match idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1pfam02627843791.40.39[                      -------                    ]CMDCarboxymuconolactone decarboxylase family. Carboxymuconolactone decarboxylase (CMD) EC: is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway. In these bifunctional proteins CMD represents the C-terminal domain, pfam00561 represents the N-terminal domain.
2PRK014064766880.62.1[                       -------------             ]gltXglutamyl-tRNA synthetase; Reviewed
3COG05991246271.82.7[                 ------------                    ]YurZUncharacterized conserved protein YurZ, alkylhydroperoxidase/carboxymuconolactone decarboxylase family
4TIGR003501525066.15[                                ------------     ]lytR_cpsA_psrcell envelope-related function transcriptional attenuator common domain. This model describes a domain of unknown function that is found in the predicted extracellular domain of a number of putative membrane-bound proteins. One of these is proteins psr, described as a penicillin binding protein 5 (PDP-5) synthesis repressor. Another is Bacillus subtilis LytR, described as a transcriptional attenuator of itself and the LytABC operon, where LytC is N-acetylmuramoyl-L-alanine amidase. A third is CpsA, a putative regulatory protein involved in exocellular polysaccharide biosynthesis. Besides the region of strong similarily represented by this model, these proteins share the property of having a short putative N-terminal cytoplasmic domain and transmembrane domain forming a signal-anchor.
5TIGR00778502364.411[                      ----                       ]ahpD_domalkylhydroperoxidase AhpD family core domain. This model represents a 51-residue core region of homology among a family of mostly uncharacterized proteins of 110 to 227 amino acids. Most members of this family contain the motif EXXXXXX
6COG56448697763.08.1[               -----------------                 ]COG5644U3 small nucleolar RNA-associated protein 14
7pfam133731292650.412[                       -----                     ]DUF2407_CDUF2407 C-terminal domain. This is a family of proteins found in fungi. The function is not known. There is a characteristic GFDRL sequence motif.
8COG20112222043.016[                      ---                        ]MetPABC-type methionine transport system, permease component
9pfam13411694342.123[                  --------                       ]MerR_1MerR HTH family regulatory protein.
10pfam111981812341.518[                      -----                      ]DUF2857Protein of unknown function (DUF2857). This is a bacterial family of uncharacterized proteins.
11pfam01466783441.128[                      --------                   ]Skp1Skp1 family, dimerization domain.
12cd00569421940.925[                      ----                       ]HTH_Hin_likeHelix-turn-helix domain of Hin and related proteins. This domain model summarizes a family of DNA-binding domains unique to bacteria and represented by the Hin protein of Salmonella. The basic HTH domain is a simple fold comprised of three core helices that form a right-handed helical bundle. The principal DNA-protein interface is formed by the third helix, the recognition helix, inserting itself into the major groove of the DNA. A diverse array of HTH domains participate in a variety of functions that depend on their DNA-binding properties. HTH_Hin represents one of the simplest versions of the HTH domains; the characterization of homologous relationships between various sequence-diverse HTH domain families remains difficult. The Hin recombinase induces the site-specific inversion of a chromosomal DNA segment containing a promoter, which controls the alternate expression of two genes by reversibly switching orientation. The Hin recombinase consists of a single polypeptide chain containing a C-terminal DNA-binding domain (HTH_Hin) and a catalytic domain.
13cd142451144540.528[                                     ---------   ]DMP12Putative DNA mimic protein DMP12. The Neisseria sp. protein DMP12 has been shown to interact with the bacterial histone-like protein HU and may do so by acting as a DNA mimic. It is likely to play a regulatory role, but not via direct competition for binding of HU, which is involved in maintenance of the bacterial nucleoid structure.
14cd135522663140.017[                                       ------    ]PBP2_Fbp_like_6Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
15pfam10911775539.274[               ------------                      ]DUF2717Protein of unknown function (DUF2717). Members in this family of proteins are annotated as gene 6.5 protein however currently there is no known function.
16PRK091945654138.720[                                        -------- ]PRK09194prolyl-tRNA synthetase; Provisional
17pfam12554483938.464[                 ---------                       ]MOZART1Mitotic-spindle organizing gamma-tubulin ring associated. The name MOZART is derived from letters of 'mitotic-spindle organizing proteins associated with a ring of gamma-tubulin'. This family operates as part of the gamma-tubulin ring complex, gamma-TuRC, one of the complexes necessary for chromosome segregation. This complex is located at centrosomes and mediates the formation of bipolar spindles in mitosis; it consists of six subunits. However, unlike the other four known subunits, this family does not carry the conserved 'Spc97-Spc98' GCP domain, so the TUBCGP nomenclature cannot be used for it. MOZART1 is required for gamma-TuRC recruitment to centrosomes.
18pfam14407602036.936[                       ----                      ]Frankia_peptideRibosomally synthesized peptide prototyped by Frankia Franean1_4349. Ribosomally synthesized peptide linked to cyclases in chloroflexi. It may have a link to cyclic nucleotide signaling.
19TIGR010644726735.038[                           --------------        ]pyruv_kinpyruvate kinase. This enzyme is a homotetramer. Some forms are active only in the presence of fructose-1,6-bisphosphate or similar phosphorylated sugars.
20PRK107922856433.651[                            -------------        ]PRK10792bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional
21PRK107822171831.829[                      ---                        ]PRK10782DL-methionine transporter permease subunit; Provisional
22cd005302933329.82.1E+02[                    ------                       ]PTEPhosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including the chemical warfare agents VX, soman, and sarin as well as the insecticide paraoxon. PTE exists as a homodimer with one active site per monomer. The active site is located next to a binuclear metal center, at the C-terminal end of a TIM alpha- beta barrel motif. The native enzyme contains two zinc ions at the active site however these can be replaced with other metals such as cobalt, cadmium, nickel or manganese and the enzyme remains active.
23pfam13348682228.961[                      ----                       ]Y_phosphatase3CTyrosine phosphatase family C-terminal region.
24PRK133791192228.847[                       ----                      ]PRK13379protocatechuate 4,5-dioxygenase subunit alpha; Provisional
25PRK130183785128.232[------------                                     ]PRK13018cell division protein FtsZ; Provisional
26COG45476203227.131[                                           ------]CobT2Cobalamin biosynthesis protein CobT (nicotinate-mononucleotide:5, 6-dimethylbenzimidazole phosphorib...
27PRK113022842226.933[ ----                                            ]PRK11302DNA-binding transcriptional regulator HexR; Provisional
28cd14310302126.742[                       ----                      ]UBA_cnDdi1_likeUBA domain found in Cryptococcus neoformans DNA-damage response protein Ddi1 and similar proteins. The family includes some uncharacterized Ddi and similar proteins which show a high level of sequence similarity with yeast Ddi1. Ddi1, also called v-SNARE-master 1 (Vsm1), is a ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in yeast. It functions as a ubiquitin association domain (UBA)- ubiquitin-like-domain (UBL) shuttle protein that is required for the proteasome to enable ubiquitin-dependent degradation of its ligands. Ddi1 contains an N-terminal UBL domain and a C-terminal UBA domain. It also harbors a central retroviral aspartyl-protease-like domain (RVP) which may be important in cell-cycle control. At this point, Ddi1 may function proteolytically during regulated protein turnover in the cell.
29COG06183328626.354[              ------------------                 ]NrnAnanoRNase/pAp phosphatase, hydrolyzes c-di-AMP and oligoRNAs
30PRK111254804425.51.8E+02[                  ----------                     ]nrfAcytochrome c nitrite reductase subunit c552; Provisional
31pfam13351845325.351[                       ------------              ]DUF4099Protein of unknown function (DUF4099). A family of uncharacterized proteins found by clustering human gut metagenomic sequences. The C-terminal repeat region of this family is DUF4098, pfam13345.
32pfam072281926024.91.9E+02[                                 --------------- ]SpoIIEStage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC: These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.
33cd08784801724.854[                       ----                      ]Death_DRsDeath Domain of Death Receptors. Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
34pfam028871175724.767[                             -----------         ]PK_CPyruvate kinase, alpha/beta domain. As well as being found in pyruvate kinase this family is found as an isolated domain in some bacterial proteins.
35PRK151103214524.735[                                      ---------  ]PRK15110antimicrobial peptide ABC transporter permease SapB; Provisional
36pfam089631133924.42.4E+02[                     --------                    ]DUF1878Protein of unknown function (DUF1878). This domain is found in a set of hypothetical bacterial proteins.
37pfam027871221823.81.9E+02[                       ---                       ]CPSase_L_D3Carbamoyl-phosphate synthetase large chain, oligomerization domain. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
38cd007792553923.745[                                        -------  ]ProRS_core_prokProlyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
39pfam10979431323.71.2E+02[                         ---                     ]DUF2786Protein of unknown function (DUF2786). This family of proteins has no known function.
40pfam156011332923.458[  ------                                         ]Imm42Immunity protein 42. A predicted immunity protein with an alpha+beta fold and conserved tyrosine and tryptophan residues. Proteins containing this domain are present in bacterial polymorphic toxin systems as an immediate gene neighbor of the toxin gene, which usually contains toxin domains of the Tox-REase-10 family.
41cd00570714323.064[  ----------                                     ]GST_N_familyGlutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.
42pfam12327953422.343[ -------                                         ]FtsZ_CFtsZ family, C-terminal domain. This family includes the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ is a GTPase, like tubulin. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea.
43cd085852378222.130[       -----------------                         ]GDPD_like_3Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity with Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.
44pfam00725971821.972[                       ----                      ]3HCDH3-hydroxyacyl-CoA dehydrogenase, C-terminal domain. This family also includes lambda crystallin. Some proteins include two copies of this domain.
45pfam112681694021.770[                       -------                   ]DUF3071Protein of unknown function (DUF3071). Some members in this family of proteins are annotated as DNA-binding proteins however this cannot be confirmed. Currently no function is known.
46pfam007493145321.63E+02[                ------------                     ]tRNA-synt_1ctRNA synthetases class I (E and Q), catalytic domain. Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organisms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
47pfam038643284721.689[                       ---------                 ]Phage_cap_EPhage major capsid protein E. Major capsid protein E is involved with the stabilisation of the condensed form of the DNA molecule in phage heads.
48cd03060711420.958[         ---                                     ]GST_N_Omega_likeGST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. Like Omega enzymes, proteins in this subfamily contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism.
49pfam107781593120.982[                       ------                    ]DehIHalocarboxylic acid dehydrogenase DehI. Haloacid dehalogenases catalyse the removal of halides from organic haloacids. DehI can process both L- and D-substrates. A crucial aspartate residue is predicted to activate a water molecule for nucleophilic attack of the substrate chiral centre resulting in an inversion of the configuration of either L- or D-substrates in contrast to D-only enzymes.