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Conserved domains on  [gi|2686749081|ref|XP_063200275|]
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hemoglobin subunit alpha-A [Chroicocephalus ridibundus]

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 7.76e-82

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: 236.70  E-value: 7.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   3 LSGSDKTNVKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHFDLQHGSAQVKAHGKKVAAALVEAANHIDDIAGALS 82
Cdd:cd08927     1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  83 KLSDLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKYR 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 7.76e-82

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: 236.70  E-value: 7.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   3 LSGSDKTNVKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHFDLQHGSAQVKAHGKKVAAALVEAANHIDDIAGALS 82
Cdd:cd08927     1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  83 KLSDLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKYR 142
Cdd:cd08927    81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Globin pfam00042
Globin;
27-137 9.61e-34

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 114.31  E-value: 9.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  27 AETLERMFATYPQTKTYFPHF----DLQHGSAQVKAHGKKVAAALVEAANHIDDIA---GALSKLSDLHAQKLRVDPVNF 99
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFeksaDDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2686749081 100 KLLGQCFLVVVAIHHPSvLTPEVHASLDKFLCAVGNVL 137
Cdd:pfam00042  81 KLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIAAAL 117
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
3-124 2.73e-07

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 46.69  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   3 LSGSDKTNVKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHfdlqhgsaQVKAHGKKVAAALVEAANHIDD---IAG 79
Cdd:COG1017     1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNG--------DMGEQRKALAAALAAYARNLDNleaLLP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2686749081  80 ALSKLSDLHAqKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHA 124
Cdd:COG1017    73 ALERLGRKHV-SYGVKPEHYPIVGEALLAALREVLGDAWTPEVAA 116
 
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 7.76e-82

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: 236.70  E-value: 7.76e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   3 LSGSDKTNVKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHFDLQHGSAQVKAHGKKVAAALVEAANHIDDIAGALS 82
Cdd:cd08927     1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAGSAQVKAHGKKVMDALGDAVKHLDDLPGALS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  83 KLSDLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKYR 142
Cdd:cd08927    81 KLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKYR 140
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 7-138 2.24e-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: 167.14  E-value: 2.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   7 DKTNVKGVFGKIggHAEEYGAETLERMFATYPQTKTYFPHFDLQH-GSAQVKAHGKKVAAALVEAANHIDDIAGALSKLS 85
Cdd:cd14765     1 EKSTIKALWGKV--NVEEYGAEALARLFVVYPWTKRYFPKFDDSSsGNPKVKAHGKKVLGALGDAVKHLDDLKNTFSDLS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2686749081  86 DLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLT 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 2.94e-44

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: 141.62  E-value: 2.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   7 DKTNVKGVFGKIggHAEEYGAETLERMFATYPQTKTYFPHF------DLQHGSAQVKAHGKKVAAALVEAANHIDDIAGA 80
Cdd:cd08925     1 EKAAITAVWGKV--DVDEVGAEALARLLIVYPWTQRYFSSFgdlssaAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKAT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2686749081  81 LSKLSDLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKY 141
Cdd:cd08925    79 FADLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
Globin pfam00042
Globin;
27-137 9.61e-34

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 114.31  E-value: 9.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  27 AETLERMFATYPQTKTYFPHF----DLQHGSAQVKAHGKKVAAALVEAANHIDDIA---GALSKLSDLHAQKLRVDPVNF 99
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFeksaDDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPANF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2686749081 100 KLLGQCFLVVVAIHHPSvLTPEVHASLDKFLCAVGNVL 137
Cdd:pfam00042  81 KLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIAAAL 117
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 11-137 1.56e-18

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: 75.95  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  11 VKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHFDLQH----GSAQVKAHGKKVAAALVEAANHIDDIAGALSKLSD 86
Cdd:cd01040     1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDldlkGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2686749081  87 LHAQ--KLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVL 137
Cdd:cd01040    81 LGKRhkRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 3-142 1.58e-18

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: 76.42  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   3 LSGSDKTNVKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHF-DLQ-----HGSAQVKAHGKKVAAAL---VEAANH 73
Cdd:cd08924     1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFkHMEdplemERSSQLRKHARRVMGALntvVENLHD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2686749081  74 IDDIAGALSKLSDLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKYR 142
Cdd:cd08924    81 PDKVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYK 149
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 11-142 4.52e-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: 59.39  E-value: 4.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  11 VKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHF-----DLQHGSAQVKAHGKKVAAALVEAANHIDDIAGALSKLS 85
Cdd:cd08926     6 VLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFkgisqDDLKSNEDLKKHGVTVLTALGEILKQKGSHEAELKPLA 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2686749081  86 DLHAQKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHASLDKFLCAVGNVLTAKYR 142
Cdd:cd08926    86 QTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYK 142
FHb-globin cd08922
Globin domain of flavohemoglobins (flavoHbs); FlavoHbs function primarily as nitric oxide ...
 21-124 1.98e-08

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: 49.50  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  21 HAEEYGAETLERMFATYPQTKTYFPHFDlQHGSAQVKAhgkkVAAALVEAANHIDD---IAGALSKLSDLHAQkLRVDPV 97
Cdd:cd08922    19 HGEEITTRFYKRMFAEHPELKNLFNMAN-QASGRQPKA----LAAAVLAYAANIDNlevLLPAVERIAHKHVS-LGVKPE 92

                          90       100
                  ....*....|....*....|....*..
gi 2686749081  98 NFKLLGQCFLVVVAIHHPSVLTPEVHA 124
Cdd:cd08922    93 HYPIVGEYLLEAIKEVLGDAATPEVLD 119
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 15-124 3.26e-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: 48.70  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  15 FGKIGGHAEEYGAETLERMFATYPQTKTYFPHFDLQhgsaqvkAHGKKVAAALVEAANHIDDIAGALSKLSDLHA--QKL 92
Cdd:cd12131     9 FAKVEPIADEAAALFYERLFELDPELKPLFKGTDME-------EQGRKLMAMLVLVVKGLDDLEALLPALQDLGRrhVKY 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2686749081  93 RVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHA 124
Cdd:cd12131    82 GVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQ 113
Hmp COG1017
Hemoglobin-like flavoprotein [Energy production and conversion];
3-124 2.73e-07

Hemoglobin-like flavoprotein [Energy production and conversion];


Pssm-ID: 440640 [Multi-domain]  Cd Length: 135  Bit Score: 46.69  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   3 LSGSDKTNVKGVFGKIGGHAEEYGAETLERMFATYPQTKTYFPHfdlqhgsaQVKAHGKKVAAALVEAANHIDD---IAG 79
Cdd:COG1017     1 LSPETIALVKASFPLVAPHGEEITARFYERLFELHPELRPLFNG--------DMGEQRKALAAALAAYARNLDNleaLLP 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2686749081  80 ALSKLSDLHAqKLRVDPVNFKLLGQCFLVVVAIHHPSVLTPEVHA 124
Cdd:COG1017    73 ALERLGRKHV-SYGVKPEHYPIVGEALLAALREVLGDAWTPEVAA 116
HmpPa-globin-like cd14780
Globin domain of Pseudomonas aeruginosa flavohemoglobin (HmpPa) and related proteins; ...
 18-125 8.75e-06

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: 42.44  E-value: 8.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  18 IGGHAEEYGAETLERMFATYPQTKTYFPHFDLQHGsAQVKAhgkkVAAALVEAANHIDD---IAGALSKLSDLHAQkLRV 94
Cdd:cd14780    16 LEAHGEAITTHFYPLMFEEYPEVRALFNQAHQASG-AQPRA----LANAVLAYARHIDRlevLGGAVSLIVNKHVS-LNI 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2686749081  95 DPVNFKLLGQCFLVVVAIHHPSVLTPEVHAS 125
Cdd:cd14780    90 LPEHYPIVGTCLLRAIREVLGDAATDEVIEA 120
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 8-112 4.14e-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: 38.07  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081   8 KTNVKGVFGKIgghaEEYGAETLERMFATYPQTKTYFP-------HFDLQHGSAQVKAHGKKVAAALVEAANHIDDIAGA 80
Cdd:cd14766     2 KKSWKGIARKI----DETGKTMFLRMLTENPELKELFPklknledEEDELRSSEILENHAARVMDTLDEAISNIENVDYV 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2686749081  81 ---LSKLSDLHAQKLRVDPVNFKLLGQCFLVVVAI 112
Cdd:cd14766    78 idlLHKVGKMHAKKPGFRPEMFWKIEEPFLEAVSE 112
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 21-110 4.91e-04

Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress.


Pssm-ID: 381286 [Multi-domain]  Cd Length: 140  Bit Score: 37.80  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  21 HAEEYGAETLERMFATYPQTKTYFpHFDLQHGSAQVKAhgkkVAAALVEAANHIDD---IAGALSKLSDLHAQkLRVDPV 97
Cdd:cd14778    19 HGVEITTEFYKNMFTEYPEVRPMF-DMEKQKSGEQPKA----LAMTVLAAAQNIENlekIRPAVEKIGKTHVN-LNVKPE 92

                          90
                  ....*....|...
gi 2686749081  98 NFKLLGQCFLVVV 110
Cdd:cd14778    93 HYPIVGACLLGAI 105
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 32-107 1.01e-03

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: 36.93  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686749081  32 RMFATYPQTKTYFpHFDLQHGSAQVKAhgkkVAAALVEAANHIDDiagaLSKLSDLHAQ------KLRVDPVNFKLLGQC 105
Cdd:cd19754    30 YMLKRYPEVKPYF-NETNQKLLRQPKI----LAFALLQYAKNIDD----LTPLSGFVEQivskhvGLQVKPEHYPIVGEC 100


                  ..
gi 2686749081 106 FL 107
Cdd:cd19754   101 LI 102
 
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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