NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|403064059|gb|AFR12558|]
View 

phosphoglucose isomerase, partial [Drosophila nr. medialis 3 KNM-2012]

Protein Classification

glucose-6-phosphate isomerase( domain architecture ID 1000311)

glucose-6-phosphate isomerase (GPI) catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate

CATH:  1.10.1390.10|3.40.50.10490
EC:  5.3.1.9
Gene Ontology:  GO:0097367|GO:0004347|GO:0006096|GO:0006094|GO:0051156
PubMed:  6115414
SCOP:  4000799

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
pgi super family cl30093
glucose-6-phosphate isomerase; Reviewed
 1-165 1.66e-108

glucose-6-phosphate isomerase; Reviewed


The actual alignment was detected with superfamily member PRK00179:

Pssm-ID: 234679  Cd Length: 548  Bit Score: 319.81  E-value: 1.66e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLH 79
Cdd:PRK00179  97 TALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEALRPYADpGLR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDDEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:PRK00179 177 VHFVSNVDGAHLAETLKKLDPETTLFIVASKTFTTQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNAEAVAEFGIDP 256


                 ....*.
gi 403064059 160 ANMFGF 165
Cdd:PRK00179 257 DNMFGF 262
 
Name Accession Description Interval E-value
pgi PRK00179
glucose-6-phosphate isomerase; Reviewed
 1-165 1.66e-108

glucose-6-phosphate isomerase; Reviewed


Pssm-ID: 234679  Cd Length: 548  Bit Score: 319.81  E-value: 1.66e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLH 79
Cdd:PRK00179  97 TALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEALRPYADpGLR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDDEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:PRK00179 177 VHFVSNVDGAHLAETLKKLDPETTLFIVASKTFTTQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNAEAVAEFGIDP 256


                 ....*.
gi 403064059 160 ANMFGF 165
Cdd:PRK00179 257 DNMFGF 262
PGI pfam00342
Phosphoglucose isomerase; Phosphoglucose isomerase catalyzes the interconversion of ...
 1-165 1.02e-92

Phosphoglucose isomerase; Phosphoglucose isomerase catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate.


Pssm-ID: 395271  Cd Length: 487  Bit Score: 277.43  E-value: 1.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059    1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPY-GKGLH 79
Cdd:pfam00342  48 VALRNRSNTPIYVDGKDVMPEVNAVLAKMKSFSERVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEALKPYsGRDLD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDDEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:pfam00342 128 VHFVSNVDGTHIAEVLKKLNPETTLFIVASKTFTTAETMTNAESAKEWLLKALKDDSAVAKHFIALSTNAEKVEEFGIDT 207


                  ....*.
gi 403064059  160 ANMFGF 165
Cdd:pfam00342 208 KNMFEF 213
Pgi COG0166
Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate ...
 1-165 1.33e-73

Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate isomerase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439936  Cd Length: 484  Bit Score: 228.10  E-value: 1.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGiepvlvDGKDVMPDVRAELQHMKEFTNKVIsgvwrg*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLH 79
Cdd:COG0166   70 GALRLPE------AGEDVMPEVREELARIKAFAEKVR-------TGKRITDVVNIGIGGSDLGPRAVIEALKPYFRdGPR 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKddEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:COG0166  137 VHFVSNVDPDYLAELLAGLDPETTLFIVISKSGTTQETLTNARVAREWLEKAGG--EDAAKHFVAVTDNAGALRAFGIDE 214


                 ....*..
gi 403064059 160 A-NMFGF 165
Cdd:COG0166  215 GyNTFPF 221
SIS_PGI_1 cd05015
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification ...
 23-165 3.12e-61

Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification is based on the alignment of the first SIS domain. PGI is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF). Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.


Pssm-ID: 240146  Cd Length: 158  Bit Score: 186.19  E-value: 3.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  23 RAELQHMKEFTNKVISGvwrg*tgKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYE 101
Cdd:cd05015    1 RAELERIKEFAEKVRSG-------KKITDVVVIGIGGSDLGPRAVYEALKPYFKgGLRLHFVSNVDPDDLAELLKKLDPE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 403064059 102 TTLFIIASKTFTTQETITNATSAKAWLLEHAKDDeaVAKHFVALSTNKEKVTA-FGIDSANMFGF 165
Cdd:cd05015   74 TTLFIVISKSGTTLETLANARLAREWLEEAGGDD--LAKHFVAITDNGSGLLKkAGIEGLNTFEI 136
 
Name Accession Description Interval E-value
pgi PRK00179
glucose-6-phosphate isomerase; Reviewed
 1-165 1.66e-108

glucose-6-phosphate isomerase; Reviewed


Pssm-ID: 234679  Cd Length: 548  Bit Score: 319.81  E-value: 1.66e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLH 79
Cdd:PRK00179  97 TALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEALRPYADpGLR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDDEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:PRK00179 177 VHFVSNVDGAHLAETLKKLDPETTLFIVASKTFTTQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNAEAVAEFGIDP 256


                 ....*.
gi 403064059 160 ANMFGF 165
Cdd:PRK00179 257 DNMFGF 262
PGI pfam00342
Phosphoglucose isomerase; Phosphoglucose isomerase catalyzes the interconversion of ...
 1-165 1.02e-92

Phosphoglucose isomerase; Phosphoglucose isomerase catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate.


Pssm-ID: 395271  Cd Length: 487  Bit Score: 277.43  E-value: 1.02e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059    1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPY-GKGLH 79
Cdd:pfam00342  48 VALRNRSNTPIYVDGKDVMPEVNAVLAKMKSFSERVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEALKPYsGRDLD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDDEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:pfam00342 128 VHFVSNVDGTHIAEVLKKLNPETTLFIVASKTFTTAETMTNAESAKEWLLKALKDDSAVAKHFIALSTNAEKVEEFGIDT 207


                  ....*.
gi 403064059  160 ANMFGF 165
Cdd:pfam00342 208 KNMFEF 213
Pgi COG0166
Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate ...
 1-165 1.33e-73

Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate isomerase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439936  Cd Length: 484  Bit Score: 228.10  E-value: 1.33e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGiepvlvDGKDVMPDVRAELQHMKEFTNKVIsgvwrg*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLH 79
Cdd:COG0166   70 GALRLPE------AGEDVMPEVREELARIKAFAEKVR-------TGKRITDVVNIGIGGSDLGPRAVIEALKPYFRdGPR 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  80 SHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKddEAVAKHFVALSTNKEKVTAFGIDS 159
Cdd:COG0166  137 VHFVSNVDPDYLAELLAGLDPETTLFIVISKSGTTQETLTNARVAREWLEKAGG--EDAAKHFVAVTDNAGALRAFGIDE 214


                 ....*..
gi 403064059 160 A-NMFGF 165
Cdd:COG0166  215 GyNTFPF 221
PLN02649 PLN02649
glucose-6-phosphate isomerase
 1-165 7.95e-64

glucose-6-phosphate isomerase


Pssm-ID: 215351 [Multi-domain]  Cd Length: 560  Bit Score: 204.89  E-value: 7.95e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGKGLHS 80
Cdd:PLN02649  99 VALRAPRLAPILVDGKNVVPEVWEVLDKIKAFSEDVRSGKWKGATGKRFTNVVSIGIGGSFLGPLFVHEALATDPEALKS 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  81 ------HFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEhAKDDEAVAKHFVALSTNKEKVTA 154
Cdd:PLN02649 179 akgrklRFLANVDPVDIARQIAQLDPETTLVVVVSKTFTTAETMLNARTVRKWLRD-ALGGLAVAKHMVAVSTNLLLVNK 257

                        170
                 ....*....|.
gi 403064059 155 FGIDSANMFGF 165
Cdd:PLN02649 258 FGIDPWNAFPF 268
SIS_PGI_1 cd05015
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification ...
 23-165 3.12e-61

Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification is based on the alignment of the first SIS domain. PGI is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF). Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.


Pssm-ID: 240146  Cd Length: 158  Bit Score: 186.19  E-value: 3.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  23 RAELQHMKEFTNKVISGvwrg*tgKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYE 101
Cdd:cd05015    1 RAELERIKEFAEKVRSG-------KKITDVVVIGIGGSDLGPRAVYEALKPYFKgGLRLHFVSNVDPDDLAELLKKLDPE 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 403064059 102 TTLFIIASKTFTTQETITNATSAKAWLLEHAKDDeaVAKHFVALSTNKEKVTA-FGIDSANMFGF 165
Cdd:cd05015   74 TTLFIVISKSGTTLETLANARLAREWLEEAGGDD--LAKHFVAITDNGSGLLKkAGIEGLNTFEI 136
PTZ00430 PTZ00430
glucose-6-phosphate isomerase; Provisional
 1-165 1.52e-54

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 185612  Cd Length: 552  Bit Score: 180.21  E-value: 1.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   1 TALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYG----- 75
Cdd:PTZ00430  94 TALRAPRGEKVVVDGKNVLEDVHEVLDRIKKFSDKIRSGEILGSTGKKLKNVICIGIGGSYLGTEFVYEALRTYGearea 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  76 -KGLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDDEAVAKHFVALSTNKEKVTA 154
Cdd:PTZ00430 174 sKGRKLRFLANVDPIDVRRATEGLDPEETLVVIISKTFTTAETMLNAKTVRQWLLDNIKSKEALSKHLCAVSTNLKLTSE 253

                        170
                 ....*....|.
gi 403064059 155 FGIDSANMFGF 165
Cdd:PTZ00430 254 FGIPDENVFGF 264
pgi PRK14095
glucose-6-phosphate isomerase; Provisional
 7-144 2.46e-29

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 237608  Cd Length: 533  Bit Score: 112.03  E-value: 2.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   7 GIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLHSHFVSN 85
Cdd:PRK14095 109 GDSVLTDEAEDMAEFSKRELERLAEFLKKVRSGEIKNSNGKKFTTVVQIGIGGSDLGPKALYLALKNYAKkDKRVHFISN 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 403064059  86 IDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKAWLLEHAKDdeaVAKHFVA 144
Cdd:PRK14095 189 VDPDDAAEVLSEIDLAKTLFIVVSKSGTTLETAANEEFVRDALKKAGLD---YKKHFIA 244
pgi PRK14096
glucose-6-phosphate isomerase; Provisional
 3-117 2.84e-21

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 237609 [Multi-domain]  Cd Length: 528  Bit Score: 89.17  E-value: 2.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059   3 LRNrgiePVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRG*TGKQITDVVNIGIGGSDLGPLMVTETLKPYGKGLHSHF 82
Cdd:PRK14096  72 LRN----PELAPTPEIRAEITETLAQIEAFAAKVHSGTIKPPNGEKFTDVLWIGIGGSALGPQFVAEALQPNSDGLNIHF 147

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 403064059  83 VSNIDGTHMAEVLKSVS--YETTLFIIASKTFTTQET 117
Cdd:PRK14096 148 IDNTDPDGIDRVLAELGdrLATTLVVVISKSGGTPET 184
PRK00973 PRK00973
glucose-6-phosphate isomerase; Provisional
 47-151 2.81e-12

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179193 [Multi-domain]  Cd Length: 446  Bit Score: 63.47  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  47 KQITDVVNIGIGGSDLGPLMVTETLKPYGKGLHS---------HFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQET 117
Cdd:PRK00973  69 KNFDNVVVLGIGGSALGNLALHYALNPLNWNELSkeerngprvFVLDNVDPEKTASILDVIDLEKTLFNVISKSGNTAET 148

                         90       100       110
                 ....*....|....*....|....*....|....
gi 403064059 118 ITNATSAKAWLLEHAKDdeaVAKHFVALsTNKEK 151
Cdd:PRK00973 149 LANYLIIRGILEKLGLD---PKKHLVFT-TDPEK 178
PRK03868 PRK03868
glucose-6-phosphate isomerase; Provisional
 49-156 9.83e-11

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 235168  Cd Length: 410  Bit Score: 58.79  E-value: 9.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  49 ITDVVNIGIGGSDLGPLMVTETLKPY---GKGLHshFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETItnatSAK 125
Cdd:PRK03868  58 IKNIVVIGIGGSSLGVKAIYSFLKNEknnKKELH--FLENTDPISINKTLSKINLENTLFIVISKSGTTIETI----SIF 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 403064059 126 AWLLEHAKDDEAVAKHFVALSTNKEKVTAFG 156
Cdd:PRK03868 132 KYLLSHFKLDQELKKNFLFITDPDSKLEQFA 162
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
 17-152 9.14e-10

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 56.13  E-value: 9.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403064059  17 DVMPDVRAELQHMKEFTNKVisgvwrg*TGKQITDVVNIGIGGSDLGPLMVTETLKP---YGKgLHShfvsnIDGTHMAE 93
Cdd:PRK09533 431 DIVEDELAHLAEYEAFAEEV--------RAEGFTDAVVLGMGGSSLGPEVLAETFGQrdgFPK-LHV-----LDSTDPAQ 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403064059  94 VL---KSVSYETTLFIIASKTFTTQETitnaTSAKAWLLEHAKD--DEAVAKHFVALS---TNKEKV 152
Cdd:PRK09533 497 VRaleAAVDLARTLFIVSSKSGGTLEP----NIFKDYFFARVKEvlGAKAGRHFVAVTdpgSSLEKV 559
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH