKALSFRDKEALEQASKELEESVIANLVQEENSDFSLLNVKAAFKTA
KSNQMRALIQDLGIRVDGRTTTEIRPISIETPFLPRTHGSCLFTRGETQS
MAVCTLGGENMAQRFEDLNGDGAARFYLQYFFPPFSVGEVGRIGSPGRRE
IGHGKLAEKALSHVLPETSRFPYIIRLESNITESNGSSSMASVCGGCLAL
MDAGVPIKAPVAGIAMGLILDRDQAIILSDISGIEDHLGDMDFKVAGTAK
GITAFQMDIKIEGITHKIMEQALAQAKQGRSHILNLMTQVLASPKGTVSK
YAPRIETMQINTSKIATVIGPGGKQIRQIIERSGAQVDINDDGVINIAAS
TQESINKAKELIEGLTGEVEVGKVYNGRVTSIATFGVFVEVLPGKEGLCH
ISELSKQKVDNISDFVKEGDKLAVKLLSINEKGQLKLSHKATLED

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCTTTTGAGACTTTTTCTGTTGCGTTAGACAAAGATAAAACATTAAT
TTTCGAGACAGGGAAAATAGCTCGCCAGGCCAGTGGGGCTGTTCTCGTCA
AAATGAACGAGACTTGGGTTTTTTCTTCAGCGTGTGCAGCCTCCTTGTCA
GAGGCTGTCGATTTTCTGCCTTTCAGAGTAGACTATCAAGAGAAGTTTTC
CTCCGCAGGAAGAACCTCTGGAGGATTTCTAAAACGTGAAGGACGGCCTT
CCGAGAGAGAAATTCTTGTTTCTCGGCTAATGGATCGCTCTTTGCGTCCG
TCGTTTCCTAATAGACTCATGCAAGATATTCAAGTCTTGTCCTACGTTTG
GTCTTACGACGGGAAAACTTTACCTGATCCTCTAGCTATTTGCGGAGCTT
CTGCCGCTTTAGCTATCTCAGAGGTTCCTCAAAATTGTATCGTTGCGGGT
GTACGCGTTGGGCTCGTCGGAGGAAAGTGGGTCATTAACCCAACCAGAGA
TGAGTTAAGTGCCTCCAAGCTGGATCTCGTCATGGCAGGAACAGCTTCTG
CAGTTTTAATGATTGAAGGACATTGCGACTTTTTAACAGAAGAGCAAGTT
CTAGAAGCCATTGCTTTTGGGCAAACCTATATAGCTAAAATATGCGATGC
TATTGAAGCATGGCAGAAAGCTATCGGCAAACAAAAGAATTTCTCTGCCG
TTCTTGATATGCCAGAAGACGTACAAAATGTAGTTTCAGATTTTATTAGA
GAAAAATTCGAAAAAGCATTGTCTTTTAGAGATAAAGAAGCTCTAGAGCA
AGCCTCGAAAGAATTAGAGGAATCCGTTATTGCTAACTTGGTTCAAGAAG
AAAACAGTGATTTTTCTTTGTTGAACGTTAAGGCTGCATTTAAGACAGCA
AAATCCAATCAAATGCGAGCTCTTATCCAAGATCTTGGTATTCGTGTAGA
TGGACGAACCACCACAGAGATTCGCCCCATTTCCATAGAGACTCCTTTTC
TTCCAAGAACACACGGAAGTTGCTTATTTACTCGCGGAGAGACGCAAAGC
ATGGCCGTATGTACGCTTGGAGGCGAAAATATGGCGCAGCGATTCGAAGA
TCTGAATGGAGATGGAGCCGCTCGCTTCTATCTACAGTATTTCTTCCCTC
CTTTCTCCGTAGGAGAAGTTGGCAGAATTGGTTCCCCAGGAAGACGTGAA
ATTGGACATGGGAAATTAGCTGAGAAAGCTTTAAGTCATGTTCTTCCTGA
GACATCACGATTCCCTTATATCATTCGCCTAGAATCTAATATTACTGAGT
CTAATGGATCTTCCTCCATGGCATCCGTATGTGGAGGCTGTCTTGCACTC
ATGGATGCTGGAGTTCCTATCAAAGCTCCCGTGGCAGGTATTGCTATGGG
CTTAATCTTAGATCGAGATCAAGCCATCATCTTGTCTGATATTTCCGGTA
TAGAAGATCATCTAGGAGATATGGACTTTAAAGTAGCCGGAACAGCTAAA
GGTATTACAGCTTTCCAAATGGATATCAAGATAGAGGGAATCACTCATAA
GATTATGGAGCAAGCTCTAGCGCAAGCTAAACAAGGGCGTAGTCATATCC
TTAATCTTATGACACAGGTTCTGGCCTCCCCTAAGGGAACTGTTTCTAAA
TATGCTCCGCGCATTGAAACTATGCAGATCAATACCTCAAAAATCGCAAC
GGTCATTGGTCCCGGAGGAAAACAAATCCGTCAAATTATCGAGCGTTCTG
GTGCGCAAGTTGACATCAATGATGACGGCGTCATTAACATAGCTGCAAGC
ACCCAAGAATCGATTAACAAAGCTAAAGAACTTATCGAAGGATTAACTGG
AGAAGTTGAAGTCGGTAAAGTTTATAATGGCCGTGTTACATCTATCGCAA
CATTTGGGGTATTCGTAGAAGTCCTCCCAGGAAAAGAAGGGCTCTGTCAT
ATTTCTGAATTGTCTAAACAAAAAGTAGACAATATCTCTGACTTTGTCAA
AGAAGGAGACAAGCTTGCTGTTAAACTCCTTAGCATTAACGAAAAAGGCC
AGTTGAAGCTGAGCCATAAGGCAACGCTGGAAGAT


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