| NZ_CP032906.1|WP_139519478.1|527897_529442_+|outer-membrane-beta-barrel-protein-HofG |
gnl|CDD|334957 |
pfam02521, HP_OMP_2, Putative outer membrane protein. This family consists of putative outer membrane proteins from Helicobacter pylori (campylobacter pylori).
|
3.34554e-179 |
| NZ_CP032906.1|WP_139535639.1|531843_533397_-|Hop-family-adhesin-AlpA |
gnl|CDD|280099 |
pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.
|
2.28325e-54 |
| NZ_CP032906.1|WP_139519488.1|503918_504521_-|6-pyruvoyl-tetrahydropterin-synthase-family-protein |
gnl|CDD|223792 |
COG0720, COG0720, 6-pyruvoyl-tetrahydropterin synthase [Coenzyme metabolism].
|
7.30996e-20 |
| NZ_CP032906.1|WP_139519486.1|505980_506892_-|polyprenyl-synthetase-family-protein |
gnl|CDD|223220 |
COG0142, IspA, Geranylgeranyl pyrophosphate synthase [Coenzyme metabolism].
|
3.31188e-73 |
| NZ_CP032906.1|WP_139519474.1|534234_536262_-|UvrD-helicase-domain-containing-protein |
gnl|CDD|223288 |
COG0210, UvrD, Superfamily I DNA and RNA helicases [DNA replication, recombination, and repair].
|
7.52445e-135 |
| NZ_CP032906.1|WP_001115881.1|510251_510458_+|4-oxalocrotonate-tautomerase-family-protein |
gnl|CDD|129125 |
TIGR00013, Probable_tautomerase_K2, 4-oxalocrotonate tautomerase family enzyme. 4-oxalocrotonate tautomerase is a homohexamer in which each monomer is very small, at about 62 amino acids. Pro-1 of the mature protein serves as a general base. The enzyme functions in meta-cleavage pathways of aromatic hydrocarbon catabolism. Because several Arg residues located near the active site in the crystal structure of Pseudomonas putida are not conserved among all members of this family, because the literature describes a general role in the isomerization of beta,gamma-unsaturated enones to their alpha,beta-isomers, and because of the presence of fairly distantly related paralogs in Campylobacter jejuni, the family is regarded as not necessarily uniform in function. [Energy metabolism, Other].
|
2.46126e-26 |
| NZ_CP032906.1|WP_001240272.1|520479_521172_+|Bax-inhibitor-1/YccA-family-protein |
gnl|CDD|198414 |
cd10432, BI-1-like_bacterial, Bacterial BAX inhibitor (BI)-1/YccA-like proteins. This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
|
1.36782e-52 |
| NZ_CP032906.1|WP_139535637.1|508369_509515_-|tRNA-pseudouridine(13)-synthase-TruD |
gnl|CDD|272903 |
TIGR00094, tRNA_pseudouridine_synthase_D, tRNA pseudouridine synthase, TruD family. an EGAD loading error caused one member to be called surE, but that's an adjacent gene. MJ11364 is a strong partial match from 50 to 230 aa. [Protein synthesis, tRNA and rRNA base modification].
|
1.09356e-136 |
| NZ_CP032906.1|WP_139535638.1|530232_531822_-|Hop-family-adhesin-AlpB |
gnl|CDD|280099 |
pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.
|
6.24762e-54 |
| NZ_CP032906.1|WP_139519481.1|519336_520335_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase |
gnl|CDD|273675 |
TIGR01534, Glyceraldehyde-3-phosphate_dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, type I. This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis].
|
3.42498e-161 |
| NZ_CP032906.1|WP_050831075.1|509511_510093_-|recombination-protein-RecR |
gnl|CDD|273176 |
TIGR00615, Recombination_protein_RecR, recombination protein RecR. All proteins in this family for which functions are known are involved in the initiation of recombination and recombinational repair. RecF is also required. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair].
|
2.19239e-97 |
| NZ_CP032906.1|WP_139519479.1|524531_524963_+|Sua5-YciO-YrdC-YwlC-family-protein |
gnl|CDD|376519 |
pfam01300, Sua5_yciO_yrdC, Telomere recombination. This domain has been shown to bind preferentially to dsRNA. The domain is found in SUA5 as well as HypF and YrdC. It has also been shown to be required for telomere recombniation in yeast.
|
2.49017e-05 |
| NZ_CP032906.1|WP_139519480.1|521269_524527_+|carbamoyl-phosphate-synthase-large-subunit |
gnl|CDD|235393 |
PRK05294, carB, carbamoyl-phosphate synthase large subunit.
|
0 |
| NZ_CP032906.1|WP_139519483.1|510517_511627_-|Hop-family-outer-membrane-protein-HopJ/HopK |
gnl|CDD|280099 |
pfam01856, HP_OMP, Helicobacter outer membrane protein. This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins.
|
7.70991e-49 |
| NZ_CP032906.1|WP_000426949.1|506907_507450_-|GTP-cyclohydrolase-I-FolE |
gnl|CDD|129173 |
TIGR00063, GTP_cyclohydrolase_1, GTP cyclohydrolase I. alternate names: Punch (Drosophila),GTP cyclohydrolase I (EC 3.5.4.16) catalyzes the biosynthesis of formic acid and dihydroneopterin triphosphate from GTP. This reaction is the first step in the biosynthesis of tetrahydrofolate in prokaryotes, of tetrahydrobiopterin in vertebrates, and of pteridine-containing pigments in insects. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid].
|
1.19934e-105 |
| NZ_CP032906.1|WP_139519487.1|505180_505984_-|5'/3'-nucleotidase-SurE |
gnl|CDD|234732 |
PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.
|
5.48341e-126 |
| NZ_CP032906.1|WP_139519485.1|507450_508431_-|zinc-metalloprotease-HtpX |
gnl|CDD|235081 |
PRK02870, PRK02870, heat shock protein HtpX; Provisional.
|
0 |
| NZ_CP032906.1|WP_139535732.1|536265_537405_-|N-6-DNA-methylase |
gnl|CDD|223897 |
COG0827, COG0827, Adenine-specific DNA methylase [DNA replication, recombination, and repair].
|
3.39102e-52 |
