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Conserved domains on  [gi|768025092|ref|XP_011528532|]
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phosphomannomutase 1 isoform X2 [Homo sapiens]

Protein Classification

HAD_PMM domain-containing protein( domain architecture ID 10505708)

HAD_PMM domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 40-261 1.71e-147

Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.


:

Pssm-ID: 397425  Cd Length: 220  Bit Score: 411.39  E-value: 1.71e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092   40 VAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGdeVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLS 119
Cdd:pfam03332   1 VKDFLQKLRKRVTIGVVGGSDLSKIQEQLGDN--VLDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  120 YMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPE 199
Cdd:pfam03332  79 YIADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEERNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768025092  200 GWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP 261
Cdd:pfam03332 159 GWDKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEIFNDPRTIGHSVTSPDDTVRILEELLKL 220
 
Name Accession Description Interval E-value
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 40-261 1.71e-147

Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.


Pssm-ID: 397425  Cd Length: 220  Bit Score: 411.39  E-value: 1.71e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092   40 VAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGdeVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLS 119
Cdd:pfam03332   1 VKDFLQKLRKRVTIGVVGGSDLSKIQEQLGDN--VLDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  120 YMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPE 199
Cdd:pfam03332  79 YIADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEERNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768025092  200 GWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP 261
Cdd:pfam03332 159 GWDKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEIFNDPRTIGHSVTSPDDTVRILEELLKL 220
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 34-258 8.26e-139

phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319784  Cd Length: 238  Bit Score: 390.10  E-value: 8.26e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  34 KKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGDEvIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDL 113
Cdd:cd02585   15 QPITPEMAEFLAELRQKVKIGVVGGSDYDKIKEQLGDNVP-LLDFDYVFPENGLVAYRDGELLSRQSIIRALGEEKLQAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092 114 INFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMIS 193
Cdd:cd02585   94 INFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEERIEFEELDKKHKIREKFVSALKEEFADKGLTFSIGGQIS 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768025092 194 FDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREI 258
Cdd:cd02585  174 FDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGNDYEIYQDPRTIGHSVTSPKDTVRILEEL 238
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 34-261 3.67e-122

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 348.10  E-value: 3.67e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  34 KKIDPEVAAFLQKLRSR-VQIGVVGGSDYCKIAEQLGDgdEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQD 112
Cdd:PTZ00174  21 NPITQEMKDTLAKLKSKgFKIGVVGGSDYPKIKEQLGE--DVLEDFDYVFSENGLVAYKDGELFHSQSILKFLGEEKLKK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092 113 LINFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMI 192
Cdd:PTZ00174  99 FINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEERDEFEKYDKEHHIREKFIQDLKKEFSDLGLKFSIGGQI 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025092 193 SFDVFPEGWDKRYCLDSLDqDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP 261
Cdd:PTZ00174 179 SFDVFPKGWDKTYCLRHLE-NDFKEIHFFGDKTFEGGNDYEIYNDPRTIGHSVKNPEDTIKILKELFLK 246
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 32-243 1.33e-12

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 65.09  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092   32 GAKKIDPEVAAFLQKLRSR-VQIGVVGGSDYCKI---AEQLGDGDEVIEKFDYVFAENGTVQYKHGrLLSKQTIQNHLge 107
Cdd:TIGR01484  14 NAHELSPETIEALERLREAgVKVVIVTGRSLAEIkelLKQLNLPLPLIAENGALIFYPGEILYIEP-SDVFEEILGIK-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  108 ellQDLINFCLSYMALLrlpkKRGTFIEFRNGMLNISPIGRSCtlEERIEFSELDKKEKIREKFVEaLKTEFAGKGLrfs 187
Cdd:TIGR01484  91 ---FEEIGAELKSLSEH----YVGTFIEDKAIAVAIHYVGAEL--GQELDSKMRERLEKIGRNDLE-LEAIYSGKTD--- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768025092  188 rggmisFDVFPEGWDKRYCLDSL---DQDSFDTIHFFGNetspGGNDFEIFADPRTVGH 243
Cdd:TIGR01484 158 ------LEVLPAGVNKGSALQALlqeLNGKKDEILAFGD----SGNDEEMFEVAGLAVA 206
 
Name Accession Description Interval E-value
PMM pfam03332
Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the ...
 40-261 1.71e-147

Eukaryotic phosphomannomutase; This enzyme EC:5.4.2.8 is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.


Pssm-ID: 397425  Cd Length: 220  Bit Score: 411.39  E-value: 1.71e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092   40 VAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGdeVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLS 119
Cdd:pfam03332   1 VKDFLQKLRKRVTIGVVGGSDLSKIQEQLGDN--VLDEFDYVFSENGLVAYKGGKLLASQSIINHLGEEKLQKLINFCLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  120 YMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPE 199
Cdd:pfam03332  79 YIADLDLPIKRGTFIEFRNGMINVSPIGRNCSQEERNEFEEYDKKHKIRQKFVEALKEEFADYGLTFSIGGQISFDVFPK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768025092  200 GWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP 261
Cdd:pfam03332 159 GWDKTYCLQHVEKDGFDTIHFFGDKTYPGGNDYEIFNDPRTIGHSVTSPDDTVRILEELLKL 220
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 34-258 8.26e-139

phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319784  Cd Length: 238  Bit Score: 390.10  E-value: 8.26e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  34 KKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGDEvIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDL 113
Cdd:cd02585   15 QPITPEMAEFLAELRQKVKIGVVGGSDYDKIKEQLGDNVP-LLDFDYVFPENGLVAYRDGELLSRQSIIRALGEEKLQAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092 114 INFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMIS 193
Cdd:cd02585   94 INFCLRYIADLDLPKKRGTFIEFRNGMINISPIGRNCSQEERIEFEELDKKHKIREKFVSALKEEFADKGLTFSIGGQIS 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768025092 194 FDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREI 258
Cdd:cd02585  174 FDVFPKGWDKTYCLRHLEEDLYEEIHFFGDKTQPGGNDYEIYQDPRTIGHSVTSPKDTVRILEEL 238
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 34-261 3.67e-122

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 348.10  E-value: 3.67e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  34 KKIDPEVAAFLQKLRSR-VQIGVVGGSDYCKIAEQLGDgdEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQD 112
Cdd:PTZ00174  21 NPITQEMKDTLAKLKSKgFKIGVVGGSDYPKIKEQLGE--DVLEDFDYVFSENGLVAYKDGELFHSQSILKFLGEEKLKK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092 113 LINFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMI 192
Cdd:PTZ00174  99 FINFCLRYIADLDIPVKRGTFIEYRNGMINISPIGRNCSQEERDEFEKYDKEHHIREKFIQDLKKEFSDLGLKFSIGGQI 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768025092 193 SFDVFPEGWDKRYCLDSLDqDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFP 261
Cdd:PTZ00174 179 SFDVFPKGWDKTYCLRHLE-NDFKEIHFFGDKTFEGGNDYEIYNDPRTIGHSVKNPEDTIKILKELFLK 246
PLN02423 PLN02423
phosphomannomutase
 34-260 2.72e-108

phosphomannomutase


Pssm-ID: 178043 [Multi-domain]  Cd Length: 245  Bit Score: 313.19  E-value: 2.72e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  34 KKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGdeVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDL 113
Cdd:PLN02423  23 KEATPEMLEFMKELRKVVTVGVVGGSDLSKISEQLGKT--VINDYDYVFSENGLVAHKDGKLIGTQSLKSFLGEDKLKEF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092 114 INFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMIS 193
Cdd:PLN02423 101 INFTLHYIADLDIPIKRGTFIEFRSGMLNVSPIGRNCSQEERDEFEKYDKVHNIRPKMVSVLREKFAHLNLTYSIGGQIS 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768025092 194 FDVFPEGWDKRYCLDSLDQdsFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFF 260
Cdd:PLN02423 181 FDVFPQGWDKTYCLQFLED--FDEIHFFGDKTYEGGNDHEIFESERTIGHTVTSPDDTREQCTALFL 245
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 32-243 1.33e-12

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 65.09  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092   32 GAKKIDPEVAAFLQKLRSR-VQIGVVGGSDYCKI---AEQLGDGDEVIEKFDYVFAENGTVQYKHGrLLSKQTIQNHLge 107
Cdd:TIGR01484  14 NAHELSPETIEALERLREAgVKVVIVTGRSLAEIkelLKQLNLPLPLIAENGALIFYPGEILYIEP-SDVFEEILGIK-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025092  108 ellQDLINFCLSYMALLrlpkKRGTFIEFRNGMLNISPIGRSCtlEERIEFSELDKKEKIREKFVEaLKTEFAGKGLrfs 187
Cdd:TIGR01484  91 ---FEEIGAELKSLSEH----YVGTFIEDKAIAVAIHYVGAEL--GQELDSKMRERLEKIGRNDLE-LEAIYSGKTD--- 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768025092  188 rggmisFDVFPEGWDKRYCLDSL---DQDSFDTIHFFGNetspGGNDFEIFADPRTVGH 243
Cdd:TIGR01484 158 ------LEVLPAGVNKGSALQALlqeLNGKKDEILAFGD----SGNDEEMFEVAGLAVA 206
 
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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