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Conserved domains on  [gi|124107612|ref|NP_001074240|]
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PR domain zinc finger protein 13 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 66-167 5.71e-63

PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits.


:

Pssm-ID: 380974  Cd Length: 103  Bit Score: 205.44  E-value: 5.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE-LVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYR 144
Cdd:cd19197    1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDyLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGGQIFYR 80

                         90       100
                 ....*....|....*....|...
gi 124107612 145 ALRDVQPGEELTVWYSNSLAQWF 167
Cdd:cd19197   81 ALRDIQPGEELTVWYSNSLAQWF 103
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 622-642 4.71e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 4.71e-04
                          10        20
                  ....*....|....*....|.
gi 124107612  622 CLYCGKLYSRKYGLKIHMRTH 642
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
635-653 6.80e-04

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.80e-04
                          10
                  ....*....|....*....
gi 124107612  635 LKIHMRTHTGYKPLKCKVC 653
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPEC 20
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 625-700 7.27e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 7.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124107612 625 CGKLYSRKYGLKIHMrthtgyKPLKCKVCLRPFGDPSNLNkhirLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRH 700
Cdd:COG5189  357 CNKKYKNQNGLKYHM------LHGHQNQKLHENPSPEKMN----IFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 185-207 1.48e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|...
gi 124107612  185 YICWYCWRTFRYPNSLKAHLRFH 207
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 66-167 5.71e-63

PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits.


Pssm-ID: 380974  Cd Length: 103  Bit Score: 205.44  E-value: 5.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE-LVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYR 144
Cdd:cd19197    1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDyLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGGQIFYR 80

                         90       100
                 ....*....|....*....|...
gi 124107612 145 ALRDVQPGEELTVWYSNSLAQWF 167
Cdd:cd19197   81 ALRDIQPGEELTVWYSNSLAQWF 103
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 62-159 5.64e-06

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 45.98  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612   62 ADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVR------------GELVDESGGSPLEWIGLIRAARNPQEQT 129
Cdd:pfam00856   6 ATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLwgpylftldedsEYCIDARALYYGNWARFINHSCDPNCEV 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 124107612  130 lEAIADLPGGQIFYRALRDVQPGEELTVWY 159
Cdd:pfam00856  86 -RVVYVNGGPRIVIFALRDIKPGEELTIDY 114
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 622-642 4.71e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 4.71e-04
                          10        20
                  ....*....|....*....|.
gi 124107612  622 CLYCGKLYSRKYGLKIHMRTH 642
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
635-653 6.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.80e-04
                          10
                  ....*....|....*....
gi 124107612  635 LKIHMRTHTGYKPLKCKVC 653
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPEC 20
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 625-700 7.27e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 7.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124107612 625 CGKLYSRKYGLKIHMrthtgyKPLKCKVCLRPFGDPSNLNkhirLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRH 700
Cdd:COG5189  357 CNKKYKNQNGLKYHM------LHGHQNQKLHENPSPEKMN----IFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
132-166 1.04e-03

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 39.94  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 124107612 132 AIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQW 166
Cdd:COG2940   88 CEADEEDGRIFIVALRDIAAGEELTYDYGLDYDEE 122
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 649-670 1.33e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|..
gi 124107612  649 KCKVCLRPFGDPSNLNKHIRLH 670
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 185-207 1.48e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|...
gi 124107612  185 YICWYCWRTFRYPNSLKAHLRFH 207
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 115-164 2.45e-03

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 38.47  E-value: 2.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 124107612   115 WIGLIRAARNPQEQtLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLA 164
Cdd:smart00317  74 LARFINHSCEPNCE-LLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYA 122
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
 667-715 3.80e-03

Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial component of the parasitic protozoan's KREPA RNA editing complex. Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. However, the C-terminal zinc-finger domain in KREPA1 has additional amino acids. KREPA1 is involved in the insertion sub-complex of editing activities and interacts with KREPA6 of the 20S editosome core complex. When KREPA1 is down-regulated, insertion editing is preferentially inhibited.


Pssm-ID: 467777  Cd Length: 449  Bit Score: 40.54  E-value: 3.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 124107612 667 IRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSlMAKAGDGPGP 715
Cdd:cd23512   89 RRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDA-KAAVVEGPGP 136
 
Name Accession Description Interval E-value
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 66-167 5.71e-63

PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 (also termed PR domain-containing protein 13) may be involved in transcriptional regulation. It mediates the balance of inhibitory and excitatory neurons in somatosensory circuits.


Pssm-ID: 380974  Cd Length: 103  Bit Score: 205.44  E-value: 5.71e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE-LVDESGGSPLEWIGLIRAARNPQEQTLEAIADLPGGQIFYR 144
Cdd:cd19197    1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDyLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGGQIFYR 80

                         90       100
                 ....*....|....*....|...
gi 124107612 145 ALRDVQPGEELTVWYSNSLAQWF 167
Cdd:cd19197   81 ALRDIQPGEELTVWYSNSLAQWF 103
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 58-164 1.16e-20

PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 (also termed PR domain-containing protein 8) may function as histone methyltransferase, preferentially acting on 'Lys-9' of histone H3.


Pssm-ID: 380969  Cd Length: 131  Bit Score: 88.26  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  58 TSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDE---SGGSPLEWIGLIRAARNPQEQTLEAIA 134
Cdd:cd19192   20 TSVVTTTDIPAGTIFGPCVLSFTLGYDIADIALKTTDKRVVPYIFRVDTGacnGSSEPSDWLRLVQPARDRHEQNLEAFR 99

                         90       100       110
                 ....*....|....*....|....*....|
gi 124107612 135 DlPGGQIFYRALRDVQPGEELTVWYSNSLA 164
Cdd:cd19192  100 K-NEGQVYFRTLRRIRKGEELLVWYSDELA 128
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 56-170 1.28e-18

PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 (also termed PR domain-containing protein 12) acts as a transcription factor that is involved in the positive regulation of histone H3-K9 dimethylation.


Pssm-ID: 380973 [Multi-domain]  Cd Length: 130  Bit Score: 82.40  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  56 SATSVNADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGEL---VDESGGSPLEWIGLIRAARNPQEQTLEA 132
Cdd:cd19196   15 AGLGVFSKTWIKEGTEMGPYTGRIVSPEDVDPCKNNNLMWEVFNEDGTVshfIDASQENHRSWMTFVNCARNEQEQNLEV 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124107612 133 IAdlPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIP 170
Cdd:cd19196   95 VQ--IGESIYYRAIKDIPPDQELLVWYGNSYNTFLGIP 130
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 66-160 2.46e-16

PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family of proteins is defined based on the conserved N-terminal PR domain, which is closely related to the Su(var)3-9, enhancer of zeste, and trithorax (SET) domains of histone methyltransferases, and is specifically called PR-SET domain. The family consists of 17 members in primates. PRDMs play diverse roles in cell-cycle regulation, differentiation, and meiotic recombination. The family also contains zinc finger protein ZFPM1 and ZFPM2. ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380932  Cd Length: 83  Bit Score: 74.54  E-value: 2.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGP------VPGTFKLgKYLSDRREPGPKKkvrmvrgelvdesggSPLEWIGLIRAARNPQEQTLEAIADlpGG 139
Cdd:cd10534    1 LPAGLELVLssipegGLGVFAR-RTIPAGTRFGPLE---------------GVVNWMRFVRPARNEEEQNLVAYQH--GG 62

                         90       100
                 ....*....|....*....|.
gi 124107612 140 QIFYRALRDVQPGEELTVWYS 160
Cdd:cd10534   63 QIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 110-170 1.27e-13

PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 (also termed PR domain-containing protein 14) acts as a transcription factor that has both positive and negative roles on transcription. It acts on regulating epigenetic modifications in the cells, playing a key role in the regulation of cell pluripotency, epigenetic reprogramming, differentiation and development. Aberrant PRDM14 expression is associated with tumorigenesis, cell migration and cell chemotherapeutic drugs resistance.


Pssm-ID: 380975  Cd Length: 133  Bit Score: 68.19  E-value: 1.27e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124107612 110 GSPLEWIGLIRAARNPQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIP 170
Cdd:cd19198   73 GSTGNWMSYVNCARYAEEQNLIAIQC--QGQIFYESCKEILQGQELLVWYGDCYLQFMGIP 131
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 60-169 9.18e-13

PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar proteins; PRDM7 (also termed PR domain-containing protein 7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. It selectively catalyzes the trimethylation of H3 lysine 4 (H3K4me3). PRDM9 (also termed PR domain-containing protein 9) is a histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 (H3K4me3) during meiotic prophase and is essential for proper meiotic progression. It also efficiently mono-, di-, and trimethylates H3K36. Aberrant PRDM9 expression is assciated with with genome instability in cancer.


Pssm-ID: 380970 [Multi-domain]  Cd Length: 129  Bit Score: 65.72  E-value: 9.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  60 VNADCCIPAGLRLGPVPG------TFKLGKYLSDRREPGPKKkvrmvrgELVDESGGSPLEWIGLIRAARNPQEQTLEAI 133
Cdd:cd19193   22 VWAEAPIPKGMVFGPYEGeivedeEAADSGYSWQIYKGGKLS-------HYIDAKDESKSNWMRYVNCARNEEEQNLVAF 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 124107612 134 ADlpGGQIFYRALRDVQPGEELTVWYSNSLAQWFDI 169
Cdd:cd19193   95 QY--RGKIYYRTCKDIAPGTELLVWYGDEYAKELGI 128
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 66-163 2.86e-11

PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also termed friend of GATA protein 1, FOG-1, friend of GATA 1, zinc finger protein 89A, or zinc finger protein multitype 1) functions as a transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. ZFPM2 (also termed friend of GATA protein 2, FOG-2, friend of GATA 2, zinc finger protein 89B, or zinc finger protein multitype 2) functions as a transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis.


Pssm-ID: 380978  Cd Length: 122  Bit Score: 61.21  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTFKLgKYLSDRREPGPKKKVRMVRGELVDESGGSPLeWIGLIRAARNPQEQTLEAIADlpGGQIFYRA 145
Cdd:cd19201   28 LPEGTRFGPYPGKLVK-EPLDPSYEWKVEAQGSKGGEGLLLLTEDSGT-WLKLVRSADDEDEANLILYFK--GGQIWCEV 103

                         90
                 ....*....|....*...
gi 124107612 146 LRDVQPGEELTVWYSNSL 163
Cdd:cd19201  104 TKDIPPGEELILVLREPL 121
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 66-165 1.36e-08

PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 (also termed PR domain-containing protein 10, or tristanin) may be involved in transcriptional regulation.


Pssm-ID: 380971  Cd Length: 128  Bit Score: 53.89  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTF------KLGKYLSDRREPGPKKKVRMvrgELVDESGGSpleWIGLIRAARNPQEQTLeaIADLPGG 139
Cdd:cd19194   28 IPKRTQFGPLEGPLvkkselKDNKIHPLELEEDDGEDLYF---DLSDENKCN---WMMFVRPAQNHLEQNL--VAYQYGQ 99

                         90       100
                 ....*....|....*....|....*.
gi 124107612 140 QIFYRALRDVQPGEELTVWYSNSLAQ 165
Cdd:cd19194  100 EIYFTTIKNIEPKQELKVWYAASYAE 125
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 66-164 3.12e-08

PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 (also termed PR domain-containing protein 15, or zinc finger protein 298 (ZNF298)) may be involved in transcriptional regulation. It plays an essential role as a chromatin factor that modulates the transcription of upstream regulators of WNT and MAPK-ERK signaling to safeguard naive pluripotency.


Pssm-ID: 380976  Cd Length: 126  Bit Score: 52.80  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVP----GTFKLGKyLSDRREPGP--KKKVRMVRGE-----LVDESGGSPL----------EWIGLIRAARN 124
Cdd:cd19199    7 LPDNLEIRQLEdgseGVFALVP-LVKRTQFGPfeAKRVARLDGFavfplKVFEKDGSVVyldtsneddcNWMMFVRPATD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124107612 125 PQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYSNSLA 164
Cdd:cd19199   86 VEHQNLTAYQQ--GEDIYFTTSRDIQPGAELRVWYAAFYA 123
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 115-165 7.56e-08

PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 (also termed PR domain-containing protein 4, or PFM1) may function as a transcription factor involved in cell differentiation.


Pssm-ID: 380966  Cd Length: 133  Bit Score: 51.70  E-value: 7.56e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124107612 115 WIGLIRAARNPQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYSNSLAQ 165
Cdd:cd19189   82 WMMFVRKARTREEQNLVAYPH--DGKIYFCTSRDIPPDQELLFYYSRDYAR 130
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 66-157 3.80e-07

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus protein and similar proteins; PRDM16 (also termed PR domain-containing protein 16, transcription factor MEL1, or MDS1/EVI1-like gene 1) functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells. It is closely related to paralog of PRDM3 (also termed MDS1 and EVI1 complex locus protein, ecotropic virus integration site 1 protein, EVI-1, myelodysplasia syndrome 1 protein, myelodysplasia syndrome-associated protein 1, or MECOM) which is a nuclear transcription factor essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). PRDM3 and PRDM16 are both directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380977  Cd Length: 135  Bit Score: 49.67  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTFKlgkylSDRREPGPKKKVRMVRGEL---VDESGGSPLEWIGLIRAARNPQEQTLEA--IADlpggQ 140
Cdd:cd19200   34 IEVGEKFGPFVGVQR-----SSVKDPTYAWEIVDEFGKVkfwIDASEPGTGNWMKYIRSAPSCEQQNLMAcqIDE----Q 104

                         90
                 ....*....|....*..
gi 124107612 141 IFYRALRDVQPGEELTV 157
Cdd:cd19200  105 IYYKVVRDIQPGEELLL 121
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 106-167 1.07e-06

PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 (also termed PR domain-containing protein 6) is a putative histone-lysine N-methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. It may specifically methylate 'Lys-20' of histone H4 when associated with other proteins and in vitro.


Pssm-ID: 380968  Cd Length: 128  Bit Score: 48.24  E-value: 1.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124107612 106 DESGGSpleWIGLIRAARNPQEQTLEAIAdlPGGQIFYRALRDVQPGEELTVWYSNSLAQWF 167
Cdd:cd19191   72 DPSKSS---WMRYIRCARHCGEQNLTVVQ--YRGCIFYRACRDIPRGTELLVWYDDSYTSFF 128
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 105-160 2.65e-06

PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 (also termed PR domain-containing protein 11) may be involved in transcription regulation.


Pssm-ID: 380972  Cd Length: 127  Bit Score: 47.16  E-value: 2.65e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124107612 105 VDESGGSPLEWIGLIRAARNPQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYS 160
Cdd:cd19195   65 IDGSDETKANWMRYVVISREEREQNLLAFQH--SEQIYFRACRDIRPGEKLRVWYS 118
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 62-159 5.64e-06

SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases). A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure.


Pssm-ID: 459965 [Multi-domain]  Cd Length: 115  Bit Score: 45.98  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612   62 ADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVR------------GELVDESGGSPLEWIGLIRAARNPQEQT 129
Cdd:pfam00856   6 ATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLwgpylftldedsEYCIDARALYYGNWARFINHSCDPNCEV 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 124107612  130 lEAIADLPGGQIFYRALRDVQPGEELTVWY 159
Cdd:pfam00856  86 -RVVYVNGGPRIVIFALRDIKPGEELTIDY 114
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 66-162 6.14e-06

PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 (also termed GATA-3-binding protein G3B, lysine N-methyltransferase 8, MTB-or MTE-binding protein, PR domain-containing protein 2, retinoblastoma protein-interacting zinc finger protein, or zinc finger protein RIZ) is S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. It may function as a DNA-binding transcription factor.


Pssm-ID: 380965  Cd Length: 123  Bit Score: 45.90  E-value: 6.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTfklGKYLSDRREP-------GPKKkvrmvRGELVDESGGSPLEWIGLIRAARNPQEQTLeaIADLPG 138
Cdd:cd19188   28 IPKGRKFGPFVGE---KKKRSQVKNNvymweiyGPKR-----GWMCVDASDPTKGNWLRYVNWARSGEEQNL--FPLQIN 97

                         90       100
                 ....*....|....*....|....
gi 124107612 139 GQIFYRALRDVQPGEELTVWYSNS 162
Cdd:cd19188   98 RAIYYKTLKPIAPGEELLCWYNGE 121
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 66-158 2.11e-05

PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, also termed PR domain-containing protein 16, or transcription factor MEL1, or MDS1/EVI1-like gene 1, functions as a transcriptional regulator. PRDM16 is preferentially expressed by hematopoietic and neuronal stem cells and is closely related to paralog of PRDM3, both of which are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380990  Cd Length: 162  Bit Score: 45.25  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPG---------TFKLGKYLSDRREPGPKKKVRMVRGEL------VDESGGSPLEWIGLIRAARNPQEQTL 130
Cdd:cd19213   44 IEAGERFGPYTGvqrstlkdtNFGWEQILNDVEVSSQEGCITKIVDDLgnekfcVDAGQAGAGSWLKYIRVACSCDEQNL 123

                         90       100
                 ....*....|....*....|....*...
gi 124107612 131 EAIAdlPGGQIFYRALRDVQPGEELTVW 158
Cdd:cd19213  124 TACQ--INEQIYYKVIKDIEPGEELLVY 149
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 66-165 8.14e-05

PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 (also termed BLIMP-1, beta-interferon gene positive regulatory domain I-binding factor, PR domain-containing protein 1, positive regulatory domain I-binding factor 1, PRDI-BF1, or PRDI-binding factor 1) acts as a transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs.


Pssm-ID: 380964 [Multi-domain]  Cd Length: 128  Bit Score: 43.08  E-value: 8.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  66 IPAGLRLGPVPGTfklgKYLSDRREPGPKKKV--RMVR-GEL---VDESGGSPLEWIGLIRAARNPQEQTLeaIADLPGG 139
Cdd:cd19187   27 IPRGTRFGPLVGE----IYTNDPVPKGANRKYfwRIYSnGEFyhyIDGFDPSKSNWMRYVNPAHSLQEQNL--VACQIGM 100

                         90       100
                 ....*....|....*....|....*.
gi 124107612 140 QIFYRALRDVQPGEELTVWYSNSLAQ 165
Cdd:cd19187  101 NIYFYTVKPIPPNQELLVWYCREFAR 126
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 622-642 4.71e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 4.71e-04
                          10        20
                  ....*....|....*....|.
gi 124107612  622 CLYCGKLYSRKYGLKIHMRTH 642
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 69-162 6.07e-04

PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 (also termed PR domain-containing protein 5) is a sequence-specific DNA-binding transcription factor that represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1.


Pssm-ID: 380967  Cd Length: 127  Bit Score: 40.35  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107612  69 GLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE---LVDESGGSPLEWIGLIRAARNPQEQTLEAIADlpGGQIFYRA 145
Cdd:cd19190   31 GEKFGPFAGEKRMPNELDESMDPRLMWEVRGSKGEvlyILDASNPRHSNWLRFVHEAPSQEQKNLAAIQE--GENIFYLA 108

                         90
                 ....*....|....*..
gi 124107612 146 LRDVQPGEELTVWYSNS 162
Cdd:cd19190  109 VDDIETDTELLIGYLDS 125
zf-H2C2_2 pfam13465
Zinc-finger double domain;
635-653 6.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.80e-04
                          10
                  ....*....|....*....
gi 124107612  635 LKIHMRTHTGYKPLKCKVC 653
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPEC 20
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 625-700 7.27e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 42.78  E-value: 7.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124107612 625 CGKLYSRKYGLKIHMrthtgyKPLKCKVCLRPFGDPSNLNkhirLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRH 700
Cdd:COG5189  357 CNKKYKNQNGLKYHM------LHGHQNQKLHENPSPEKMN----IFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
132-166 1.04e-03

SET domain-containing protein (function unknown) [General function prediction only];


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 39.94  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 124107612 132 AIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQW 166
Cdd:COG2940   88 CEADEEDGRIFIVALRDIAAGEELTYDYGLDYDEE 122
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 649-670 1.33e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|..
gi 124107612  649 KCKVCLRPFGDPSNLNKHIRLH 670
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 185-207 1.48e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.51  E-value: 1.48e-03
                          10        20
                  ....*....|....*....|...
gi 124107612  185 YICWYCWRTFRYPNSLKAHLRFH 207
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 115-164 2.45e-03

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on outlier plant homologues


Pssm-ID: 214614 [Multi-domain]  Cd Length: 124  Bit Score: 38.47  E-value: 2.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 124107612   115 WIGLIRAARNPQEQtLEAIADLPGGQIFYRALRDVQPGEELTVWYSNSLA 164
Cdd:smart00317  74 LARFINHSCEPNCE-LLFVEVNGDDRIVIFALRDIKPGEELTIDYGSDYA 122
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
 667-715 3.80e-03

Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial component of the parasitic protozoan's KREPA RNA editing complex. Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. However, the C-terminal zinc-finger domain in KREPA1 has additional amino acids. KREPA1 is involved in the insertion sub-complex of editing activities and interacts with KREPA6 of the 20S editosome core complex. When KREPA1 is down-regulated, insertion editing is preferentially inhibited.


Pssm-ID: 467777  Cd Length: 449  Bit Score: 40.54  E-value: 3.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 124107612 667 IRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSlMAKAGDGPGP 715
Cdd:cd23512   89 RRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDA-KAAVVEGPGP 136
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 677-700 5.69e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.93  E-value: 5.69e-03
                          10        20
                  ....*....|....*....|....
gi 124107612  677 YRCEFCGKVLVRRRDLERHVKSRH 700
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24
zf-BED pfam02892
BED zinc finger;
661-701 6.13e-03

BED zinc finger;


Pssm-ID: 427043  Cd Length: 44  Bit Score: 35.04  E-value: 6.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 124107612  661 SNLNKHIRLHAEGNTPYRCEFCGKVLVRRRD---LERHVKSRHP 701
Cdd:pfam02892   1 SKVWKYFRELPLDETKAVCRYCGKILSRGGGtsnLIRHLRRKHP 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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