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Conserved domains on  [gi|4504349|ref|NP_000509|]
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hemoglobin subunit beta [Homo sapiens]

Protein Classification

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.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-146 7.89e-87

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: 249.48  E-value: 7.89e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    8 EKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFA 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504349   88 TLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKY 146
Cdd:cd08925  81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
 
Name Accession Description Interval E-value
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-146 7.89e-87

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: 249.48  E-value: 7.89e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    8 EKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFA 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504349   88 TLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKY 146
Cdd:cd08925  81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Globin pfam00042
Globin;
27-142 8.29e-35

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 117.00  E-value: 8.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349     27 EALGRLLVVYPWTQRFFESFGDlsTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLK---GTFATLSELHCDKLHVDPEN 103
Cdd:pfam00042   2 EILARLFTAYPDTKAYFPRFEK--SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 4504349    104 FRLLGNVLVCVLAHHFGkEFTPPVQAAYQKVVAGVANAL 142
Cdd:pfam00042  80 FKLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 8-146 7.89e-87

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: 249.48  E-value: 7.89e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    8 EKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFA 87
Cdd:cd08925   1 EKAAITAVWGKVDVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504349   88 TLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKY 146
Cdd:cd08925  81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 8-143 4.10e-74

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: 217.22  E-value: 4.10e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    8 EKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTpdavmGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFA 87
Cdd:cd14765   1 EKSTIKALWGKVNVEEYGAEALARLFVVYPWTKRYFPKFDDSSS-----GNPKVKAHGKKVLGALGDAVKHLDDLKNTFS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504349   88 TLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALA 143
Cdd:cd14765  76 DLSELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 4-146 1.43e-44

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: 142.71  E-value: 1.43e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    4 LTPEEKSAVTALWGKV--NVDEVGGEALGRLLVVYPWTQRFFESFgDLSTpdavmGNPKVKAHGKKVLGAFSDGLAHLDN 81
Cdd:cd08927   1 LSAADKALIKALWGKIagHAEAIGAEALARMFLSFPQTKTYFPHF-DLSA-----GSAQVKAHGKKVMDALGDAVKHLDD 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504349   82 LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKY 146
Cdd:cd08927  75 LPGALSKLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKY 139
Globin pfam00042
Globin;
27-142 8.29e-35

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 117.00  E-value: 8.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349     27 EALGRLLVVYPWTQRFFESFGDlsTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLK---GTFATLSELHCDKLHVDPEN 103
Cdd:pfam00042   2 EILARLFTAYPDTKAYFPRFEK--SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 4504349    104 FRLLGNVLVCVLAHHFGkEFTPPVQAAYQKVVAGVANAL 142
Cdd:pfam00042  80 FKLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 12-142 2.59e-20

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: 80.58  E-value: 2.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349   12 VTALWGKV--NVDEVGGEALGRLLVVYPWTQRFFESFGDLstPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATL 89
Cdd:cd01040   1 VKSSWARVkkDKEEFGVAIFLRLFEANPELKKLFPKFAGV--DLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALL 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4504349   90 SEL---HCdKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANAL 142
Cdd:cd01040  79 RKLgkrHK-RRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 4-136 3.04e-20

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: 81.04  E-value: 3.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    4 LTPEEKSAVTALWGKV--NVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN 81
Cdd:cd08924   1 LTEAERKVIQDTWARVyaNCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504349   82 ---LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVA 136
Cdd:cd08924  81 pdkVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRG 138
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 11-146 9.81e-17

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: 71.72  E-value: 9.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349   11 AVTALWGKVNVD--EVGGEALGRLLVVYPWTQRFFESFGDLSTpDAVMGNPKVKAHGKKVLGAFSDGL----AHLDNLKg 84
Cdd:cd08926   5 LVLKVWAKVEADltGIGQEVLLRLFKEHPETQEHFPKFKGISQ-DDLKSNEDLKKHGVTVLTALGEILkqkgSHEAELK- 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504349   85 tfaTLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKY 146
Cdd:cd08926  83 ---PLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANY 141
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 20-135 5.19e-06

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: 43.46  E-value: 5.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349   20 NVDEVGGEALGRLLVVYPWTQRFFESFGDL-STPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSEL---HCD 95
Cdd:cd14766  11 KIDETGKTMFLRMLTENPELKELFPKLKNLeDEEDELRSSEILENHAARVMDTLDEAISNIENVDYVIDLLHKVgkmHAK 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4504349   96 KLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVV 135
Cdd:cd14766  91 KPGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTI 130
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 16-140 1.32e-05

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: 42.15  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349   16 WGKV--NVDEVGGEALGRLLVVYPWTQRFFESFgDLstpdavmgnpkvKAHGKKVLGAFSDGLAHLDNLKGTFATLSELH 93
Cdd:cd12131   9 FAKVepIADEAAALFYERLFELDPELKPLFKGT-DM------------EEQGRKLMAMLVLVVKGLDDLEALLPALQDLG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 4504349   94 cdKLHVD----PENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVAN 140
Cdd:cd12131  76 --RRHVKygvkPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAG 124
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 76-139 1.13e-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: 36.45  E-value: 1.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4504349   76 LAHLDNLKGTFATLSELHCD--KLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVA 139
Cdd:cd19753  53 VENLDDPDGLVPFLAQLGRDhrKYGVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIA 118
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 4-136 1.39e-03

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: 36.89  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504349    4 LTPEEKSAVTALWGKV--NVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMgNPKVKAHGKKVLGAFSDGLAHLDN 81
Cdd:cd12137   1 LTERQKQLIESSWSILqeDIAKVGVIMFVRLFETHPDCKDAFFPFRDVDLEDLRH-SKELRAHGLRVLSFVEKSLARLHQ 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4504349   82 LKGTFATLSEL---HCdKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVA 136
Cdd:cd12137  80 PDKLEELLHELgrkHY-RYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFR 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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