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Conserved domains on  [gi|862669336|ref|NP_001295025|]
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cytokine-like nuclear factor N-PAC isoform 2 [Homo sapiens]

Protein Classification

NAD(P)-dependent oxidoreductase; NAD(P)-binding domain-containing protein( domain architecture ID 11566665)

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase| NAD(P)-binding domain-containing protein may function as NAD(P)-dependent oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 268-545 1.11e-102

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 310.51  E-value: 1.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 268 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 341
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKaealvaAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 342 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 421
Cdd:COG2084   82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 422 GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDL 501
Cdd:COG2084  162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 862669336 502 RLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:COG2084  242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 6-90 1.77e-48

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


:

Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 162.77  E-value: 1.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   6 LRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKK-CFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVD 84
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKkMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                 ....*.
gi 862669336  85 AVEEFL 90
Cdd:cd05836   81 AIEEYI 86
DUF4603 super family cl21214
Domain of unknown function (DUF4603); This protein family is a domain of unknown function. In ...
 110-173 1.96e-03

Domain of unknown function (DUF4603); This protein family is a domain of unknown function. In particular, this domain lies at the C-terminal end of a protein found in eukaryotes.


The actual alignment was detected with superfamily member pfam15376:

Pssm-ID: 464684  Cd Length: 1293  Bit Score: 41.33  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   110 RRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRV---SSGSSERGS---------KSPLK------RAQEQSPRKR 171
Cdd:pfam15376  229 RRSKKEKENRFHNGAAEEKSAVHSKKQVRHRSEGKYRPrswSSGSSEAGSsssgnqgdmKTSIKfvkvrhKSREAVRNKK 308


                   ..
gi 862669336   172 GR 173
Cdd:pfam15376  309 GR 310
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 268-545 1.11e-102

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 310.51  E-value: 1.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 268 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 341
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKaealvaAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 342 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 421
Cdd:COG2084   82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 422 GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDL 501
Cdd:COG2084  162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 862669336 502 RLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:COG2084  242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 268-545 5.90e-52

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 179.09  E-value: 5.90e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 268 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAE------KEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 341
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEavaeviAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 342 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 421
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 422 GEV--GNAAKM--MLIVNMVqgsfMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYI 497
Cdd:PRK11559 163 GDIgaGNVTKLanQVIVALN----IAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLH 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 862669336 498 QKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:PRK11559 239 IKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 269-422 9.95e-49

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 165.72  E-value: 9.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  269 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPsGVL 342
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKveelvaAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  343 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 422
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 6-90 1.77e-48

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 162.77  E-value: 1.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   6 LRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKK-CFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVD 84
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKkMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                 ....*.
gi 862669336  85 AVEEFL 90
Cdd:cd05836   81 AIEEYI 86
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 269-545 3.81e-45

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 160.83  E-value: 3.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  269 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVL 342
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVadellaAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  343 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 422
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  423 EVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLR 502
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 862669336  503 LAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQAL 283
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 9-91 4.47e-23

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 93.26  E-value: 4.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336    9 GDLVWGKLGRYPPWPGKIVNPPKD----LKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKE-EMIKINKGK----RF 79
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELpenvLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEfEYLKKKKKKkkkkAF 80

                          90
                  ....*....|..
gi 862669336   80 QQAVDAVEEFLR 91
Cdd:pfam00855  81 KKALEEAEEALK 92
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 6-63 1.69e-15

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 70.84  E-value: 1.69e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 862669336     6 LRLGDLVWGKLGRYPPWPGKIVNPPKD---LKKPRGK-KCFFVKFFGTEDHAWIKVEQLKPY 63
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTpdnIMKRKSDeNLYPVLFFGDKDTAWIPSSKLFPL 62
DUF4603 pfam15376
Domain of unknown function (DUF4603); This protein family is a domain of unknown function. In ...
 110-173 1.96e-03

Domain of unknown function (DUF4603); This protein family is a domain of unknown function. In particular, this domain lies at the C-terminal end of a protein found in eukaryotes.


Pssm-ID: 464684  Cd Length: 1293  Bit Score: 41.33  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   110 RRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRV---SSGSSERGS---------KSPLK------RAQEQSPRKR 171
Cdd:pfam15376  229 RRSKKEKENRFHNGAAEEKSAVHSKKQVRHRSEGKYRPrswSSGSSEAGSsssgnqgdmKTSIKfvkvrhKSREAVRNKK 308


                   ..
gi 862669336   172 GR 173
Cdd:pfam15376  309 GR 310
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 210-333 2.91e-03

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 39.94  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 210 VKDAdphfhhFLLSQTEKPA------VCYQAIT--KKLKiceEET----GSTSI-QAADSTAVNGSITPTDKKIGFLGLG 276
Cdd:cd05213  117 VKNA------YKLAKEAGTSgkllnrLFQKAIKvgKRVR---TETgisrGAVSIsSAAVELAEKIFGNLKGKKVLVIGAG 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 862669336 277 LMGSGIVSNLLKMGHT-VTVWNRTAEKEGARLGRTPAEVVS---------TCDITFACVSDPKAAKD 333
Cdd:cd05213  188 EMGELAAKHLAAKGVAeITIANRTYERAEELAKELGGNAVPldellellnEADVVISATGAPHYAKI 254
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 268-545 1.11e-102

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 310.51  E-value: 1.11e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 268 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 341
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKaealvaAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 342 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 421
Cdd:COG2084   82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 422 GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDL 501
Cdd:COG2084  162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 862669336 502 RLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:COG2084  242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 268-545 5.90e-52

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 179.09  E-value: 5.90e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 268 KKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAE------KEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGV 341
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEavaeviAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 342 LQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFL 421
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 422 GEV--GNAAKM--MLIVNMVqgsfMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYI 497
Cdd:PRK11559 163 GDIgaGNVTKLanQVIVALN----IAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLH 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 862669336 498 QKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:PRK11559 239 IKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 269-422 9.95e-49

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 165.72  E-value: 9.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  269 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPsGVL 342
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKveelvaAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  343 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 422
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 6-90 1.77e-48

PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called 3-hydroxyisobutyrate dehydrogenase-like protein, cytokine-like nuclear factor N-PAC, nuclear protein NP60, or nuclear protein of 60 kDa, is a putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. It recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3). GLYR1 enhances the activity of MAP2K4 and MAP2K6 kinases to phosphorylate p38-alpha. In addition to the PWWP domain, GLYR1 also contains an AT-hook and a C-terminal NAD-binding domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438961 [Multi-domain]  Cd Length: 86  Bit Score: 162.77  E-value: 1.77e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   6 LRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKK-CFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVD 84
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKkMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                 ....*.
gi 862669336  85 AVEEFL 90
Cdd:cd05836   81 AIEEYI 86
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 269-545 3.81e-45

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 160.83  E-value: 3.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  269 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK------EGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVL 342
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVadellaAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  343 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 422
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  423 EVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLR 502
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 862669336  503 LAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQAL 283
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
269-542 3.79e-35

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 133.83  E-value: 3.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 269 KIGFLGLGLMGSGIVSNLLKMGHTVTVWN------RTAEKEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVL 342
Cdd:PRK15461   3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDvnpqavDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 343 QGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLG 422
Cdd:PRK15461  83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 423 EVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNqGQLASI--FLDQKCQNILQGNFKPDFYLKYIQKD 500
Cdd:PRK15461 163 GPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMS-GTAAGKghFTTTWPNKVLKGDLSPAFMIDLAHKD 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 862669336 501 LRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVY 542
Cdd:PRK15461 242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
269-544 1.95e-29

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 117.82  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 269 KIGFLGLGLMGSGIVSNLLKMGHT--VTVWNRTAE---KEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQ 343
Cdd:PRK15059   2 KLGFIGLGIMGTPMAINLARAGHQlhVTTIGPVADellSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 344 GIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGE 423
Cdd:PRK15059  82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 424 VGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRL 503
Cdd:PRK15059 162 NGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLNL 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 862669336 504 AIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRA 544
Cdd:PRK15059 242 ALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQA 282
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 9-89 1.47e-24

PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, is a small domain consisting of 100-150 amino acids and is composed of a five-stranded antiparallel beta-barrel followed by a helical region. It is found in numerous proteins that are involved in cell division, growth, and differentiation. Most PWWP-domain proteins seem to be nuclear, often DNA-binding, proteins that function as transcription factors regulating a variety of developmental processes. PWWP domains specifically recognize DNA and histone methylated lysines at the level of the nucleosome. Based on the fact that other regions of PWWP-domain proteins are responsible for nuclear localization and DNA-binding, is likely that the PWWP domain acts as a site for protein-protein binding interactions, influencing chromatin remodeling and thereby regulating transcriptional processes. Some PWWP-domain proteins have been linked to cancer or other diseases; some are known to function as growth factors.


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 97.57  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNP---PKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINK--GKRFQQAV 83
Cdd:cd05162    1 GDLVWAKLKGYPWWPARVVDPeelPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGFKKEFKKKKkkSKKFKKAV 80


                 ....*.
gi 862669336  84 DAVEEF 89
Cdd:cd05162   81 EEAEEA 86
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 425-545 2.32e-23

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 95.28  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  425 GNAAKMmlIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKC-QNILQGNFKPDFYLKYIQKDLRL 503
Cdd:pfam14833   3 GQAVKA--ANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFpQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 862669336  504 AIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 9-91 4.47e-23

PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain binds to Histone-4 methylated at lysine-20, H4K20me, suggesting that it is methyl-lysine recognition motif. Removal of two conserved aromatic residues in a hydrophobic cavity created by this domain within the full-length protein, Pdp1, abolishes the interaction o f the protein with H4K20me3. In fission yeast, Set9 is the sole enzyme that catalyzes all three states of H4K20me, and Set9-mediated H4K20me is required for efficient recruitment of checkpoint protein Crb2 to sites of DNA damage. The methylation of H4K20 is involved in a diverse array of cellular processes, such as organizing higher-order chromatin, maintaining genome stability, and regulating cell-cycle progression.


Pssm-ID: 459964 [Multi-domain]  Cd Length: 92  Bit Score: 93.26  E-value: 4.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336    9 GDLVWGKLGRYPPWPGKIVNPPKD----LKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKE-EMIKINKGK----RF 79
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEELpenvLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEfEYLKKKKKKkkkkAF 80

                          90
                  ....*....|..
gi 862669336   80 QQAVDAVEEFLR 91
Cdd:pfam00855  81 KKALEEAEEALK 92
PLN02858 PLN02858
fructose-bisphosphate aldolase
 266-545 2.87e-22

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 101.47  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  266 TDKKIGFLGLGLMGSGIVSNLLKMGHTVT---VWNRTA---EKEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPS 339
Cdd:PLN02858  323 PVKRIGFIGLGAMGFGMASHLLKSNFSVCgydVYKPTLvrfENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDL 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  340 GVLQGIRPGKCYVDMSTVDADTVTELAQVI--VSRGGRFLEAPVSGNQQLSNDGMLVILAAG-DRGLyEDCSSCFQAMGK 416
Cdd:PLN02858  403 GAVSALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGtDEAL-KSAGSVLSALSE 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  417 TSFFLGEVGNAAKMMLIVN-MVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLK 495
Cdd:PLN02858  482 KLYVIKGGCGAGSGVKMVNqLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALD 561

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 862669336  496 YIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:PLN02858  562 IFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVY 611
PLN02858 PLN02858
fructose-bisphosphate aldolase
 266-545 2.09e-19

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 92.61  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  266 TDKKIGFLGLGLMGSGIVSNLLKMGHTVTVW-------NRTAEKEGARLGrTPAEVVSTCDITFACVSDPKAAKDLVLGP 338
Cdd:PLN02858    3 SAGVVGFVGLDSLSFELASSLLRSGFKVQAFeistplmEKFCELGGHRCD-SPAEAAKDAAALVVVLSHPDQVDDVFFGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  339 SGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGR--FLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGK 416
Cdd:PLN02858   82 EGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  417 TSFFL-GEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLK 495
Cdd:PLN02858  162 KLYTFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLN 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 862669336  496 YIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAY 545
Cdd:PLN02858  242 VLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVW 291
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 9-88 6.78e-19

PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The HRP family includes hepatoma-derived growth factor (HDGF), and HDGF-related proteins (HRPs). HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It is a prognostic factor in several types of cancer. HDGFL1 is also called PWWP domain-containing protein 1 (PWWP1). Its biological function remains unclear. HDGFL2, also called HDGF-related protein 2 (HRP-2), or hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. HDGFL3, also called HDGF-related protein 3 (HRP-3), enhances DNA synthesis and may play a role in cell proliferation. The family also includes PC4 and SFRS1-interacting protein (PSIP) and similar proteins. PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Members of the HRP family contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438959 [Multi-domain]  Cd Length: 82  Bit Score: 81.06  E-value: 6.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKkcFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEE 88
Cdd:cd05834    4 GDLVFAKVKGYPPWPARIDEIPEGAKIPKNK--YPVFFYGTHETAFLKPKDLFPYEENKEKYGKPRKRKGFNEGLWEIEN 81
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 9-89 2.02e-16

second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the second PWWP domain. The family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438963 [Multi-domain]  Cd Length: 96  Bit Score: 74.58  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVN----PPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINK---GKRFQQ 81
Cdd:cd05838    3 GDIVWVKLGNYRWWPAEILHprevPDNIQSLPHPPGEFPVRFFGSHDYYWVHRGRVFLFEEGDKGSKEKSKkslDKSFKR 82


                 ....*....
gi 862669336  82 AV-DAVEEF 89
Cdd:cd05838   83 ALkEANEAF 91
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 6-63 1.69e-15

domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 70.84  E-value: 1.69e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 862669336     6 LRLGDLVWGKLGRYPPWPGKIVNPPKD---LKKPRGK-KCFFVKFFGTEDHAWIKVEQLKPY 63
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMTpdnIMKRKSDeNLYPVLFFGDKDTAWIPSSKLFPL 62
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 9-89 5.85e-13

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like protein ATX3, ATX4, ATX5, and similar proteins; The family includes A. thaliana ATX3 (also called protein SET domain group 14, or trithorax-homolog protein 3), ATX4 (also called protein SET domain group 16, or trithorax-homolog protein 4) and ATX5 (also called protein SET domain group 29, or trithorax-homolog protein 5), which belong to the histone-lysine methyltransferase family. They show distinct phylogenetic origins from the family of ATX1 and ATX2. They are multi-domain containing protein that consists of an N-terminal PWWP domain, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438971 [Multi-domain]  Cd Length: 100  Bit Score: 65.08  E-value: 5.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNP---PKDLKKPRGKKCFFVKFFGTE---DHAWIKVEQLKPY----HAHKEEMIKINKG-K 77
Cdd:cd20143    3 GDLVWAKVGTHPFWPARVVEPaeqAEEVRRRCVPGSLCVYFFGPGgsrDYGWVRRSMIFPFtddlARFQTQKIKNKKRpQ 82

                         90
                 ....*....|....*.
gi 862669336  78 RFQQAVD----AVEEF 89
Cdd:cd20143   83 EFQEALEeaklADAGF 98
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 7-93 2.75e-12

PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family includes DNMT3A and DNMT3B, which are required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, may preferentially methylate nucleosomal DNA within the nucleosome core region. DNMT3B may function as a transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Members of this family contains a PWWP domain that is responsible for establishing DNA methylation patterns during embryogenesis and gametogenesis. In tumorigenesis, DNA methylation by DNMT3B is known to play a role in the inactivation of tumor suppressor genes. In addition, a point mutation in the PWWP domain of DNMT3B has been identified in patients with ICF (immunodeficiency, centromeric instability, and facial anomalie) syndrome , a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438960 [Multi-domain]  Cd Length: 89  Bit Score: 62.66  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   7 RLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGteDHAW--IKVEQLKPYHAHKEEMIKI-NKGKRFQQAV 83
Cdd:cd05835    1 KIGDLVWAKLKGSPWWPGIVVSHKDCGQKPPAEGSVWVFWFG--DHKVseVPLDKILPFAEFFNKFYISkNSSKLYKKAV 78

                         90
                 ....*....|.
gi 862669336  84 D-AVEEFLRRA 93
Cdd:cd05835   79 YeALKEAAERS 89
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 7-94 9.74e-11

PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like proteins ATX1, ATX2, and similar proteins; This family includes A. thaliana ATX1 and ATX2, which are sister paralogs originating from a segmental chromosomal duplication. They are plant counterparts of the Drosophila melanogaster trithorax (TRX) and mammalian mixed-lineage leukemia (MLL1) proteins. ATX1, also called protein SET domain group 27, or trithorax-homolog protein 1 (TRX-homolog protein 1), is a methyltransferase that trimethylates histone H3 at lysine 4 (H3K4me3). It also acts as a histone modifier and as a positive effector of gene expression. ATX1 regulates transcription from diverse classes of genes implicated in biotic and abiotic stress responses. It is involved in dehydration stress signaling in both abscisic acid (ABA)-dependent and ABA-independent pathways. ATX2, also called protein SET domain group 30, or trithorax-homolog protein 2 (TRX-homolog protein 2), is involved in dimethylating histone H3 at lysine 4 (H3K4me2). Both ATX1 and ATX2 are multi-domain containing proteins that consist of an N-terminal PWWP domain, FYRN- and FYRC (DAST, domain associated with SET in trithorax) domains, a canonical plant homeodomain (PHD) domain, a non-canonical extended PHD (ePHD) domain, and a C-terminal SET domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438970 [Multi-domain]  Cd Length: 97  Bit Score: 58.52  E-value: 9.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   7 RLGDLVWGKLGRYPPWPGKIVN---------PPKDLKKPRGkkcFFVKFFGTEDHAWIKVEQL--------KPYHAHKee 69
Cdd:cd20142    1 SPGDVVWAKVKGYPMWPALVIDeehaercglEANRPGKKGT---VPVQFFGTYEVARLNPKKVvgfskgldLKYHSKC-- 75

                         90       100
                 ....*....|....*....|....*
gi 862669336  70 mikinKGKRFQQAVDAVEEFLRRAK 94
Cdd:cd20142   76 -----KAPVFRQALEEAERYLKEGK 95
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 7-87 1.81e-10

PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility group protein 1-like 2 (HMG-1L2), is a heparin-binding protein that acts as a transcriptional repressor with mitogenic activity for fibroblasts. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438976 [Multi-domain]  Cd Length: 87  Bit Score: 57.34  E-value: 1.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   7 RLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKcFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAV 86
Cdd:cd20148    2 KCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANK-YQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEI 80


                 .
gi 862669336  87 E 87
Cdd:cd20148   81 E 81
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
 8-87 2.03e-10

PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called G/T mismatch-binding protein (GTBP or GTMBP), MutS protein homolog 6, or MutS-alpha 160 kDa subunit (p160), is a mismatch repair protein homologous to bacterial MutS. It is a component of the post-replicative DNA mismatch repair system (MMR). It heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, it forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Mutations in MSH6 have been linked to increased cancer susceptibility, particularly in hereditary nonpolyposis colorectal cancer in humans. MSH6 contains a PWWP domain, but its role in MSH6 remains unclear. MSH6 orthologs found in Saccharomyces cerevisiae, Caenorhabditis elegans, and Arabidopsis thaliana lack the PWWP domain. PWWP domains typically recognize DNA and histone methylated lysines.


Pssm-ID: 438962  Cd Length: 103  Bit Score: 57.68  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   8 LGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKC--FFVKFFG-TEDHAWIKVEQLKPY------HAHKEEMIKINKGKR 78
Cdd:cd05837    3 PGDLVWAKLEGYPWWPSLVCNHPTTGFHKKFGKKgeVHVQFFDdPPSRAWVKAKNVKPFtgsddkEFQKGGMFFSKDPKW 82

                         90
                 ....*....|..
gi 862669336  79 ---FQQAVDAVE 87
Cdd:cd05837   83 kkaVKEADKALK 94
PWWP_HDGFL3 cd20150
PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also ...
 7-87 2.36e-10

PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also called HDGF-related protein 3 (HRP-3), is the only hepatoma-derived growth factor (HDGF)-related protein (HRP) family member whose expression is almost restricted to the nervous tissue. It enhances DNA synthesis and may play a role in cell proliferation. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438978 [Multi-domain]  Cd Length: 93  Bit Score: 57.38  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   7 RLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKcFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAV 86
Cdd:cd20150    7 KAGDLVFAKMKGYPHWPARIDELPEGAVKPPANK-YPIFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEGLWEI 85


                 .
gi 862669336  87 E 87
Cdd:cd20150   86 E 86
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 9-88 4.89e-10

PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar proteins; ScIOC4 functions as a component of the ISW1B complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. The ISW1B complex acts within coding regions to control the amount of RNA polymerase II released into productive elongation and to coordinate elongation with termination and pre-mRNA processing. The family also includes Schizosaccharomyces pombe PWWP domain-containing proteins 1 and 2 (SpPDP1 and SpPDP2). SpPDP1 associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. Members of this family contain a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438965  Cd Length: 94  Bit Score: 56.54  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNP---------PKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYhahKEEMIK--INKGK 77
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEellpknvlkAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPL---TKEEIDkfLSKSK 77

                         90
                 ....*....|..
gi 862669336  78 RFQQA-VDAVEE 88
Cdd:cd05840   78 RKNKDlIEAYEV 89
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 9-88 9.11e-10

PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is a methyl-CpG-binding protein that binds to heterochromatin. It does not interact with either methylated or unmethylated DNA. MBD5 acts as a transcriptional regulator responsible for 2q23.1 deletion syndrome. It belongs to the MBD family proteins, which play central roles in transcriptional regulation and development. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438969  Cd Length: 92  Bit Score: 55.79  E-value: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKkcFFVKFFGTEDHAWIKVEQLKPY------HaHKEEMIKINKGKR---F 79
Cdd:cd20141    4 GDLVWGQIRGFPSWPGKLVSENDVGKTNEGK--VWVSWFGDHSFGQVEPDKLKTLsegleaH-HRARKRTRKGRKLnnhL 80

                         90
                 ....*....|
gi 862669336  80 QQAV-DAVEE 88
Cdd:cd20141   81 EAAIqEAMSE 90
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 9-95 1.73e-09

PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family includes HUA2-like proteins 1-3 (HULK1-3), which are probable transcription factors that act with partial redundancy with each other. They may play diverse and essential roles in the control of plant development, physiology and flowering time. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438975 [Multi-domain]  Cd Length: 92  Bit Score: 54.80  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKiVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPY-----HAHKEEMIKINKGKRFQQAV 83
Cdd:cd20147    1 GDLVLAKVKGFPAWPAQ-VSEPEDWGSAPDPKKVFVHFFGTQQIGFCNPGELSEFteeikQSLLARTLKKKKGSDFSRAV 79

                         90
                 ....*....|..
gi 862669336  84 DAVEEFLRRAKG 95
Cdd:cd20147   80 KEICELYEERKG 91
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
 9-87 1.91e-09

PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called CLL-associated antigen KW-7, dense fine speckles 70 kDa protein (DFS 70), lens epithelium-derived growth factor (LEDGF), or transcriptional coactivator p75/p52, acts as a transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438979 [Multi-domain]  Cd Length: 88  Bit Score: 54.60  E-value: 1.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKcFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVE 87
Cdd:cd20151    4 GDLIFAKMKGYPHWPARVDEVPDGAVKPPTNK-LPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEID 81
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 8-83 2.31e-09

first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein family consists of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1 that are critical in maintaining the chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising in suppressing cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and play nonredundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). This model corresponds to the first PWWP domain. This family also includes Drosophila melanogaster maternal-effect sterile 4 (dMes4) that may act as a histone-lysine N-methyltransferase required for wing morphogenesis. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438972  Cd Length: 114  Bit Score: 55.01  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   8 LGDLVWGKLGRYPPWPGKIVNPPK-DL---KKPRGKKC---FFVKFFGTED-HAWIKVEQLKPYH------AHKEEMIK- 72
Cdd:cd20144    1 VGDLVWAKVSGHPWWPCMVTYDPEsGLytkIKGSGGRTyrqYHVQFFGDNGeRGWVSEKSLMPFEgkekfeELVKELKKk 80

                         90
                 ....*....|..
gi 862669336  73 -INKGKRFQQAV 83
Cdd:cd20144   81 aKKKSKKAKLEK 92
PWWP_ZCWPW2 cd20146
PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ...
 6-88 6.21e-09

PWWP domain found in zinc finger CW-type PWWP domain protein 2 (ZCWPW2) and similar proteins; ZCWPW2 is a histone H3K4me3 reader. In addition to the PWWP domain, ZCWPW2 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438974  Cd Length: 113  Bit Score: 53.84  E-value: 6.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   6 LRLGDLVWGKLGRYPPWPGKIVNPPKDlkkprGKKCFF----------VKFFGTE-DHAWIKVEQLKPYHAH-KEEMIKI 73
Cdd:cd20146    9 LPLGSLVWAKMTGYPRWPAILTPDPIC-----GEYVDYdedgevekyhVEFLGKPhSHAWISAKSVEPYNSNtKTPKCKT 83

                         90
                 ....*....|....*.
gi 862669336  74 NKGKRFQQAVD-AVEE 88
Cdd:cd20146   84 KKSKKRKKSYEsALEE 99
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 6-87 1.17e-08

PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also called HDGF-related protein 2 (HRP-2), or Hepatoma-derived growth factor 2 (HDGF-2), is involved in cellular growth control, through the regulation of cyclin D1 expression. It contains a PWWP domain, which is necessary for DNA binding.


Pssm-ID: 438977 [Multi-domain]  Cd Length: 84  Bit Score: 52.21  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   6 LRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCfFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDA 85
Cdd:cd20149    1 FKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKY-PIFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKRKGFNEGLWE 79


                 ..
gi 862669336  86 VE 87
Cdd:cd20149   80 IQ 81
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
 7-68 9.19e-08

first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438991  Cd Length: 130  Bit Score: 51.09  E-value: 9.19e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 862669336   7 RLGDLVWGKLGRYPPWPGKIVNPPK----DLKKPRGKKCFFVKFFGTE-DHAWIKVEQLKPYHAHKE 68
Cdd:cd20163    2 QVGDLVWSKVGTYPWWPCMVSSDPQlevhTKINTRGAREYHVQFFSSQpERAWVHEKRVREYKGHKQ 68
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
 9-88 1.42e-07

PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ZCWPW1 is a histone H3K4me3 reader. It is associated with late-onset Alzheimer's disease (LOAD). In addition to the PWWP domain, ZCWPW1 contains a zinc finger CW (zf-CW) domain that is a histone modification reader for the histone H3 tail with trimethylated K4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438973  Cd Length: 115  Bit Score: 49.86  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNPPkdlkkprGKKCFF-------------VKFFGTE-DHAWIKVEQLKPY--HAHKEEMIK 72
Cdd:cd20145    9 GSLVWAKMPGYPWWPAMVEDDP-------DTEEFFwldeesdiptkyhVTFFDKPvSRAWVRASSIKPFtdNSNEPNLTK 81

                         90
                 ....*....|....*.
gi 862669336  73 INKGKRFQQAVDAVEE 88
Cdd:cd20145   82 KKGKKYKKRLNEAVEM 97
PWWP_NSD1_rpt2 cd20164
second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...
 10-88 1.81e-07

second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1, also called H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, androgen receptor coactivator 267 kDa protein, androgen receptor-associated protein of 267 kDa, H3-K36-HMTase H4-K20-HMTase, Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438992  Cd Length: 96  Bit Score: 49.10  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  10 DLVWGKLGRYPPWPGKIVNP---PKDLKKPR---GKkcFFVKFFGTEDHAWIKVEQLKPYH----AHKEEMIKINKG--- 76
Cdd:cd20164    4 EVVWVKVGRYRWWPAEVCHPksiPTNIQKMKhdiGE--FPVLFFGSNDYLWTHQARVFPYMegdvSSKDKMGKGVDGtyk 81

                         90
                 ....*....|..
gi 862669336  77 KRFQQAVDAVEE 88
Cdd:cd20164   82 KALQEAAVRFEE 93
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
 6-83 6.66e-07

PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family includes PWWP2A and its paralog PWWP2B. PWWP2A is a H2A.Z-specific chromatin binding protein which may play an important role in the neural crest stem cell migration and differentiation during early development. It is also required for proper mitosis progression. PWWP2A and PWWP2B form a stable complex with NuRD subunits MTA1/2/3:HDAC1/2:RBBP4/7, but not with MBD2/3, p66alpha/beta, and CHD3/4. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438968  Cd Length: 92  Bit Score: 47.64  E-value: 6.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   6 LRLGDLVWGKLGRYPPWPGKIV------NPPKDLKKPRGKkcffVKFFGTEDHAWIKVEQLKPYhahkEEMIKI--NKGK 77
Cdd:cd20140    4 LRVGDIVWGKIHGFPWWPGRILsitvsrDDNGELSTQEAH----VSWFGSSTTSYMPCSQLYPF----LEDFKLryNKKK 75


                 ....*...
gi 862669336  78 R--FQQAV 83
Cdd:cd20140   76 RgpYKEAV 83
PWWP_BS69 cd20159
PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger ...
 10-91 7.86e-07

PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438987  Cd Length: 85  Bit Score: 47.20  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  10 DLVWGKLGRYPPWPGKIVnppkdlkKPRGKKCfFVKFFG-TEDHAWIKVEQLKPYHAHKeEMIKINKGKRFQQAVDAVEE 88
Cdd:cd20159    8 ELVWAKQKGFPYWPAKVI-------QKEDNQY-DVRFFGgHHQRAWIPKENIKPITTSP-KQLKVKRTAGWNKACEELKK 78


                 ...
gi 862669336  89 FLR 91
Cdd:cd20159   79 HQE 81
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 266-347 1.01e-06

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 50.45  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 266 TDKKIGFLGLGLMGSGIVSNLLKMGHT---VTVWNRTAEK-------EGARLGRTPAEVVSTCDITFACVsDPKAAKDlv 335
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERlealaerYGVRVTTDNAEAAAQADVVVLAV-KPQDLAE-- 77

                         90
                 ....*....|..
gi 862669336 336 lgpsgVLQGIRP 347
Cdd:COG0345   78 -----VLEELAP 84
PWWP_NSD3_rpt2 cd20166
second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...
 10-81 1.24e-06

second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; NSD3, also called histone-lysine N-methyltransferase NSD3, protein whistle, WHSC1-like 1 isoform 9 with methyltransferase activity to lysine, or Wolf-Hirschhorn syndrome candidate 1-like protein 1 (WHSC1-like protein 1, or WHSC1L1), is a lysine methyltransferase encoded by gene NSD3, which is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD3 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, five plant-homeodomain (PHD) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438994  Cd Length: 95  Bit Score: 46.89  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  10 DLVWGKLGRYPPWPGKIVNPP------KDLKKPRGKkcFFVKFFGTEDHAWIKVEQLKPY----HAHKEEMIKINK---- 75
Cdd:cd20166    4 QIVWVKLGNYRWWPAEICNPRsvplniQGLKHDIGD--FPVFFFGSHDYYWVHQGRVFPYvegdKSFAEGQTSINKtfkk 81

                         90
                 ....*....|.
gi 862669336  76 -----GKRFQQ 81
Cdd:cd20166   82 aleeaAKRFQE 92
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
269-316 1.42e-06

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 50.13  E-value: 1.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 862669336 269 KIGFLGLGLMGSGIVSNLLKMGHTVTVWNR------TAEKEGARLGRTPAEVVS 316
Cdd:PRK09599   2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRnpeaveALAEEGATGADSLEELVA 55
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
 4-63 1.59e-06

first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and similar proteins; NSD1, also called H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, androgen receptor coactivator 267 kDa protein, androgen receptor-associated protein of 267 kDa, H3-K36-HMTase H4-K20-HMTase, Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD domains are involved in protein-protein interactions. The model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438989  Cd Length: 116  Bit Score: 47.08  E-value: 1.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 862669336   4 VSLRLGDLVWGKLGRYPPWPGKIVNPP-----KDLKKPRGKKC--FFVKFFGT-EDHAWIKVEQLKPY 63
Cdd:cd20161    2 VKYEVGDLVWAKFSRRPWWPCRICADPlldthSKMKVPSRRPCrqYYVETLGElTEKAWVAAKAVVPF 69
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 9-54 2.75e-06

PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF family of proteins includes BRPF1, BRD1/BRPF2, and BRPF3. They are scaffold proteins that form monocytic leukemic zinc-finger protein (MOZ)/MOZ-related factor (MORF) H3 histone acetyltransferase (HAT) complexes with other regulatory subunits, such as inhibitor of growth 5 (ING5) and Esa1-associated factor 6 ortholog (EAF6). BRPF proteins have multiple domains, including a plant homeodomain (PHD) zinc finger followed by a non-canonical extended PHD (ePHD) finger, C2HC5HC2H, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PHD finger binds to lysine 4 of histone H3 (K4H3), the bromodomain interacts with acetylated lysines on N-terminal tails of histones and other proteins, and the PWWP domain shows histone-binding and chromatin association properties.


Pssm-ID: 438964  Cd Length: 106  Bit Score: 46.11  E-value: 2.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPGKIVNP--------------PKDLKKPRGKKCFFVKFFGTEdHAW 54
Cdd:cd05839    4 GDLVWAKCRGYPWYPAEIVDPkdpkegngvpipvpPDRVLKKSNEKLYLVLFFDAK-RTW 62
PWWP_NSD2_rpt2 cd20165
second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...
 7-81 3.91e-06

second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, an high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the second PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438993  Cd Length: 96  Bit Score: 45.33  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   7 RLGDLVWGKLGRYPPWPGKIVNP---PKDLKKPR---GKkcFFVKFFGTEDHAWIKVEQLKPYhahkeemIKINKGKRFQ 80
Cdd:cd20165    1 RFQDIIWVKLGNYRWWPAEVCHPknvPPNIQKMKheiGE--FPVFFFGSKDYYWTHQARVFPY-------MEGDRGSKYQ 71


                 .
gi 862669336  81 Q 81
Cdd:cd20165   72 G 72
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 9-92 4.28e-06

PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, also called PWWP domain-containing DNA repair factor 3A (PWWP3A), or protein expandere (EXPAND1), is a melanoma-associated antigen (MAA) that belongs to the mutated or aberrantly expressed type of MAAs, along with antigens such as CDK4, beta-catenin, gp100-in4, p15, and N-acetylglucosaminyltransferase V. It is highly expressed in several types of human cancers and involved in the DNA damage response pathway by contributing to the maintenance of chromatin architecture. MUM-1 is recruited to the vicinity of DNA breaks by TP53BP1 and plays an accessory role to facilitate damage-induced chromatin changes and promoting chromatin relaxation. It is required for efficient DNA repair and cell survival following DNA damage. This subfamily also includes mutated melanoma-associated antigen 1-like protein 1 (MUM1L1), also called MUM1-like protein 1, or PWWP domain-containing DNA repair factor 3B (PWWP3B). Its biological function remains unclear. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438967  Cd Length: 90  Bit Score: 44.94  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   9 GDLVWGKLGRYPPWPG---KIVNPPKDLK-----KPRGKKCFFVKFFgtedhawikveQLKPYHAH-KEEMIKINK---- 75
Cdd:cd06080    4 GDIVWAKYRKYPYWPAvvkSVYKKPKKASvlfleLPPEKKGIKVSLK-----------KLKPFDCKeKEELLEEGKespy 72

                         90
                 ....*....|....*..
gi 862669336  76 GKRFQQAVDAVEEFLRR 92
Cdd:cd06080   73 SEDFKEAVELAEDYLIK 89
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
270-344 7.24e-06

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 47.09  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 270 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK---------EGARlGRTPAEVVSTCDITFACVsDPKAAKDLVLGPSG 340
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKaaalaaelgPGAR-AGTNAEAAAAADVVVLAV-PYEAVPDVLESLGD 78


                 ....
gi 862669336 341 VLQG 344
Cdd:COG2085   79 ALAG 82
PRK07680 PRK07680
late competence protein ComER; Validated
 269-347 1.54e-05

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 46.89  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 269 KIGFLGLGLMG-----SGIVSNLLKMGHtVTVWNRTAEK--------EGARLGRTPAEVVSTCDITFACVsdpkaaKDLV 335
Cdd:PRK07680   2 NIGFIGTGNMGtilieAFLESGAVKPSQ-LTITNRTPAKayhikeryPGIHVAKTIEEVISQSDLIFICV------KPLD 74

                         90
                 ....*....|..
gi 862669336 336 LGPsgVLQGIRP 347
Cdd:PRK07680  75 IYP--LLQKLAP 84
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
 11-92 3.35e-05

PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a plant homeodomain (PHD) finger, a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438988  Cd Length: 91  Bit Score: 42.55  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  11 LVWGKLGRYPPWPGK---IVNPPKDlkkprgkkcffVKFFGTEDHAWIKVEQLKPYhahKEEM---IKINKGKrFQQAVD 84
Cdd:cd20160    9 LVWAKLKGFPFWPAKalrVNNGQVD-----------VRFFGAHDRAWVPVKDCYLY---SKEPptsVKKKKSG-LDEAME 73


                 ....*...
gi 862669336  85 AVEEFLRR 92
Cdd:cd20160   74 ELEIHIEK 81
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 270-302 5.55e-05

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 45.83  E-value: 5.55e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 862669336 270 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK 302
Cdd:COG0362    5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEK 37
PWWP_BS69-like cd05841
PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...
 11-58 2.76e-04

PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; Protein BS69, also called zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. BS69 is a multi-domain protein, containing bromo, plant homeodomain (PHD), proline-tryptophan-tryptophan-proline (PWWP), and MYeloid translocation protein 8, Nervy and DEAF-1 (MYND) domains. The specific role of the PWWP domain within BS69 is not clearly identified, but BS69 functions in chromatin remodeling, consistent with other PWWP-containing proteins. PRKCBP1, also called cutaneous T-cell lymphoma-associated antigen se14-3 (CTCL-associated antigen se14-3), Rack7, or zinc finger MYND domain-containing protein 8 (ZMYND8), is a novel receptor for activated C-kinase (RACK)-like protein that may play an important role in the activation and regulation of PKC-beta I, and the PKC signaling cascade. It also has been identified as a formin homology-2-domain containing protein 1 (FHOD1)-binding protein that may be involved in FHOD1-regulated actin polymerization and transcription. Moreover, PRKCBP1 may function as a REST co-repressor 2 (RCOR2) interacting factor. They form a RCOR2/ZMYND8 complex which might be involved in the regulation of neural differentiation. PRKCBP1 contains a PHD finger, a bromodomain, and a PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438966  Cd Length: 89  Bit Score: 40.07  E-value: 2.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 862669336  11 LVWGKLGRYPPWPGKIVNPPKDLkkprgkkcFFVKFFGTEDHAWIKVE 58
Cdd:cd05841    9 LVWVKLDGFPFWPAKVMGTKDGQ--------VDVRFFGDYDRAWLPSK 48
PWWP_DNMT3A cd20154
PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA ...
 8-62 3.52e-04

PWWP domain found in DNA (cytosine-5)-methyltransferase 3A (DNMT3A); DNMT3A, also called DNA methyltransferase HsaIIIA, DNA MTase HsaIIIA, or M.HsaIIIA, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It modifies DNA in a non-processive manner and also methylates non-CpG sites. It may preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. DNMT3A is recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. It contains a PWWP domain that binds methylated histone.


Pssm-ID: 438982  Cd Length: 134  Bit Score: 40.72  E-value: 3.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 862669336   8 LGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKP 62
Cdd:cd20154    8 IGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMP 62
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 270-302 4.64e-04

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 42.85  E-value: 4.64e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 862669336 270 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEK 302
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEK 36
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
 8-68 8.49e-04

first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; NSD2, also called histone-lysine N-methyltransferase NSD2, multiple myeloma SET domain-containing protein (MMSET), or protein trithorax-5 Wolf-Hirschhorn syndrome candidate 1 protein (WHSC1), is overexpressed frequently in the t(4;14) translocation in 15% to 20% of multiple myeloma. It plays important roles in cancer cell proliferation, survival, and tumor growth, through mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. It also enhances androgen receptor (AR)-mediated transcription. The principal chromatin-regulatory activity of NSD2 is dimethylation of histone H3 at lysine 36 (H3K36me2). NSD2 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-prolin motif (PWWP) domains, a high mobility group (HMG) box, five PHD (plant-homeodomain) zinc finger motifs, and an NSD-specific Cys-His rich domain (C5HCH). The SET domain is responsible for histone methyltransferase activity. The PWWP, HMG, and PHD domains mediate chromatin interaction and recognition of histone marks. This model corresponds to the first PWWP domain. The PWWP domain specifically recognizes DNA and histone methylated lysines.


Pssm-ID: 438990  Cd Length: 128  Bit Score: 39.51  E-value: 8.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 862669336   8 LGDLVWGKLGRYPPWPGKIVNPP--KDLKKPRGKKCFF----VKFFG-TEDHAWIKVEQLKPYHAHKE 68
Cdd:cd20162    3 VGDLVWSKVSGYPWWPCMVSADPllHSHTKLKGQKKSArqyhVQFFGdAPERAWIFEKSLVPFEGEGQ 70
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 269-404 1.16e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 40.95  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 269 KIGFLGLGLMGSGIVSNLLKMGHTVT-VWNRT---AEKEGARLGRTPA----EVVSTCDITFACVSD---PKAAKDLVLG 337
Cdd:COG5495    5 KIGIIGAGRVGTALAAALRAAGHEVVgVYSRSpasAERAAALLGAVPAldleELAAEADLVLLAVPDdaiAEVAAGLAAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 338 ----------------PSGVLQ-----GIRPGKCYVDMS-TVDADTVTELAQVIVsrggrFLEAPVSGNQQLSN-----D 390
Cdd:COG5495   85 galrpgqlvvhtsgalGSDVLApaaraGALTGSFHPLQTfSGPREDLERLAGIPF-----AIEGDEEALPVLEAlaealG 159

                        170
                 ....*....|....
gi 862669336 391 GMLVILAAGDRGLY 404
Cdd:COG5495  160 GEPFVIDSEQRPLY 173
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
271-355 1.57e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 37.98  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336  271 GFLGLGLMGSGIVSNLLKMG-HTVTVWNR--------TAEKEGARL-GRTPAEVVSTCDITFACVSdPKAAKDLVlgpsG 340
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANSrnpekaeeLAEEYGVGAtAVDNEEAAEEADVVFLAVK-PEDAPDVL----S 75

                          90
                  ....*....|....*
gi 862669336  341 VLQGIRPGKCYVDMS 355
Cdd:pfam03807  76 ELSDLLKGKIVISIA 90
DUF4603 pfam15376
Domain of unknown function (DUF4603); This protein family is a domain of unknown function. In ...
 110-173 1.96e-03

Domain of unknown function (DUF4603); This protein family is a domain of unknown function. In particular, this domain lies at the C-terminal end of a protein found in eukaryotes.


Pssm-ID: 464684  Cd Length: 1293  Bit Score: 41.33  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336   110 RRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRV---SSGSSERGS---------KSPLK------RAQEQSPRKR 171
Cdd:pfam15376  229 RRSKKEKENRFHNGAAEEKSAVHSKKQVRHRSEGKYRPrswSSGSSEAGSsssgnqgdmKTSIKfvkvrhKSREAVRNKK 308


                   ..
gi 862669336   172 GR 173
Cdd:pfam15376  309 GR 310
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 270-336 2.53e-03

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 38.37  E-value: 2.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 862669336  270 IGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAE-----KEGARLGRTPAEVVSTCDITFACVSDPKAAkDLVL 336
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAElaaikKNGLRLTSPGGERIVPPPAVTSASESLGPI-DLVI 71
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 210-333 2.91e-03

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 39.94  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 210 VKDAdphfhhFLLSQTEKPA------VCYQAIT--KKLKiceEET----GSTSI-QAADSTAVNGSITPTDKKIGFLGLG 276
Cdd:cd05213  117 VKNA------YKLAKEAGTSgkllnrLFQKAIKvgKRVR---TETgisrGAVSIsSAAVELAEKIFGNLKGKKVLVIGAG 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 862669336 277 LMGSGIVSNLLKMGHT-VTVWNRTAEKEGARLGRTPAEVVS---------TCDITFACVSDPKAAKD 333
Cdd:cd05213  188 EMGELAAKHLAAKGVAeITIANRTYERAEELAKELGGNAVPldellellnEADVVISATGAPHYAKI 254
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 267-325 5.91e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 38.59  E-value: 5.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 862669336 267 DKKIGFLGLGLMGSGIVSNLLKMG---HTVTVWNRTAEKE-------GARLGRTPAEVVSTCDITFACV 325
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRaalaeeyGVRAATDNQEAAQEADVVVLAV 70
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 268-376 8.01e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 38.57  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 862669336 268 KKIGFLGLGLMGSGIVSNLLKMG--HTVTVWNR------TAEKEGA--RLGRTPAEVVSTCDITFACVSdPKAAKDLVlg 337
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRspetleRALELGVidRAATDLEEAVADADLVVLAVP-VGATIEVL-- 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 862669336 338 pSGVLQGIRPGKCYVDMSTVDADTVTELAQVIvSRGGRF 376
Cdd:COG0287   79 -AELAPHLKPGAIVTDVGSVKGAVVEAAEALL-PDGVRF 115
 
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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