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Conserved domains on  [gi|24647278|ref|NP_732082|]
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globin 1, isoform C [Drosophila melanogaster]

Protein Classification

globin( domain architecture ID 10099307)

M-family globin similar to a variety of single-domain globins such as myoglobin and hemoglobin

CATH:  1.10.490.10
Gene Ontology:  GO:0019825|GO:0020037|GO:0005344|GO:0005506|GO:0015671
PubMed:  32863222|16061809|19281958|23209182
SCOP:  4000551

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 9-142 4.71e-25

myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd.


:

Pssm-ID: 381254  Cd Length: 133  Bit Score: 92.90  E-value: 4.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   9 IKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFPFRDVPLEELSGNARFRAHAGRIIRVFDESIQVLgqdGDLEKLDEI 88
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDLKGSPEFKAHAKRVVGALDSLIDNL---DDPEALDAL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24647278  89 WTKIAVSHIPRTVSKESYNQLKGVILDVLTAACS--LDESQAATWAKLVDHVYGII 142
Cdd:cd01040  78 LRKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGeaFTPEVEAAWRKLLDYIANAI 133
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 9-142 4.71e-25

myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd.


Pssm-ID: 381254  Cd Length: 133  Bit Score: 92.90  E-value: 4.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   9 IKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFPFRDVPLEELSGNARFRAHAGRIIRVFDESIQVLgqdGDLEKLDEI 88
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDLKGSPEFKAHAKRVVGALDSLIDNL---DDPEALDAL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24647278  89 WTKIAVSHIPRTVSKESYNQLKGVILDVLTAACS--LDESQAATWAKLVDHVYGII 142
Cdd:cd01040  78 LRKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGeaFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
25-142 4.56e-15

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 66.93  E-value: 4.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278    25 AAILTQFFNRFPSNLEKFPFRDVPLEELSGNARFRAHAGRIIRVFDESIQVLgqdGDLEKLDEIWTKIAVSHIP-RTVSK 103
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSADDLKGSPKFKAHGKKVLAALGEAVKHL---DDLAALNAALKKLGARHKEkRGVDP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24647278   104 ESYNQLKGVILDVLTAACSL--DESQAAtWAKLVDHVYGII 142
Cdd:pfam00042  78 ANFKLFGEALLVVLAEHLGEftPETKAA-WDKALDVIAAAL 117
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 9-142 4.71e-25

myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) and single-domain globins: FHbs, Ngbs/neuroglobins, Cygb/cytoglobins, GbE/avian eye specific globin E, GbX/globin X, amphibian GbY/globin Y, Mb/myoglobin, HbA/hemoglobin-alpha, HbB/hemoglobin-beta, SDgbs/single-domain globins related to FHbs, and Adgb/androglobin. The M family exhibits the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments (named A through H). In Adgbs, the globin domain is split into two: helices C-H are followed by helices A-B and the two parts are separated by the IQ motif. Although rearranged, the globin domain of most Adgbs contains a number of conserved residues which play critical roles in heme-coordination and gas ligand binding. Adgbs have been omitted from this A-H helix cd.


Pssm-ID: 381254  Cd Length: 133  Bit Score: 92.90  E-value: 4.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   9 IKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFPFRDVPLEELSGNARFRAHAGRIIRVFDESIQVLgqdGDLEKLDEI 88
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDLKGSPEFKAHAKRVVGALDSLIDNL---DDPEALDAL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24647278  89 WTKIAVSHIPRTVSKESYNQLKGVILDVLTAACS--LDESQAATWAKLVDHVYGII 142
Cdd:cd01040  78 LRKLGKRHKRRGVTPEHFEVFGEALLETLEEVLGeaFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
25-142 4.56e-15

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 66.93  E-value: 4.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278    25 AAILTQFFNRFPSNLEKFPFRDVPLEELSGNARFRAHAGRIIRVFDESIQVLgqdGDLEKLDEIWTKIAVSHIP-RTVSK 103
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRFEKSADDLKGSPKFKAHGKKVLAALGEAVKHL---DDLAALNAALKKLGARHKEkRGVDP 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24647278   104 ESYNQLKGVILDVLTAACSL--DESQAAtWAKLVDHVYGII 142
Cdd:pfam00042  78 ANFKLFGEALLVVLAEHLGEftPETKAA-WDKALDVIAAAL 117
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 5-139 1.37e-12

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: 61.40  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   5 EVQLIKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFP-FRDVP-LEELSGNARFRAHAGRIIRVFDESIQVLgqdGDL 82
Cdd:cd08924   5 ERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSqFKHMEdPLEMERSSQLRKHARRVMGALNTVVENL---HDP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647278  83 EKLDEIWTKIAVSH-IPRTVSKESYNQLKGVILDVLTAA---CSLDESQAAtWAKLVDHVY 139
Cdd:cd08924  82 DKVSSVLALVGKAHaLKHKVEPVYFKILSGVILEVLAEEfaqDFTPEVQSA-WSKLRGLIY 141
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 4-97 2.75e-05

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: 41.67  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   4 DEVQLIKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFP-FRDVPLEELSGNARFRAHAGRIIRVFDEsiqVLGQDGDL 82
Cdd:cd08926   1 ADWDLVLKVWAKVEADLTGIGQEVLLRLFKEHPETQEHFPkFKGISQDDLKSNEDLKKHGVTVLTALGE---ILKQKGSH 77

                        90
                ....*....|....*
gi 24647278  83 EkldEIWTKIAVSHI 97
Cdd:cd08926  78 E---AELKPLAQTHA 89
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 7-142 9.84e-05

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: 40.19  E-value: 9.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   7 QLIKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFPF---RDVPLEElsgNARFRAHAGRIIRVFDESIQVLGQDGDLE 83
Cdd:cd14784   7 ALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFlrdSTVPLEK---NPKLKPHAMSVFVMTCEAAVQLRKAGKVT 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24647278  84 KLDEIWTKIAVSHIPRTVSKESYNQLKGVILDVLTAACSLDESQA--ATWAKLVDHVYGII 142
Cdd:cd14784  84 VRESKLKRLGATHVKYGVVDEHFEVVKFALLETIKEAVPDMWSPEmkSAWGEAYDQLVAAI 144
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 1-111 3.77e-04

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: 38.43  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   1 MNSDEVQLIKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKF-PFRDVPLEELSGNARFRAHAGRIIRVFDESIQVLGQd 79
Cdd:cd12137   1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFfPFRDVDLEDLRHSKELRAHGLRVLSFVEKSLARLHQ- 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 24647278  80 gdLEKLDEIWTKIAVSHIpRTVSKESYNQLKG 111
Cdd:cd12137  80 --PDKLEELLHELGRKHY-RYNAKVKYVDLVG 108
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 1-146 1.53e-03

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: 36.74  E-value: 1.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278   1 MNSDEVQLIKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKF-----PFRDVPlEELSgNARFRAHAGRIIRVFDESIQV 75
Cdd:cd08920   1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFqyngrQFSSPQ-DCLS-SPEFLDHIRKVMLVIDAAVSH 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647278  76 LgqdGDLEKLDEIWTKIAVSHIPRTVSKESYNQLKGVIL----DVLTAACSLDESQAatWAKLvdhvYGIIFKAI 146
Cdd:cd08920  79 L---EDLSSLEEYLTSLGRKHRAVGVKLESFSTVGESLLymleSSLGPAFTPDTREA--WSTL----YGAVVQAM 144
Globin-like cd01067
Globin-like protein superfamily; This globin-like domain superfamily contains a wide variety ...
 26-142 3.96e-03

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: 35.12  E-value: 3.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647278  26 AILTQFFNRF---PSNLEKFpfrdvpleelSGNARFRAHAGRIIRVFdesIQVLGQDGDLEKLDEIWTKIAVSHIPRTVS 102
Cdd:cd01067  11 EIVDDFYDRLfalPSLSELF----------SPPGRLAKCIRKQMHFL---RYALYGLVDGDSIEEGLAGLGEAHKSLGVP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24647278 103 KESYNQLKGVILDVLTAACSLDESQAA--TWAKLVDHVYGII 142
Cdd:cd01067  78 ISYFIAALNVMKDVLTELLGDKFTPAAgeAWTKIFDYIISSM 119
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 9-77 4.15e-03

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: 35.37  E-value: 4.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24647278   9 IKKTWEIPVATPTDSGAAILTQFFNRFPSNLEKFPFRDVPL---EELSGNARFRAHAGRIIRVFDESIQVLG 77
Cdd:cd14766   1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEdeeDELRSSEILENHAARVMDTLDEAISNIE 72
 
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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