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Conserved domains on  [gi|568948098|ref|XP_006541057|]
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ubiquitin-conjugating enzyme E2 variant 3 isoform X1 [Mus musculus]

Protein Classification

ubiquitin-conjugating enzyme E2 variant 3( domain architecture ID 10530350)

ubiquitin-conjugating enzyme E2 variant 3 (UEV-3) may be a negative regulator of polyubiquitination

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 183-359 4.84e-77

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05293:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 312  Bit Score: 240.20  E-value: 4.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLDIF----NLPNVEISKDLSASAHSKVVIFTANSLG 257
Cdd:cd05293    4 NKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGeAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAGARQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 258 GSESY-LHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVLKV 336
Cdd:cd05293   84 NEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAERLGV 163

                        170       180
                 ....*....|....*....|...
gi 568948098 337 QTSGKEVWVVGEQGENKVCSWSG 359
Cdd:cd05293  164 APSSVHGWIIGEHGDSSVPVWSG 186
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-138 3.69e-61

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


:

Pssm-ID: 399041  Cd Length: 119  Bit Score: 192.47  E-value: 3.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098   21 TVEELKNVSVSFPHFRYSVDTYVFKDTSQKDLLNFTGTIPVMYQGKTYNIPIRFWILDSHPFAPPICFLKPTANMEISVG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568948098  101 KHVDAKGRIYLPYLQNWSHPKSAIVGLIKEMIAKFQEE 138
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 183-359 4.84e-77

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of eukaryotic LDHs. Vertebrate LDHs are non-allosteric. This is in contrast to some bacterial LDHs that are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133429 [Multi-domain]  Cd Length: 312  Bit Score: 240.20  E-value: 4.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLDIF----NLPNVEISKDLSASAHSKVVIFTANSLG 257
Cdd:cd05293    4 NKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGeAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAGARQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 258 GSESY-LHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVLKV 336
Cdd:cd05293   84 NEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAERLGV 163

                        170       180
                 ....*....|....*....|...
gi 568948098 337 QTSGKEVWVVGEQGENKVCSWSG 359
Cdd:cd05293  164 APSSVHGWIIGEHGDSSVPVWSG 186
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-138 3.69e-61

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


Pssm-ID: 399041  Cd Length: 119  Bit Score: 192.47  E-value: 3.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098   21 TVEELKNVSVSFPHFRYSVDTYVFKDTSQKDLLNFTGTIPVMYQGKTYNIPIRFWILDSHPFAPPICFLKPTANMEISVG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568948098  101 KHVDAKGRIYLPYLQNWSHPKSAIVGLIKEMIAKFQEE 138
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-143 4.81e-54

ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467408  Cd Length: 126  Bit Score: 174.42  E-value: 4.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098  19 DLTVEELKNVSVSFPHFRYSVDTYVFKDTSQKDLLNFTGTIPVMYQGKTYNIPIRFWILDSHPFAPPICFLKPTANMEI- 97
Cdd:cd11685    1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIi 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568948098  98 SVGKHVDAKGRIYLPYLQNWSHPKSAIVGLIKEMIAKFQEELPLYS 143
Cdd:cd11685   81 KPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
PLN02602 PLN02602
lactate dehydrogenase
 177-358 3.17e-37

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 137.59  E-value: 3.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 177 HENKILNKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQGTMdLDIFN----LPNVEI--SKDLSASAHSKVVI 250
Cdd:PLN02602  32 SPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDVNPDKLRGEM-LDLQHaaafLPRTKIlaSTDYAVTAGSDLCI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 251 FTANSLGGS-ESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYI 329
Cdd:PLN02602 111 VTAGARQIPgESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFL 190

                        170       180
                 ....*....|....*....|....*....
gi 568948098 330 ITSVLKVQTSGKEVWVVGEQGENKVCSWS 358
Cdd:PLN02602 191 IADHLDVNAQDVQAYIVGEHGDSSVALWS 219
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 183-358 9.43e-23

Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439809 [Multi-domain]  Cd Length: 302  Bit Score: 97.01  E-value: 9.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQGT-MDLD---IFNLPNVEI-SKDLSASAHSKVVIFTA-NSL 256
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEaLDLAdafPLLGFDVKItAGDYEDLADADVVVITAgAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 257 GGSESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVLKV 336
Cdd:COG0039   81 KPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGV 160

                        170       180
                 ....*....|....*....|..
gi 568948098 337 QTSGKEVWVVGEQGENKVCSWS 358
Cdd:COG0039  161 SPRDVHAYVLGEHGDSMVPLWS 182
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 183-316 2.65e-16

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 395010 [Multi-domain]  Cd Length: 141  Bit Score: 74.95  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098  183 NKITVVG-SGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDL---DIFNLPNVEIS-KDLSASAHSKVVIFTAnsl 256
Cdd:pfam00056   1 VKVAVVGaAGGVGQSLAFLLANKGLADELVLYDIVKEKLEGvAMDLshgSTFLLVPGIVGgGDYEDLKDADVVVITA--- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568948098  257 gG-----SESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVG 316
Cdd:pfam00056  78 -GvprkpGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
 
Name Accession Description Interval E-value
LDH_1 cd05293
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 183-359 4.84e-77

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of eukaryotic LDHs. Vertebrate LDHs are non-allosteric. This is in contrast to some bacterial LDHs that are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133429 [Multi-domain]  Cd Length: 312  Bit Score: 240.20  E-value: 4.84e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLDIF----NLPNVEISKDLSASAHSKVVIFTANSLG 257
Cdd:cd05293    4 NKVTVVGVGQVGMACAISILAKGLADELVLVDVVEDKLKGeAMDLQHGsaflKNPKIEADKDYSVTANSKVVIVTAGARQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 258 GSESY-LHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVLKV 336
Cdd:cd05293   84 NEGESrLDLVQRNVDIFKGIIPKLVKYSPNAILLVVSNPVDIMTYVAWKLSGLPKHRVIGSGCNLDSARFRYLIAERLGV 163

                        170       180
                 ....*....|....*....|...
gi 568948098 337 QTSGKEVWVVGEQGENKVCSWSG 359
Cdd:cd05293  164 APSSVHGWIIGEHGDSSVPVWSG 186
UEV pfam05743
UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101) ...
 21-138 3.69e-61

UEV domain; This family includes the eukaryotic tumour susceptibility gene 101 protein (TSG101). Altered transcripts of this gene have been detected in sporadic breast cancers and many other human malignancies. However, the involvement of this gene in neoplastic transformation and tumorigenesis is still elusive. TSG101 is required for normal cell function of embryonic and adult tissues but that this gene is not a tumour suppressor for sporadic forms of breast cancer. This family is related to the ubiquitin conjugating enzymes.


Pssm-ID: 399041  Cd Length: 119  Bit Score: 192.47  E-value: 3.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098   21 TVEELKNVSVSFPHFRYSVDTYVFKDTSQKDLLNFTGTIPVMYQGKTYNIPIRFWILDSHPFAPPICFLKPTANMEISVG 100
Cdd:pfam05743   1 TFKDLVNVLRKFPNLKPRTDVYTFNDGSSKLLLNLYGTIPVTYKGNTYNIPILIWLPDTYPFSPPICYVKPTASMVIKVN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568948098  101 KHVDAKGRIYLPYLQNWSHPKSAIVGLIKEMIAKFQEE 138
Cdd:pfam05743  81 HHVDAQGRVYLPYLHNWNHPSSNLVDLVQELAQVFQED 118
UEV_TSG101-like cd11685
ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the ...
 19-143 4.81e-54

ubiquitin E2 variant (UEV) domain of TSG101 and related proteins; This subfamily includes the UEV domain of eukaryotic tumor susceptibility gene 101 protein (TSG101, also known as ESCRT-I complex subunit TSG101, vacuolar protein-sorting protein 23, or Vps23) which functions in endocytic trafficking. TSG101 is a component of the ESCRT (endosomal sorting complex required for transport)-I complex, one of four complexes (ESCRT 0, -I, -II, -III) in the vacuolar protein sorting pathway. TSG101 also facilitates HIV-1 virus budding from infected cells, perhaps by linking the p6 domain of the viral structural Gag protein to the vacuolar protein sorting machinery. The UEV domain of TSG101 binds to an essential tetrapeptide motif within the p6 domain of the structural Gag protein and also to ubiquitin. UEVs are homologous to E2 ubiquitin ligases but lack the conserved cysteine residue required for catalytic activity.


Pssm-ID: 467408  Cd Length: 126  Bit Score: 174.42  E-value: 4.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098  19 DLTVEELKNVSVSFPHFRYSVDTYVFKDTSQKDLLNFTGTIPVMYQGKTYNIPIRFWILDSHPFAPPICFLKPTANMEI- 97
Cdd:cd11685    1 DRVREDLLNLLQKYPSLKPKTDTFTFNDGSSKLLLCLTGTIPITYRGSTYNIPITIWLPETYPYSPPIVYVVPTPSMMIi 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568948098  98 SVGKHVDAKGRIYLPYLQNWSHPKSAIVGLIKEMIAKFQEELPLYS 143
Cdd:cd11685   81 KPHPHVDPNGRVYLPYLSEWNPPSSNLVDLVQELSAVFSEEPPVYS 126
PLN02602 PLN02602
lactate dehydrogenase
 177-358 3.17e-37

lactate dehydrogenase


Pssm-ID: 178212 [Multi-domain]  Cd Length: 350  Bit Score: 137.59  E-value: 3.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 177 HENKILNKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQGTMdLDIFN----LPNVEI--SKDLSASAHSKVVI 250
Cdd:PLN02602  32 SPTRRHTKVSVVGVGNVGMAIAQTILTQDLADELALVDVNPDKLRGEM-LDLQHaaafLPRTKIlaSTDYAVTAGSDLCI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 251 FTANSLGGS-ESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYI 329
Cdd:PLN02602 111 VTAGARQIPgESRLNLLQRNVALFRKIIPELAKYSPDTILLIVSNPVDVLTYVAWKLSGFPANRVIGSGTNLDSSRFRFL 190

                        170       180
                 ....*....|....*....|....*....
gi 568948098 330 ITSVLKVQTSGKEVWVVGEQGENKVCSWS 358
Cdd:PLN02602 191 IADHLDVNAQDVQAYIVGEHGDSSVALWS 219
LDH_like cd00300
L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent ...
 185-358 9.34e-31

L-lactate dehydrogenase-like enzymes; Members of this subfamily are tetrameric NAD-dependent 2-hydroxycarboxylate dehydrogenases including LDHs, L-2-hydroxyisocaproate dehydrogenases (L-HicDH), and LDH-like malate dehydrogenases (MDH). Dehydrogenases catalyze the conversion of carbonyl compounds to alcohols or amino acids. LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. L-HicDH catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133418 [Multi-domain]  Cd Length: 300  Bit Score: 118.91  E-value: 9.34e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 185 ITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLD----IFNLPNVEISKDLSASAHSKVVIFTA--NSLG 257
Cdd:cd00300    1 ITIIGAGNVGAAVAFALIAKGLASELVLVDVNEEKAKGdALDLShasaFLATGTIVRGGDYADAADADIVVITAgaPRKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 258 GsESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVLKVQ 337
Cdd:cd00300   81 G-ETRLDLINRNAPILRSVITNLKKYGPDAIILVVSNPVDILTYVAQKLSGLPKNRVIGSGTLLDSARFRSLLAEKLDVD 159

                        170       180
                 ....*....|....*....|.
gi 568948098 338 TSGKEVWVVGEQGENKVCSWS 358
Cdd:cd00300  160 PQSVHAYVLGEHGDSQVVAWS 180
LDH_2 cd05292
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 183-358 4.02e-25

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed predominantly of bacterial LDHs and a few fungal LDHs. Bacterial LDHs may be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133428 [Multi-domain]  Cd Length: 308  Bit Score: 103.72  E-value: 4.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLD---IFNLPNVEISKDLSASAHSKVVIFTAnslGG 258
Cdd:cd05292    1 MKVAIVGAGFVGSTTAYALLLRGLASEIVLVDINKAKAEGeAMDLAhgtPFVKPVRIYAGDYADCKGADVVVITA---GA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 259 S----ESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVL 334
Cdd:cd05292   78 NqkpgETRLDLLKRNVAIFKEIIPQILKYAPDAILLVVTNPVDVLTYVAYKLSGLPPNRVIGSGTVLDTARFRYLLGEHL 157

                        170       180
                 ....*....|....*....|....
gi 568948098 335 KVQTSGKEVWVVGEQGENKVCSWS 358
Cdd:cd05292  158 GVDPRSVHAYIIGEHGDSEVAVWS 181
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 183-358 9.43e-23

Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439809 [Multi-domain]  Cd Length: 302  Bit Score: 97.01  E-value: 9.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQGT-MDLD---IFNLPNVEI-SKDLSASAHSKVVIFTA-NSL 256
Cdd:COG0039    1 MKVAIIGAGNVGSTLAFRLASGGLADELVLIDINEGKAEGEaLDLAdafPLLGFDVKItAGDYEDLADADVVVITAgAPR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 257 GGSESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSVLKV 336
Cdd:COG0039   81 KPGMSRLDLLEANAKIFKSVGEAIKKYAPDAIVLVVTNPVDVMTYIAQKASGLPKERVIGMGTVLDSARFRSFLAEKLGV 160

                        170       180
                 ....*....|....*....|..
gi 568948098 337 QTSGKEVWVVGEQGENKVCSWS 358
Cdd:COG0039  161 SPRDVHAYVLGEHGDSMVPLWS 182
ldh PRK00066
L-lactate dehydrogenase; Reviewed
 179-358 3.28e-21

L-lactate dehydrogenase; Reviewed


Pssm-ID: 178836 [Multi-domain]  Cd Length: 315  Bit Score: 92.65  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 179 NKILNKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLD---IFNLPNVEISKDLSASAHSKVVIFTA- 253
Cdd:PRK00066   3 KKQHNKVVLVGDGAVGSSYAYALVNQGIADELVIIDINKEKAEGdAMDLShavPFTSPTKIYAGDYSDCKDADLVVITAg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 254 -NSLGGsESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITS 332
Cdd:PRK00066  83 aPQKPG-ETRLDLVEKNLKIFKSIVGEVMASGFDGIFLVASNPVDILTYATWKLSGFPKERVIGSGTSLDSARFRYMLSE 161

                        170       180
                 ....*....|....*....|....*.
gi 568948098 333 VLKVQTSGKEVWVVGEQGENKVCSWS 358
Cdd:PRK00066 162 KLDVDPRSVHAYIIGEHGDTEFPVWS 187
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
 183-358 8.97e-19

L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133427 [Multi-domain]  Cd Length: 306  Bit Score: 85.60  E-value: 8.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDLD--IFNLPN-VEISK-DLSASAHSKVVIFTA-NSL 256
Cdd:cd05291    1 RKVVIIGAGHVGSSFAYSLVNQGIADELVLIDINEEKAEGeALDLEdaLAFLPSpVKIKAgDYSDCKDADIVVITAgAPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 257 GGSESYLHAVQSNVDMFRALVPAL------GhysqhaVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYII 330
Cdd:cd05291   81 KPGETRLDLLEKNAKIMKSIVPKIkasgfdG------IFLVASNPVDVITYVVQKLSGLPKNRVIGTGTSLDTARLRRAL 154

                        170       180
                 ....*....|....*....|....*...
gi 568948098 331 TSVLKVQTSGKEVWVVGEQGENKVCSWS 358
Cdd:cd05291  155 AEKLNVDPRSVHAYVLGEHGDSQFVAWS 182
Ldh_1_N pfam00056
lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic ...
 183-316 2.65e-16

lactate/malate dehydrogenase, NAD binding domain; L-lactate dehydrogenases are metabolic enzymes which catalyze the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyze the interconversion of malate to oxaloacetate. The enzyme participates in the citric acid cycle. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. N-terminus (this family) is a Rossmann NAD-binding fold. C-terminus is an unusual alpha+beta fold.


Pssm-ID: 395010 [Multi-domain]  Cd Length: 141  Bit Score: 74.95  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098  183 NKITVVG-SGDLGIACTLAISAKGIADKLLLLDLSDGMSQG-TMDL---DIFNLPNVEIS-KDLSASAHSKVVIFTAnsl 256
Cdd:pfam00056   1 VKVAVVGaAGGVGQSLAFLLANKGLADELVLYDIVKEKLEGvAMDLshgSTFLLVPGIVGgGDYEDLKDADVVVITA--- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568948098  257 gG-----SESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVG 316
Cdd:pfam00056  78 -GvprkpGMTRLDLLNVNAKIFKSIGPALAKYAPNAIVLVVSNPVDILTYVAWKASGFPPNRVFG 141
PRK06223 PRK06223
malate dehydrogenase; Reviewed
 183-354 2.90e-16

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 78.63  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSdGMSQG-TMDL------DIFNLpNVEISKDLSASAHSKVVIFTAns 255
Cdd:PRK06223   3 KKISIIGAGNVGATLAHLLALKELGDVVLFDIVE-GVPQGkALDIaeaapvEGFDT-KITGTNDYEDIAGSDVVVITA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 256 lgGS-----ESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYII 330
Cdd:PRK06223  79 --GVprkpgMSRDDLLGINAKIMKDVAEGIKKYAPDAIVIVVTNPVDAMTYVALKESGFPKNRVIGMAGVLDSARFRTFI 156

                        170       180
                 ....*....|....*....|....*.
gi 568948098 331 TSVLKVqtSGKEV--WVVGEQGENKV 354
Cdd:PRK06223 157 AEELNV--SVKDVtaFVLGGHGDSMV 180
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
 185-354 1.85e-15

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 75.97  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 185 ITVVGSGDLGIACTLAISAKGIADKLLLLDLSdGMSQGtMDLDI--------FNlPNVEISKDLSASAHSKVVIFTANSL 256
Cdd:cd01339    1 ISIIGAGNVGATLAQLLALKELGDVVLLDIVE-GLPQG-KALDIsqaapilgSD-TKVTGTNDYEDIAGSDVVVITAGIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 257 ---GGSESYLhaVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSV 333
Cdd:cd01339   78 rkpGMSRDDL--LGTNAKIVKEVAENIKKYAPNAIVIVVTNPLDVMTYVAYKASGFPRNRVIGMAGVLDSARFRYFIAEE 155

                        170       180
                 ....*....|....*....|...
gi 568948098 334 LKVqtSGKEV--WVVGEQGENKV 354
Cdd:cd01339  156 LGV--SVKDVqaMVLGGHGDTMV 176
LDH-like_MDH_nadp cd05294
A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The ...
 233-354 2.79e-10

A lactate dehydrogenases-like structure with malate dehydrogenase enzymatic activity; The LDH-like MDH proteins have a lactate dehyhydrogenase-like (LDH-like) structure and malate dehydrogenase (MDH) enzymatic activity. This subgroup is composed of some archaeal LDH-like MDHs that prefer NADP(H) rather than NAD(H) as a cofactor. One member, MJ0490 from Methanococcus jannaschii, has been observed to form dimers and tetramers during crystalization, although it is believed to exist primarilly as a tetramer in solution. In addition to its MDH activity, MJ0490 also possesses fructose-1,6-bisphosphate-activated LDH activity. Members of this subgroup have a higher sequence similarity to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)- binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133430 [Multi-domain]  Cd Length: 309  Bit Score: 60.88  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 233 NVEISKDLSASAHSKVVIFTAN-SLGGSESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPA 311
Cdd:cd05294   60 EIKISSDLSDVAGSDIVIITAGvPRKEGMSRLDLAKKNAKIVKKYAKQIAEFAPDTKILVVTNPVDVMTYKALKESGFDK 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568948098 312 TRVVGIGCNLDSQRLQYIITSVLKVQTSGKEVWVVGEQGENKV 354
Cdd:cd05294  140 NRVFGLGTHLDSLRFKVAIAKHFNVHISEVHTRIIGEHGDSMV 182
LDH_3 cd05290
A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes ...
 184-359 1.26e-09

A subgroup of L-lactate dehydrogenases; L-lactate dehydrogenases (LDH) are tetrameric enzymes catalyzing the last step of glycolysis in which pyruvate is converted to L-lactate. This subgroup is composed of some bacterial LDHs from firmicutes, gammaproteobacteria, and actinobacteria. Vertebrate LDHs are non-allosteric, but some bacterial LDHs are activated by an allosteric effector such as fructose-1,6-bisphosphate. LDHs are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenase, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133426 [Multi-domain]  Cd Length: 307  Bit Score: 58.88  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 184 KITVVGSGDLGIACTLAISAKGIADKLLLLDLSDGMSQGTMdLD------IFNLPNVEI-SKDLSASAHSKVVIFTAN-S 255
Cdd:cd05290    1 KLVVIGAGHVGSAVLNYALALGLFSEIVLIDVNEGVAEGEA-LDfhhataLTYSTNTKIrAGDYDDCADADIIVITAGpS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 256 L--GGSESYLHAVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQYIITSv 333
Cdd:cd05290   80 IdpGNTDDRLDLAQTNAKIIREIMGNITKVTKEAVIILITNPLDIAVYIAATEFDYPANKVIGTGTMLDTARLRRIVAD- 158

                        170       180
                 ....*....|....*....|....*...
gi 568948098 334 lKVQTSGKEV--WVVGEQGENKVCSWSG 359
Cdd:cd05290  159 -KYGVDPKNVtgYVLGEHGSHAFPVWSL 185
PTZ00117 PTZ00117
malate dehydrogenase; Provisional
 184-354 3.94e-08

malate dehydrogenase; Provisional


Pssm-ID: 173409 [Multi-domain]  Cd Length: 319  Bit Score: 54.34  E-value: 3.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 184 KITVVGSGDLGIACTLAISAKGIADKLLLLDLSdGMSQG-TMDL-----------DIFNLPNVEISKDlsasahSKVVIF 251
Cdd:PTZ00117   7 KISMIGAGQIGSTVALLILQKNLGDVVLYDVIK-GVPQGkALDLkhfstlvgsniNILGTNNYEDIKD------SDVVVI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 252 TA---NSLGGSESYLHAVqsNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQY 328
Cdd:PTZ00117  80 TAgvqRKEEMTREDLLTI--NGKIMKSVAESVKKYCPNAFVICVTNPLDCMVKVFQEKSGIPSNKICGMAGVLDSSRFRC 157

                        170       180
                 ....*....|....*....|....*.
gi 568948098 329 IITSVLKVQTSGKEVWVVGEQGENKV 354
Cdd:PTZ00117 158 NLAEKLGVSPGDVSAVVIGGHGDLMV 183
PTZ00082 PTZ00082
L-lactate dehydrogenase; Provisional
 183-354 4.06e-08

L-lactate dehydrogenase; Provisional


Pssm-ID: 173376 [Multi-domain]  Cd Length: 321  Bit Score: 54.31  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 183 NKITVVGSGDLGIACTLAISAKGIADKLLLLDLSdGMSQGTMdLDIFNLP-------NVEISKDLSASAHSKVVIFTANS 255
Cdd:PTZ00082   7 RKISLIGSGNIGGVMAYLIVLKNLGDVVLFDIVK-NIPQGKA-LDISHSNviagsnsKVIGTNNYEDIAGSDVVIVTAGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568948098 256 LG--------GSESYLhaVQSNVDMFRALVPALGHYSQHAVLLVASQPVEIMSYVTWKLSTFPATRVVGIGCNLDSQRLQ 327
Cdd:PTZ00082  85 TKrpgksdkeWNRDDL--LPLNAKIMDEVAEGIKKYCPNAFVIVITNPLDVMVKLLQEHSGLPKNKVCGMAGVLDSSRLR 162

                        170       180
                 ....*....|....*....|....*..
gi 568948098 328 YIITSVLKVQTSGKEVWVVGEQGENKV 354
Cdd:PTZ00082 163 TYIAEKLGVNPRDVHASVIGAHGDKMV 189
 
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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