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Chain D, Hemoglobin subunit beta
hemoglobin beta-like protein( domain architecture ID 10172378)
hemoglobin beta-like protein is either one of gamma, delta, epsilon, or related 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
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Name | Accession | Description | Interval | E-value | |||
Hb-beta-like | cd08925 | Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ... |
7-145 | 1.01e-90 | |||
Hemoglobin beta, gamma, delta, epsilon, and related 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. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors. : Pssm-ID: 381262 Cd Length: 139 Bit Score: 259.49 E-value: 1.01e-90
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Name | Accession | Description | Interval | E-value | |||
Hb-beta-like | cd08925 | Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ... |
7-145 | 1.01e-90 | |||
Hemoglobin beta, gamma, delta, epsilon, and related 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. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors. Pssm-ID: 381262 Cd Length: 139 Bit Score: 259.49 E-value: 1.01e-90
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Globin | pfam00042 | Globin; |
25-141 | 8.90e-39 | |||
Globin; Pssm-ID: 459646 [Multi-domain] Cd Length: 117 Bit Score: 127.02 E-value: 8.90e-39
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Hmp | COG1017 | Hemoglobin-like flavoprotein [Energy production and conversion]; |
4-141 | 3.00e-06 | |||
Hemoglobin-like flavoprotein [Energy production and conversion]; Pssm-ID: 440640 [Multi-domain] Cd Length: 135 Bit Score: 43.99 E-value: 3.00e-06
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Name | Accession | Description | Interval | E-value | |||
Hb-beta-like | cd08925 | Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ... |
7-145 | 1.01e-90 | |||
Hemoglobin beta, gamma, delta, epsilon, and related 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. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors. Pssm-ID: 381262 Cd Length: 139 Bit Score: 259.49 E-value: 1.01e-90
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Hb | cd14765 | Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ... |
7-142 | 1.38e-75 | |||
Hemoglobins; 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. Other Hb types are: HbA2 (alpha2delta2) which, in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary Hb throughout most of gestation. These Hb types have differences in O2 affinity and in their interactions with allosteric effectors. Pssm-ID: 381278 Cd Length: 131 Bit Score: 221.07 E-value: 1.38e-75
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Hb-alpha-like | cd08927 | Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ... |
4-145 | 8.47e-50 | |||
Hemoglobin alpha, zeta, mu, theta, and related 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. Other Hb types are: HbA2 (alpha2delta2) which in normal individuals, is naturally expressed at a low level; Hb Portland-1 (zeta2gamma2), Hb Gower-1 (zeta2epsilon2), and Hb Gower-2 (alpha2epsilon2), which are Hbs present during the embryonic period; and fetal hemoglobin (HbF, alpha2gamma2), the primary hemoglobin throughout most of gestation. These Hbs types have differences in O2 affinity and in their interactions with allosteric effectors. Pssm-ID: 381263 Cd Length: 140 Bit Score: 155.81 E-value: 8.47e-50
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Globin | pfam00042 | Globin; |
25-141 | 8.90e-39 | |||
Globin; Pssm-ID: 459646 [Multi-domain] Cd Length: 117 Bit Score: 127.02 E-value: 8.90e-39
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Mb-like | cd01040 | myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ... |
11-141 | 5.27e-23 | |||
myoglobin-like; M family globin domain; This 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 M family exhibits 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). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd. Pssm-ID: 381254 Cd Length: 133 Bit Score: 87.51 E-value: 5.27e-23
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Cygb | cd08924 | Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ... |
4-145 | 6.54e-22 | |||
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to bind O2, NO and carbon monoxide. It has both nitric oxide dioxygenase and lipid peroxidase activities, and potentially participates in the maintenance of normal phenotype by implementing a homeostatic effect, to counteract stress conditions imposed on a cell. Cygb is implicated in multiple human pathologies: it is up-regulated in fibrosis and neurodegenerative disorders, and down-regulated in multiple cancer types, and may have a tumor suppressor role. It is expressed ubiquitously across a broad range of vertebrate organs including liver, heart, brain, lung, retina, and gut. In the human brain, it was detected at high levels in the habenula, hypothalamus, thalamus, hippocampus and pontine tegmental nuclei, detected at a low level in the cerebral cortex, and undetected in the cerebellar cortex. Pssm-ID: 271275 Cd Length: 153 Bit Score: 85.28 E-value: 6.54e-22
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Mb | cd08926 | Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ... |
7-145 | 1.30e-18 | |||
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein whose expression has long been considered limited to cardiomyocytes and striated skeletal muscle cell, however it has recently been found localized in a wide variety of tissues including smooth muscle cells. As a physiological catalyst, it can modulate reactive oxygen species levels, facilitate oxygen diffusion within the cell, and scavenge or generate NO depending on oxygen tensions within the cell. Through its NO dioxygenase and nitrite reductase activities, Mb regulates mitochondrial function in energy-demanding tissues. Pssm-ID: 271277 Cd Length: 148 Bit Score: 76.73 E-value: 1.30e-18
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HGbI-like | cd12131 | Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ... |
7-138 | 7.77e-09 | |||
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a single-domain heme-containing protein isolated from Methylacidiphilum infernorum, an aerobic acidophilic and thermophilic methanotroph. M. infernorum grows optimally at pH 2.0 and 60C and its home is New Zealand's Hell's Gate geothermal park. The physiological role of HGbI has yet to be determined. It has an extremely strong resistance to auto-oxidation, and has fast oxygen-binding/slow release characteristics. Its CO on-rate is comparable to the O2 on-rate, and it is able to bind acetate with high affinity in the ferric state. The coordination of the heme iron changes in the ferrous form from pentacoordinate at low pH to predominantly hexacoordinate at high pH; in the ferric form, it is predominantly hexacoordinate at all pH. Pssm-ID: 381269 [Multi-domain] Cd Length: 128 Bit Score: 50.63 E-value: 7.77e-09
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CeGLB25-like | cd14766 | Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ... |
19-137 | 3.82e-07 | |||
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 genes encoding globins that are all transcribed. These are very diverse in gene and protein structure and are localized in a variety of cells. The C. elegans globin GLB-25 (locus tag T06A1.3), like the majority of them, was expressed in neuronal cells in the head and tail portions of the body and in the nerve cord. Pssm-ID: 381279 Cd Length: 137 Bit Score: 46.16 E-value: 3.82e-07
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Ngb | cd08920 | Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ... |
4-143 | 1.12e-06 | |||
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly expressed in neurons of the brain and retina. In the human brain, it is highly expressed in the hypothalamus, amygdala, and in the pontine tegmental nuclei. It affords protection of brain neurons from ischemia and hypoxia. In rats, it plays a role in the neuroprotection of limb ischemic preconditioning (LIP). It plays roles as: a sensor of oxygen levels; a store or reservoir for oxygen; a facilitator for oxygen transport; a regulator of ROS; and a scavenger of nitric oxide. It also functions in the protection against apoptosis and in sleep regulation. This subgroup contains Ngb from mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles; the functionally pentacoordinated acoelomorph Symsagittifera roscoffensis Ngb does not belong to this subgroup. Pssm-ID: 271272 Cd Length: 148 Bit Score: 45.21 E-value: 1.12e-06
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Hmp | COG1017 | Hemoglobin-like flavoprotein [Energy production and conversion]; |
4-141 | 3.00e-06 | |||
Hemoglobin-like flavoprotein [Energy production and conversion]; Pssm-ID: 440640 [Multi-domain] Cd Length: 135 Bit Score: 43.99 E-value: 3.00e-06
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GbX | cd12137 | Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ... |
4-143 | 4.71e-05 | |||
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central nervous system, and appears to be associated with the sensory system. GbX is likely to be attached to the cell membrane via S-palmitoylation and N-myristoylation. It's unlikely to have a true respiratory function as it is membrane-associated. It has been suggested that it may protect the lipids in the cell membrane from oxidation or act as a redox-sensing or signaling protein. Zebrafish GbX is hexacoordinate, and displays cooperative O2 binding. Pssm-ID: 271287 Cd Length: 145 Bit Score: 40.75 E-value: 4.71e-05
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Mb-like_oxidoreductase | cd19753 | Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ... |
62-140 | 2.35e-03 | |||
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. NO scavenging by flavoHb attenuates the expression of the nitrosative stress response, affects the swarming behavior of Escherichia coli, and maintains squid-Vibrio fischeri and Medicago truncatula-Sinorhizobium meliloti symbioses. Pssm-ID: 381293 [Multi-domain] Cd Length: 121 Bit Score: 35.68 E-value: 2.35e-03
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