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Conserved domains on  [gi|1845864322|gb|QKD76962|]
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hemoglobin, partial [Auchenoplax crinita]

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) ...
 16-149 3.22e-28

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: 101.38  E-value: 3.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  16 IRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLEeIKDKVKLRSHASRVFHAISSLIDNLDDLELVVSIVQ 95
Cdd:cd01040     1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLD-LKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1845864322  96 KTVGDHYPRNIVAADYEKLFNTIVAFLAMALGESFSEETKTGWINMAGVLMGVI 149
Cdd:cd01040    80 KLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 16-149 3.22e-28

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: 101.38  E-value: 3.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  16 IRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLEeIKDKVKLRSHASRVFHAISSLIDNLDDLELVVSIVQ 95
Cdd:cd01040     1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLD-LKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1845864322  96 KTVGDHYPRNIVAADYEKLFNTIVAFLAMALGESFSEETKTGWINMAGVLMGVI 149
Cdd:cd01040    80 KLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
32-153 1.85e-15

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 68.08  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  32 VAFFLYFFEKNRDLQQKFPDFrDKSLEEIKDKVKLRSHASRVFHAISSLIDNLDDLELVVSIVQKTVGDH-YPRNIVAAD 110
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRF-EKSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPAN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845864322 111 YEKLFNTIVAFLAMALGEsFSEETKTGWINmagvLMGVINAQL 153
Cdd:pfam00042  80 FKLFGEALLVVLAEHLGE-FTPETKAAWDK----ALDVIAAAL 117
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 16-149 3.22e-28

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: 101.38  E-value: 3.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  16 IRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLEeIKDKVKLRSHASRVFHAISSLIDNLDDLELVVSIVQ 95
Cdd:cd01040     1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLD-LKGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1845864322  96 KTVGDHYPRNIVAADYEKLFNTIVAFLAMALGESFSEETKTGWINMAGVLMGVI 149
Cdd:cd01040    80 KLGKRHKRRGVTPEHFEVFGEALLETLEEVLGEAFTPEVEAAWRKLLDYIANAI 133
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 8-156 7.12e-17

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: 72.95  E-value: 7.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322   8 LSEKETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRD-KSLEEIKDKVKLRSHASRVFHAISSLIDNLDD 86
Cdd:cd08924     1 LTEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHmEDPLEMERSSQLRKHARRVMGALNTVVENLHD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845864322  87 LELVVSIVQKTVGDHYPRNIVAADYEK-LFNTIVAFLAMALGESFSEETKTGWINMAGVLMGVINAQLKQL 156
Cdd:cd08924    81 PDKVSSVLALVGKAHALKHKVEPVYFKiLSGVILEVLAEEFAQDFTPEVQSAWSKLRGLIYSHVTAAYKEV 151
Globin pfam00042
Globin;
32-153 1.85e-15

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 68.08  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  32 VAFFLYFFEKNRDLQQKFPDFrDKSLEEIKDKVKLRSHASRVFHAISSLIDNLDDLELVVSIVQKTVGDH-YPRNIVAAD 110
Cdd:pfam00042   1 AEILARLFTAYPDTKAYFPRF-EKSADDLKGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARHkEKRGVDPAN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845864322 111 YEKLFNTIVAFLAMALGEsFSEETKTGWINmagvLMGVINAQL 153
Cdd:pfam00042  80 FKLFGEALLVVLAEHLGE-FTPETKAAWDK----ALDVIAAAL 117
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 8-138 7.19e-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: 51.53  E-value: 7.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322   8 LSEKETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLEEIKDKVKLRSHASRVFHAISSLIDNLDDL 87
Cdd:cd12137     1 LTERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFFPFRDVDLEDLRHSKELRAHGLRVLSFVEKSLARLHQP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845864322  88 ELVVSIVQKTVGDHYPRNIVAADYEKLFNTIVAFLAMALGESFSEETKTGW 138
Cdd:cd12137    81 DKLEELLHELGRKHYRYNAKVKYVDLVGQQFIFAIEPVLKEQWTPELEEAW 131
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 12-148 1.47e-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: 50.24  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  12 ETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQqkfPDFRDKSLEEIKDKVklrshasrvFHAISSLIDNLDDLELVV 91
Cdd:cd12131     1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELK---PLFKGTDMEEQGRKL---------MAMLVLVVKGLDDLEALL 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1845864322  92 SIVQKTVGDHYPRNIVAADYEKLFNTIVAFLAMALGESFSEETKTGWINMAGVLMGV 148
Cdd:cd12131    69 PALQDLGRRHVKYGVKPEHYPLVGEALLWTLEEGLGDEWTPEVKQAWTDAYGILAGT 125
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 8-138 4.41e-08

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: 49.41  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322   8 LSEKETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDkSLEEIKDKVKLRSHASRVFHAISSLIDNLDDL 87
Cdd:cd08923     1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLKD-SDEIPENNPKLKAHAMKVFKMTCESAIQLRKK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845864322  88 ELVV----------SI-VQKTVGD-HYPrnIVAadyEKLFNTIVAflamALGESFSEETKTGW 138
Cdd:cd08923    80 GKVVvadttlkrlgSVhLKKGVADpHFE--VVK---EALLKTIKE----AVGDKWSEEMKCAW 133
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 8-146 1.46e-06

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: 45.21  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322   8 LSEKETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFP--DFRDKSLEEIKDKVKLRSHASRVFHAISSLIDNLD 85
Cdd:cd08920     1 LSRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPDLLPLFQynGRQFSSPQDCLSSPEFLDHIRKVMLVIDAAVSHLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1845864322  86 DL----ELVVSIVQKtvgdHYPRNIVAADYEKLFNTIVAFLAMALGESFSEETKTGWINMAGVLM 146
Cdd:cd08920    81 DLssleEYLTSLGRK----HRAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREAWSTLYGAVV 141
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 16-132 1.84e-06

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: 45.00  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322  16 IRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFR--DKSLEEIKDKVKLRSHASRVFHAISSLIDNLDDLELVVSI 93
Cdd:cd14766     1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKnlEDEEDELRSSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845864322  94 VQKTVGDHYPRNIVAADYeklFNTI-VAFLAM---ALGESFSE 132
Cdd:cd14766    81 LHKVGKMHAKKPGFRPEM---FWKIeEPFLEAvseTLGDRYTD 120
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 9-74 2.53e-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: 42.12  E-value: 2.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845864322   9 SEKETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLeEIKDKVKLRSHASRVF 74
Cdd:cd14784     2 SEEQEALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLRDSTV-PLEKNPKLKPHAMSVF 66
Mb cd08926
Animal Myoglobins; Myoglobin (Mb) is a monomeric pentacoordinate heme-bound globin protein ...
 20-81 3.50e-04

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: 38.98  E-value: 3.50e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845864322  20 WEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLEEIKDKVKLRSHASRVFHAISSLI 81
Cdd:cd08926    10 WAKVEADLTGIGQEVLLRLFKEHPETQEHFPKFKGISQDDLKSNEDLKKHGVTVLTALGEIL 71
FHb_fungal-globin cd19754
Globin domain of fungal flavohemoglobin; FlavoHbs function primarily as nitric oxide ...
 8-147 1.35e-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: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845864322   8 LSEKETKLIRASWEVVKKDFKANSVAFFLYFFEKNRDLQQKFPDFRDKSLEEikdkvklrshaSRVF-HAISSLIDNLDD 86
Cdd:cd19754     1 LTPAQIKIIKDSVPILESLGVKLTEKFYKYMLKRYPEVKPYFNETNQKLLRQ-----------PKILaFALLQYAKNIDD 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1845864322  87 L----ELVVSIVQKTVG-----DHYPrnIVAadyEKLFNTIVAFL--AMALGEsFSEETKTGWINMAGVLMG 147
Cdd:cd19754    70 LtplsGFVEQIVSKHVGlqvkpEHYP--IVG---ECLIETMKELLpeAVATDE-FIEAWTTAYGNLANILID 135
 
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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