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Conserved domains on  [gi|1078194988|gb|AOV86090|]
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phosphoglycerate kinase, partial [Wallemia muriae]

Protein Classification

phosphoglycerate kinase( domain architecture ID 199)

phosphoglycerate kinase catalyzes the conversion of ATP and 3-phospho-D-glycerate to ADP and 3-phospho-D-glyceroyl phosphate

CATH:  3.40.50.1260
EC:  2.7.2.3
PubMed:  2124145|6689547
SCOP:  4000818

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phosphoglycerate_kinase super family cl00198
Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the ...
1-229 2.62e-131

Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the high-energy phosphate group of 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate. This reaction represents the first of the two substrate-level phosphorylation events in the glycolytic pathway. Substrate-level phosphorylation is defined as production of ATP by a process, which is catalyzed by water-soluble enzymes in the cytosol; not involving membranes and ion gradients.


The actual alignment was detected with superfamily member PTZ00005:

Pssm-ID: 444741  Cd Length: 417  Bit Score: 376.33  E-value: 2.62e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKAVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PTZ00005   40 RIKATLPTIKYLLEQGAKSVVLMSHLGRPDGRRVEKYSLKPVVPKLEELLGKKVTFLNDCVGPEVEEACANAKNGSVILL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDEQGNKIKADQAAVDSFRQQLTKLGDVYVNDAFGTAHRAHSSVSGVKLDTRAAGFLVKKELEYFAR 160
Cdd:PTZ00005  120 ENLRFHIEEEGKGVDANGNKVKADKEEVKKFRKSLTKLGDIYVNDAFGTAHRAHSSMVGVDLPVKVAGFLMKKELDYFSK 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 161 VLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKA-EGVTIGDSLFDKAGFEKVDEI 229
Cdd:PTZ00005  200 ALENPQRPFLAILGGAKVADKIQLIKNLLDKVDEMIIGGGMAFTFKKVlDNMPIGKSLFDEEGAKIVKEI 269
 
Name Accession Description Interval E-value
PTZ00005 PTZ00005
phosphoglycerate kinase; Provisional
1-229 2.62e-131

phosphoglycerate kinase; Provisional


Pssm-ID: 173310  Cd Length: 417  Bit Score: 376.33  E-value: 2.62e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKAVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PTZ00005   40 RIKATLPTIKYLLEQGAKSVVLMSHLGRPDGRRVEKYSLKPVVPKLEELLGKKVTFLNDCVGPEVEEACANAKNGSVILL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDEQGNKIKADQAAVDSFRQQLTKLGDVYVNDAFGTAHRAHSSVSGVKLDTRAAGFLVKKELEYFAR 160
Cdd:PTZ00005  120 ENLRFHIEEEGKGVDANGNKVKADKEEVKKFRKSLTKLGDIYVNDAFGTAHRAHSSMVGVDLPVKVAGFLMKKELDYFSK 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 161 VLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKA-EGVTIGDSLFDKAGFEKVDEI 229
Cdd:PTZ00005  200 ALENPQRPFLAILGGAKVADKIQLIKNLLDKVDEMIIGGGMAFTFKKVlDNMPIGKSLFDEEGAKIVKEI 269
Phosphoglycerate_kinase cd00318
Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the ...
1-229 2.81e-116

Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the high-energy phosphate group of 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate. This reaction represents the first of the two substrate-level phosphorylation events in the glycolytic pathway. Substrate-level phosphorylation is defined as production of ATP by a process, which is catalyzed by water-soluble enzymes in the cytosol; not involving membranes and ion gradients.


Pssm-ID: 238195  Cd Length: 397  Bit Score: 337.30  E-value: 2.81e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:cd00318    31 RIRAALPTIKYLLEQGAK-VVLLSHLGRPKGEPNEKYSLAPVAKALSELLGQPVTFANDCVGPEAEEAVEALKPGDVLLL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDeqgnkikaDQAAVDSFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:cd00318   110 ENVRFYPEEEGKRDD--------DKEADEEFAKKLASLGDVYVNDAFGTAHRAHASMVGIaLLLPSAAGFLMEKELKYLA 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKAGFEKVDEI 229
Cdd:cd00318   182 KALENPERPFVAILGGAKVSDKIQVIENLLDKVDYLIIGGGMAFTFLKAQGMDIGKSLFEEDGIELAKSL 251
PGK pfam00162
Phosphoglycerate kinase;
1-229 3.65e-113

Phosphoglycerate kinase;


Pssm-ID: 425495  Cd Length: 370  Bit Score: 328.56  E-value: 3.65e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPnAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:pfam00162  25 RIRAALPTIKYLLEKGAK-VILMSHLGRPKGKD-DKFSLKPVAERLSELLGKPVKFADDCIGPEAEAAIAALKPGEVLLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEgsrkdeqgnkiKADQAavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:pfam00162 103 ENVRFYKEEE-----------KNDPE----FAKKLASLADVYVNDAFGTAHRAHASTVGVaKFLPSAAGFLMEKELEALS 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKAGFEKVDEI 229
Cdd:pfam00162 168 KALENPERPFVAILGGAKVSDKIGVIENLLDKVDKLIIGGGMANTFLKAQGYEIGKSLVEEDKIELAKEL 237
Pgk COG0126
3-phosphoglycerate kinase [Carbohydrate transport and metabolism]; 3-phosphoglycerate kinase ...
1-230 6.18e-106

3-phosphoglycerate kinase [Carbohydrate transport and metabolism]; 3-phosphoglycerate kinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439896  Cd Length: 389  Bit Score: 310.80  E-value: 6.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:COG0126    32 RIRAALPTIKYLLEKGAK-VILLSHLGRPKGKVDPKYSLKPVAERLSELLGKPVKFVDDCIGEEAEAAVAALKPGEVLLL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEgsrkdeqgnkiKADQAavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:COG0126   111 ENLRFHPEEE-----------KNDPE----FAKKLASLGDVYVNDAFGTAHRAHASTVGIaKLLPSAAGFLMEKELEALG 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKagfEKVDEIK 230
Cdd:COG0126   176 KALENPERPFVAILGGAKVSDKIGVIENLLEKVDKLLIGGGMANTFLKAQGYDVGKSLVEE---DKIDTAK 243
 
Name Accession Description Interval E-value
PTZ00005 PTZ00005
phosphoglycerate kinase; Provisional
1-229 2.62e-131

phosphoglycerate kinase; Provisional


Pssm-ID: 173310  Cd Length: 417  Bit Score: 376.33  E-value: 2.62e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKAVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PTZ00005   40 RIKATLPTIKYLLEQGAKSVVLMSHLGRPDGRRVEKYSLKPVVPKLEELLGKKVTFLNDCVGPEVEEACANAKNGSVILL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDEQGNKIKADQAAVDSFRQQLTKLGDVYVNDAFGTAHRAHSSVSGVKLDTRAAGFLVKKELEYFAR 160
Cdd:PTZ00005  120 ENLRFHIEEEGKGVDANGNKVKADKEEVKKFRKSLTKLGDIYVNDAFGTAHRAHSSMVGVDLPVKVAGFLMKKELDYFSK 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 161 VLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKA-EGVTIGDSLFDKAGFEKVDEI 229
Cdd:PTZ00005  200 ALENPQRPFLAILGGAKVADKIQLIKNLLDKVDEMIIGGGMAFTFKKVlDNMPIGKSLFDEEGAKIVKEI 269
Phosphoglycerate_kinase cd00318
Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the ...
1-229 2.81e-116

Phosphoglycerate kinase (PGK) is a monomeric enzyme which catalyzes the transfer of the high-energy phosphate group of 1,3-bisphosphoglycerate to ADP, forming ATP and 3-phosphoglycerate. This reaction represents the first of the two substrate-level phosphorylation events in the glycolytic pathway. Substrate-level phosphorylation is defined as production of ATP by a process, which is catalyzed by water-soluble enzymes in the cytosol; not involving membranes and ion gradients.


Pssm-ID: 238195  Cd Length: 397  Bit Score: 337.30  E-value: 2.81e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:cd00318    31 RIRAALPTIKYLLEQGAK-VVLLSHLGRPKGEPNEKYSLAPVAKALSELLGQPVTFANDCVGPEAEEAVEALKPGDVLLL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDeqgnkikaDQAAVDSFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:cd00318   110 ENVRFYPEEEGKRDD--------DKEADEEFAKKLASLGDVYVNDAFGTAHRAHASMVGIaLLLPSAAGFLMEKELKYLA 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKAGFEKVDEI 229
Cdd:cd00318   182 KALENPERPFVAILGGAKVSDKIQVIENLLDKVDYLIIGGGMAFTFLKAQGMDIGKSLFEEDGIELAKSL 251
PGK pfam00162
Phosphoglycerate kinase;
1-229 3.65e-113

Phosphoglycerate kinase;


Pssm-ID: 425495  Cd Length: 370  Bit Score: 328.56  E-value: 3.65e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPnAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:pfam00162  25 RIRAALPTIKYLLEKGAK-VILMSHLGRPKGKD-DKFSLKPVAERLSELLGKPVKFADDCIGPEAEAAIAALKPGEVLLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEgsrkdeqgnkiKADQAavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:pfam00162 103 ENVRFYKEEE-----------KNDPE----FAKKLASLADVYVNDAFGTAHRAHASTVGVaKFLPSAAGFLMEKELEALS 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKAGFEKVDEI 229
Cdd:pfam00162 168 KALENPERPFVAILGGAKVSDKIGVIENLLDKVDKLIIGGGMANTFLKAQGYEIGKSLVEEDKIELAKEL 237
Pgk COG0126
3-phosphoglycerate kinase [Carbohydrate transport and metabolism]; 3-phosphoglycerate kinase ...
1-230 6.18e-106

3-phosphoglycerate kinase [Carbohydrate transport and metabolism]; 3-phosphoglycerate kinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439896  Cd Length: 389  Bit Score: 310.80  E-value: 6.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:COG0126    32 RIRAALPTIKYLLEKGAK-VILLSHLGRPKGKVDPKYSLKPVAERLSELLGKPVKFVDDCIGEEAEAAVAALKPGEVLLL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEgsrkdeqgnkiKADQAavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:COG0126   111 ENLRFHPEEE-----------KNDPE----FAKKLASLGDVYVNDAFGTAHRAHASTVGIaKLLPSAAGFLMEKELEALG 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKagfEKVDEIK 230
Cdd:COG0126   176 KALENPERPFVAILGGAKVSDKIGVIENLLEKVDKLLIGGGMANTFLKAQGYDVGKSLVEE---DKIDTAK 243
pgk PRK00073
phosphoglycerate kinase; Provisional
1-230 2.03e-97

phosphoglycerate kinase; Provisional


Pssm-ID: 234613  Cd Length: 389  Bit Score: 288.88  E-value: 2.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGqPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PRK00073   34 RIRAALPTIKYLLEKGAK-VILLSHLGRPKG-EDPEFSLAPVAKRLSELLGKEVKFVDDCIGEEAREAIAALKDGEVLLL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEgsrkdeqgnkiKADQAavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV--KLDTRAAGFLVKKELEYF 158
Cdd:PRK00073  112 ENVRFNKGEE-----------KNDPE----LAKKLASLGDVFVNDAFGTAHRAHASTVGIakFLKPAAAGFLMEKELEAL 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078194988 159 ARVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKagfEKVDEIK 230
Cdd:PRK00073  177 GKALENPERPFVAILGGAKVSDKIGVLENLLEKVDKLIIGGGMANTFLKAQGYNVGKSLVEE---DLIDTAK 245
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
1-230 4.65e-80

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 251.96  E-value: 4.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQPNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PRK13962   37 RIRAALPTIKYLLDHGAK-VILVSHLGRPKGEFDPKFSMAPVAKRLSELLGKEVIFAKDVIGDDAKKAVAQLKEGDVLLL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEgsrkdeqgnkiKADQAavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGV-KLDTRAAGFLVKKELEYFA 159
Cdd:PRK13962  116 ENVRFHKEET-----------KNDPE----FAKELASLADIYVNDAFGTAHRAHASTAGVaEYLPAVAGFLMEKEIEFLG 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1078194988 160 RVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDKagfEKVDEIK 230
Cdd:PRK13962  181 KALANPQRPFVAILGGAKVSDKIGVIENLLEKVDKLLIGGGMAYTFLKAKGYEVGKSLVEE---DKLDLAK 248
PLN02282 PLN02282
phosphoglycerate kinase
1-220 6.16e-63

phosphoglycerate kinase


Pssm-ID: 165923  Cd Length: 401  Bit Score: 201.35  E-value: 6.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQpNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PLN02282   41 RIRAAVPTIKYLMGHGAR-VILCSHLGRPKGV-TPKYSLKPLVPRLSELLGVEVVMANDCIGEEVEKLVAELPEGGVLLL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDeqgnkikadqaavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGVK--LDTRAAGFLVKKELEYF 158
Cdd:PLN02282  119 ENVRFYKEEEKNDPE---------------FAKKLASLADVYVNDAFGTAHRAHASTEGVAkyLKPSVAGFLMQKELDYL 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078194988 159 ARVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDK 220
Cdd:PLN02282  184 VGAVANPKKPFAAIVGGSKVSTKIGVIESLLEKVDILLLGGGMIFTFYKAQGYSVGSSLVEE 245
PLN03034 PLN03034
phosphoglycerate kinase; Provisional
1-220 7.13e-63

phosphoglycerate kinase; Provisional


Pssm-ID: 178602 [Multi-domain]  Cd Length: 481  Bit Score: 203.31  E-value: 7.13e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988   1 RIVGALPTIKYAQEKGAKaVVLMSHMGRPDGQpNAKYSLKIVADELEKQLNQKVIFANDCVGADVENTVNSAPKGAIVLL 80
Cdd:PLN03034  116 RIRAAIPTIKYLISNGAK-VILSSHLGRPKGV-TPKFSLAPLVPRLSELLGIQVVKADDCIGPEVEKLVASLPEGGVLLL 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1078194988  81 ENLRFHIEEEGSRKDeqgnkikadqaavdsFRQQLTKLGDVYVNDAFGTAHRAHSSVSGVK--LDTRAAGFLVKKELEYF 158
Cdd:PLN03034  194 ENVRFYKEEEKNEPE---------------FAKKLASLADLYVNDAFGTAHRAHASTEGVTkfLKPSVAGFLLQKELDYL 258
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1078194988 159 ARVLEAPERPFLAILGGAKVSDKIQLIDNMLEKVNSLIICGGMAYTFKKAEGVTIGDSLFDK 220
Cdd:PLN03034  259 VGAVSNPKRPFAAIVGGSKVSSKIGVIESLLEKCDILLLGGGMIFTFYKAQGLSVGSSLVEE 320
 
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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