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Conserved domains on  [gi|157278270|ref|NP_001098237|]
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cytoglobin-1 [Oryzias latipes]

Protein Classification

Cygb domain-containing protein( domain architecture ID 10172376)

Cygb domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 17-169 3.05e-102

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: 290.59  E-value: 3.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAEELEKSSQLRKHARRVMNAINTLVESLDN 96
Cdd:cd08924    1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157278270  97 SDKVSSVLNAVGKAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIKAVYEELGW 169
Cdd:cd08924   81 PDKVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVGW 153
 
Name Accession Description Interval E-value
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 17-169 3.05e-102

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: 290.59  E-value: 3.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAEELEKSSQLRKHARRVMNAINTLVESLDN 96
Cdd:cd08924    1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157278270  97 SDKVSSVLNAVGKAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIKAVYEELGW 169
Cdd:cd08924   81 PDKVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVGW 153
Globin pfam00042
Globin;
41-157 4.64e-29

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 103.52  E-value: 4.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270   41 VAILVRLFVNFPSSKQYFSQFKHieDAEELEKSSQLRKHARRVMNAINTLVESLDNSDKVSSVLNAVGKAHAIRHKVDPV 120
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEK--SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHKEKRGVDPA 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 157278270  121 YFKILSGVILEVLGEAYPQvMTAEVASAWTNLLAILC 157
Cdd:pfam00042  79 NFKLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIA 114
 
Name Accession Description Interval E-value
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 17-169 3.05e-102

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: 290.59  E-value: 3.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAEELEKSSQLRKHARRVMNAINTLVESLDN 96
Cdd:cd08924    1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157278270  97 SDKVSSVLNAVGKAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIKAVYEELGW 169
Cdd:cd08924   81 PDKVSSVLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVGW 153
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 25-157 1.00e-34

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: 118.71  E-value: 1.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  25 IQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDaeELEKSSQLRKHARRVMNAINTLVESLDNSDKVSSVL 104
Cdd:cd01040    1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDL--DLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157278270 105 NAVGKAHAiRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILC 157
Cdd:cd01040   79 RKLGKRHK-RRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIA 130
Globin pfam00042
Globin;
41-157 4.64e-29

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 103.52  E-value: 4.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270   41 VAILVRLFVNFPSSKQYFSQFKHieDAEELEKSSQLRKHARRVMNAINTLVESLDNSDKVSSVLNAVGKAHAIRHKVDPV 120
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEK--SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHKEKRGVDPA 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 157278270  121 YFKILSGVILEVLGEAYPQvMTAEVASAWTNLLAILC 157
Cdd:pfam00042  79 NFKLFGEALLVVLAEHLGE-FTPETKAAWDKALDVIA 114
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 29-169 2.28e-25

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: 95.22  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  29 WAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAEeLEKSSQLRKHARRVMNAintLVESLDNSDKVSSVLNAVG 108
Cdd:cd08926   10 WAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGISQDD-LKSNEDLKKHGVTVLTA---LGEILKQKGSHEAELKPLA 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157278270 109 KAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIKAVYEELGW 169
Cdd:cd08926   86 QTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGF 146
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 17-157 2.76e-25

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: 94.56  E-value: 2.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDaeelekSSQLRKHARRVMNAINTLVESLDN 96
Cdd:cd08927    1 LSAADKALIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSAG------SAQVKAHGKKVMDALGDAVKHLDD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157278270  97 sdkVSSVLNAVGKAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILC 157
Cdd:cd08927   75 ---LPGALSKLSDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVS 132
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 17-161 1.03e-21

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: 85.43  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIeDAEELEKSSQLRKHARRVMNAINTLVESLDN 96
Cdd:cd12137    1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFRDV-DLEDLRHSKELRAHGLRVLSFVEKSLARLHQ 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157278270  97 SDKVSSVLNAVGKAHaIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIK 161
Cdd:cd12137   80 PDKLEELLHELGRKH-YRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAWKTLFRYLTYVMK 143
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 21-157 4.59e-17

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: 73.44  E-value: 4.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  21 ERVMIQDSWAKVyqNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAEELEKSSQLRKHARRVMNAINTLVESLDNsdkV 100
Cdd:cd08925    1 EKAAITAVWGKV--DVDEVGAEALARLLIVYPWTQRYFSSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDD---I 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157278270 101 SSVLNAVGKAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILC 157
Cdd:cd08925   76 KATFADLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVV 132
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 21-157 5.83e-17

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: 72.77  E-value: 5.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  21 ERVMIQDSWAKVyqNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAeelekSSQLRKHARRVMNAintLVESLDNSDKV 100
Cdd:cd14765    1 EKSTIKALWGKV--NVEEYGAEALARLFVVYPWTKRYFPKFDDSSSG-----NPKVKAHGKKVLGA---LGDAVKHLDDL 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157278270 101 SSVLNAVGKAHAIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILC 157
Cdd:cd14765   71 KNTFSDLSELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVA 127
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 25-137 1.02e-15

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: 69.66  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  25 IQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKHIEDAEELEKSSQ-LRKHARRVMNAINTLVESLDNSDKVSSV 103
Cdd:cd14766    1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEEDELRSSEiLENHAARVMDTLDEAISNIENVDYVIDL 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157278270 104 LNAVGKAHAIRHKVDPVYFKILSGVIL----EVLGEAY 137
Cdd:cd14766   81 LHKVGKMHAKKPGFRPEMFWKIEEPFLeavsETLGDRY 118
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 24-156 3.51e-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: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  24 MIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFsqfkhiedaeeleKSSQLRKHARRVMNAINTLVESLDNSDKVSSV 103
Cdd:cd12131    4 LVQQSFAKVEPIADEAAALFYERLFELDPELKPLF-------------KGTDMEEQGRKLMAMLVLVVKGLDDLEALLPA 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157278270 104 LNAVGKAHAiRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAIL 156
Cdd:cd12131   71 LQDLGRRHV-KYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGIL 122
Globin-like cd01067
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 28-157 5.52e-11

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: 57.08  E-value: 5.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  28 SWAKVYQNCDDAGVAILVRLFVNfPSSKQYFSQFKhiedaeelekssQLRKHARRVMNAINTLVESLDNSDKVSSVLNAV 107
Cdd:cd01067    1 AWGYLEENQEEIVDDFYDRLFAL-PSLSELFSPPG------------RLAKCIRKQMHFLRYALYGLVDGDSIEEGLAGL 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157278270 108 GKAHaIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILC 157
Cdd:cd01067   68 GEAH-KSLGVPISYFIAALNVMKDVLTELLGDKFTPAAGEAWTKIFDYII 116
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 17-162 9.81e-09

Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. Also belonging to this family is ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit; it may have evolved from class1 nsHbs. Lbs are pentacoordinate, and facilitate the diffusion of O2 to the respiring Rhizobium bacteroids within root nodules. They may have evolved from class 2 nonsymbiotic hemoglobins (class2 nsHb).


Pssm-ID: 381261  Cd Length: 147  Bit Score: 51.72  E-value: 9.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKhiEDAEELEKSSQLRKHARRVMNAINTLVESLDN 96
Cdd:cd08923    1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLK--DSDEIPENNPKLKAHAMKVFKMTCESAIQLRK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157278270  97 SDKV---SSVLNAVGKAHAIRHKVDPvYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIKA 162
Cdd:cd08923   79 KGKVvvaDTTLKRLGSVHLKKGVADP-HFEVVKEALLKTIKEAVGDKWSEEMKCAWGEAYDQLAAAIKK 146
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 18-162 3.13e-08

Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric hexacoordinate Trema tomentosa nsHb and the dimeric hexacoordinate nsHb from monocot barley. This subfamily also includes ParaHb, a dimeric pentacoordinate Hb from the root nodules of Parasponia andersonii, a non-legume capable of symbiotic nitrogen fixation. ParaHb is unusual in that it has different heme redox potentials for each subunit.


Pssm-ID: 381291  Cd Length: 149  Bit Score: 50.21  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  18 TDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFSQFKhiEDAEELEKSSQLRKHARRVMNAINTLVESLDNS 97
Cdd:cd14784    2 SEEQEALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLR--DSTVPLEKNPKLKPHAMSVFVMTCEAAVQLRKA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157278270  98 DKVS---SVLNAVGKAHaIRHKVDPVYFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAILCCSIKA 162
Cdd:cd14784   80 GKVTvreSKLKRLGATH-VKYGVVDEHFEVVKFALLETIKEAVPDMWSPEMKSAWGEAYDQLVAAIKA 146
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 17-156 3.34e-08

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: 50.22  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157278270  17 LTDKERVMIQDSWAKVYQNCDDAGVAILVRLFVNFPSSKQYFS-QFKHIEDAEELEKSSQLRKHARRVMNAINTLVESLD 95
Cdd:cd08920    1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQyNGRQFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157278270  96 NSDKVSSVLNAVGKAH-AIRHKVDPvyFKILSGVILEVLGEAYPQVMTAEVASAWTNLLAIL 156
Cdd:cd08920   81 DLSSLEEYLTSLGRKHrAVGVKLES--FSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAV 140
 
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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