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Conserved domains on  [gi|403063989|gb|AFR12523|]
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phosphoglucose isomerase, partial [Drosophila sp. 4 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

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List of domain hits

 Name Accession Description Interval E-value
pgi super family cl30093
glucose-6-phosphate isomerase; Reviewed
 1-167 1.48e-111

glucose-6-phosphate isomerase; Reviewed


The actual alignment was detected with superfamily member PRK00179:

Pssm-ID: 234679  Cd Length: 548  Bit Score: 327.52  E-value: 1.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PRK00179  87 NTTEDRAVLHTALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDDEAVAKHFVALSTNK 159
Cdd:PRK00179 167 LRPYADpGLRVHFVSNVDGAHLAETLKKLDPETTLFIVASKTFTTQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNA 246


                 ....*...
gi 403063989 160 EKVTAFGI 167
Cdd:PRK00179 247 EAVAEFGI 254
 
Name Accession Description Interval E-value
pgi PRK00179
glucose-6-phosphate isomerase; Reviewed
 1-167 1.48e-111

glucose-6-phosphate isomerase; Reviewed


Pssm-ID: 234679  Cd Length: 548  Bit Score: 327.52  E-value: 1.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PRK00179  87 NTTEDRAVLHTALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDDEAVAKHFVALSTNK 159
Cdd:PRK00179 167 LRPYADpGLRVHFVSNVDGAHLAETLKKLDPETTLFIVASKTFTTQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNA 246


                 ....*...
gi 403063989 160 EKVTAFGI 167
Cdd:PRK00179 247 EAVAEFGI 254
PGI pfam00342
Phosphoglucose isomerase; Phosphoglucose isomerase catalyzes the interconversion of ...
 1-167 5.10e-97

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


Pssm-ID: 395271  Cd Length: 487  Bit Score: 288.60  E-value: 5.10e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989    1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:pfam00342  38 NSTENRAVLHVALRNRSNTPIYVDGKDVMPEVNAVLAKMKSFSERVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   81 LKPY-GKGLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDDEAVAKHFVALSTNK 159
Cdd:pfam00342 118 LKPYsGRDLDVHFVSNVDGTHIAEVLKKLNPETTLFIVASKTFTTAETMTNAESAKEWLLKALKDDSAVAKHFIALSTNA 197


                  ....*...
gi 403063989  160 EKVTAFGI 167
Cdd:pfam00342 198 EKVEEFGI 205
Pgi COG0166
Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate ...
 1-167 2.89e-79

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: 242.74  E-value: 2.89e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGiepvlvDGKDVMPDVRAELQHMKEFTNKVIsgvwrgcTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:COG0166   60 NPTEGRAVLHGALRLPE------AGEDVMPEVREELARIKAFAEKVR-------TGKRITDVVNIGIGGSDLGPRAVIEA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKddEAVAKHFVALSTNK 159
Cdd:COG0166  127 LKPYFRdGPRVHFVSNVDPDYLAELLAGLDPETTLFIVISKSGTTQETLTNARVAREWLEKAGG--EDAAKHFVAVTDNA 204


                 ....*...
gi 403063989 160 EKVTAFGI 167
Cdd:COG0166  205 GALRAFGI 212
SIS_PGI_1 cd05015
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification ...
 33-167 1.92e-57

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: 176.95  E-value: 1.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  33 RAELQHMKEFTNKVISGvwrgctgKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYE 111
Cdd:cd05015    1 RAELERIKEFAEKVRSG-------KKITDVVVIGIGGSDLGPRAVYEALKPYFKgGLRLHFVSNVDPDDLAELLKKLDPE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 403063989 112 TTLFIIASKTFTTQETITNATSAKTWLLEHAKDDeaVAKHFVALSTNKEKVTA-FGI 167
Cdd:cd05015   74 TTLFIVISKSGTTLETLANARLAREWLEEAGGDD--LAKHFVAITDNGSGLLKkAGI 128
 
Name Accession Description Interval E-value
pgi PRK00179
glucose-6-phosphate isomerase; Reviewed
 1-167 1.48e-111

glucose-6-phosphate isomerase; Reviewed


Pssm-ID: 234679  Cd Length: 548  Bit Score: 327.52  E-value: 1.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PRK00179  87 NTTEDRAVLHTALRNPSNTPILVDGQDVMPEVHAVLARMKAFAEAVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDDEAVAKHFVALSTNK 159
Cdd:PRK00179 167 LRPYADpGLRVHFVSNVDGAHLAETLKKLDPETTLFIVASKTFTTQETLTNAHSARDWFLAAGGDEAAVAKHFVAVSTNA 246


                 ....*...
gi 403063989 160 EKVTAFGI 167
Cdd:PRK00179 247 EAVAEFGI 254
PGI pfam00342
Phosphoglucose isomerase; Phosphoglucose isomerase catalyzes the interconversion of ...
 1-167 5.10e-97

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


Pssm-ID: 395271  Cd Length: 487  Bit Score: 288.60  E-value: 5.10e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989    1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:pfam00342  38 NSTENRAVLHVALRNRSNTPIYVDGKDVMPEVNAVLAKMKSFSERVRSGEWKGYTGKAITDVVNIGIGGSDLGPVMVTEA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   81 LKPY-GKGLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDDEAVAKHFVALSTNK 159
Cdd:pfam00342 118 LKPYsGRDLDVHFVSNVDGTHIAEVLKKLNPETTLFIVASKTFTTAETMTNAESAKEWLLKALKDDSAVAKHFIALSTNA 197


                  ....*...
gi 403063989  160 EKVTAFGI 167
Cdd:pfam00342 198 EKVEEFGI 205
Pgi COG0166
Glucose-6-phosphate isomerase [Carbohydrate transport and metabolism]; Glucose-6-phosphate ...
 1-167 2.89e-79

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: 242.74  E-value: 2.89e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGiepvlvDGKDVMPDVRAELQHMKEFTNKVIsgvwrgcTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:COG0166   60 NPTEGRAVLHGALRLPE------AGEDVMPEVREELARIKAFAEKVR-------TGKRITDVVNIGIGGSDLGPRAVIEA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKddEAVAKHFVALSTNK 159
Cdd:COG0166  127 LKPYFRdGPRVHFVSNVDPDYLAELLAGLDPETTLFIVISKSGTTQETLTNARVAREWLEKAGG--EDAAKHFVAVTDNA 204


                 ....*...
gi 403063989 160 EKVTAFGI 167
Cdd:COG0166  205 GALRAFGI 212
PLN02649 PLN02649
glucose-6-phosphate isomerase
 1-167 8.30e-69

glucose-6-phosphate isomerase


Pssm-ID: 215351 [Multi-domain]  Cd Length: 560  Bit Score: 217.98  E-value: 8.30e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PLN02649  89 NSTEDRAVLHVALRAPRLAPILVDGKNVVPEVWEVLDKIKAFSEDVRSGKWKGATGKRFTNVVSIGIGGSFLGPLFVHEA 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYGKGLHS------HFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEhAKDDEAVAKHFVA 154
Cdd:PLN02649 169 LATDPEALKSakgrklRFLANVDPVDIARQIAQLDPETTLVVVVSKTFTTAETMLNARTVRKWLRD-ALGGLAVAKHMVA 247

                        170
                 ....*....|...
gi 403063989 155 LSTNKEKVTAFGI 167
Cdd:PLN02649 248 VSTNLLLVNKFGI 260
PTZ00430 PTZ00430
glucose-6-phosphate isomerase; Provisional
 1-167 1.35e-59

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 185612  Cd Length: 552  Bit Score: 193.70  E-value: 1.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNRGIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PTZ00430  84 NTTENRAVLHTALRAPRGEKVVVDGKNVLEDVHEVLDRIKKFSDKIRSGEILGSTGKKLKNVICIGIGGSYLGTEFVYEA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  81 LKPYG------KGLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDDEAVAKHFVA 154
Cdd:PTZ00430 164 LRTYGeareasKGRKLRFLANVDPIDVRRATEGLDPEETLVVIISKTFTTAETMLNAKTVRQWLLDNIKSKEALSKHLCA 243

                        170
                 ....*....|...
gi 403063989 155 LSTNKEKVTAFGI 167
Cdd:PTZ00430 244 VSTNLKLTSEFGI 256
SIS_PGI_1 cd05015
Phosphoglucose isomerase (PGI) contains two SIS (Sugar ISomerase) domains. This classification ...
 33-167 1.92e-57

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: 176.95  E-value: 1.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  33 RAELQHMKEFTNKVISGvwrgctgKQITDVVNIGIGGSDLGPLMVTETLKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYE 111
Cdd:cd05015    1 RAELERIKEFAEKVRSG-------KKITDVVVIGIGGSDLGPRAVYEALKPYFKgGLRLHFVSNVDPDDLAELLKKLDPE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 403063989 112 TTLFIIASKTFTTQETITNATSAKTWLLEHAKDDeaVAKHFVALSTNKEKVTA-FGI 167
Cdd:cd05015   74 TTLFIVISKSGTTLETLANARLAREWLEEAGGDD--LAKHFVAITDNGSGLLKkAGI 128
pgi PRK14095
glucose-6-phosphate isomerase; Provisional
 2-154 6.60e-35

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 237608  Cd Length: 533  Bit Score: 127.44  E-value: 6.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   2 ITENRAVLHTALRNR-GIEPVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PRK14095  93 PSENRPVLHTATRGQvGDSVLTDEAEDMAEFSKRELERLAEFLKKVRSGEIKNSNGKKFTTVVQIGIGGSDLGPKALYLA 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 403063989  81 LKPYGK-GLHSHFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETITNATSAKTWLLEHAKDdeaVAKHFVA 154
Cdd:PRK14095 173 LKNYAKkDKRVHFISNVDPDDAAEVLSEIDLAKTLFIVVSKSGTTLETAANEEFVRDALKKAGLD---YKKHFIA 244
pgi PRK14096
glucose-6-phosphate isomerase; Provisional
 1-127 8.15e-25

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 237609 [Multi-domain]  Cd Length: 528  Bit Score: 99.19  E-value: 8.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989   1 NITENRAVLHTALRNrgiePVLVDGKDVMPDVRAELQHMKEFTNKVISGVWRGCTGKQITDVVNIGIGGSDLGPLMVTET 80
Cdd:PRK14096  60 NPDEGRMVGHYWLRN----PELAPTPEIRAEITETLAQIEAFAAKVHSGTIKPPNGEKFTDVLWIGIGGSALGPQFVAEA 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 403063989  81 LKPYGKGLHSHFVSNIDGTHMAEVLKSVS--YETTLFIIASKTFTTQET 127
Cdd:PRK14096 136 LQPNSDGLNIHFIDNTDPDGIDRVLAELGdrLATTLVVVISKSGGTPET 184
PRK00973 PRK00973
glucose-6-phosphate isomerase; Provisional
 57-161 1.82e-12

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179193 [Multi-domain]  Cd Length: 446  Bit Score: 63.86  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  57 KQITDVVNIGIGGSDLGPLMVTETLKPYGKGLHS---------HFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQET 127
Cdd:PRK00973  69 KNFDNVVVLGIGGSALGNLALHYALNPLNWNELSkeerngprvFVLDNVDPEKTASILDVIDLEKTLFNVISKSGNTAET 148

                         90       100       110
                 ....*....|....*....|....*....|....
gi 403063989 128 ITNATSAKTWLLEHAKDdeaVAKHFVALsTNKEK 161
Cdd:PRK00973 149 LANYLIIRGILEKLGLD---PKKHLVFT-TDPEK 178
PRK03868 PRK03868
glucose-6-phosphate isomerase; Provisional
 59-166 8.70e-11

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 235168  Cd Length: 410  Bit Score: 59.18  E-value: 8.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  59 ITDVVNIGIGGSDLGPLMVTETLKPY---GKGLHshFVSNIDGTHMAEVLKSVSYETTLFIIASKTFTTQETItnatSAK 135
Cdd:PRK03868  58 IKNIVVIGIGGSSLGVKAIYSFLKNEknnKKELH--FLENTDPISINKTLSKINLENTLFIVISKSGTTIETI----SIF 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 403063989 136 TWLLEHAKDDEAVAKHFVALSTNKEKVTAFG 166
Cdd:PRK03868 132 KYLLSHFKLDQELKKNFLFITDPDSKLEQFA 162
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
 27-162 3.59e-09

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 54.59  E-value: 3.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063989  27 DVMPDVRAELQHMKEFTNKVisgvwrgcTGKQITDVVNIGIGGSDLGPLMVTETLKP---YGKgLHShfvsnIDGTHMAE 103
Cdd:PRK09533 431 DIVEDELAHLAEYEAFAEEV--------RAEGFTDAVVLGMGGSSLGPEVLAETFGQrdgFPK-LHV-----LDSTDPAQ 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403063989 104 VL---KSVSYETTLFIIASKTFTTQETitnaTSAKTWLLEHAKD--DEAVAKHFVALS---TNKEKV 162
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.
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