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Conserved domains on  [gi|86565347|ref|NP_500166|]
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Globin domain-containing protein [Caenorhabditis elegans]

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) ...
 15-156 1.82e-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: 97.91  E-value: 1.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  15 LRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKFNTGG--RSKEIEFHALRFMQVLESVVKTLDNPETLNPLCDN 92
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDlkGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86565347  93 LGRVHGRlsesRGFRTHHWGVFIECTLFHFRKVLGQdtyfhrmDALDKVIINWRIIIRLLIKQM 156
Cdd:cd01040  81 LGKRHKR----RGVTPEHFEVFGEALLETLEEVLGE-------AFTPEVEAAWRKLLDYIANAI 133
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 15-156 1.82e-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: 97.91  E-value: 1.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  15 LRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKFNTGG--RSKEIEFHALRFMQVLESVVKTLDNPETLNPLCDN 92
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDlkGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86565347  93 LGRVHGRlsesRGFRTHHWGVFIECTLFHFRKVLGQdtyfhrmDALDKVIINWRIIIRLLIKQM 156
Cdd:cd01040  81 LGKRHKR----RGVTPEHFEVFGEALLETLEEVLGE-------AFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
33-140 1.17e-13

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 65.77  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347    33 IFEMIFNQSPDTRQLFPFMKFNTGG--RSKEIEFHALRFMQVLESVVKTLDNPETLNPLCDNLGRVHgrlSESRGFRTHH 110
Cdd:pfam00042   3 ILARLFTAYPDTKAYFPRFEKSADDlkGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARH---KEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 86565347   111 WGVFIECtlfhFRKVLGQdtYFHRMDALDK 140
Cdd:pfam00042  80 FKLFGEA----LLVVLAE--HLGEFTPETK 103
 
Name Accession Description Interval E-value
Mb-like cd01040
myoglobin-like; M family globin domain; This family includes chimeric (FHbs/flavohemoglobins) ...
 15-156 1.82e-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: 97.91  E-value: 1.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  15 LRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKFNTGG--RSKEIEFHALRFMQVLESVVKTLDNPETLNPLCDN 92
Cdd:cd01040   1 VKSSWARVKKDKEEFGVAIFLRLFEANPELKKLFPKFAGVDLDlkGSPEFKAHAKRVVGALDSLIDNLDDPEALDALLRK 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86565347  93 LGRVHGRlsesRGFRTHHWGVFIECTLFHFRKVLGQdtyfhrmDALDKVIINWRIIIRLLIKQM 156
Cdd:cd01040  81 LGKRHKR----RGVTPEHFEVFGEALLETLEEVLGE-------AFTPEVEAAWRKLLDYIANAI 133
Globin pfam00042
Globin;
33-140 1.17e-13

Globin;


Pssm-ID: 459646 [Multi-domain]  Cd Length: 117  Bit Score: 65.77  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347    33 IFEMIFNQSPDTRQLFPFMKFNTGG--RSKEIEFHALRFMQVLESVVKTLDNPETLNPLCDNLGRVHgrlSESRGFRTHH 110
Cdd:pfam00042   3 ILARLFTAYPDTKAYFPRFEKSADDlkGSPKFKAHGKKVLAALGEAVKHLDDLAALNAALKKLGARH---KEKRGVDPAN 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 86565347   111 WGVFIECtlfhFRKVLGQdtYFHRMDALDK 140
Cdd:pfam00042  80 FKLFGEA----LLVVLAE--HLGEFTPETK 103
GbX cd12137
Globin_X (GbX); Zebrafish globin X (GbX) is expressed at low levels in neurons of the central ...
 8-101 9.04e-10

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: 55.77  E-value: 9.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347   8 SQEEKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLF-PF--MKFNTGGRSKEIEFHALRFMQVLESVVKTLDNPE 84
Cdd:cd12137   2 TERQKQLIESSWSILQEDIAKVGVIMFVRLFETHPDCKDAFfPFrdVDLEDLRHSKELRAHGLRVLSFVEKSLARLHQPD 81

                        90
                ....*....|....*..
gi 86565347  85 TLNPLCDNLGRVHGRLS 101
Cdd:cd12137  82 KLEELLHELGRKHYRYN 98
HGbI-like cd12131
Hell's gate globin I (HGbI) from Methylacidophilum infernorum and related proteins; HGbI is a ...
 11-129 6.09e-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: 6.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  11 EKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFpfmkfntggRSKEIEFHALRFMQVLESVVKTLDNPETLNPLC 90
Cdd:cd12131   1 QIELVQQSFAKVEPIADEAAALFYERLFELDPELKPLF---------KGTDMEEQGRKLMAMLVLVVKGLDDLEALLPAL 71

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 86565347  91 DNLGRVHGRLsesrGFRTHHWGVFIECTLFHFRKVLGQD 129
Cdd:cd12131  72 QDLGRRHVKY----GVKPEHYPLVGEALLWTLEEGLGDE 106
CeGLB25-like cd14766
Caenorhabditis elegans globin GLB-25, and related globins; The C. elegans genome contains 33 ...
 15-156 9.04e-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: 47.32  E-value: 9.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  15 LRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKFNTGGR-----SKEIEFHALRFMQVLESVVKTLDNPETLNPL 89
Cdd:cd14766   1 LKKSWKGIARKIDETGKTMFLRMLTENPELKELFPKLKNLEDEEdelrsSEILENHAARVMDTLDEAISNIENVDYVIDL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86565347  90 CDNLGRVHGRLSesrGFRTHhwgVF--IECTLFHFRKVLGQDTYFHRMDALdkviinWRIIIRLLIKQM 156
Cdd:cd14766  81 LHKVGKMHAKKP---GFRPE---MFwkIEEPFLEAVSETLGDRYTDNMENI------YRKTIKFILQTL 137
Ngb cd08920
Neuroglobins; The Ngb described in this subfamily is a hexacoordinated heme globin chiefly ...
 8-160 1.27e-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: 47.14  E-value: 1.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347   8 SQEEKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDtrqLFPFMKFNTGGRSK------EIEF--HALRFMQVLESVVKT 79
Cdd:cd08920   2 SRPQKELIRESWRSVSRSPLEHGTVLFSRLFELEPD---LLPLFQYNGRQFSSpqdclsSPEFldHIRKVMLVIDAAVSH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  80 LDNPETLNPLCDNLGRVHgrlsESRGFRTHHWGVFIECTLFHFRKVLGQDTYFHRMDAldkviinWRIIIRLLIKQMKRG 159
Cdd:cd08920  79 LEDLSSLEEYLTSLGRKH----RAVGVKLESFSTVGESLLYMLESSLGPAFTPDTREA-------WSTLYGAVVQAMSRG 147


                .
gi 86565347 160 F 160
Cdd:cd08920 148 W 148
class1_nsHb-like cd14784
Class 1 nonsymbiotic hemoglobins and related proteins; Class1 nsHbs include the dimeric ...
 7-52 5.35e-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: 42.50  E-value: 5.35e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 86565347   7 FSQEEKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMK 52
Cdd:cd14784   1 FSEEQEALVKKSWAVMKKDAAELGLKFFLKIFEIAPSAKQLFSFLR 46
Mb-like_oxidoreductase cd19753
Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This ...
 15-97 1.35e-04

Globin domain of uncharacterized oxidoreductases containing a FAD/NADH binding domain; This subfamily is composed of uncharacterized proteins containing an N-terminal myoglobin-like (M family globin) domain and a C-terminal oxygenase reductase FAD/NADH binding domain belonging to the ferredoxin reductase (FNR) family and is usually part of multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. The domain architecture of this subfamily is similar to flavohemoglobins, which function primarily as nitric oxide dioxygenases (NODs, EC 1.14.12.17), converting NO and O2 to inert NO3- (nitrate). 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.


Pssm-ID: 381293 [Multi-domain]  Cd Length: 121  Bit Score: 40.69  E-value: 1.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347  15 LRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKfntggrskeiEFHALRFMQVLESVVKTLDNPETLNPLCDNLG 94
Cdd:cd19753   1 LRASLAAVEDGPDELARRFYARLFAEAPELRDLFPADM----------DAQRDRLARALTHVVENLDDPDGLVPFLAQLG 70


                ...
gi 86565347  95 RVH 97
Cdd:cd19753  71 RDH 73
VtHb-like_SDgb cd14778
Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is ...
 8-145 1.73e-04

Vitreoscilla stercoraria hemoglobin and related proteins; single-domain globins; VtHb is homodimeric, and may both transport oxygen to terminal respiratory oxidases, and provide resistance to nitrosative stress. It has medium oxygen affinity and displays cooperative ligand-binding properties. VHb has biotechnological application, its expression in heterologous hosts (bacteria and plants) has improved growth and productivity under microaerobic conditions. Another member of this subfamily Campylobacter jejuni hemoglobin (Cgb) is monomeric, and plays a role in detoxifying NO. Along with a truncated globin Ctb, it is up-regulated by the transcription factor NssR in response to nitrosative stress.


Pssm-ID: 381286 [Multi-domain]  Cd Length: 140  Bit Score: 40.88  E-value: 1.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347   8 SQEEKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKFNTGGRSKeiefhALRfMQVLeSVVKTLDNPETLN 87
Cdd:cd14778   2 DQQTIEIIKSTVPVLKEHGVEITTEFYKNMFTEYPEVRPMFDMEKQKSGEQPK-----ALA-MTVL-AAAQNIENLEKIR 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 86565347  88 PLCDNLGRVHGRLsesrGFRTHHWGVFIECTLFHFRKVLGQdtyfhrmDALDKVIINW 145
Cdd:cd14778  75 PAVEKIGKTHVNL----NVKPEHYPIVGACLLGAIKEVLGD-------TATDEILEAW 121
Cygb cd08924
Cytoglobin and related globins; Cygb is a hexacoordinated heme-containing protein, able to ...
 8-97 1.86e-04

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: 40.98  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565347   8 SQEEKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMKFNTGG----RSKEIEFHALRFMQVLESVVKTLDNP 83
Cdd:cd08924   2 TEAERKVIQDTWARVYANCEDVGVAILVRFFVNFPSAKQYFSQFKHMEDPlemeRSSQLRKHARRVMGALNTVVENLHDP 81

                        90
                ....*....|....
gi 86565347  84 ETLNPLCDNLGRVH 97
Cdd:cd08924  82 DKVSSVLALVGKAH 95
class1-2_nsHbs_Lbs cd08923
Class1 nonsymbiotic hemoglobins (nsHbs), class II nsHbs, leghemoglobins (Lbs,) and related ...
 7-52 3.76e-04

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: 39.78  E-value: 3.76e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 86565347   7 FSQEEKDILRRSWKVLDKNLNHTAYNIFEMIFNQSPDTRQLFPFMK 52
Cdd:cd08923   1 FTEKQEALVKSSWEVLKKNIPQLSLRFFLLILEIAPAAKDMFSFLK 46
 
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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