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Conserved domains on  [gi|6754162|ref|NP_034535|]
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hemoglobin subunit zeta [Mus musculus]

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 ...
 7-142 2.80e-79

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: 230.15  E-value: 2.80e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    7 ERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLSE 86
Cdd:cd08927   5 DKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALSKLSD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6754162   87 LHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR 142
Cdd:cd08927  85 LHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 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 ...
 7-142 2.80e-79

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: 230.15  E-value: 2.80e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    7 ERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLSE 86
Cdd:cd08927   5 DKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALSKLSD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6754162   87 LHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR 142
Cdd:cd08927  85 LHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Globin pfam00042
Globin;
27-137 1.85e-33

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 113.54  E-value: 1.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162     27 TETLERLFCSYPQTKTYFPHF----DLHHGSQQLRAHGFKIMTAVGDAVKSIDN---LSSALTKLSELHAYILRVDPVNF 99
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFeksaDDLKGSPKFKAHGKKVLAALGEAVKHLDDlaaLNAALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 6754162    100 KLLSHCLLVTMAARFPaDFTPEVHEAWDKFMSILSSIL 137
Cdd:pfam00042  81 KLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
3-139 4.51e-13

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 61.71  E-value: 4.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPhfdlhhgsQQLRAHGFKIMTAVGDAVKSIDNLSSALT 82
Cdd:COG1017   1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFN--------GDMGEQRKALAAALAAYARNLDNLEALLP 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   83 KLSEL---HAYiLRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTE 139
Cdd:COG1017  73 ALERLgrkHVS-YGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIA 131
 
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 ...
 7-142 2.80e-79

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: 230.15  E-value: 2.80e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    7 ERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLSE 86
Cdd:cd08927   5 DKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALSKLSD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6754162   87 LHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR 142
Cdd:cd08927  85 LHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 7-138 7.71e-54

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: 165.60  E-value: 7.71e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    7 ERAIIMSMWEKmaAQAEPIGTETLERLFCSYPQTKTYFPHFD-LHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLS 85
Cdd:cd14765   1 EKSTIKALWGK--VNVEEYGAEALARLFVVYPWTKRYFPKFDdSSSGNPKVKAHGKKVLGALGDAVKHLDDLKNTFSDLS 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6754162   86 ELHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILT 138
Cdd:cd14765  79 ELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAALS 131
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 7-141 6.90e-43

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: 138.16  E-value: 6.90e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    7 ERAIIMSMWEKMaaQAEPIGTETLERLFCSYPQTKTYFPHF-DLHH-----GSQQLRAHGFKIMTAVGDAVKSIDNLSSA 80
Cdd:cd08925   1 EKAAITAVWGKV--DVDEVGAEALARLLIVYPWTQRYFSSFgDLSSaaaiaGNPKVAAHGKKVLGALGEAIKHLDDIKAT 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754162   81 LTKLSELHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKY 141
Cdd:cd08925  79 FADLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Globin pfam00042
Globin;
27-137 1.85e-33

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 113.54  E-value: 1.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162     27 TETLERLFCSYPQTKTYFPHF----DLHHGSQQLRAHGFKIMTAVGDAVKSIDN---LSSALTKLSELHAYILRVDPVNF 99
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFeksaDDLKGSPKFKAHGKKVLAALGEAVKHLDDlaaLNAALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 6754162    100 KLLSHCLLVTMAARFPaDFTPEVHEAWDKFMSILSSIL 137
Cdd:pfam00042  81 KLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 3-142 2.25e-30

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: 106.85  E-value: 2.25e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDlH-------HGSQQLRAHGFKIMTAVGDAVKSID 75
Cdd:cd08924   1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFK-HmedplemERSSQLRKHARRVMGALNTVVENLH 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   76 N---LSSALTKLSELHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR 142
Cdd:cd08924  80 DpdkVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYK 149
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 11-137 2.53e-21

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: 83.27  E-value: 2.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   11 IMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHH----GSQQLRAHGFKIMTAVGDAVKSIDN---LSSALTK 83
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDldlkGSPEFKAHAKRVVGALDSLIDNLDDpeaLDALLRK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6754162   84 LSELHAYiLRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSIL 137
Cdd:cd01040  81 LGKRHKR-RGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 11-142 5.38e-20

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: 80.19  E-value: 5.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   11 IMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHF-----DLHHGSQQLRAHGFKIMTAVGDAVKSIDNLSSALTKLS 85
Cdd:cd08926   6 VLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFkgisqDDLKSNEDLKKHGVTVLTALGEILKQKGSHEAELKPLA 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6754162   86 ELHAYILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEKYR 142
Cdd:cd08926  86 QTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYK 142
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 9-139 1.44e-15

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: 67.96  E-value: 1.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    9 AIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLhhgsqqlRAHGFKIMTAVGDAVKSIDN---LSSALTKLS 85
Cdd:cd12131   3 ELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTDM-------EEQGRKLMAMLVLVVKGLDDleaLLPALQDLG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6754162   86 ELHA-YilRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTE 139
Cdd:cd12131  76 RRHVkY--GVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMIE 128
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
3-139 4.51e-13

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 61.71  E-value: 4.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPhfdlhhgsQQLRAHGFKIMTAVGDAVKSIDNLSSALT 82
Cdd:COG1017   1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFN--------GDMGEQRKALAAALAAYARNLDNLEALLP 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   83 KLSEL---HAYiLRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTE 139
Cdd:COG1017  73 ALERLgrkHVS-YGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIA 131
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 8-140 4.56e-09

Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. 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. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development. This family also includes some single-domain goblins (SDgbs).


Pssm-ID: 381260  Cd Length: 140  Bit Score: 51.42  E-value: 4.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    8 RAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQlrahgfKIM-TAVGDAVKSIDNLS---SALTK 83
Cdd:cd08922   6 IAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFNMANQASGRQP------KALaAAVLAYAANIDNLEvllPAVER 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6754162   84 LSELHAyILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEK 140
Cdd:cd08922  80 IAHKHV-SLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAEAYGFLADILIER 135
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 3-139 7.86e-08

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: 48.06  E-value: 7.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHF------DLHHgSQQLRAHGFKIMTAVGDAVKSIDN 76
Cdd:cd12137   1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFrdvdleDLRH-SKELRAHGLRVLSFVEKSLARLHQ 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754162   77 LSSALTKLSEL---H-AYILRVDPVNfkLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTE 139
Cdd:cd12137  80 PDKLEELLHELgrkHyRYNAKVKYVD--LVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTYVMKE 144
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 3-138 4.21e-07

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: 46.37  E-value: 4.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQ-------LRAHGFKIMTAVGDAVKSID 75
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSPQdclsspeFLDHIRKVMLVIDAAVSHLE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754162   76 NLSSA---LTKLSELHAYIlRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILT 138
Cdd:cd08920  81 DLSSLeeyLTSLGRKHRAV-GVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMS 145
Globin-like cd01067
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 14-137 2.43e-06

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: 43.60  E-value: 2.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   14 MWEKMAAQAEPIGTETLERLFCSyPQTKTYFPHFDlhhgsqQLRAHGFKIMTAVGDAVKSI---DNLSSALTKLSELHAy 90
Cdd:cd01067   1 AWGYLEENQEEIVDDFYDRLFAL-PSLSELFSPPG------RLAKCIRKQMHFLRYALYGLvdgDSIEEGLAGLGEAHK- 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6754162   91 ILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSIL 137
Cdd:cd01067  73 SLGVPISYFIAALNVMKDVLTELLGDKFTPAAGEAWTKIFDYIISSM 119
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 32-137 5.95e-05

Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. 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. FlavoHb expression affects Aspergillus nidulans sexual development and mycotoxin production, and Dictyostelium discoideum development.


Pssm-ID: 381294  Cd Length: 141  Bit Score: 40.40  E-value: 5.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   32 RLFCSYPQTKTYFphfdlHHGSQQLRAHGFKIMTAVGDAVKSIDNLssalTKLSELHAYI------LRVDPVNFKLLSHC 105
Cdd:cd19754  30 YMLKRYPEVKPYF-----NETNQKLLRQPKILAFALLQYAKNIDDL----TPLSGFVEQIvskhvgLQVKPEHYPIVGEC 100

                        90       100       110
                ....*....|....*....|....*....|...
gi 6754162  106 LLVTMAARFP-ADFTPEVHEAWDKFMSILSSIL 137
Cdd:cd19754 101 LIETMKELLPeAVATDEFIEAWTTAYGNLANIL 133
FHb-globin_3 cd14783
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 9-140 9.21e-05

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways.


Pssm-ID: 271316  Cd Length: 140  Bit Score: 39.75  E-value: 9.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    9 AIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQlRAhgfkIMTAVGDAVKSIDN---LSSALTKLS 85
Cdd:cd14783   7 DIVKSTAPILEENGETLTRHFYKRMFEHNPEVKPFFNPAHQHSGSQQ-RA----LAAAICAYAANIDNlevLGNAVELIA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6754162   86 ELHAYiLRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEK 140
Cdd:cd14783  82 QKHAS-LGIKPEHYPIVGSNLLASIREVLGDAATDDIIEAWSEAYGFLADILIGR 135
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 15-100 2.11e-04

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: 38.84  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   15 WEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHH-------GSQQLRAHGFKIMTAVGDAVKSIDNLSSA---LTKL 84
Cdd:cd14766   5 WKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEdeedelrSSEILENHAARVMDTLDEAISNIENVDYVidlLHKV 84

                        90
                ....*....|....*.
gi 6754162   85 SELHAYILRVDPVNFK 100
Cdd:cd14766  85 GKMHAKKPGFRPEMFW 100
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 3-139 2.61e-04

Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; Flavohemoglobins (flavoHbs) function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. The physiological role of HmpPa is thought to be detoxification of NO under aerobic conditions.


Pssm-ID: 381288  Cd Length: 140  Bit Score: 38.59  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQlRAhgfkIMTAVGDAVKSIDN---LSS 79
Cdd:cd14780   1 LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFNQAHQASGAQP-RA----LANAVLAYARHIDRlevLGG 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162   80 ALTKLSELHAYiLRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTE 139
Cdd:cd14780  76 AVSLIVNKHVS-LNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAWGAAYQQLADLLIA 134
Yhb1-globin-like cd14777
Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; ...
 3-128 1.05e-03

Globin domain of Saccharomyces cerevisiae flavohemoglobin (Yhb1p) and related domains; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. S. cerevisiae Yhb1p has been shown to protect against nitrosative stress and to control ferric reductase activity; it may participate in regulating the activity of plasma membrane ferric reductase(s). Also included in this subfamily is Dictyostelium discoideum FlavoHb, the expression of which affects D. discoideum development.


Pssm-ID: 381285  Cd Length: 140  Bit Score: 36.94  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    3 LMKNERAIIMSMWEKMAAQAEPIGTETLERLFCSYPQTKTYFPHFDLHHGSQQlrahgfkimTAVGDAV----KSIDNLS 78
Cdd:cd14777   1 LSEKTIQIVKSTVPVLKEKGTEITKRFYKRMFEEHPELLNIFNQTNQKKGLQQ---------TALANTVyaaaKHIDNLE 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6754162   79 ---SALTKLSELHAyILRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDK 128
Cdd:cd14777  72 vilPVVKQIAHKHR-ALGVKPEHYPIVGENLLAAIKEVLGDAATDEILEAWEK 123
FHb-globin_1 cd14781
Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function ...
 9-140 7.84e-03

Globin domain of flavohemoglobins (flavoHbs); uncharacterized subgroup; FlavoHbs function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). They have an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD- and FAD-binding domain, and use the reducing power of cellular NAD(P)H to drive regeneration of the ferrous heme. They protect from nitrosative stress (the broad range of cellular toxicities caused by NO), and modulate NO signaling pathways. This subfamily may contain some single-domain goblins (SDgbs).


Pssm-ID: 381289  Cd Length: 139  Bit Score: 34.37  E-value: 7.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754162    9 AIIMSMWEKMAAQAEPIGTETLERLFCSyPQTKTYFPHFDlHHGSQQLRAhgfkIMTAVGDAVKSIDNL---SSALTKLS 85
Cdd:cd14781   7 AIVKATVPALEEHGVAITAAMYKRLFED-PEIKALFNQAA-QKSGEQPRA----LAGAILAYAKNIDNLgalGSAVERIA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6754162   86 ELHAYiLRVDPVNFKLLSHCLLVTMAARFPADFTPEVHEAWDKFMSILSSILTEK 140
Cdd:cd14781  81 QKHVG-LHIKPEHYPHVATALLGAIKDVLGDAATDEVLEAWGEAYWFLADILINR 134
 
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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