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Conserved domains on  [gi|2751289394|ref|XP_034323744|]
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neuroglobin isoform X1 [Magallana gigas]

Protein Classification

globin family protein; hemoglobin alpha subunit family protein( domain architecture ID 10201291)

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| 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
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 113-247 2.28e-66

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: 202.55  E-value: 2.28e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 113 IIKSWKGIARDLHATGVTMFLRMFQEYDDLRKFFKFGDYKESS--DLLQNKIFQNHVMLVMHTLDEAICSMGDTDYVMEM 190
Cdd:cd14766     1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEedELRSSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2751289394 191 LRGVGKSHRRLPEFNFMIFSRIEEPFLIAVKETLGDRYSANMDNIYRKTVKFIIREL 247
Cdd:cd14766    81 LHKVGKMHAKKPGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL 137
 
Name Accession Description Interval E-value
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 113-247 2.28e-66

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: 202.55  E-value: 2.28e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 113 IIKSWKGIARDLHATGVTMFLRMFQEYDDLRKFFKFGDYKESS--DLLQNKIFQNHVMLVMHTLDEAICSMGDTDYVMEM 190
Cdd:cd14766     1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEedELRSSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2751289394 191 LRGVGKSHRRLPEFNFMIFSRIEEPFLIAVKETLGDRYSANMDNIYRKTVKFIIREL 247
Cdd:cd14766    81 LHKVGKMHAKKPGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL 137
Globin pfam00042
Globin;
132-226 8.59e-09

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 52.29  E-value: 8.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 132 FLRMFQEYDDLRKFFKFGDYkESSDLLQNKIFQNHVMLVMHTLDEAICSMGDTDYVMEMLRGVGKSH---RRLPEFNFMI 208
Cdd:pfam00042   4 LARLFTAYPDTKAYFPRFEK-SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkekRGVDPANFKL 82

                          90
                  ....*....|....*...
gi 2751289394 209 FSRIeepFLIAVKETLGD 226
Cdd:pfam00042  83 FGEA---LLVVLAEHLGE 97
 
Name Accession Description Interval E-value
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 113-247 2.28e-66

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: 202.55  E-value: 2.28e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 113 IIKSWKGIARDLHATGVTMFLRMFQEYDDLRKFFKFGDYKESS--DLLQNKIFQNHVMLVMHTLDEAICSMGDTDYVMEM 190
Cdd:cd14766     1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEedELRSSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2751289394 191 LRGVGKSHRRLPEFNFMIFSRIEEPFLIAVKETLGDRYSANMDNIYRKTVKFIIREL 247
Cdd:cd14766    81 LHKVGKMHAKKPGFRPEMFWKIEEPFLEAVSETLGDRYTDNMENIYRKTIKFILQTL 137
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 113-247 6.22e-20

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: 82.89  E-value: 6.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 113 IIKSWKGIARDLHATGVTMFLRMFQEYDDLRKFFKFGDyKESSDLLQNKIFQNHVMLVMHTLDEAICSMGDTDYVMEMLR 192
Cdd:cd01040     1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFA-GVDLDLKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2751289394 193 GVGKSHRRL---PEFnfmiFSRIEEPFLIAVKETLGDRYSANMDNIYRKTVKFIIREL 247
Cdd:cd01040    80 KLGKRHKRRgvtPEH----FEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 105-233 1.53e-13

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: 66.17  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 105 LTTRDKYQIIKSWKGIARDLHATGVTMFLRMFQEYDDLRK-FFKFGDyKESSDLLQNKIFQNHVMLVMHTLDEAICSMGD 183
Cdd:cd12137     1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDaFFPFRD-VDLEDLRHSKELRAHGLRVLSFVEKSLARLHQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2751289394 184 TDYVMEMLRGVGKSHRRL---PEFnfmiFSRIEEPFLIAVKETLGDRYSANMD 233
Cdd:cd12137    80 PDKLEELLHELGRKHYRYnakVKY----VDLVGQQFIFAIEPVLKEQWTPELE 128
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 105-251 2.80e-09

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: 54.46  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 105 LTTRDKYQIIKSWKGIARDLHATGVTMFLRMFQEYDDLRKFFKFGDYKESS--DLLQNKIFQNHVMLVMHTLDEAICSMG 182
Cdd:cd08920     1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQYNGRQFSSpqDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2751289394 183 DTDYVMEMLRGVGKSHRRLpEFNFMIFSRIEEPFLIAVKETLGDRYSANMDNIYRKTVKFIIRELSQGF 251
Cdd:cd08920    81 DLSSLEEYLTSLGRKHRAV-GVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVVQAMSRGW 148
Globin pfam00042
Globin;
132-226 8.59e-09

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 52.29  E-value: 8.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 132 FLRMFQEYDDLRKFFKFGDYkESSDLLQNKIFQNHVMLVMHTLDEAICSMGDTDYVMEMLRGVGKSH---RRLPEFNFMI 208
Cdd:pfam00042   4 LARLFTAYPDTKAYFPRFEK-SADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkekRGVDPANFKL 82

                          90
                  ....*....|....*...
gi 2751289394 209 FSRIeepFLIAVKETLGD 226
Cdd:pfam00042  83 FGEA---LLVVLAEHLGE 97
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 105-198 1.14e-05

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: 44.45  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 105 LTTRDKYQIIKSWKGIARDLHATGVTMFLRMFQEYDDLRKFF-KFGDYKESSDLLQNKIFQNHVMLVMHTLDEAICSMGD 183
Cdd:cd08924     1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFsQFKHMEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                          90
                  ....*....|....*
gi 2751289394 184 TDYVMEMLRGVGKSH 198
Cdd:cd08924    81 PDKVSSVLALVGKAH 95
Hb-beta-like cd08925
Hemoglobin beta, gamma, delta, epsilon, and related Hb subunits; Hb is the oxygen transport ...
 109-251 1.86e-04

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: 40.32  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751289394 109 DKYQIIKSWKGIarDLHATGVTMFLRMFQEYDDLRKFF-KFGDYKESSDLLQNKIFQNHVMLVMHTLDEAICSMGDTDYV 187
Cdd:cd08925     1 EKAAITAVWGKV--DVDEVGAEALARLLIVYPWTQRYFsSFGDLSSAAAIAGNPKVAAHGKKVLGALGEAIKHLDDIKAT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2751289394 188 MEMLRgvGKSHRRL---PEfNFMIFSRIeepFLIAVKETLGDRYSANMDNIYRKTVKFIIRELSQGF 251
Cdd:cd08925    79 FADLS--EKHSEKLhvdPE-NFKLLGDC---LVVVLAAHFGKEFTPEVQAAWEKFFAVVVDALSKGY 139
 
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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