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Conserved domains on  [gi|1622920637|ref|XP_028701147|]
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PR domain zinc finger protein 15 isoform X3 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SET super family cl40432
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
1-50 1.04e-30

SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, Enhancer-of-zeste, Trithorax (SET) domain superfamily corresponds to SET domain-containing lysine methyltransferases, which catalyze site and state-specific methylation of lysine residues in histones that are fundamental in epigenetic regulation of gene activation and silencing in eukaryotic organisms. 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 has 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 N-SET and C-SET. C-SET forms an unusual and conserved knot-like structure of probable functional importance. In addition to N-SET and C-SET, an insert region (I-SET) and flanking regions of high structural variability form part of the overall structure. Some family members contain a pre-SET domain, which is found in a number of histone methyltransferases (HMTase), and a post-SET domain, which harbors a zinc-binding site.


The actual alignment was detected with superfamily member cd19199:

Pssm-ID: 394802  Cd Length: 126  Bit Score: 117.52  E-value: 1.04e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 50
Cdd:cd19199     77 MMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
560-729 1.41e-06

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  560 CSICNRRFALKATYHAHMVIHRENLPdPNVQKYIHPCEICGRIFNSIGNLERHK--LIHTG--VKSHAC--EQCGKSFAR 633
Cdd:COG5048    257 ASESPRSSLPTASSQSSSPNESDSSS-EKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSR 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  634 KDMLKEHMRVHDNVREYLC--AECGKGMKTK-----HALRHHMKLHKGIKEYEC--KECHRRFAQKINMLKHCKRHT--G 702
Cdd:COG5048    336 NDALKRHILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfR 415
                          170       180
                   ....*....|....*....|....*..
gi 1622920637  703 IKDFMCELCGKTFSERNTMETHKLIHT 729
Cdd:COG5048    416 PYNCKNPPCSKSFNRHYNLIPHKKIHT 442
PRK10819 super family cl35954
transport protein TonB; Provisional
111-195 7.81e-04

transport protein TonB; Provisional


The actual alignment was detected with superfamily member PRK10819:

Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 42.36  E-value: 7.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  111 PPgsQSEAAAPEKEQDtPRGDPPAVPENENVAP-----KEQKKKPRRGRKPKASKAEQPLVIVEDKEPAEQVAEIITEVP 185
Cdd:PRK10819    60 PP--QAVQPPPEPVVE-PEPEPEPIPEPPKEAPvvipkPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTA 136
                           90
                   ....*....|
gi 1622920637  186 PDEPVSATPD 195
Cdd:PRK10819   137 PARPTSSTAT 146
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
256-278 3.91e-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: 35.74  E-value: 3.91e-03
                           10        20
                   ....*....|....*....|...
gi 1622920637  256 YQCNICSKIFQNSSNLSRHVRSH 278
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
1-50 1.04e-30

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: 117.52  E-value: 1.04e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 50
Cdd:cd19199     77 MMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
560-729 1.41e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  560 CSICNRRFALKATYHAHMVIHRENLPdPNVQKYIHPCEICGRIFNSIGNLERHK--LIHTG--VKSHAC--EQCGKSFAR 633
Cdd:COG5048    257 ASESPRSSLPTASSQSSSPNESDSSS-EKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSR 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  634 KDMLKEHMRVHDNVREYLC--AECGKGMKTK-----HALRHHMKLHKGIKEYEC--KECHRRFAQKINMLKHCKRHT--G 702
Cdd:COG5048    336 NDALKRHILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfR 415
                          170       180
                   ....*....|....*....|....*..
gi 1622920637  703 IKDFMCELCGKTFSERNTMETHKLIHT 729
Cdd:COG5048    416 PYNCKNPPCSKSFNRHYNLIPHKKIHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
608-633 1.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.42e-04
                           10        20
                   ....*....|....*....|....*.
gi 1622920637  608 NLERHKLIHTGVKSHACEQCGKSFAR 633
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PRK10819 PRK10819
transport protein TonB; Provisional
111-195 7.81e-04

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 42.36  E-value: 7.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  111 PPgsQSEAAAPEKEQDtPRGDPPAVPENENVAP-----KEQKKKPRRGRKPKASKAEQPLVIVEDKEPAEQVAEIITEVP 185
Cdd:PRK10819    60 PP--QAVQPPPEPVVE-PEPEPEPIPEPPKEAPvvipkPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTA 136
                           90
                   ....*....|
gi 1622920637  186 PDEPVSATPD 195
Cdd:PRK10819   137 PARPTSSTAT 146
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
256-278 3.91e-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: 35.74  E-value: 3.91e-03
                           10        20
                   ....*....|....*....|...
gi 1622920637  256 YQCNICSKIFQNSSNLSRHVRSH 278
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
1-50 1.04e-30

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: 117.52  E-value: 1.04e-30
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 50
Cdd:cd19199     77 MMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
1-50 7.10e-21

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: 89.33  E-value: 7.10e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 50
Cdd:cd19194     78 MMFVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFL 127
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
1-42 5.76e-18

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: 79.55  E-value: 5.76e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 42
Cdd:cd10534     41 MRFVRPARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWY 82
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
1-50 2.79e-15

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: 73.65  E-value: 2.79e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 50
Cdd:cd19189     83 MMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQL 132
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
1-49 4.34e-12

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: 64.27  E-value: 4.34e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKK 49
Cdd:cd19187     79 MRYVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARR 127
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
1-48 6.42e-11

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: 60.71  E-value: 6.42e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAK 48
Cdd:cd19193     77 MRYVNCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAK 124
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
1-54 2.91e-10

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: 59.33  E-value: 2.91e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKMDKPM 54
Cdd:cd19198     79 MSYVNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVWYGDCYLQFMGIPV 132
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
1-50 2.65e-09

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: 56.40  E-value: 2.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 50
Cdd:cd19195     76 MRYVVISREEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRL 125
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
1-53 1.78e-08

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: 53.90  E-value: 1.78e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKMDKP 53
Cdd:cd19196     78 MTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGIP 130
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
1-42 7.85e-07

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: 49.35  E-value: 7.85e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHG-SDVYFTTSRDIPPGTELRVWY 42
Cdd:cd19192     81 LRLVQPARDRHEQNLEAFRKNeGQVYFRTLRRIRKGEELLVWY 123
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
1-42 8.64e-07

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: 49.01  E-value: 8.64e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 42
Cdd:cd19191     79 MRYIRCARHCGEQNLTVVQYRGCIFYRACRDIPRGTELLVWY 120
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
560-729 1.41e-06

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.01  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  560 CSICNRRFALKATYHAHMVIHRENLPdPNVQKYIHPCEICGRIFNSIGNLERHK--LIHTG--VKSHAC--EQCGKSFAR 633
Cdd:COG5048    257 ASESPRSSLPTASSQSSSPNESDSSS-EKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSR 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  634 KDMLKEHMRVHDNVREYLC--AECGKGMKTK-----HALRHHMKLHKGIKEYEC--KECHRRFAQKINMLKHCKRHT--G 702
Cdd:COG5048    336 NDALKRHILLHTSISPAKEklLNSSSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfR 415
                          170       180
                   ....*....|....*....|....*..
gi 1622920637  703 IKDFMCELCGKTFSERNTMETHKLIHT 729
Cdd:COG5048    416 PYNCKNPPCSKSFNRHYNLIPHKKIHT 442
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
1-42 2.75e-06

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: 47.34  E-value: 2.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 42
Cdd:cd19201     76 LKLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVL 117
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
3-43 9.82e-06

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: 45.20  E-value: 9.82e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622920637    3 LVRPAAEAEHQNLTAYQ--HGSDVYFTTSRDIPPGTELRVWYA 43
Cdd:cd19197     54 LVRAARNNQEQNLEAIAdlPGGQIFYRALRDIQPGEELTVWYS 96
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
1-42 1.71e-05

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: 45.12  E-value: 1.71e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 42
Cdd:cd19188     77 LRYVNWARSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWY 118
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
247-700 1.73e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 48.54  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  247 KQLGEHKRVYQCNICSKIFQNSSNLSRHVRSH-GDKLFKC--EECAKLFSRKESLKQHVSYKHSRNEVDGEYRyRCGTCE 323
Cdd:COG5048     25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHtGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKS-LPLSNS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  324 KTFRIESALE-FHNCRTGLIAHPGEGGPGGSRLRDLPDDKTF----QCEMCFRFF--STNSNLSKHKKKHGDKKFACEVC 396
Cdd:COG5048    104 KASSSSLSSSsSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNlrnnPLPGNNSSSvnTPQSNSLHPPLPANSLSKDPSSN 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  397 SKMFYRKDVMLDHqRRHLEGVRRVKREDLEAGGENLV-RYKKEPSGCPVCGKVFSCRSNMNKHLLTHGDKKYT-CEICGR 474
Cdd:COG5048    184 LSLLISSNVSTSI-PSSSENSPLSSSYSIPSSSSDQNlENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSsASESPR 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  475 KFFRVDVLRDHIHVHFkdialmdDHQREEFIGKIGISSEENDDNSDESaDSEPHKYSCkrcqltfgrgkeylKHIMEVHK 554
Cdd:COG5048    263 SSLPTASSQSSSPNES-------DSSSEKGFSLPIKSKQCNISFSRSS-PLTRHLRSV--------------NHSGESLK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  555 EKGYGCSICNRRFALKATYHAHMVIHrenLPDPNVQKYIhpcEICGRIFNSIGNLERHKLIH-----TGVKSHACE--QC 627
Cdd:COG5048    321 PFSCPYSLCGKLFSRNDALKRHILLH---TSISPAKEKL---LNSSSKFSPLLNNEPPQSLQqykdlKNDKKSETLsnSC 394
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622920637  628 GKSFARKDMLKEHMRVHDNVREYLC--AECGKGMKTKHALRHHMKLHKgIKEYECKECHRRFaqkiNMLKHCKRH 700
Cdd:COG5048    395 IRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHT-NHAPLLCSILKSF----RRDLDLSNH 464
zf-H2C2_2 pfam13465
Zinc-finger double domain;
608-633 1.42e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 39.66  E-value: 1.42e-04
                           10        20
                   ....*....|....*....|....*.
gi 1622920637  608 NLERHKLIHTGVKSHACEQCGKSFAR 633
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
1-47 6.97e-04

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: 40.81  E-value: 6.97e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622920637    1 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY-AAFYA 47
Cdd:cd19200     82 MKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMkAAVYP 129
PRK10819 PRK10819
transport protein TonB; Provisional
111-195 7.81e-04

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 42.36  E-value: 7.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622920637  111 PPgsQSEAAAPEKEQDtPRGDPPAVPENENVAP-----KEQKKKPRRGRKPKASKAEQPLVIVEDKEPAEQVAEIITEVP 185
Cdd:PRK10819    60 PP--QAVQPPPEPVVE-PEPEPEPIPEPPKEAPvvipkPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTA 136
                           90
                   ....*....|
gi 1622920637  186 PDEPVSATPD 195
Cdd:PRK10819   137 PARPTSSTAT 146
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
622-644 1.57e-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: 36.89  E-value: 1.57e-03
                           10        20
                   ....*....|....*....|...
gi 1622920637  622 HACEQCGKSFARKDMLKEHMRVH 644
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
106-175 2.29e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 41.82  E-value: 2.29e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622920637  106 QAKSLPPGSQSEAAAPEKEQDTPRGDPPAVPENENVAP----KEQKKKPRRGRKPKASKAEQPlvivED--KEPAE 175
Cdd:PRK01297    13 EAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAAPAAAApraeKPKKDKPRRERKPKPASLWKL----EDfvVEPQE 84
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
256-278 3.91e-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: 35.74  E-value: 3.91e-03
                           10        20
                   ....*....|....*....|...
gi 1622920637  256 YQCNICSKIFQNSSNLSRHVRSH 278
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
584-646 7.72e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 7.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622920637  584 LPDPNVQKYIHPCEICGRIFNSIGNLERHKLIHTGVKSHACEQCGKSFARKDM--LKEHMRVHDN 646
Cdd:COG5048     24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHN 88
 
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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