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Conserved domains on  [gi|427787955|gb|JAA59429|]
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Putative actin regulatory protein [Rhipicephalus pulchellus]

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 ...
 279-558 3.55e-100

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 304.73  E-value: 3.55e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVL 358
Cdd:COG2084    3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 359 HEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLG 438
Cdd:COG2084   83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 439 EVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQKDLC 518
Cdd:COG2084  163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 427787955 519 LAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 558
Cdd:COG2084  243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALI 282
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 5-90 5.87e-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: 180.11  E-value: 5.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEALE 84
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                 ....*.
gi 427787955  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 ...
 279-558 3.55e-100

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 304.73  E-value: 3.55e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVL 358
Cdd:COG2084    3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 359 HEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLG 438
Cdd:COG2084   83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 439 EVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQKDLC 518
Cdd:COG2084  163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 427787955 519 LAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 558
Cdd:COG2084  243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALI 282
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 5-90 5.87e-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: 180.11  E-value: 5.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEALE 84
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                 ....*.
gi 427787955  85 AIEDYV 90
Cdd:cd05836   81 AIEEYI 86
garR PRK11559
tartronate semialdehyde reductase; Provisional
 278-557 1.38e-49

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 173.31  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 278 LKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGV 357
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 358 LHEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYL 437
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 438 GEVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQKDL 517
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 427787955 518 CLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSAL 282
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 279-438 9.05e-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: 166.11  E-value: 9.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNcGVL 358
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  359 HEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLG 438
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 282-557 7.95e-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: 143.79  E-value: 7.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  282 FLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVLHEI 361
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  362 KDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLGEVG 441
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  442 NGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGD-----LNS---------AVISQKGqaiIEGTFATN 507
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSgrcwsSDTynpvpgvmpQAPASNG---YQGGFGTA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 427787955  508 MPLqhlqKDLCLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:TIGR01692 238 LML----KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSV 283
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 8-91 2.86e-25

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: 99.81  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955    8 GDPVWAKMKGFSPWPGKVANPT---KEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEASKEQF-----SKSSKTASF 79
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEelpENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEylkkkKKKKKKKAF 80

                          90
                  ....*....|..
gi 427787955   80 KEALEAIEDYVK 91
Cdd:pfam00855  81 KKALEEAEEALK 92
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 5-64 3.48e-14

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 67.37  E-value: 3.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427787955     5 YNIGDPVWAKMKGFSPWPGKVANPtkEVKRPALKKPMHCI-----FFFGTNNYAWIQEDQIKPYE 64
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISP--KMTPDNIMKRKSDEnlypvLFFGDKDTAWIPSSKLFPLT 63
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 279-558 3.55e-100

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 304.73  E-value: 3.55e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVL 358
Cdd:COG2084    3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 359 HEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLG 438
Cdd:COG2084   83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 439 EVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQKDLC 518
Cdd:COG2084  163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 427787955 519 LAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 558
Cdd:COG2084  243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALI 282
PWWP_GLYR1 cd05836
PWWP domain found in glyoxylate reductase 1 (GLYR1) and similar proteins; GLYR1, also called ...
 5-90 5.87e-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: 180.11  E-value: 5.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEALE 84
Cdd:cd05836    1 FKIGDLVWAKMKGFPPWPGKIVNPPPDLKKPPRKKKMHCVYFFGSENYAWIEDENIKPYEEFKEEMLKSKKSAGFKDAVE 80


                 ....*.
gi 427787955  85 AIEDYV 90
Cdd:cd05836   81 AIEEYI 86
garR PRK11559
tartronate semialdehyde reductase; Provisional
 278-557 1.38e-49

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 173.31  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 278 LKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGV 357
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 358 LHEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYL 437
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 438 GEVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQKDL 517
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 427787955 518 CLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSAL 282
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 279-438 9.05e-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: 166.11  E-value: 9.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNcGVL 358
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  359 HEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLG 438
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 282-557 7.95e-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: 143.79  E-value: 7.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  282 FLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVLHEI 361
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  362 KDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLGEVG 441
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  442 NGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGD-----LNS---------AVISQKGqaiIEGTFATN 507
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSgrcwsSDTynpvpgvmpQAPASNG---YQGGFGTA 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 427787955  508 MPLqhlqKDLCLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:TIGR01692 238 LML----KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSV 283
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
278-557 1.30e-33

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 129.76  E-value: 1.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 278 LKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSkCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGV 357
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPV-ADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 358 LHEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYL 437
Cdd:PRK15059  80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 438 GEVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQKDL 517
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 427787955 518 CLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:PRK15059 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSAL 279
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
279-562 3.44e-31

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 123.04  E-value: 3.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVL 358
Cdd:PRK15461   3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 359 HEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFYLG 438
Cdd:PRK15461  83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 439 EVGNGSKMSLIlNMLLGTTLAGL-AEAMALCDRAELSQKDLLEILelgdlnSAVISQKGQ-------AIIEGTFATNMPL 510
Cdd:PRK15461 163 GPGMGIRVKLI-NNYMSIALNALsAEAAVLCEALGLSFDVALKVM------SGTAAGKGHftttwpnKVLKGDLSPAFMI 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 427787955 511 QHLQKDLCLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVYIRTR 562
Cdd:PRK15461 236 DLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVR 287
PWWP pfam00855
PWWP domain; The PWWP domain is named after a conserved Pro-Trp-Trp-Pro motif. The domain ...
 8-91 2.86e-25

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: 99.81  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955    8 GDPVWAKMKGFSPWPGKVANPT---KEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEASKEQF-----SKSSKTASF 79
Cdd:pfam00855   1 GDLVWAKLKGYPWWPARVVDPEelpENVLKPKKKDGEYLVRFFGDSEFAWVKPKDLKPFDEGDEFEylkkkKKKKKKKAF 80

                          90
                  ....*....|..
gi 427787955   80 KEALEAIEDYVK 91
Cdd:pfam00855  81 KKALEEAEEALK 92
PLN02858 PLN02858
fructose-bisphosphate aldolase
 279-557 3.39e-25

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 110.71  E-value: 3.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFGNCGVL 358
Cdd:PLN02858  326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  359 HEIKDNKGYVEMTSIDPDTSQDISEAI--MLRGGRYLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIGRHAFY 436
Cdd:PLN02858  406 SALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYV 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  437 L-GEVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPLQHLQK 515
Cdd:PLN02858  486 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 427787955  516 DLCLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:PLN02858  566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAV 607
PWWP cd05162
PWWP (Pro-Trp-Trp-Pro) domain; The PWWP domain, named for a conserved Pro-Trp-Trp-Pro motif, ...
 8-89 2.92e-24

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


Pssm-ID: 438958 [Multi-domain]  Cd Length: 86  Bit Score: 96.80  E-value: 2.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVANP--TKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEAS--KEQFSKSSKTASFKEAL 83
Cdd:cd05162    1 GDLVWAKLKGYPWWPARVVDPeeLPEEVGKKKKKGGVLVQFFGDNDYAWVKSKNIKPFEEGfkKEFKKKKKKSKKFKKAV 80


                 ....*.
gi 427787955  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 4.14e-23

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: 93.39  E-value: 4.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPmhcIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEALE 84
Cdd:cd05834    1 FKPGDLVFAKVKGYPPWPARIDEIPEGAKIPKNKYP---VFFYGTHETAFLKPKDLFPYEENKEKYGKPRKRKGFNEGLW 77


                 ...
gi 427787955  85 AIE 87
Cdd:cd05834   78 EIE 80
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 441-558 3.12e-19

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: 83.73  E-value: 3.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  441 GNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQK-GQAIIEGTFATNMPLQHLQKDLCL 519
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKfPQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 427787955  520 AIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAVY 558
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAII 119
PLN02858 PLN02858
fructose-bisphosphate aldolase
 274-557 4.79e-18

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 88.37  E-value: 4.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  274 SPSNLKFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCVSNSHAAKEMVFG 353
Cdd:PLN02858    1 AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  354 NCGVLHEIKDNKGYVEMTSIDPDTSQDISEAIMLRGGR--YLEAPVSGSKKPAEDGTLIILAAGDRSLFNDCASCFEAIG 431
Cdd:PLN02858   81 DEGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  432 RHAFYL-GEVGNGSKMSLILNMLLGTTLAGLAEAMALCDRAELSQKDLLEILELGDLNSAVISQKGQAIIEGTFATNMPL 510
Cdd:PLN02858  161 QKLYTFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 427787955  511 QHLQKDLCLAIGIGDQLEQPLPVTAAANEVFKHAKKHGYAEHDASAV 557
Cdd:PLN02858  241 NVLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSL 287
PWWP_HDGF cd20148
PWWP domain found in Hepatoma-derived growth factor (HDGF); HDGF, also called high mobility ...
 5-88 1.25e-16

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: 75.06  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVanptKEVKRPALKKPM--HCIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEA 82
Cdd:cd20148    1 YKCGDLVFAKMKGYPHWPARI----DEMPEAAVKSTAnkYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEG 76


                 ....*.
gi 427787955  83 LEAIED 88
Cdd:cd20148   77 LWEIEN 82
PWWP_HDGFL3 cd20150
PWWP domain found in Hepatoma-derived growth factor-related protein 3 (HDGFL3); HDGFL3, also ...
 4-88 1.94e-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: 72.02  E-value: 1.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   4 KYNIGDPVWAKMKGFSPWPGKVAN-PTKEVKRPALKKPmhcIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEA 82
Cdd:cd20150    5 EYKAGDLVFAKMKGYPHWPARIDElPEGAVKPPANKYP---IFFFGTHETAFLGPKDLFPYKEYKDKFGKSNKRKGFNEG 81


                 ....*.
gi 427787955  83 LEAIED 88
Cdd:cd20150   82 LWEIEN 87
PWWP_PSIP cd20151
PWWP domain found in PC4 and SFRS1-interacting protein (PSIP); PSIP, also called ...
 8-88 2.88e-15

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: 71.17  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVAN-PTKEVKRPALKKPmhcIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEALEAI 86
Cdd:cd20151    4 GDLIFAKMKGYPHWPARVDEvPDGAVKPPTNKLP---IFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEI 80


                 ..
gi 427787955  87 ED 88
Cdd:cd20151   81 DN 82
PWWP_DNMT3 cd05835
PWWP domain found in the DNA (cytosine-5)-methyltransferase 3 (DNMT3) family; The DNMT3 family ...
 6-91 1.32e-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: 69.21  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   6 NIGDPVWAKMKGFSPWPGKVANpTKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKT-ASFKEA-L 83
Cdd:cd05835    1 KIGDLVWAKLKGSPWWPGIVVS-HKDCGQKPPAEGSVWVFWFGDHKVSEVPLDKILPFAEFFNKFYISKNSsKLYKKAvY 79


                 ....*...
gi 427787955  84 EAIEDYVK 91
Cdd:cd05835   80 EALKEAAE 87
PWWP smart00293
domain with conserved PWWP motif; conservation of Pro-Trp-Trp-Pro residues
 5-64 3.48e-14

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


Pssm-ID: 214603 [Multi-domain]  Cd Length: 63  Bit Score: 67.37  E-value: 3.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427787955     5 YNIGDPVWAKMKGFSPWPGKVANPtkEVKRPALKKPMHCI-----FFFGTNNYAWIQEDQIKPYE 64
Cdd:smart00293   1 FKPGDLVWAKMKGFPWWPALVISP--KMTPDNIMKRKSDEnlypvLFFGDKDTAWIPSSKLFPLT 63
PWWP_HDGFL2 cd20149
PWWP domain found in Hepatoma-derived growth factor-related protein 2 (HDGFL2); HDGFL2, also ...
 8-88 1.01e-13

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: 66.85  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVANPTK-EVKRPALKKPmhcIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEALEAI 86
Cdd:cd20149    4 GDLVFAKMKGYPHWPARIDDIADgAVKPPPNKYP---IFFFGTHETAFLGPKDLFPYDKYKDKYGKPNKRKGFNEGLWEI 80


                 ..
gi 427787955  87 ED 88
Cdd:cd20149   81 QN 82
PWWP_NSD_rpt2 cd05838
second PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 8-89 1.32e-12

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: 63.80  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVANPTKEVKRPALKKP---MHCIFFFGTNNYAWIQEDQIKPYE---ASKEQFSKSSKTASFKE 81
Cdd:cd05838    3 GDIVWVKLGNYRWWPAEILHPREVPDNIQSLPHppgEFPVRFFGSHDYYWVHRGRVFLFEegdKGSKEKSKKSLDKSFKR 82


                 ....*....
gi 427787955  82 AL-EAIEDY 89
Cdd:cd05838   83 ALkEANEAF 91
PWWP_AtATX3-like cd20143
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 6-85 3.62e-12

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: 62.77  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   6 NIGDPVWAKMKGFSPWPGKVANPT---KEVKRPALKKPMhCIFFFG---TNNYAWIQEDQIKPYEASKEQFS-----KSS 74
Cdd:cd20143    1 VEGDLVWAKVGTHPFWPARVVEPAeqaEEVRRRCVPGSL-CVYFFGpggSRDYGWVRRSMIFPFTDDLARFQtqkikNKK 79

                         90
                 ....*....|.
gi 427787955  75 KTASFKEALEA 85
Cdd:cd20143   80 RPQEFQEALEE 90
PWWP_BS69 cd20159
PWWP domain found in protein BS69 and similar proteins; Protein BS69, also called zinc finger ...
 11-95 7.01e-12

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: 61.46  E-value: 7.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  11 VWAKMKGFSPWPGKVANPTK---EVKrpalkkpmhciFFFGTNNYAWIQEDQIKPYEASKEQfSKSSKTASFKEALEAIE 87
Cdd:cd20159   10 VWAKQKGFPYWPAKVIQKEDnqyDVR-----------FFGGHHQRAWIPKENIKPITTSPKQ-LKVKRTAGWNKACEELK 77


                 ....*...
gi 427787955  88 DYVKNLPE 95
Cdd:cd20159   78 KHQELLEE 85
PWWP_PRKCBP1 cd20160
PWWP domain found in protein kinase C-binding protein 1 (PRKCBP1) and similar proteins; ...
 11-96 1.24e-11

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: 61.04  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  11 VWAKMKGFSPWPGKV---ANPTKEVKrpalkkpmhcifFFGTNNYAWIQEDQIkpYEASKEQ-FSKSSKTASFKEALEAI 86
Cdd:cd20160   10 VWAKLKGFPFWPAKAlrvNNGQVDVR------------FFGAHDRAWVPVKDC--YLYSKEPpTSVKKKKSGLDEAMEEL 75

                         90
                 ....*....|
gi 427787955  87 EDYVKNLPEQ 96
Cdd:cd20160   76 EIHIEKLREK 85
PWWP_ScIOC4-like cd05840
PWWP domain found in Saccharomyces cerevisiae ISWI one complex protein 4 (ScIOC4) and similar ...
 8-84 4.08e-11

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: 59.62  E-value: 4.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVANP--------TKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKP--------YEASKEQFS 71
Cdd:cd05840    1 GDLVLAKVKGYPPWPAMVLPEellpknvlKAKKRKPKSKKTVYPVQFFPDNEYYWVSPSSLKPltkeeidkFLSKSKRKN 80

                         90
                 ....*....|...
gi 427787955  72 KSSKTAsFKEALE 84
Cdd:cd05840   81 KDLIEA-YEVALE 92
PWWP_ZCWPW1 cd20145
PWWP domain found in zinc finger CW-type PWWP domain protein 1 (ZCWPW1) and similar proteins; ...
 3-87 6.19e-10

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: 56.79  E-value: 6.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   3 TKYNIGDPVWAKMKGFSPWPGKVAN-P-TK---EVKRPAlKKPMHC-IFFFGTN-NYAWIQEDQIKPY-EASKEQFSKSS 74
Cdd:cd20145    4 TKYTPGSLVWAKMPGYPWWPAMVEDdPdTEeffWLDEES-DIPTKYhVTFFDKPvSRAWVRASSIKPFtDNSNEPNLTKK 82

                         90
                 ....*....|....
gi 427787955  75 KTASFKEAL-EAIE 87
Cdd:cd20145   83 KGKKYKKRLnEAVE 96
PWWP_MSH6 cd05837
PWWP domain found in DNA mismatch repair protein MSH6 and similar proteins; MSH6, also called ...
 5-88 9.12e-10

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


Pssm-ID: 438962  Cd Length: 103  Bit Score: 56.14  E-value: 9.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVAN-PTKEVKRPALKKP-MHCIFFFGTNNYAWIQEDQIKPY------EASKEQFSKSSKT 76
Cdd:cd05837    1 FSPGDLVWAKLEGYPWWPSLVCNhPTTGFHKKFGKKGeVHVQFFDDPPSRAWVKAKNVKPFtgsddkEFQKGGMFFSKDP 80

                         90
                 ....*....|....*
gi 427787955  77 A---SFKEALEAIED 88
Cdd:cd05837   81 KwkkAVKEADKALKL 95
PWWP_DNMT3B cd20155
PWWP domain found in DNA (cytosine-5)-methyltransferase 3B (DNMT3B); DNMT3B, also called DNA ...
 7-111 1.83e-09

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: 55.65  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   7 IGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKpMHCIFFFGTNNYAWIQEDQIKPYEASKEQFSKSS--KTASFKEAL- 83
Cdd:cd20155    2 IGELVWGKIKGFSWWPAMVVSWRATGKRQASSG-MRWLQWFGDGKFSEVSADKLVSLTAFSQHFNLSTynKLVSYRKAMy 80

                         90       100
                 ....*....|....*....|....*...
gi 427787955  84 EAIEDYVKnLPEQPVRSSDLPSIDEEIS 111
Cdd:cd20155   81 HALEVARV-RAGKTFPSSPGESLEDQLK 107
PWWP_AtATX1-like cd20142
PWWP domain found in Arabidopsis thaliana histone-lysine N-methyltransferase trithorax-like ...
 8-94 1.46e-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: 52.35  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVANPTKEVKR---PALKKPMHCIF--FFGTNNYAWIQEDQIKPYEAS-KEQFSKSSKTASFKE 81
Cdd:cd20142    3 GDVVWAKVKGYPMWPALVIDEEHAERCgleANRPGKKGTVPvqFFGTYEVARLNPKKVVGFSKGlDLKYHSKCKAPVFRQ 82

                         90
                 ....*....|....*
gi 427787955  82 ALEAIEDYVK--NLP 94
Cdd:cd20142   83 ALEEAERYLKegKLP 97
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
279-333 2.48e-08

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 55.53  E-value: 2.48e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 427787955 279 KFGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVKAGAYKGLTPADVVAA 333
Cdd:PRK09599   2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAK 56
PWWP_HULK cd20147
PWWP domain found in Arabidopsis thaliana protein HUA2-LIKE (HULK) family; The HULK family ...
 8-87 4.87e-08

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: 50.57  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPGKVANPTKEVKRPALKKpmHCIFFFGTNNYAWIQEDQIKPY-----EASKEQFSKSSKTASFKEA 82
Cdd:cd20147    1 GDLVLAKVKGFPAWPAQVSEPEDWGSAPDPKK--VFVHFFGTQQIGFCNPGELSEFteeikQSLLARTLKKKKGSDFSRA 78


                 ....*
gi 427787955  83 LEAIE 87
Cdd:cd20147   79 VKEIC 83
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 276-341 1.11e-07

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: 53.14  E-value: 1.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 276 SNLKFGFLGLGNMGQGMVKNLINSG---HHITVWNRTPSKCRDFVKA-GAYKGLTPADVVAASDITFCCV 341
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVLAV 70
PWWP_NSD2_rpt1 cd20162
first PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar proteins; ...
 5-80 1.94e-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: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKV-ANP-----TKEVKRPALKKPMHCIFFFGTNNYAWIQEDQIKPYEAsKEQFSK----SS 74
Cdd:cd20162    1 YNVGDLVWSKVSGYPWWPCMVsADPllhshTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVPFEG-EGQFEQlcqeSA 79


                 ....*.
gi 427787955  75 KTASFK 80
Cdd:cd20162   80 KQAPTK 85
PRK07680 PRK07680
late competence protein ComER; Validated
 278-341 2.32e-07

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 52.28  E-value: 2.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 427787955 278 LKFGFLGLGNMGQGMVKNLINSG----HHITVWNRTPSKCRDFVKagAYKGL----TPADVVAASDITFCCV 341
Cdd:PRK07680   1 MNIGFIGTGNMGTILIEAFLESGavkpSQLTITNRTPAKAYHIKE--RYPGIhvakTIEEVISQSDLIFICV 70
PWWP_NSD3_rpt2 cd20166
second PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar ...
 11-84 2.58e-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: 48.82  E-value: 2.58e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 427787955  11 VWAKMKGFSPWPGKVANP-TKEVKRPALKKPM--HCIFFFGTNNYAWIQEDQIKPYEASKEQFS--KSSKTASFKEALE 84
Cdd:cd20166    6 VWVKLGNYRWWPAEICNPrSVPLNIQGLKHDIgdFPVFFFGSHDYYWVHQGRVFPYVEGDKSFAegQTSINKTFKKALE 84
PWWP_BRPF cd05839
PWWP domain found in the bromodomain and PHD finger-containing (BRPF) protein family; The BRPF ...
 5-84 2.92e-07

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: 48.80  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKE-----VKRPALK--------KPMHCIFFFGT-NNYAWIQEDQIKP-------- 62
Cdd:cd05839    1 LEPGDLVWAKCRGYPWYPAEIVDPKDPkegngVPIPVPPdrvlkksnEKLYLVLFFDAkRTWGWLPRNKLRPlgvdeeld 80

                         90       100
                 ....*....|....*....|....*.
gi 427787955  63 ----YEASKEQFSKSSKTAsFKEALE 84
Cdd:cd05839   81 klklSEAKKSKRRKEVRKA-YERACK 105
PWWP_BS69-like cd05841
PWWP domain found in protein BS69, protein kinase C-binding protein 1 (PRKCBP1) and similar ...
 11-95 8.50e-07

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: 47.01  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  11 VWAKMKGFSPWPGKVanptkevkrpalkkpMHC------IFFFGTNNYAWIQEDQI----KPYEASKEQFSKSSKTASFK 80
Cdd:cd05841   10 VWVKLDGFPFWPAKV---------------MGTkdgqvdVRFFGDYDRAWLPSKNVtlhtREIVSTLPDSSESKDKRTLK 74

                         90
                 ....*....|....*
gi 427787955  81 EALEAIEDYVKNLPE 95
Cdd:cd05841   75 KAIKELERHIALLRQ 89
PWWP_MBD5 cd20141
PWWP domain found in methyl-CpG-binding domain protein 5 (MBD5) and similar proteins; MBD5, is ...
 5-85 1.53e-06

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: 46.54  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPMHCiffFGTNNYAWIQEDQIKpyeaskeqfskssktaSFKEALE 84
Cdd:cd20141    1 FNVGDLVWGQIRGFPSWPGKLVSENDVGKTNEGKVWVSW---FGDHSFGQVEPDKLK----------------TLSEGLE 61


                 .
gi 427787955  85 A 85
Cdd:cd20141   62 A 62
PWWP_NSD2_rpt2 cd20165
second PWWP domain found in nuclear SET domain-containing protein 2 (NSD2) and similar ...
 9-87 1.66e-06

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


Pssm-ID: 438993  Cd Length: 96  Bit Score: 46.49  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   9 DPVWAKMKGFSPWPGKVANPtKEVKrPALKKPMHCI-----FFFGTNNYAWIQEDQIKPY----EASKEQFSKSSKTAsF 79
Cdd:cd20165    4 DIIWVKLGNYRWWPAEVCHP-KNVP-PNIQKMKHEIgefpvFFFGSKDYYWTHQARVFPYmegdRGSKYQGGKGIGKV-F 80


                 ....*...
gi 427787955  80 KEALEAIE 87
Cdd:cd20165   81 KNALQEAE 88
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
281-347 4.99e-06

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 47.47  E-value: 4.99e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 281 GFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVK---AGAyKGLTPADVVAASDITFCCVSNSHAA 347
Cdd:COG2085    2 GIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAelgPGA-RAGTNAEAAAAADVVVLAVPYEAVP 70
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 280-329 7.38e-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: 7.38e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 427787955 280 FGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVK-AGAYKGLTPAD 329
Cdd:COG0362    5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAeHGKGKNIVGTY 55
PWWP_PWWP2 cd20140
PWWP domain found in the PWWP domain-containing protein 2 (PWWP2) family; The PWWP2 family ...
 5-82 8.44e-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: 44.17  E-value: 8.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPMH-CIFFFGTNNYAWIQEDQIKPYEASKEQFSKSSKTASFKEA 82
Cdd:cd20140    4 LRVGDIVWGKIHGFPWWPGRILSITVSRDDNGELSTQEaHVSWFGSSTTSYMPCSQLYPFLEDFKLRYNKKKRGPYKEA 82
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
281-341 9.23e-06

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 44.14  E-value: 9.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 427787955  281 GFLGLGNMGQGMVKNLINSGHH--ITVWNRTPSKCRDFVKAGAYK--GLTPADVVAASDITFCCV 341
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEYGVGatAVDNEEAAEEADVVFLAV 65
PWWP_NSD1_rpt2 cd20164
second PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) ...
 9-93 1.11e-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: 44.10  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   9 DPVWAKMKGFSPWPGKVANPtKEVKrPALKKPMHCI-----FFFGTNNYAWIQEDQIKPY----EASKEQFSKSSkTASF 79
Cdd:cd20164    4 EVVWVKVGRYRWWPAEVCHP-KSIP-TNIQKMKHDIgefpvLFFGSNDYLWTHQARVFPYmegdVSSKDKMGKGV-DGTY 80

                         90
                 ....*....|....
gi 427787955  80 KEALEAIEDYVKNL 93
Cdd:cd20164   81 KKALQEAAVRFEEL 94
PWWP_NSD_rpt1 cd20144
first PWWP domain found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
 7-72 5.54e-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: 42.69  E-value: 5.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 427787955   7 IGDPVWAKMKGFSPWPGKVAN-P-----TKEVKRPALKKPMHCIFFFGTNN-YAWIQEDQIKPYEaSKEQFSK 72
Cdd:cd20144    1 VGDLVWAKVSGHPWWPCMVTYdPesglyTKIKGSGGRTYRQYHVQFFGDNGeRGWVSEKSLMPFE-GKEKFEE 72
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 276-341 9.29e-05

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 44.37  E-value: 9.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 427787955 276 SNLKFGFLGLGNMGQGMVKNLINSG---HHITVWNRTPSKcRDFVKA--GAYKGLTPADVVAASDITFCCV 341
Cdd:PRK11880   1 MMKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEK-RAALAEeyGVRAATDNQEAAQEADVVVLAV 70
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 261-351 1.16e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 44.79  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955 261 VERISDVLRSKHVspsnLkfgFLGLGNMGQGMVKNLINSG-HHITVWNRTPSKCRDFVKAGAYKGLTPAD---VVAASDI 336
Cdd:PRK00045 173 AKQIFGDLSGKKV----L---VIGAGEMGELVAKHLAEKGvRKITVANRTLERAEELAEEFGGEAIPLDElpeALAEADI 245

                         90
                 ....*....|....*..
gi 427787955 337 TFCCVSNSHA--AKEMV 351
Cdd:PRK00045 246 VISSTGAPHPiiGKGMV 262
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 280-318 2.05e-04

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 44.01  E-value: 2.05e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 427787955 280 FGFLGLGNMGQGMVKNLINSGHHITVWNRTPSKCRDFVK 318
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVK 42
PWWP_MUM1-like cd06080
PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins; MUM-1, ...
 8-93 3.48e-04

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: 39.54  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   8 GDPVWAKMKGFSPWPG---KVANPTKEVkrpalkkpmhCIFFFGtnnyaWIQEDQ--------IKPYE-ASKEQF----S 71
Cdd:cd06080    4 GDIVWAKYRKYPYWPAvvkSVYKKPKKA----------SVLFLE-----LPPEKKgikvslkkLKPFDcKEKEELleegK 68

                         90       100
                 ....*....|....*....|..
gi 427787955  72 KSSKTASFKEALEAIEDYVKNL 93
Cdd:cd06080   69 ESPYSEDFKEAVELAEDYLIKK 90
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 278-341 4.25e-04

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 42.25  E-value: 4.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 427787955 278 LKFGFLGLGNMGQGMVKNLINSG-----HHITVWNRTPSKCRDFVKAGAYKGLTPADVVAASDITFCCV 341
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGvvppsRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAV 69
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 261-351 8.74e-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: 39.86  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955  261 VERISDVLRSKHVspsnlkfGFLGLGNMGQGMVKNLINSG-HHITVWNRTPSKCRDFVKAGAYKGLTP----ADVVAASD 335
Cdd:pfam01488   3 AKKIFGDLKDKKV-------LLIGAGEMGELVAKHLLAKGaKEVTIANRTIERAQELAEKFGGVEALPlddlKEYLAEAD 75

                          90
                  ....*....|....*...
gi 427787955  336 ITFCCVSNSHA--AKEMV 351
Cdd:pfam01488  76 IVISATSSPTPiiTKEMV 93
PWWP_NSD3_rpt1 cd20163
first PWWP domain found in nuclear SET domain-containing protein 3 (NSD3) and similar proteins; ...
 5-68 1.01e-03

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: 39.53  E-value: 1.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   5 YNIGDPVWAKMKGFSPWPGKVA-NP-----TKEVKRPAlkKPMHCIFFFGTNNYAWIQEDQIKPYEASKE 68
Cdd:cd20163    1 FQVGDLVWSKVGTYPWWPCMVSsDPqlevhTKINTRGA--REYHVQFFSSQPERAWVHEKRVREYKGHKQ 68
PWWP_NSD1_rpt1 cd20161
first PWWP domain found in nuclear receptor-binding SET domain-containing protein 1 (NSD1) and ...
 4-72 1.57e-03

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: 38.61  E-value: 1.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 427787955   4 KYNIGDPVWAKMKGFSPWPGKV-ANPTKEV----KRPALKKP-MHCIFFFGT-NNYAWIQEDQIKPYEaSKEQFSK 72
Cdd:cd20161    3 KYEVGDLVWAKFSRRPWWPCRIcADPLLDThskmKVPSRRPCrQYYVETLGElTEKAWVAAKAVVPFE-GRHQFEE 77
PWWP_PWWP2A cd20152
PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); PWWP2A is a H2A.Z-specific ...
 7-100 1.91e-03

PWWP domain found in PWWP domain-containing protein 2A (PWWP2A); 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 its paralog 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: 438980  Cd Length: 122  Bit Score: 38.45  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427787955   7 IGDPVWAKMKGFSPWPGKVANPTKEVKRPALKKPMHC-IFFFGTNNYAWIQEDQIKPY-EASKEQFSKSSKTASFKEALE 84
Cdd:cd20152   22 VGDIVWAKIYGFPWWPARILAITVSRKDNGLLVRQEArISWFGSPTTSFLALSQLAPFlENFQSRFNKKRKGLYRKAITE 101

                         90
                 ....*....|....*.
gi 427787955  85 AIEDYVKNLPEqpVRS 100
Cdd:cd20152  102 AAKAAKQLTPE--VRA 115
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
288-336 2.15e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 40.88  E-value: 2.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 427787955 288 MGQGMVKNLINSGHHITVWNRTPSKCRDFVkAGAYKGltpADVVAASDI 336
Cdd:PRK09287   1 MGKNLALNIASHGYTVAVYNRTPEKTDEFL-AEEGKG---KKIVPAYTL 45
 
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.
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