match idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1pfam029051466942.653[                                 ----------      ]EBV-NA1Epstein Barr virus nuclear antigen-1, DNA-binding domain. This domain has a ferredoxin-like fold.
2pfam13974804641.539[        -------                                  ]YebOYebO-like protein. This short protein is uncharacterized. It seems likely to be of phage origin. The protein is also found in a variety of enteric bacteria.
3pfam003352216440.690[  --------                                       ]TetraspanninTetraspanin family.
4cd014934258738.639[                                 -------------   ]APPBP1_RUBUbiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.
5pfam05570292435.029[                                             --- ]DUF765Circovirus protein of unknown function (DUF765). This family consists of several short (27-30aa) porcine and bovine circovirus ORF6 proteins of unknown function.
6PRK10878723731.928[           ----                                  ]PRK10878hypothetical protein; Provisional
7cd12095392627.769[       ---                                       ]TM_ErbB3Transmembrane domain of ErbB3, a Protein Tyrosine Kinase. ErbB3 (HER3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane (TM) helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. ErbB receptors are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. ErbB3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. ErbB3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The ErbB2-ErbB3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. The TM domain not only serves as a membrane anchor, but also plays an important role in receptor dimerization and optimal activation. Mutations in the TM domain of ErbB receptors have been associated with increased breast cancer risk. ErbB3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells.
8pfam101161293726.093[                                  -----          ]Host_attachProtein required for attachment to host cells. Members of this family of bacterial proteins are required for the attachment of the bacterium to host cells.
9pfam0342817710225.41.4E+02[   --------------                                ]RP-CReplication protein C N-terminal domain. Replication protein C is involved in the early stages of viral DNA replication.
10PRK10591926224.81.9E+02[ ---------                                       ]PRK10591hypothetical protein; Provisional
11cd097362892723.831[                    ---                          ]Csy2_I-FCRISPR/Cas system-associated RAMP superfamily protein Csy2. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein; predicted Cas5 ortholog
12cd060992137322.747[            ----------                           ]CS_ACL-C_CCLCitrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL.
13PRK136591035321.52.6E+02[        -------                                  ]PRK13659hypothetical protein; Provisional
14PRK107354819421.51.3E+02[                           ------------          ]tldDprotease TldD; Provisional
15pfam107391293320.61.6E+02[        ----                                     ]DUF2550Protein of unknown function (DUF2550). This family is conserved in Corynebacterineae. The function is not known though most members are annotated as either secreted, or membrane, proteins.