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Conserved domains on  [gi|124107614|ref|NP_067633|]
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PR domain zinc finger protein 13 [Homo sapiens]

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 ...
18-119 4.86e-64

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: 207.36  E-value: 4.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE-LVDESGGSPLEWIGLIRAARNSQEQTLEAIADLPGGQIFYR 96
Cdd:cd19197    1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDyLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGGQIFYR 80
                         90       100
                 ....*....|....*....|...
gi 124107614  97 ALRDVQPGEELTVWYSNSLAQWF 119
Cdd:cd19197   81 ALRDIQPGEELTVWYSNSLAQWF 103
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
575-595 5.54e-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: 37.66  E-value: 5.54e-04
                          10        20
                  ....*....|....*....|.
gi 124107614  575 CLYCGKLYSRKYGLKIHMRTH 595
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
578-653 6.54e-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: 6.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124107614 578 CGKLYSRKYGLKIHMrthtgyKPLKCKVCLRPFGDPSNLNkhirLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRH 653
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 ...
137-159 1.76e-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: 36.12  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|...
gi 124107614  137 YICWYCWRTFRYPNSLKAHLRFH 159
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 ...
18-119 4.86e-64

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: 207.36  E-value: 4.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE-LVDESGGSPLEWIGLIRAARNSQEQTLEAIADLPGGQIFYR 96
Cdd:cd19197    1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDyLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGGQIFYR 80
                         90       100
                 ....*....|....*....|...
gi 124107614  97 ALRDVQPGEELTVWYSNSLAQWF 119
Cdd:cd19197   81 ALRDIQPGEELTVWYSNSLAQWF 103
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
14-111 5.43e-05

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: 42.90  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614   14 ADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVR------------GELVDESGGSPLEWIGLIraarN-SQEQ 80
Cdd:pfam00856   6 ATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLwgpylftldedsEYCIDARALYYGNWARFI----NhSCDP 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 124107614   81 TLEAIAD--LPGGQIFYRALRDVQPGEELTVWY 111
Cdd:pfam00856  82 NCEVRVVyvNGGPRIVIFALRDIKPGEELTIDY 114
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
575-595 5.54e-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: 37.66  E-value: 5.54e-04
                          10        20
                  ....*....|....*....|.
gi 124107614  575 CLYCGKLYSRKYGLKIHMRTH 595
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
578-653 6.54e-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: 6.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124107614 578 CGKLYSRKYGLKIHMrthtgyKPLKCKVCLRPFGDPSNLNkhirLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRH 653
Cdd:COG5189  357 CNKKYKNQNGLKYHM------LHGHQNQKLHENPSPEKMN----IFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
588-606 7.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.11e-04
                          10
                  ....*....|....*....
gi 124107614  588 LKIHMRTHTGYKPLKCKVC 606
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPEC 20
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
84-118 9.37e-04

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 39.94  E-value: 9.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 124107614  84 AIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQW 118
Cdd:COG2940   88 CEADEEDGRIFIVALRDIAAGEELTYDYGLDYDEE 122
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
137-159 1.76e-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: 36.12  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|...
gi 124107614  137 YICWYCWRTFRYPNSLKAHLRFH 159
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
92-116 2.51e-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: 2.51e-03
                           10        20
                   ....*....|....*....|....*
gi 124107614    92 QIFYRALRDVQPGEELTVWYSNSLA 116
Cdd:smart00317  98 RIVIFALRDIKPGEELTIDYGSDYA 122
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
620-680 8.40e-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: 39.38  E-value: 8.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124107614 620 IRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSLLAKA-GDGPGAEPGYPPEPGDPK 680
Cdd:cd23512   89 RRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDAKAAVVeGPGPGEIIGSAPRVSAVK 150
 
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 ...
18-119 4.86e-64

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: 207.36  E-value: 4.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE-LVDESGGSPLEWIGLIRAARNSQEQTLEAIADLPGGQIFYR 96
Cdd:cd19197    1 IPAGLRLGPVPGIFKLGKYLSDRKEPGNKKKVRRVRGDyLVDESGSPATEWIGLVRAARNNQEQNLEAIADLPGGQIFYR 80
                         90       100
                 ....*....|....*....|...
gi 124107614  97 ALRDVQPGEELTVWYSNSLAQWF 119
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 ...
8-116 2.88e-21

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: 90.18  E-value: 2.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614   8 PATSVSADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGELVDE---SGGSPLEWIGLIRAARNSQEQTLEA 84
Cdd:cd19192   18 IFTSVVTTTDIPAGTIFGPCVLSFTLGYDIADIALKTTDKRVVPYIFRVDTGacnGSSEPSDWLRLVQPARDRHEQNLEA 97
                         90       100       110
                 ....*....|....*....|....*....|..
gi 124107614  85 IADlPGGQIFYRALRDVQPGEELTVWYSNSLA 116
Cdd:cd19192   98 FRK-NEGQVYFRTLRRIRKGEELLVWYSDELA 128
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
8-122 1.29e-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: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614   8 PATSVSADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGEL---VDESGGSPLEWIGLIRAARNSQEQTLEA 84
Cdd:cd19196   15 AGLGVFSKTWIKEGTEMGPYTGRIVSPEDVDPCKNNNLMWEVFNEDGTVshfIDASQENHRSWMTFVNCARNEQEQNLEV 94
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124107614  85 IAdlPGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIP 122
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 ...
18-112 4.13e-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: 73.77  E-value: 4.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGP------VPGTFKLgKYLSDRREPGPKKkvrmvrgelvdesggSPLEWIGLIRAARNSQEQTLEAIADlpGG 91
Cdd:cd10534    1 LPAGLELVLssipegGLGVFAR-RTIPAGTRFGPLE---------------GVVNWMRFVRPARNEEEQNLVAYQH--GG 62
                         90       100
                 ....*....|....*....|.
gi 124107614  92 QIFYRALRDVQPGEELTVWYS 112
Cdd:cd10534   63 QIYFRTTRDIPPGEELLVWYS 83
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
12-121 8.06e-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: 8.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  12 VSADCCIPAGLRLGPVPG------TFKLGKYLSDRREPGPKKkvrmvrgELVDESGGSPLEWIGLIRAARNSQEQTLEAI 85
Cdd:cd19193   22 VWAEAPIPKGMVFGPYEGeivedeEAADSGYSWQIYKGGKLS-------HYIDAKDESKSNWMRYVNCARNEEEQNLVAF 94
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 124107614  86 ADlpGGQIFYRALRDVQPGEELTVWYSNSLAQWFDI 121
Cdd:cd19193   95 QY--RGKIYYRTCKDIAPGTELLVWYGDEYAKELGI 128
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
62-122 8.59e-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: 65.88  E-value: 8.59e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124107614  62 GSPLEWIGLIRAARNSQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYSNSLAQWFDIP 122
Cdd:cd19198   73 GSTGNWMSYVNCARYAEEQNLIAIQC--QGQIFYESCKEILQGQELLVWYGDCYLQFMGIP 131
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
18-115 3.40e-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: 60.82  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTFKLgKYLSDRREPGPKKKVRMVRGELVDESGGSPLeWIGLIRAARNSQEQTLEAIADlpGGQIFYRA 97
Cdd:cd19201   28 LPEGTRFGPYPGKLVK-EPLDPSYEWKVEAQGSKGGEGLLLLTEDSGT-WLKLVRSADDEDEANLILYFK--GGQIWCEV 103
                         90
                 ....*....|....*...
gi 124107614  98 LRDVQPGEELTVWYSNSL 115
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 ...
18-117 3.18e-09

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: 55.44  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTF------KLGKYLSDRREPGPKKKVRMvrgELVDESGGSpleWIGLIRAARNSQEQTLeaIADLPGG 91
Cdd:cd19194   28 IPKRTQFGPLEGPLvkkselKDNKIHPLELEEDDGEDLYF---DLSDENKCN---WMMFVRPAQNHLEQNL--VAYQYGQ 99
                         90       100
                 ....*....|....*....|....*.
gi 124107614  92 QIFYRALRDVQPGEELTVWYSNSLAQ 117
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 ...
18-116 1.71e-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: 53.19  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVP----GTFKLGKyLSDRREPGP--KKKVRMVRGE-----LVDESGGSPL----------EWIGLIRAARN 76
Cdd:cd19199    7 LPDNLEIRQLEdgseGVFALVP-LVKRTQFGPfeAKRVARLDGFavfplKVFEKDGSVVyldtsneddcNWMMFVRPATD 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 124107614  77 SQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYSNSLA 116
Cdd:cd19199   86 VEHQNLTAYQQ--GEDIYFTTSRDIQPGAELRVWYAAFYA 123
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
18-109 6.23e-08

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: 51.98  E-value: 6.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTFKlgkylSDRREPGPKKKVRMVRGEL---VDESGGSPLEWIGLIRAARNSQEQTLEA--IADlpggQ 92
Cdd:cd19200   34 IEVGEKFGPFVGVQR-----SSVKDPTYAWEIVDEFGKVkfwIDASEPGTGNWMKYIRSAPSCEQQNLMAcqIDE----Q 104
                         90
                 ....*....|....*..
gi 124107614  93 IFYRALRDVQPGEELTV 109
Cdd:cd19200  105 IYYKVVRDIQPGEELLL 121
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
67-117 7.39e-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: 7.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124107614  67 WIGLIRAARNSQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYSNSLAQ 117
Cdd:cd19189   82 WMMFVRKARTREEQNLVAYPH--DGKIYFCTSRDIPPDQELLFYYSRDYAR 130
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
58-119 5.55e-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: 5.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124107614  58 DESGGSpleWIGLIRAARNSQEQTLEAIAdlPGGQIFYRALRDVQPGEELTVWYSNSLAQWF 119
Cdd:cd19191   72 DPSKSS---WMRYIRCARHCGEQNLTVVQ--YRGCIFYRACRDIPRGTELLVWYDDSYTSFF 128
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
18-114 1.64e-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: 47.44  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTfklGKYLSDRREP-------GPKKkvrmvRGELVDESGGSPLEWIGLIRAARNSQEQTLeaIADLPG 90
Cdd:cd19188   28 IPKGRKFGPFVGE---KKKRSQVKNNvymweiyGPKR-----GWMCVDASDPTKGNWLRYVNWARSGEEQNL--FPLQIN 97
                         90       100
                 ....*....|....*....|....
gi 124107614  91 GQIFYRALRDVQPGEELTVWYSNS 114
Cdd:cd19188   98 RAIYYKTLKPIAPGEELLCWYNGE 121
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
57-112 1.94e-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: 47.54  E-value: 1.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124107614  57 VDESGGSPLEWIGLIRAARNSQEQTLEAIADlpGGQIFYRALRDVQPGEELTVWYS 112
Cdd:cd19195   65 IDGSDETKANWMRYVVISREEREQNLLAFQH--SEQIYFRACRDIRPGEKLRVWYS 118
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
18-110 8.35e-06

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: 46.41  E-value: 8.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPG---------TFKLGKYLSDRREPGPKKKVRMVRGEL------VDESGGSPLEWIGLIRAARNSQEQTL 82
Cdd:cd19213   44 IEAGERFGPYTGvqrstlkdtNFGWEQILNDVEVSSQEGCITKIVDDLgnekfcVDAGQAGAGSWLKYIRVACSCDEQNL 123
                         90       100
                 ....*....|....*....|....*...
gi 124107614  83 EAIAdlPGGQIFYRALRDVQPGEELTVW 110
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 ...
18-117 3.25e-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: 43.85  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  18 IPAGLRLGPVPGTfklgKYLSDRREPGPKKKV--RMVR-GEL---VDESGGSPLEWIGLIRAARNSQEQTLeaIADLPGG 91
Cdd:cd19187   27 IPRGTRFGPLVGE----IYTNDPVPKGANRKYfwRIYSnGEFyhyIDGFDPSKSNWMRYVNPAHSLQEQNL--VACQIGM 100
                         90       100
                 ....*....|....*....|....*.
gi 124107614  92 QIFYRALRDVQPGEELTVWYSNSLAQ 117
Cdd:cd19187  101 NIYFYTVKPIPPNQELLVWYCREFAR 126
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
14-111 5.43e-05

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: 42.90  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614   14 ADCCIPAGLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVR------------GELVDESGGSPLEWIGLIraarN-SQEQ 80
Cdd:pfam00856   6 ATEDIPKGEFIGEYVEVLLITKEEADKRELLYYDKLELRLwgpylftldedsEYCIDARALYYGNWARFI----NhSCDP 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 124107614   81 TLEAIAD--LPGGQIFYRALRDVQPGEELTVWY 111
Cdd:pfam00856  82 NCEVRVVyvNGGPRIVIFALRDIKPGEELTIDY 114
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
21-114 3.77e-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: 41.12  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124107614  21 GLRLGPVPGTFKLGKYLSDRREPGPKKKVRMVRGE---LVDESGGSPLEWIGLIRAARNSQEQTLEAIADlpGGQIFYRA 97
Cdd:cd19190   31 GEKFGPFAGEKRMPNELDESMDPRLMWEVRGSKGEvlyILDASNPRHSNWLRFVHEAPSQEQKNLAAIQE--GENIFYLA 108
                         90
                 ....*....|....*..
gi 124107614  98 LRDVQPGEELTVWYSNS 114
Cdd:cd19190  109 VDDIETDTELLIGYLDS 125
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
575-595 5.54e-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: 37.66  E-value: 5.54e-04
                          10        20
                  ....*....|....*....|.
gi 124107614  575 CLYCGKLYSRKYGLKIHMRTH 595
Cdd:pfam00096   3 CPDCGKSFSRKSNLKRHLRTH 23
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
578-653 6.54e-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: 6.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124107614 578 CGKLYSRKYGLKIHMrthtgyKPLKCKVCLRPFGDPSNLNkhirLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRH 653
Cdd:COG5189  357 CNKKYKNQNGLKYHM------LHGHQNQKLHENPSPEKMN----IFSAKDKPYRCEVCDKRYKNLNGLKYHRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
588-606 7.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 7.11e-04
                          10
                  ....*....|....*....
gi 124107614  588 LKIHMRTHTGYKPLKCKVC 606
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPEC 20
SET COG2940
SET domain-containing protein (function unknown) [General function prediction only];
84-118 9.37e-04

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


Pssm-ID: 442183 [Multi-domain]  Cd Length: 134  Bit Score: 39.94  E-value: 9.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 124107614  84 AIADLPGGQIFYRALRDVQPGEELTVWYSNSLAQW 118
Cdd:COG2940   88 CEADEEDGRIFIVALRDIAAGEELTYDYGLDYDEE 122
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
602-623 1.60e-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: 36.12  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|..
gi 124107614  602 KCKVCLRPFGDPSNLNKHIRLH 623
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
137-159 1.76e-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: 36.12  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|...
gi 124107614  137 YICWYCWRTFRYPNSLKAHLRFH 159
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
92-116 2.51e-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: 2.51e-03
                           10        20
                   ....*....|....*....|....*
gi 124107614    92 QIFYRALRDVQPGEELTVWYSNSLA 116
Cdd:smart00317  98 RIVIFALRDIKPGEELTIDYGSDYA 122
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
630-653 5.83e-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: 5.83e-03
                          10        20
                  ....*....|....*....|....
gi 124107614  630 YRCEFCGKVLVRRRDLERHVKSRH 653
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24
zf-BED pfam02892
BED zinc finger;
614-654 6.16e-03

BED zinc finger;


Pssm-ID: 427043  Cd Length: 44  Bit Score: 35.04  E-value: 6.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 124107614  614 SNLNKHIRLHAEGNTPYRCEFCGKVLVRRRD---LERHVKSRHP 654
Cdd:pfam02892   1 SKVWKYFRELPLDETKAVCRYCGKILSRGGGtsnLIRHLRRKHP 44
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
620-680 8.40e-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: 39.38  E-value: 8.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124107614 620 IRLHAEGNTPYRCEFCGKVLVRRRDLERHVKSRHPGQSLLAKA-GDGPGAEPGYPPEPGDPK 680
Cdd:cd23512   89 RRLPVDPTMRFHCSACGKAFRLRFSAEHHVKLRHPSDAKAAVVeGPGPGEIIGSAPRVSAVK 150
SET cd08161
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain superfamily; The Su(var)3-9, ...
66-111 8.52e-03

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.


Pssm-ID: 380914 [Multi-domain]  Cd Length: 72  Bit Score: 35.69  E-value: 8.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 124107614  66 EWIGLIRAARNSQEQTLEAIADLPGG--QIFYRALRDVQPGEELTVWY 111
Cdd:cd08161   24 EVIGLARFINHSCEPNCEFEEVYVGGkpRVFIVALRDIKAGEELTVDY 71
 
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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