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Conserved domains on  [gi|392877714|gb|AFM87689|]
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Myoglobin [Callorhinchus milii]

Protein Classification

globin family protein( domain architecture ID 10172380)

globin family protein is an all-helical protein that may bind porphyrins, phycobilins, and other non-heme cofactors, and may play various roles including as a sensor or transporter of oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 2-149 5.68e-88

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: 253.15  E-value: 5.68e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   2 CDWDLINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPLGQLTSNADVKTHGNTVFKALGDVVKQKGKHASN 81
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGISQDDLKSNEDLKKHGVTVLTALGEILKQKGSHEAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392877714  82 LQALATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSELEDLYKKGGFQS 149
Cdd:cd08926   81 LKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148
 
Name Accession Description Interval E-value
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 2-149 5.68e-88

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: 253.15  E-value: 5.68e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   2 CDWDLINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPLGQLTSNADVKTHGNTVFKALGDVVKQKGKHASN 81
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGISQDDLKSNEDLKKHGVTVLTALGEILKQKGSHEAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392877714  82 LQALATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSELEDLYKKGGFQS 149
Cdd:cd08926   81 LKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148
Globin pfam00042
Globin;
25-138 5.33e-28

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 100.06  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   25 VLLRLFEEHPETKAHFPKFKDiPLGQLTSNADVKTHGNTVFKALGDVVKQKGKHA---SNLQALATTHINKHKIPPQNFT 101
Cdd:pfam00042   3 ILARLFTAYPDTKAYFPRFEK-SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPANFK 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392877714  102 LITNVILKVFAEKFpGEMTAPAQEAFSKAFKAICSEL 138
Cdd:pfam00042  82 LFGEALLVVLAEHL-GEFTPETKAAWDKALDVIAAAL 117
 
Name Accession Description Interval E-value
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 2-149 5.68e-88

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: 253.15  E-value: 5.68e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   2 CDWDLINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPLGQLTSNADVKTHGNTVFKALGDVVKQKGKHASN 81
Cdd:cd08926    1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGISQDDLKSNEDLKKHGVTVLTALGEILKQKGSHEAE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392877714  82 LQALATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSELEDLYKKGGFQS 149
Cdd:cd08926   81 LKPLAQTHATKHKIPPKYFELITEIIVKVLAEKHPSEMGAPAQAAFSKAFELICSDIEANYKELGFQG 148
Globin pfam00042
Globin;
25-138 5.33e-28

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 100.06  E-value: 5.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   25 VLLRLFEEHPETKAHFPKFKDiPLGQLTSNADVKTHGNTVFKALGDVVKQKGKHA---SNLQALATTHINKHKIPPQNFT 101
Cdd:pfam00042   3 ILARLFTAYPDTKAYFPRFEK-SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAalnAALKKLGARHKEKRGVDPANFK 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 392877714  102 LITNVILKVFAEKFpGEMTAPAQEAFSKAFKAICSEL 138
Cdd:pfam00042  82 LFGEALLVVLAEHL-GEFTPETKAAWDKALDVIAAAL 117
Hb cd14765
Hemoglobins; Hb is the oxygen transport protein of erythrocytes. It is an allosterically ...
 5-138 2.41e-23

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: 88.56  E-value: 2.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   5 DLINKVWAKVEEDLAGnGQTvLLRLFEEHPETKAHFPKFKDIPLGqltsNADVKTHGNTVFKALGDVVKQKGKHASNLQA 84
Cdd:cd14765    3 STIKALWGKVNVEEYG-AEA-LARLFVVYPWTKRYFPKFDDSSSG----NPKVKAHGKKVLGALGDAVKHLDDLKNTFSD 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392877714  85 LATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSEL 138
Cdd:cd14765   77 LSELHADKLHVDPENFKLLSDCLIVVLAAHLGKEFTPEVHAAWDKFLAVVAAAL 130
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 7-138 2.45e-23

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: 88.67  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   7 INKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPLgQLTSNADVKTHGNTVFKALGDVVK---QKGKHASNLQ 83
Cdd:cd01040    1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDL-DLKGSPEFKAHAKRVVGALDSLIDnldDPEALDALLR 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392877714  84 ALATTHInKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSEL 138
Cdd:cd01040   80 KLGKRHK-RRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 6-147 1.48e-22

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: 87.20  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   6 LINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDI--PLgQLTSNADVKTHGNTVFKALGDVVKQKG---KHAS 80
Cdd:cd08924    8 VIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMedPL-EMERSSQLRKHARRVMGALNTVVENLHdpdKVSS 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392877714  81 NLQALATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSELEDLYKKGGF 147
Cdd:cd08924   87 VLALVGKAHALKHKVEPVYFKILSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEVGW 153
Hb-alpha-like cd08927
Hemoglobin alpha, zeta, mu, theta, and related Hb subunits; Hb is the oxygen transport protein ...
 6-142 3.65e-18

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: 75.30  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   6 LINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPlgqltSNADVKTHGNTVFKALGDVVKQKGKHASNLQAL 85
Cdd:cd08927    8 LIKALWGKIAGHAEAIGAEALARMFLSFPQTKTYFPHFDLSA-----GSAQVKAHGKKVMDALGDAVKHLDDLPGALSKL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 392877714  86 ATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSELEDLY 142
Cdd:cd08927   83 SDLHAYKLRVDPVNFKLLSHCILVTLAAHLPEDFTPEVHAALDKFLAAVSHVLSSKY 139
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 5-138 7.68e-18

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: 74.60  E-value: 7.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   5 DLINKVWAKVEEDLAGnGQTvLLRLFEEHPETKAHFPKFKDI-PLGQLTSNADVKTHGNTVFKALGDVVKQKGKHASNLQ 83
Cdd:cd08925    3 AAITAVWGKVDVDEVG-AEA-LARLLIVYPWTQRYFSSFGDLsSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKATFA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392877714  84 ALATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSEL 138
Cdd:cd08925   81 DLSEKHSEKLHVDPENFKLLGDCLVVVLAAHFGKEFTPEVQAAWEKFFAVVVDAL 135
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 6-138 3.96e-10

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: 54.83  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   6 LINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKD--IPLGQltsNADVKTHGNTVFKALGDVVKQKGKHA---- 79
Cdd:cd14784    8 LVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLRDstVPLEK---NPKLKPHAMSVFVMTCEAAVQLRKAGkvtv 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392877714  80 --SNLQALATTHInKHKIPPQNFTLITNVILKVFAEKFPG----EMTAPAQEAFSKAFKAICSEL 138
Cdd:cd14784   85 reSKLKRLGATHV-KYGVVDEHFEVVKFALLETIKEAVPDmwspEMKSAWGEAYDQLVAAIKAEM 148
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 5-68 1.31e-09

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: 53.07  E-value: 1.31e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392877714   5 DLINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPLGQLTSNADVKTHG----NTVFKAL 68
Cdd:cd12137    7 QLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFRDVDLEDLRHSKELRAHGlrvlSFVEKSL 74
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 9-138 7.78e-07

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: 45.39  E-value: 7.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   9 KVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPL--GQLTSNADVKTHGNTVFKALGDVVKQKGK--HA-SNLQ 83
Cdd:cd14766    3 KSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDeeDELRSSEILENHAARVMDTLDEAISNIENvdYViDLLH 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392877714  84 ALATTHINKHKIPPQNFTLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAICSEL 138
Cdd:cd14766   83 KVGKMHAKKPGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL 137
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 6-137 2.85e-06

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: 44.40  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714   6 LINKVWAKVEEDLAGNGQTVLLRLFEEHPETKAHFPKFKDIPlGQLTSNADVKTHGNTVFKALGDV---VKQKGK---HA 79
Cdd:cd08923    8 LVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKDSD-EIPENNPKLKAHAMKVFKMTCESaiqLRKKGKvvvAD 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392877714  80 SNLQALATTHINKHKIPPQnFTLITNVILK----VFAEKFPGEMTAPAQEAFSKAFKAICSE 137
Cdd:cd08923   87 TTLKRLGSVHLKKGVADPH-FEVVKEALLKtikeAVGDKWSEEMKCAWGEAYDQLAAAIKKE 147
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 28-134 9.70e-05

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: 39.84  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392877714  28 RLFEEHPETKAHFPkfkdiplgqltsNADVKTHGNTVFKALGDVVkqkgKHASN-------LQALATTHInKHKIPPQNF 100
Cdd:cd12131   26 RLFELDPELKPLFK------------GTDMEEQGRKLMAMLVLVV----KGLDDleallpaLQDLGRRHV-KYGVKPEHY 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 392877714 101 TLITNVILKVFAEKFPGEMTAPAQEAFSKAFKAI 134
Cdd:cd12131   89 PLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGIL 122
 
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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