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Conserved domains on  [gi|701301708|ref|XP_010011369|]
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PREDICTED: hemoglobin subunit pi [Nestor notabilis]

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 ...
 3-142 1.91e-88

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: 253.65  E-value: 1.91e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHFDLSQGSTQLRGHGSKVMNAIGEAVKNIDDIRGALA 82
Cdd:cd08927    1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  83 KLSELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTEKYR 142
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 ...
 3-142 1.91e-88

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: 253.65  E-value: 1.91e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHFDLSQGSTQLRGHGSKVMNAIGEAVKNIDDIRGALA 82
Cdd:cd08927    1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  83 KLSELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTEKYR 142
Cdd:cd08927   81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Globin pfam00042
Globin;
27-137 2.20e-36

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 120.86  E-value: 2.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   27 AESLERLFSSYPQTKTYFPHF----DLSQGSTQLRGHGSKVMNAIGEAVKNIDDI---RGALAKLSELHAYILRVDPVNF 99
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFeksaDDLKGSPKFKAHGKKVLAALGEAVKHLDDLaalNAALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 701301708  100 KLLSHCILCSVAARYPnDFTPEVHAAWDKFLSSVSSVL 137
Cdd:pfam00042  81 KLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
3-139 6.43e-11

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 56.32  E-value: 6.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHfdlsqgstQLRGHGSKVMNAIGEAVKNIDD---IRG 79
Cdd:COG1017    1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNG--------DMGEQRKALAAALAAYARNLDNleaLLP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  80 ALAKLSELHAYiLRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTE 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 ...
 3-142 1.91e-88

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: 253.65  E-value: 1.91e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHFDLSQGSTQLRGHGSKVMNAIGEAVKNIDDIRGALA 82
Cdd:cd08927    1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  83 KLSELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTEKYR 142
Cdd:cd08927   81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 7-138 1.54e-57

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: 175.23  E-value: 1.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   7 EKAAVVTIWAKVatQADAIGAESLERLFSSYPQTKTYFPHFD-LSQGSTQLRGHGSKVMNAIGEAVKNIDDIRGALAKLS 85
Cdd:cd14765    1 EKSTIKALWGKV--NVEEYGAEALARLFVVYPWTKRYFPKFDdSSSGNPKVKAHGKKVLGALGDAVKHLDDLKNTFSDLS 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 701301708  86 ELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLT 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 4.20e-50

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: 156.65  E-value: 4.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   7 EKAAVVTIWAKVatQADAIGAESLERLFSSYPQTKTYFPHF-DLS-----QGSTQLRGHGSKVMNAIGEAVKNIDDIRGA 80
Cdd:cd08925    1 EKAAITAVWGKV--DVDEVGAEALARLLIVYPWTQRYFSSFgDLSsaaaiAGNPKVAAHGKKVLGALGEAIKHLDDIKAT 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 701301708  81 LAKLSELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTEKY 141
Cdd:cd08925   79 FADLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Globin pfam00042
Globin;
27-137 2.20e-36

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 120.86  E-value: 2.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   27 AESLERLFSSYPQTKTYFPHF----DLSQGSTQLRGHGSKVMNAIGEAVKNIDDI---RGALAKLSELHAYILRVDPVNF 99
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFeksaDDLKGSPKFKAHGKKVLAALGEAVKHLDDLaalNAALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 701301708  100 KLLSHCILCSVAARYPnDFTPEVHAAWDKFLSSVSSVL 137
Cdd:pfam00042  81 KLFGEALLVVLAEHLG-EFTPETKAAWDKALDVIAAAL 117
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 3-142 2.89e-32

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: 111.86  E-value: 2.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHF-DLS-----QGSTQLRGHGSKVMNAIGEAVKNIDD 76
Cdd:cd08924    1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFkHMEdplemERSSQLRKHARRVMGALNTVVENLHD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 701301708  77 ---IRGALAKLSELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTEKYR 142
Cdd:cd08924   81 pdkVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYK 149
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 11-137 7.97e-25

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: 92.13  E-value: 7.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  11 VVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHFD----LSQGSTQLRGHGSKVMNAIGEAVKNIDD---IRGALAK 83
Cdd:cd01040    1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAgvdlDLKGSPEFKAHAKRVVGALDSLIDNLDDpeaLDALLRK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 701301708  84 LSELHAYiLRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVL 137
Cdd:cd01040   81 LGKRHKR-RGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 6-142 6.26e-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: 79.81  E-value: 6.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   6 AEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHFD-LSQG----STQLRGHGSKVMNAIGEAVKNIDDIRGA 80
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKgISQDdlksNEDLKKHGVTVLTALGEILKQKGSHEAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 701301708  81 LAKLSELHAYILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTEKYR 142
Cdd:cd08926   81 LKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYK 142
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 7-139 5.66e-16

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: 69.12  E-value: 5.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   7 EKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHFDlsqgstqLRGHGSKVMNAIGEAVKNIDDIRGALAKLSE 86
Cdd:cd12131    1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLFKGTD-------MEEQGRKLMAMLVLVVKGLDDLEALLPALQD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 701301708  87 LHAyilR-----VDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTE 139
Cdd:cd12131   74 LGR---RhvkygVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGTMIE 128
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
3-139 6.43e-11

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 56.32  E-value: 6.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHfdlsqgstQLRGHGSKVMNAIGEAVKNIDD---IRG 79
Cdd:COG1017    1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNG--------DMGEQRKALAAALAAYARNLDNleaLLP 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  80 ALAKLSELHAYiLRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTE 139
Cdd:COG1017   73 ALERLGRKHVS-YGVKPEHYPIVGEALLAALREVLGDAWTPEVAAAWAEAYGLLADVMIA 131
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 3-139 5.94e-07

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: 45.75  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHF-DLSQG----STQLRGHGSKVMNAIGEAVKNIDDI 77
Cdd:cd12137    1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFrDVDLEdlrhSKELRAHGLRVLSFVEKSLARLHQP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 701301708  78 RGALAKLSEL---H-AYILRVDPVNfkLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSVLTE 139
Cdd:cd12137   81 DKLEELLHELgrkHyRYNAKVKYVD--LVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTYVMKE 144
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 3-128 1.45e-06

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: 44.88  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYFPHfdlsqgSTQLRGHGSKVM-NAIGEAVKNIDD---IR 78
Cdd:cd08922    1 LSEETIAIVKATAPVLAEHGEEITTRFYKRMFAEHPELKNLFNM------ANQASGRQPKALaAAVLAYAANIDNlevLL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 701301708  79 GALAKLSELHAyILRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDK 128
Cdd:cd08922   75 PAVERIAHKHV-SLGVKPEHYPIVGEYLLEAIKEVLGDAATPEVLDAWAE 123
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 15-100 1.62e-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: 39.23  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  15 WAKVATQADAIGAESLERLFSSYPQTKTYFP-------HFDLSQGSTQLRGHGSKVMNAIGEAVKNIDDIRGA---LAKL 84
Cdd:cd14766    5 WKGIARKIDETGKTMFLRMLTENPELKELFPklknledEEDELRSSEILENHAARVMDTLDEAISNIENVDYVidlLHKV 84

                         90
                 ....*....|....*.
gi 701301708  85 SELHAYILRVDPVNFK 100
Cdd:cd14766   85 GKMHAKKPGFRPEMFW 100
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 3-126 1.83e-03

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: 36.28  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708   3 LTQAEKAAVVTIWAKVATQADAIGAESLERLFSSYPQTKTYF--PHfdlSQGSTQLRGhgskVMNAIGEAVKNIDD---I 77
Cdd:cd14780    1 LSPHQIAIIKATVPALEAHGEAITTHFYPLMFEEYPEVRALFnqAH---QASGAQPRA----LANAVLAYARHIDRlevL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 701301708  78 RGALAKLSELHAYiLRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAW 126
Cdd:cd14780   74 GGAVSLIVNKHVS-LNILPEHYPIVGTCLLRAIREVLGDAATDEVIEAW 121
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 15-136 1.99e-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: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 701301708  15 WAKVATQADAIgAESL-ERLFSSYPQTKTYFPhfdlsqgsTQLRGHGSKVMNAIGEAVKNIDDIRGALAKLSEL---HA- 89
Cdd:cd19753    5 LAAVEDGPDEL-ARRFyARLFAEAPELRDLFP--------ADMDAQRDRLARALTHVVENLDDPDGLVPFLAQLgrdHRk 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 701301708  90 YilRVDPVNFKLLSHCILCSVAARYPNDFTPEVHAAWDKFLSSVSSV 136
Cdd:cd19753   76 Y--GVAPEHYPAVGAALLAALRHFAGEAWTPELEAAWAEAYTLIAGV 120
 
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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