MULTISPECIES: globin-like protein [Priestia]
globin family protein; hemoglobin alpha subunit family protein( domain architecture ID 10201299)
globin family protein is an all-helical protein that may bind porphyrins, phycobilins, and other non-heme cofactors, and may play various roles including as a sensor or transporter of oxygen| hemoglobin alpha subunit family protein is either one of alpha, zeta, mu, theta, or related hemoglobin (Hb) subunits. Hb is the oxygen transport protein of erythrocytes. It is an allosterically modulated heterotetramer. Hemoglobin A (HbA) is the most common Hb in adult humans, and is formed from two alpha-chains and two beta-chains (alpha2beta2). An equilibrium exists between deoxygenated/unliganded/T(tense state) Hb having low oxygen affinity, and oxygenated /liganded/R(relaxed state) Hb having a high oxygen affinity. Various endogenous heterotropic effectors bind Hb to modulate its oxygen affinity and cooperative behavior, e.g. hydrogen ions, chloride ions, carbon dioxide and 2,3-bisphosphoglycerate. Hb is also an allosterically regulated nitrite reductase; the plasma nitrite anion may be activated by hemoglobin in areas of hypoxia to bring about vasodilation.
List of domain hits
Name | Accession | Description | Interval | E-value | |||
TrHb2_Bs-trHb-like_O | cd14772 | Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like; The M- and S families exhibit ... |
9-124 | 8.60e-74 | |||
Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include monomeric Bacillus subtilis trHb (Bs-trHb), which exhibits an extremely high oxygen affinity, and a dimeric TrHb2 from the thermophilic aerobic spore forming bacterium Geobacillus stearothermophilus(Gs-trHb). : Pssm-ID: 381281 Cd Length: 116 Bit Score: 215.35 E-value: 8.60e-74
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Name | Accession | Description | Interval | E-value | |||
TrHb2_Bs-trHb-like_O | cd14772 | Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like; The M- and S families exhibit ... |
9-124 | 8.60e-74 | |||
Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include monomeric Bacillus subtilis trHb (Bs-trHb), which exhibits an extremely high oxygen affinity, and a dimeric TrHb2 from the thermophilic aerobic spore forming bacterium Geobacillus stearothermophilus(Gs-trHb). Pssm-ID: 381281 Cd Length: 116 Bit Score: 215.35 E-value: 8.60e-74
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YjbI | COG2346 | Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]; |
7-124 | 6.94e-45 | |||
Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]; Pssm-ID: 441915 Cd Length: 120 Bit Score: 142.32 E-value: 6.94e-45
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Bac_globin | pfam01152 | Bacterial-like globin; This family of heme binding proteins are found mainly in bacteria. ... |
9-124 | 8.62e-37 | |||
Bacterial-like globin; This family of heme binding proteins are found mainly in bacteria. However they can also be found in some protozoa and plants as well. Pssm-ID: 395917 Cd Length: 121 Bit Score: 121.75 E-value: 8.62e-37
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Name | Accession | Description | Interval | E-value | |||
TrHb2_Bs-trHb-like_O | cd14772 | Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like; The M- and S families exhibit ... |
9-124 | 8.60e-74 | |||
Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include monomeric Bacillus subtilis trHb (Bs-trHb), which exhibits an extremely high oxygen affinity, and a dimeric TrHb2 from the thermophilic aerobic spore forming bacterium Geobacillus stearothermophilus(Gs-trHb). Pssm-ID: 381281 Cd Length: 116 Bit Score: 215.35 E-value: 8.60e-74
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TrHb2_O | cd08917 | Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 2 (O); The M- and S families exhibit ... |
9-124 | 1.77e-52 | |||
Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 2 (O); The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2s include the dimeric Arabidopsis thaliana TrHb2 AtGLB3. GLB3 is likely to have a function distinct from other plant globins: it exhibits a low O2 affinity, an unusual concentration-independent binding of O2 and CO, and does not respond to any of the treatments that induce plant 3-on-3 globins. Other TrHb2's include Bacillus subtilis trHb (Bs-trHb) which exhibits an extremely high oxygen affinity, and Pseudoalteromonas haloplanktis PhHbO (encoded by the PSHAa0030 gene) which appears to be involved in oxidative and nitrosative stress resistance. Pssm-ID: 381258 Cd Length: 116 Bit Score: 161.34 E-value: 1.77e-52
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YjbI | COG2346 | Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]; |
7-124 | 6.94e-45 | |||
Truncated hemoglobin YjbI [Inorganic ion transport and metabolism]; Pssm-ID: 441915 Cd Length: 120 Bit Score: 142.32 E-value: 6.94e-45
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TrHb2_PhHbO-like_O | cd14773 | Truncated hemoglobins, group 2 (O); Pseudoalteromonas haloplanktis PhHbO like; The M- and S ... |
9-124 | 1.47e-41 | |||
Truncated hemoglobins, group 2 (O); Pseudoalteromonas haloplanktis PhHbO like; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include Pseudoalteromonas haloplanktis PhHbO (encoded by the PSHAa0030 gene) which appears to be involved in oxidative and nitrosative stress resistance. Pssm-ID: 381282 Cd Length: 119 Bit Score: 133.82 E-value: 1.47e-41
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TrHb2_Mt-trHbO-like_O | cd14771 | Truncated hemoglobins, group 2 (O); Mycobacterium tuberculosis hemoglobin O like; The M- and S ... |
9-125 | 1.91e-38 | |||
Truncated hemoglobins, group 2 (O); Mycobacterium tuberculosis hemoglobin O like; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). This group includes a Mycobacterium tuberculosis TrHb2, Mt-trHbO, encoded by the Mycobacterium tuberculosis glbO gene, which is expressed throughout the Mycobacterium growth phase. It also includes a TrHb2 from the thermophilic Thermobifida fusca ( Tf-trHb) which has a high thermostability and at the optimal growth temperature for Thermobifida fusca (between 55 and 60 degrees C ), it is capable of efficient O2 binding and release. Tf-trHb shares a relatively slow rate of oxygen binding with Mt-trHbO. Pssm-ID: 381280 Cd Length: 119 Bit Score: 125.85 E-value: 1.91e-38
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Bac_globin | pfam01152 | Bacterial-like globin; This family of heme binding proteins are found mainly in bacteria. ... |
9-124 | 8.62e-37 | |||
Bacterial-like globin; This family of heme binding proteins are found mainly in bacteria. However they can also be found in some protozoa and plants as well. Pssm-ID: 395917 Cd Length: 121 Bit Score: 121.75 E-value: 8.62e-37
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TrHb | cd14756 | Truncated Mb-fold globins, T family; The M- and S families exhibit the canonical secondary ... |
10-122 | 3.47e-33 | |||
Truncated Mb-fold globins, T family; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Typical of the TrHb1s (N) group is a protein matrix tunnel. An example of a TrHb1 is Mycobacterium tuberculosis TrHb1/Mt-trHbN which is expressed during the Mycobacterium stationary phase, and plays a specific defense role against nitrosative stress. TrHb2s include the dimeric Arabidopsis thaliana TrHb2 AtGLB3. GLB3 is likely to have a function distinct from other plant globins: it exhibits a low O2 affinity, an unusual concentration-independent binding of O2 and CO, and does not respond to any of the treatments that induce plant 3-on-3 globins. TrHb3s include Campylobacter jejuni Ctb, encoded by Cj0465c, which may play a role in moderating O2 flux within C. jejuni. Pssm-ID: 381270 [Multi-domain] Cd Length: 111 Bit Score: 112.50 E-value: 3.47e-33
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TrHb2_HGbIV-like_O | cd14774 | hell's gate globin IV and similar truncated hemoglobins, group 2 (O); The M- and S families ... |
14-126 | 2.54e-21 | |||
hell's gate globin IV and similar truncated hemoglobins, group 2 (O); The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Pssm-ID: 381283 Cd Length: 131 Bit Score: 82.73 E-value: 2.54e-21
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TrHb1_N | cd00454 | truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 1 (N); The M- and S families exhibit ... |
10-111 | 5.04e-18 | |||
truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 1 (N); The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Typical of the TrHb1s (N) group is a protein matrix tunnel. It includes a Mycobacterium tuberculosis TrHb1, Mt-trHbN, which is encoded by the glbN gene. Mt-trHbN is expressed during the Mycobacterium stationary phase, and plays a specific defense role against nitrosative stress. The cyanobacterium Synechococcus sp. PCC 7002 TrHb1 GlbN, is constitutively expressed, and likely also protects cells from reactive nitrogen species. Pssm-ID: 381253 Cd Length: 111 Bit Score: 73.73 E-value: 5.04e-18
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TrHb2_AtGlb3-like_O | cd19755 | nonsymbiotic haemoglobin Ahb3 (GLB3) and similar truncated hemoglobins, group 2 (O); The M- ... |
9-110 | 8.68e-18 | |||
nonsymbiotic haemoglobin Ahb3 (GLB3) and similar truncated hemoglobins, group 2 (O); The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). This subfamily includes the dimeric Arabidopsis thaliana TrHb2 AtGLB3. GLB3 is likely to have a function distinct from other plant globins: it exhibits a low O2 affinity, an unusual concentration-independent binding of O2 and CO, and does not respond to any of the treatments that induce plant 3-on-3 globins. Pssm-ID: 381295 Cd Length: 119 Bit Score: 73.55 E-value: 8.68e-18
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TrHb2_O-like | cd14775 | Truncated hemoglobins, group 2 (O); uncharacterized subgroup; The M- and S families exhibit ... |
9-108 | 1.62e-17 | |||
Truncated hemoglobins, group 2 (O); uncharacterized subgroup; The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Pssm-ID: 381284 Cd Length: 119 Bit Score: 72.66 E-value: 1.62e-17
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Globin-like | cd01067 | Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ... |
18-101 | 1.07e-16 | |||
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety of all-helical proteins that bind porphyrins, phycobilins, and other non-heme cofactors, and play various roles in all three kingdoms of life, including sensors or transporters of oxygen. It includes the M/myoglobin-like, S/sensor globin, and T/truncated globin (TrHb) families, and the phycobiliproteins (PBPs). The M family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The S family includes GCS/globin-coupled sensors, Pgbs/protoglobins, and SSDgbs/sensor single domain globins. The T family is classified into three main groups: TrHb1s (N), TrHb2s (O) and TrHb3s (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). For M family Adgbs, this globin domain is permuted, such that C-H are followed by A-B. The T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. PBPs bind the linear tetrapyrrole chromophore, phycobilin, a prosthetic group chemically and metabolically related to iron protoporphyrin IX/protoheme. Examples of other globin-like domains which bind non-heme cofactors include those of the Bacillus anthracis sporulation inhibitors pXO1-118 and pXO2-61 which bind fatty acid and halide in vitro, and the globin-like domain of Bacillus subtilis RsbRA which is presumed to channel sensory input to the C-terminal sulfate transporter/ anti-sigma factor antagonist (STAT) domain. RsbRA is a component of the sigma B-activating stressosome, and a regulator of the RNA polymerase sigma factor subunit sigma (B). Pssm-ID: 381255 [Multi-domain] Cd Length: 119 Bit Score: 70.56 E-value: 1.07e-16
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TrHb3_P | cd08916 | Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 3 (P); The M- and S families exhibit ... |
18-122 | 1.41e-08 | |||
Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 3 (P); The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb3s include Campylobacter jejuni Ctb, encoded by Cj0465c, which may play a role in moderating O2 flux within C. jejuni. Pssm-ID: 381257 Cd Length: 116 Bit Score: 49.46 E-value: 1.41e-08
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globin_sensor | cd01068 | Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ... |
15-52 | 4.29e-04 | |||
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain. Pssm-ID: 381256 [Multi-domain] Cd Length: 146 Bit Score: 37.94 E-value: 4.29e-04
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Protoglobin | pfam11563 | Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also ... |
15-58 | 1.73e-03 | |||
Protoglobin; This family includes protoglobin from Methanosarcina acetivorans C2A. It is also found near the N-terminus of the Haem-based aerotactic transducer HemAT in Bacillus subtilis. It is part of the haemoglobin superfamily. Protoglobin has specific loops and an amino-terminal extension which leads to the burying of the haem within the matrix of the protein. Protoglobin-specific apolar tunnels allow the access of O2, CO and NO to the haem distal site. In HemAT it acts as an oxygen sensor domain. It can also recognize cyanide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 431935 [Multi-domain] Cd Length: 149 Bit Score: 36.41 E-value: 1.73e-03
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