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Conserved domains on  [gi|2064643014|ref|XP_042145879|]
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putative oxidoreductase GLYR1 homolog isoform X1 [Ixodes scapularis]

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 ...
 291-570 6.92e-102

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 309.35  E-value: 6.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVL 370
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 371 QEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLG 450
Cdd:COG2084    83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 451 DVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQKDIC 530
Cdd:COG2084   163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2064643014 531 LAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 570
Cdd:COG2084   243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALI 282
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 5-90 1.89e-55

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: 181.65  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAVE 84
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                  ....*.
gi 2064643014  85 AIEDYV 90
Cdd:cd05836    81 AIEEYI 86
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 291-570 6.92e-102

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 309.35  E-value: 6.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVL 370
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 371 QEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLG 450
Cdd:COG2084    83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 451 DVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQKDIC 530
Cdd:COG2084   163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2064643014 531 LAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 570
Cdd:COG2084   243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALI 282
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 5-90 1.89e-55

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: 181.65  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAVE 84
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                  ....*.
gi 2064643014  85 AIEDYV 90
Cdd:cd05836    81 AIEEYI 86
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 291-450 7.66e-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: 166.88  E-value: 7.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNcGVL 370
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 371 QEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLG 450
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
garR PRK11559
tartronate semialdehyde reductase; Provisional
 290-569 1.00e-48

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 171.00  E-value: 1.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 290 LKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGV 369
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 370 LQEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYL 449
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 450 GDVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQKDI 529
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2064643014 530 CLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSAL 282
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 294-569 1.99e-39

3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]


Pssm-ID: 130753 [Multi-domain]  Cd Length: 288  Bit Score: 145.71  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 294 FLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVLQEI 373
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 374 RNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLGDVG 453
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 454 NGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELG-------DLNSPIITQKGQAI----IEGTFATHMPL 522
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSsgrcwssDTYNPVPGVMPQAPasngYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2064643014 523 qhlqKDICLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:TIGR01692 241 ----KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSV 283
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 8-91 7.41e-24

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: 95.57  E-value: 7.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANPT---KDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPYEGKKD-----QLSKSSKTASF 79
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEelpENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEfeylkKKKKKKKKKAF 80

                          90
                  ....*....|..
gi 2064643014  80 KEAVEAIEDYVK 91
Cdd:pfam00855  81 KKALEEAEEALK 92
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 5-64 7.47e-14

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 66.21  E-value: 7.47e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064643014    5 YNIGDPVWAKMKGFSPWPGKVANPTKDvkRPALKKP-----MQCIFFFGTNNYAWIQEDQIQPYE 64
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMT--PDNIMKRksdenLYPVLFFGDKDTAWIPSSKLFPLT 63
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 273-364 2.63e-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: 40.33  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 273 VERISDVLKQKRVspsnlkfGFLGLGNMGQGMVKNLINSG-HHITVWNRTPSKCRDFVK---AGATKGLTPADVVAASDV 348
Cdd:cd05213   169 AEKIFGNLKGKKV-------LVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEELAKelgGNAVPLDELLELLNEADV 241

                          90
                  ....*....|....*.
gi 2064643014 349 TFCCVSNSHAAKEMVF 364
Cdd:cd05213   242 VISATGAPHYAKIVER 257
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 291-570 6.92e-102

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 309.35  E-value: 6.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVL 370
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 371 QEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLG 450
Cdd:COG2084    83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 451 DVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQKDIC 530
Cdd:COG2084   163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2064643014 531 LAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 570
Cdd:COG2084   243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALI 282
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 5-90 1.89e-55

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: 181.65  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAVE 84
Cdd:cd05836     1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                  ....*.
gi 2064643014  85 AIEDYV 90
Cdd:cd05836    81 AIEEYI 86
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 291-450 7.66e-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: 166.88  E-value: 7.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNcGVL 370
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 371 QEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLG 450
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
garR PRK11559
tartronate semialdehyde reductase; Provisional
 290-569 1.00e-48

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 171.00  E-value: 1.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 290 LKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGV 369
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 370 LQEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYL 449
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 450 GDVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQKDI 529
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2064643014 530 CLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSAL 282
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 294-569 1.99e-39

3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]


Pssm-ID: 130753 [Multi-domain]  Cd Length: 288  Bit Score: 145.71  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 294 FLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVLQEI 373
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 374 RNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLGDVG 453
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 454 NGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELG-------DLNSPIITQKGQAI----IEGTFATHMPL 522
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSsgrcwssDTYNPVPGVMPQAPasngYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2064643014 523 qhlqKDICLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:TIGR01692 241 ----KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSV 283
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
290-569 1.52e-33

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 129.37  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 290 LKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSkCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGV 369
Cdd:PRK15059    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPV-ADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 370 LQEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYL 449
Cdd:PRK15059   80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 450 GDVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQKDI 529
Cdd:PRK15059  160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2064643014 530 CLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:PRK15059  240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSAL 279
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
291-574 5.91e-31

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 122.27  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVL 370
Cdd:PRK15461    3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 371 QEIRNNKGYVEMTSIDPDTSQDISEAILLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFYLG 450
Cdd:PRK15461   83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 451 DVGNGSKMNLIlNMLLGTTLAGLS-EAMALCDRAELSQKDLLEILelgdlnspiitqKGQAIIEGTFATHMPLQHLQ--- 526
Cdd:PRK15461  163 GPGMGIRVKLI-NNYMSIALNALSaEAAVLCEALGLSFDVALKVM------------SGTAAGKGHFTTTWPNKVLKgdl 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2064643014 527 ----------KDICLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVYIRTR 574
Cdd:PRK15461  230 spafmidlahKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVR 287
PLN02858 PLN02858
fructose-bisphosphate aldolase
 291-569 2.12e-25

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 111.48  E-value: 2.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFGNCGVL 370
Cdd:PLN02858   326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  371 QEIRNNKGYVEMTSIDPDTSQDISEAI--LLRGGRYLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIGRHAFY 448
Cdd:PLN02858   406 SALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYV 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  449 L-GDVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPLQHLQK 527
Cdd:PLN02858   486 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2064643014  528 DICLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:PLN02858   566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAV 607
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 8-91 7.41e-24

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: 95.57  E-value: 7.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANPT---KDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPYEGKKD-----QLSKSSKTASF 79
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEelpENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEfeylkKKKKKKKKKAF 80

                          90
                  ....*....|..
gi 2064643014  80 KEAVEAIEDYVK 91
Cdd:pfam00855  81 KKALEEAEEALK 92
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 8-89 1.76e-23

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: 94.49  E-value: 1.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANP--TKDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPYEG--KKDQLSKSSKTASFKEAV 83
Cdd:cd05162     1 GDLVWAKLKGYPWWPARVVDPeeLPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEgfKKEFKKKKKKSKKFKKAV 80


                  ....*.
gi 2064643014  84 EAIEDY 89
Cdd:cd05162    81 EEAEEA 86
PWWP_HRP cd05834
PWWP domain found in hepatoma-derived growth factor (HDGF)-related protein (HRP) family; The ...
 5-87 5.70e-22

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: 89.92  E-value: 5.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPmqcIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAVE 84
Cdd:cd05834     1 FKPGDLVFAKVKGYPPWPARIDEIPEGAKIPKNKYP---VFFYGTHETAFLKPKDLFPYEENKEKYGKPRKRKGFNEGLW 77


                  ...
gi 2064643014  85 AIE 87
Cdd:cd05834    78 EIE 80
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 453-570 1.43e-18

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: 81.80  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 453 GNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQK-GQAIIEGTFATHMPLQHLQKDICL 531
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKfPQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2064643014 532 AIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 570
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAII 119
PLN02858 PLN02858
fructose-bisphosphate aldolase
 286-569 3.51e-18

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 88.76  E-value: 3.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  286 SPSNLKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKEMVFG 365
Cdd:PLN02858     1 AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  366 NCGVLQEIRNNKGYVEMTSIDPDTSQDISEAILLRGGR--YLEAPVSGSKKPAEDGTLIILAAGERSLFNDCASCFEAIG 443
Cdd:PLN02858    81 DEGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMC 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  444 RHAFYL-GDVGNGSKMNLILNMLLGTTLAGLSEAMALCDRAELSQKDLLEILELGDLNSPIITQKGQAIIEGTFATHMPL 522
Cdd:PLN02858   161 QKLYTFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFL 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2064643014  523 QHLQKDICLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 569
Cdd:PLN02858   241 NVLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSL 287
PWWP_HDGFL3 cd20150
PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also ...
 4-88 8.06e-15

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: 70.09  E-value: 8.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   4 KYNIGDPVWAKMKGFSPWPGKVAN-PTKDVKRPALKKPmqcIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEA 82
Cdd:cd20150     5 EYKAGDLVFAKMKGYPHWPARIDElPEGAVKPPANKYP---IFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEG 81


                  ....*.
gi 2064643014  83 VEAIED 88
Cdd:cd20150    82 LWEIEN 87
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
 8-88 6.09e-14

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: 67.32  E-value: 6.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVAN-PTKDVKRPALKKPmqcIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAVEAI 86
Cdd:cd20151     4 GDLIFAKMKGYPHWPARVDEvPDGAVKPPTNKLP---IFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEI 80


                  ..
gi 2064643014  87 ED 88
Cdd:cd20151    81 DN 82
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 5-64 7.47e-14

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 66.21  E-value: 7.47e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064643014    5 YNIGDPVWAKMKGFSPWPGKVANPTKDvkRPALKKP-----MQCIFFFGTNNYAWIQEDQIQPYE 64
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISPKMT--PDNIMKRksdenLYPVLFFGDKDTAWIPSSKLFPLT 63
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 6-91 8.20e-14

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: 66.90  E-value: 8.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   6 NIGDPVWAKMKGFSPWPGKVANpTKDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQP-YEGKKDQLSKSSKTASFKEAV- 83
Cdd:cd05835     1 KIGDLVWAKLKGSPWWPGIVVS-HKDCGQKPPAEGSVWVFWFGDHKVSEVPLDKILPfAEFFNKFYISKNSSKLYKKAVy 79


                  ....*...
gi 2064643014  84 EAIEDYVK 91
Cdd:cd05835    80 EALKEAAE 87
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 5-88 1.91e-13

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: 66.20  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVAN-PTKDVKRPALKKPmqcIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAV 83
Cdd:cd20148     1 YKCGDLVFAKMKGYPHWPARIDEmPEAAVKSTANKYQ---VFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGL 77


                  ....*
gi 2064643014  84 EAIED 88
Cdd:cd20148    78 WEIEN 82
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 8-89 7.53e-13

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: 64.57  E-value: 7.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPMQ---CIFFFGTNNYAWIQEDQIQPY-EGKKDQLSKSSK--TASFKE 81
Cdd:cd05838     3 GDIVWVKLGNYRWWPAEILHPREVPDNIQSLPHPPgefPVRFFGSHDYYWVHRGRVFLFeEGDKGSKEKSKKslDKSFKR 82


                  ....*....
gi 2064643014  82 AV-EAIEDY 89
Cdd:cd05838    83 ALkEANEAF 91
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 8-88 1.21e-12

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: 63.77  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANpTKD--VKRPALKKPmqcIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAVEA 85
Cdd:cd20149     4 GDLVFAKMKGYPHWPARIDD-IADgaVKPPPNKYP---IFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKRKGFNEGLWE 79


                  ...
gi 2064643014  86 IED 88
Cdd:cd20149    80 IQN 82
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 6-85 1.58e-11

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: 60.85  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   6 NIGDPVWAKMKGFSPWPGKVANPT---KDVKRPALKKPMqCIFFFG---TNNYAWIQEDQIQPY----EGKKDQLSKSSK 75
Cdd:cd20143     1 VEGDLVWAKVGTHPFWPARVVEPAeqaEEVRRRCVPGSL-CVYFFGpggSRDYGWVRRSMIFPFtddlARFQTQKIKNKK 79

                          90
                  ....*....|.
gi 2064643014  76 TAS-FKEAVEA 85
Cdd:cd20143    80 RPQeFQEALEE 90
PWWP_BS69 cd20159
PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger ...
 11-84 1.64e-11

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: 60.30  E-value: 1.64e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064643014  11 VWAKMKGFSPWPGKVANPTK---DVKrpalkkpmqciFFFGTNNYAWIQEDQIQPYEGKKDQLsKSSKTASFKEAVE 84
Cdd:cd20159    10 VWAKQKGFPYWPAKVIQKEDnqyDVR-----------FFGGHHQRAWIPKENIKPITTSPKQL-KVKRTAGWNKACE 74
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
 11-91 4.63e-10

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: 56.42  E-value: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  11 VWAKMKGFSPWPGKV---ANPTKDVKrpalkkpmqcifFFGTNNYAWIQEDQIQPYEgKKDQLSKSSKTASFKEAVEAIE 87
Cdd:cd20160    10 VWAKLKGFPFWPAKAlrvNNGQVDVR------------FFGAHDRAWVPVKDCYLYS-KEPPTSVKKKKSGLDEAMEELE 76


                  ....
gi 2064643014  88 DYVK 91
Cdd:cd20160    77 IHIE 80
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 8-87 5.42e-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: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANP--------TKDVKRPALKKPMQCIFFFGTNNYAWIQEDQIQPY--EGKKDQLSKSSKTA 77
Cdd:cd05840     1 GDLVLAKVKGYPPWPAMVLPEellpknvlKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPLtkEEIDKFLSKSKRKN 80

                          90
                  ....*....|
gi 2064643014  78 sfKEAVEAIE 87
Cdd:cd05840    81 --KDLIEAYE 88
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
 3-87 3.03e-09

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: 54.86  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   3 TKYNIGDPVWAKMKGFSPWPGKV-----------ANPTKDvkrpalkKPMQC-IFFFGTN-NYAWIQEDQIQPYEG-KKD 68
Cdd:cd20145     4 TKYTPGSLVWAKMPGYPWWPAMVeddpdteeffwLDEESD-------IPTKYhVTFFDKPvSRAWVRASSIKPFTDnSNE 76

                          90       100
                  ....*....|....*....|
gi 2064643014  69 QLSKSSKTASFKEAV-EAIE 87
Cdd:cd20145    77 PNLTKKKGKKYKKRLnEAVE 96
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
291-345 5.79e-09

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 57.45  E-value: 5.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2064643014 291 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGLTPADVVAA 345
Cdd:PRK09599    2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAK 56
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
 5-96 1.15e-08

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: 53.06  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVAN-PTKDVKRpALKKPMQC-IFFFG-TNNYAWIQEDQIQPYEGKKDQLSKS-----SKT 76
Cdd:cd05837     1 FSPGDLVWAKLEGYPWWPSLVCNhPTTGFHK-KFGKKGEVhVQFFDdPPSRAWVKAKNVKPFTGSDDKEFQKggmffSKD 79

                          90       100
                  ....*....|....*....|
gi 2064643014  77 ASFKEAVEAIEDYVKTMPEQ 96
Cdd:cd05837    80 PKWKKAVKEADKALKLSVEE 99
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 288-353 1.24e-08

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: 56.23  E-value: 1.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 288 SNLKFGFLGLGNMGQGMVKNLINSG---HHITVWNRTPSKCRDFVKA-GATKGLTPADVVAASDVTFCCV 353
Cdd:COG0345     1 MSMKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVLAV 70
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 5-85 3.69e-08

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: 51.50  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKD-----VKRPALK--------KPMQCIFFFGT-NNYAWIQEDQIQP--YEGKKD 68
Cdd:cd05839     1 LEPGDLVWAKCRGYPWYPAEIVDPKDPkegngVPIPVPPdrvlkksnEKLYLVLFFDAkRTWGWLPRNKLRPlgVDEELD 80

                          90
                  ....*....|....*....
gi 2064643014  69 Q--LSKSSKTASFKEAVEA 85
Cdd:cd05839    81 KlkLSEAKKSKRRKEVRKA 99
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 8-91 4.24e-08

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: 51.20  E-value: 4.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANPTKDVKR-----PALKKPMQCIFFFGTNNYAWIQEDQIQPYE-GKKDQLSKSSKTASFKE 81
Cdd:cd20142     3 GDVVWAKVKGYPMWPALVIDEEHAERCgleanRPGKKGTVPVQFFGTYEVARLNPKKVVGFSkGLDLKYHSKCKAPVFRQ 82

                          90
                  ....*....|
gi 2064643014  82 AVEAIEDYVK 91
Cdd:cd20142    83 ALEEAERYLK 92
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
 7-111 4.88e-08

PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA methyltransferase HsaIIIB, DNA MTase HsaIIIB, or M.HsaIIIB, is required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. It 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. 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 anomalies) syndrome, a rare autosomal recessive disorder characterized by hypomethylation of classical satellite DNA.


Pssm-ID: 438983  Cd Length: 117  Bit Score: 51.41  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   7 IGDPVWAKMKGFSPWPGKVANPTKDVKRPALKKpMQCIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSS--KTASFKEAV- 83
Cdd:cd20155     2 IGELVWGKIKGFSWWPAMVVSWRATGKRQASSG-MRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTynKLVSYRKAMy 80

                          90       100
                  ....*....|....*....|....*...
gi 2064643014  84 EAIEdYVKTMPEQPVRSSDLPSIDEELS 111
Cdd:cd20155    81 HALE-VARVRAGKTFPSSPGESLEDQLK 107
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 8-87 1.30e-07

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: 49.41  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPMqcIFFFGTNNYAWIQEDQIQPYEGKKDQLS-----KSSKTASFKEA 82
Cdd:cd20147     1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKKVF--VHFFGTQQIGFCNPGELSEFTEEIKQSLlartlKKKKGSDFSRA 78


                  ....*
gi 2064643014  83 VEAIE 87
Cdd:cd20147    79 VKEIC 83
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
 5-80 2.23e-07

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: 49.91  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKV-ANP-------TKDVKRPALKKPMQciFFFGTNNYAWIQEDQIQPYEGKK--DQL-SKS 73
Cdd:cd20162     1 YNVGDLVWSKVSGYPWWPCMVsADPllhshtkLKGQKKSARQYHVQ--FFGDAPERAWIFEKSLVPFEGEGqfEQLcQES 78


                  ....*..
gi 2064643014  74 SKTASFK 80
Cdd:cd20162    79 AKQAPTK 85
PWWP_NSD3_rpt2 cd20166
second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...
 11-84 3.51e-07

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: 48.43  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  11 VWAKMKGFSPWPGKVANP------TKDVKRPALKKPmqcIFFFGTNNYAWIQEDQIQPY-EGKKDQLS-KSSKTASFKEA 82
Cdd:cd20166     6 VWVKLGNYRWWPAEICNPrsvplnIQGLKHDIGDFP---VFFFGSHDYYWVHQGRVFPYvEGDKSFAEgQTSINKTFKKA 82


                  ..
gi 2064643014  83 VE 84
Cdd:cd20166    83 LE 84
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 5-61 4.53e-07

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: 48.08  E-value: 4.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKDVKRPALKKPMQCiffFGTNNYAWIQEDQIQ 61
Cdd:cd20141     1 FNVGDLVWGQIRGFPSWPGKLVSENDVGKTNEGKVWVSW---FGDHSFGQVEPDKLK 54
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
293-359 9.47e-07

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 49.78  E-value: 9.47e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064643014 293 GFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKA--GATKGLTPADVVAASDVTFCCVSNSHAA 359
Cdd:COG2085     2 GIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAElgPGARAGTNAEAAAAADVVVLAVPYEAVP 70
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
 5-88 1.39e-06

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: 46.49  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVANPTKDVKRP-ALKKPMQCIFFFGTNNYAWIQEDQIQPYEGKKDQLSKSSKTASFKEAV 83
Cdd:cd20140     4 LRVGDIVWGKIHGFPWWPGRILSITVSRDDNgELSTQEAHVSWFGSSTTSYMPCSQLYPFLEDFKLRYNKKKRGPYKEAV 83


                  ....*.
gi 2064643014  84 -EAIED 88
Cdd:cd20140    84 rQALEA 89
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
293-353 2.68e-06

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 45.69  E-value: 2.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064643014 293 GFLGLGNMGQGMVKNLINSGHH--ITVWNRTPSKCRDFVKA---GATkGLTPADVVAASDVTFCCV 353
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEygvGAT-AVDNEEAAEEADVVFLAV 65
PRK07680 PRK07680
late competence protein ComER; Validated
 290-353 2.91e-06

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 49.20  E-value: 2.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 290 LKFGFLGLGNMGQGMVKNLINSG----HHITVWNRTPSKCRDFVKA--GATKGLTPADVVAASDVTFCCV 353
Cdd:PRK07680    1 MNIGFIGTGNMGTILIEAFLESGavkpSQLTITNRTPAKAYHIKERypGIHVAKTIEEVISQSDLIFICV 70
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 292-341 8.38e-06

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: 48.53  E-value: 8.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2064643014 292 FGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVK-AGATKGLTPAD 341
Cdd:COG0362     5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAeHGKGKNIVGTY 55
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 290-374 1.18e-05

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 47.26  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 290 LKFGFLGLGNMGQGMVKNLINSG-----HHITVWNRTPSKCRDFVKAGATKGLTPADVVAASDVTFCCVSNSHAAKemvf 364
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARGLVASGvvppsRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKD---- 76

                          90
                  ....*....|
gi 2064643014 365 gncgVLQEIR 374
Cdd:PLN02688   77 ----VLTELR 82
PWWP_BS69-like cd05841
PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...
 11-91 1.68e-05

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: 43.54  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014  11 VWAKMKGFSPWPGKVanptkdvkrpalkkpMQC------IFFFGTNNYAWIQEDQIQPYEGKKDQL----SKSSKTASFK 80
Cdd:cd05841    10 VWVKLDGFPFWPAKV---------------MGTkdgqvdVRFFGDYDRAWLPSKNVTLHTREIVSTlpdsSESKDKRTLK 74

                          90
                  ....*....|.
gi 2064643014  81 EAVEAIEDYVK 91
Cdd:cd05841    75 KAIKELERHIA 85
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 288-353 1.76e-05

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 46.68  E-value: 1.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064643014 288 SNLKFGFLGLGNMGQGMVKNLINSG---HHITVWNRTPSKcRDFVKA--GATKGLTPADVVAASDVTFCCV 353
Cdd:PRK11880    1 MMKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEK-RAALAEeyGVRAATDNQEAAQEADVVVLAV 70
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 8-89 2.29e-05

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: 43.01  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   8 GDPVWAKMKGFSPWPGKVanptKDVKrpalKKPMQ-CIFFFGtnnyaWIQEDQ--------IQPYEGK-----KDQLSKS 73
Cdd:cd06080     4 GDIVWAKYRKYPYWPAVV----KSVY----KKPKKaSVLFLE-----LPPEKKgikvslkkLKPFDCKekeelLEEGKES 70

                          90
                  ....*....|....*.
gi 2064643014  74 SKTASFKEAVEAIEDY 89
Cdd:cd06080    71 PYSEDFKEAVELAEDY 86
PWWP_NSD1_rpt2 cd20164
second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...
 9-84 2.53e-05

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: 43.33  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   9 DPVWAKMKGFSPWPGKVANPtKDVKRPALKKPMQC----IFFFGTNNYAWIQEDQIQPY-EGKKDQLSKSSK--TASFKE 81
Cdd:cd20164     4 EVVWVKVGRYRWWPAEVCHP-KSIPTNIQKMKHDIgefpVLFFGSNDYLWTHQARVFPYmEGDVSSKDKMGKgvDGTYKK 82


                  ...
gi 2064643014  82 AVE 84
Cdd:cd20164    83 ALQ 85
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 7-68 2.90e-05

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: 43.46  E-value: 2.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064643014   7 IGDPVWAKMKGFSPWPGKVAN-P-----TKDVKRPALKKPM---QcifFFGTNN-YAWIQEDQIQPYEGKKD 68
Cdd:cd20144     1 VGDLVWAKVSGHPWWPCMVTYdPesglyTKIKGSGGRTYRQyhvQ---FFGDNGeRGWVSEKSLMPFEGKEK 69
PWWP_NSD2_rpt2 cd20165
second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...
 9-87 4.41e-05

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: 42.64  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   9 DPVWAKMKGFSPWPGKVANPtKDVKrPALKKPMQCI-----FFFGTNNYAWIQEDQIQPY-EGkkDQLSKSSKTAS---- 78
Cdd:cd20165     4 DIIWVKLGNYRWWPAEVCHP-KNVP-PNIQKMKHEIgefpvFFFGSKDYYWTHQARVFPYmEG--DRGSKYQGGKGigkv 79


                  ....*....
gi 2064643014  79 FKEAVEAIE 87
Cdd:cd20165    80 FKNALQEAE 88
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
 5-78 8.63e-05

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: 42.61  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   5 YNIGDPVWAKMKGFSPWPGKVA-NP-----TKDVKRPALKKPMQciFFFGTNNYAWIQEDQIQPYEGKK--DQL-SKSSK 75
Cdd:cd20163     1 FQVGDLVWSKVGTYPWWPCMVSsDPqlevhTKINTRGAREYHVQ--FFSSQPERAWVHEKRVREYKGHKqyEELlAEATK 78


                  ...
gi 2064643014  76 TAS 78
Cdd:cd20163    79 QAS 81
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 273-363 1.21e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 44.79  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 273 VERISDVLKQKRVspsnLkfgFLGLGNMGQGMVKNLINSG-HHITVWNRTPSKCRDFVKAGATKGLTPAD---VVAASDV 348
Cdd:PRK00045  173 AKQIFGDLSGKKV----L---VIGAGEMGELVAKHLAEKGvRKITVANRTLERAEELAEEFGGEAIPLDElpeALAEADI 245

                          90
                  ....*....|....*..
gi 2064643014 349 TFCCVSNSHA--AKEMV 363
Cdd:PRK00045  246 VISSTGAPHPiiGKGMV 262
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 292-337 1.44e-04

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 44.39  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2064643014 292 FGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGATKGL 337
Cdd:PTZ00142    4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAKEGNT 49
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
 4-66 2.37e-04

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: 40.92  E-value: 2.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014   4 KYNIGDPVWAKMKGFSPWPGKV-ANPTKDV----KRPALKKPMQC-IFFFGT-NNYAWIQEDQIQPYEGK 66
Cdd:cd20161     3 KYEVGDLVWAKFSRRPWWPCRIcADPLLDThskmKVPSRRPCRQYyVETLGElTEKAWVAAKAVVPFEGR 72
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 273-363 2.48e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 41.40  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 273 VERISDVLKQKRVspsnlkfGFLGLGNMGQGMVKNLINSG-HHITVWNRTPSKCRDFVKAGATKGLTP----ADVVAASD 347
Cdd:pfam01488   3 AKKIFGDLKDKKV-------LLIGAGEMGELVAKHLLAKGaKEVTIANRTIERAQELAEKFGGVEALPlddlKEYLAEAD 75

                          90
                  ....*....|....*...
gi 2064643014 348 VTFCCVSNSHA--AKEMV 363
Cdd:pfam01488  76 IVISATSSPTPiiTKEMV 93
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 273-364 2.63e-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: 40.33  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064643014 273 VERISDVLKQKRVspsnlkfGFLGLGNMGQGMVKNLINSG-HHITVWNRTPSKCRDFVK---AGATKGLTPADVVAASDV 348
Cdd:cd05213   169 AEKIFGNLKGKKV-------LVIGAGEMGELAAKHLAAKGvAEITIANRTYERAEELAKelgGNAVPLDELLELLNEADV 241

                          90
                  ....*....|....*.
gi 2064643014 349 TFCCVSNSHAAKEMVF 364
Cdd:cd05213   242 VISATGAPHYAKIVER 257
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
300-340 2.92e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 40.49  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2064643014 300 MGQGMVKNLINSGHHITVWNRTPSKCRDFVK-AGATKGLTPA 340
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAeEGKGKKIVPA 42
 
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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