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Conserved domains on  [gi|122388|sp|P20854|]
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RecName: Full=Hemoglobin subunit alpha; AltName: Full=Alpha-globin; AltName: Full=Hemoglobin alpha chain; Contains: RecName: Full=Hemopressin

Protein Classification

hemoglobin alpha subunit family protein( domain architecture ID 10172381)

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.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 2-141 6.45e-83

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: 239.39  E-value: 6.45e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHFDVSHGSAQVKAHGKKVADALANAASHLDDLPNALS 81
Cdd:cd08927   1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388    82 ALSDLHAHKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLTSKYR 141
Cdd:cd08927  81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
 
Name Accession Description Interval E-value
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 2-141 6.45e-83

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: 239.39  E-value: 6.45e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHFDVSHGSAQVKAHGKKVADALANAASHLDDLPNALS 81
Cdd:cd08927   1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388    82 ALSDLHAHKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLTSKYR 141
Cdd:cd08927  81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Globin pfam00042
Globin;
26-136 7.02e-31

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 106.99  E-value: 7.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388      26 AEALERMFLSFPTTKTYFPHFDVSH----GSAQVKAHGKKVADALANAASHLDDLPN---ALSALSDLHAHKLRVDPVNF 98
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSAddlkGSPKFKAHGKKVLAALGEAVKHLDDLAAlnaALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 122388      99 KLLSHCLLVTLAcHHPAEFTPAVHASLDKFLATVATVL 136
Cdd:pfam00042  81 KLFGEALLVVLA-EHLGEFTPETKAAWDKALDVIAAAL 117
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
2-136 7.39e-12

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 58.63  E-value: 7.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHfdvshgsaQVKAHGKKVADALANAASHLDDLPNALS 81
Cdd:COG1017   1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNG--------DMGEQRKALAAALAAYARNLDNLEALLP 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 122388    82 ALSDL-HAH-KLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVL 136
Cdd:COG1017  73 ALERLgRKHvSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVM 129
 
Name Accession Description Interval E-value
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 2-141 6.45e-83

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: 239.39  E-value: 6.45e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHFDVSHGSAQVKAHGKKVADALANAASHLDDLPNALS 81
Cdd:cd08927   1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388    82 ALSDLHAHKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLTSKYR 141
Cdd:cd08927  81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 6-137 1.20e-56

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: 172.92  E-value: 1.20e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     6 DKTNVKAAWDKIggHGGEYGAEALERMFLSFPTTKTYFPHFD-VSHGSAQVKAHGKKVADALANAASHLDDLPNALSALS 84
Cdd:cd14765   1 EKSTIKALWGKV--NVEEYGAEALARLFVVYPWTKRYFPKFDdSSSGNPKVKAHGKKVLGALGDAVKHLDDLKNTFSDLS 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 122388    85 DLHAHKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLT 137
Cdd:cd14765  79 ELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 6-140 5.99e-38

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: 125.44  E-value: 5.99e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     6 DKTNVKAAWDKIGGHggEYGAEALERMFLSFPTTKTYFPHF-DVSH-----GSAQVKAHGKKVADALANAASHLDDLPNA 79
Cdd:cd08925   1 EKAAITAVWGKVDVD--EVGAEALARLLIVYPWTQRYFSSFgDLSSaaaiaGNPKVAAHGKKVLGALGEAIKHLDDIKAT 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122388    80 LSALSDLHAHKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLTSKY 140
Cdd:cd08925  79 FADLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Globin pfam00042
Globin;
26-136 7.02e-31

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 106.99  E-value: 7.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388      26 AEALERMFLSFPTTKTYFPHFDVSH----GSAQVKAHGKKVADALANAASHLDDLPN---ALSALSDLHAHKLRVDPVNF 98
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSAddlkGSPKFKAHGKKVLAALGEAVKHLDDLAAlnaALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 122388      99 KLLSHCLLVTLAcHHPAEFTPAVHASLDKFLATVATVL 136
Cdd:pfam00042  81 KLFGEALLVVLA-EHLGEFTPETKAAWDKALDVIAAAL 117
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 2-141 4.31e-21

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: 82.97  E-value: 4.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHF------DVSHGSAQVKAHGKKVADALANAASHLDD 75
Cdd:cd08924   1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFkhmedpLEMERSSQLRKHARRVMGALNTVVENLHD 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122388    76 ---LPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLTSKYR 141
Cdd:cd08924  81 pdkVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYK 149
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 10-136 2.00e-19

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: 78.27  E-value: 2.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388    10 VKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHFDVSH----GSAQVKAHGKKVADALANAASHLDDLPNALSALSD 85
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDldlkGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 122388    86 LHA-HKLR-VDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVL 136
Cdd:cd01040  81 LGKrHKRRgVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
2-136 7.39e-12

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 58.63  E-value: 7.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHfdvshgsaQVKAHGKKVADALANAASHLDDLPNALS 81
Cdd:COG1017   1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNG--------DMGEQRKALAAALAAYARNLDNLEALLP 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 122388    82 ALSDL-HAH-KLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVL 136
Cdd:COG1017  73 ALERLgRKHvSYGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVM 129
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 25-141 8.20e-12

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: 59.01  E-value: 8.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388    25 GAEALERMFLSFPTTKTYFPHF-----DVSHGSAQVKAHGKKVADALANAASHLDDLPNALSALSDLHAHKLRVDPVNFK 99
Cdd:cd08926  21 GQEVLLRLFKEHPETQEHFPKFkgisqDDLKSNEDLKKHGVTVLTALGEILKQKGSHEAELKPLAQTHATKHKIPPKYFE 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 122388   100 LLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLTSKYR 141
Cdd:cd08926 101 LITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYK 142
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 6-135 1.03e-08

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: 50.24  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     6 DKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFPHFDVshgsaqvKAHGKKVADALANAASHLDDLPNALSALSD 85
Cdd:cd12131   1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTDM-------EEQGRKLMAMLVLVVKGLDDLEALLPALQD 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 122388    86 LHA-H-KLRVDPVNFKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATV 135
Cdd:cd12131  74 LGRrHvKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGT 125
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 25-99 6.25e-03

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: 34.60  E-value: 6.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388    25 GAEALERMFLSFPTTKTYFP-------HFDVSHGSAQVKAHGKKVADALANAASHLDDLPNA---LSALSDLHAHKLRVD 94
Cdd:cd14766  16 GKTMFLRMLTENPELKELFPklknledEEDELRSSEILENHAARVMDTLDEAISNIENVDYVidlLHKVGKMHAKKPGFR 95


                ....*
gi 122388    95 PVNFK 99
Cdd:cd14766  96 PEMFW 100
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 2-137 7.65e-03

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: 34.43  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122388     2 LSAADKTNVKAAWDKIGGHGGEYGAEALERMFLSFPTTKTYFpHFDVSH--------GSAQVKAHGKKVADALANAASHL 73
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLF-QYNGRQfsspqdclSSPEFLDHIRKVMLVIDAAVSHL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122388    74 DDLPNALSALSDLhAHKLRVDPVN---FKLLSHCLLVTLACHHPAEFTPAVHASLDKFLATVATVLT 137
Cdd:cd08920  80 EDLSSLEEYLTSL-GRKHRAVGVKlesFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMS 145
 
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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