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Conserved domains on  [gi|954563610|ref|XP_014605678|]
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PREDICTED: MDS1 and EVI1 complex locus protein EVI1-B-like isoform X3 [Polistes canadensis]

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, ...
 148-256 5.90e-21

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 cd19201:

Pssm-ID: 394802  Cd Length: 122  Bit Score: 89.33  E-value: 5.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  148 QEWVSLVPEVEVGGSAPGgpqVRARKDIPRGTRFGPFSCKWVR-------------IVGSGSKGWLDASHESRNWLKYIR 214
Cdd:cd19201     4 PGELELRKPSQDAGRSGG---VWAKQPLPEGTRFGPYPGKLVKepldpsyewkveaQGSKGGEGLLLLTEDSGTWLKLVR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 954563610  215 STASPHLVNLKHILIGGEIIYETIRDIAIGEELFLGLREPLQ 256
Cdd:cd19201    81 SADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLREPLL 122
zf-H2C2_2 pfam13465
Zinc-finger double domain;
854-878 2.94e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 2.94e-06
                           10        20
                   ....*....|....*....|....*
gi 954563610   854 NLTRHLRTHTGEQPYKCKYCERSFS 878
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 840-862 8.47e-06

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: 43.06  E-value: 8.47e-06
                           10        20
                   ....*....|....*....|...
gi 954563610   840 YSCKFCGKVFPRSANLTRHLRTH 862
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PTZ00395 super family cl33180
Sec24-related protein; Provisional
 468-648 3.97e-05

Sec24-related protein; Provisional


The actual alignment was detected with superfamily member PTZ00395:

Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 47.76  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  468 STTP-TGPPGTMPQLpSSAPSPFLVYPRPPVSlpgGLPFY-PPSLMAPYPGI-FPNAPnFLNSPLIFPPKLDETEKPNRS 544
Cdd:PTZ00395  410 SNAGySNPGNSNPGY-NNAPNSNTPYNNPPNS---NTPYSnPPNSNPPYSNLpYSNTP-YSNAPLSNAPPSSAKDHHSAY 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  545 ESPRKERFTPPRIHSQHSKISPSA----GEEATSLFRPSPARPLVQQQQQQQPTSESEEDQS-KRRDNVGQQSNEKKMEI 619
Cdd:PTZ00395  485 HAAYQHRAANQPAANLPTANQPAAnnfhGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGIaKREDHPEGGTNRQKYEQ 564

                         170       180       190
                  ....*....|....*....|....*....|.
gi 954563610  620 --ETSNNASSTEESTDQplDLRVQTKKQDVF 648
Cdd:PTZ00395  565 sdEESVESSSSENSSEN--ENEVTDKGEEIY 593
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 415-437 1.19e-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: 37.28  E-value: 1.19e-03
                           10        20
                   ....*....|....*....|...
gi 954563610   415 FQCEVCFKAYTQFSNLCRHKRMH 437
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 868-891 2.89e-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: 2.89e-03
                           10        20
                   ....*....|....*....|....
gi 954563610   868 YKCKYCERSFSISSNLQRHVRnIH 891
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
 
Name Accession Description Interval E-value
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 148-256 5.90e-21

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: 89.33  E-value: 5.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  148 QEWVSLVPEVEVGGSAPGgpqVRARKDIPRGTRFGPFSCKWVR-------------IVGSGSKGWLDASHESRNWLKYIR 214
Cdd:cd19201     4 PGELELRKPSQDAGRSGG---VWAKQPLPEGTRFGPYPGKLVKepldpsyewkveaQGSKGGEGLLLLTEDSGTWLKLVR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 954563610  215 STASPHLVNLKHILIGGEIIYETIRDIAIGEELFLGLREPLQ 256
Cdd:cd19201    81 SADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLREPLL 122
zf-H2C2_2 pfam13465
Zinc-finger double domain;
854-878 2.94e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 2.94e-06
                           10        20
                   ....*....|....*....|....*
gi 954563610   854 NLTRHLRTHTGEQPYKCKYCERSFS 878
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 840-862 8.47e-06

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: 43.06  E-value: 8.47e-06
                           10        20
                   ....*....|....*....|...
gi 954563610   840 YSCKFCGKVFPRSANLTRHLRTH 862
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 468-648 3.97e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 47.76  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  468 STTP-TGPPGTMPQLpSSAPSPFLVYPRPPVSlpgGLPFY-PPSLMAPYPGI-FPNAPnFLNSPLIFPPKLDETEKPNRS 544
Cdd:PTZ00395  410 SNAGySNPGNSNPGY-NNAPNSNTPYNNPPNS---NTPYSnPPNSNPPYSNLpYSNTP-YSNAPLSNAPPSSAKDHHSAY 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  545 ESPRKERFTPPRIHSQHSKISPSA----GEEATSLFRPSPARPLVQQQQQQQPTSESEEDQS-KRRDNVGQQSNEKKMEI 619
Cdd:PTZ00395  485 HAAYQHRAANQPAANLPTANQPAAnnfhGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGIaKREDHPEGGTNRQKYEQ 564

                         170       180       190
                  ....*....|....*....|....*....|.
gi 954563610  620 --ETSNNASSTEESTDQplDLRVQTKKQDVF 648
Cdd:PTZ00395  565 sdEESVESSSSENSSEN--ENEVTDKGEEIY 593
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 169-249 4.82e-05

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: 43.86  E-value: 4.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610    169 VRARKDIPRGTRFGPFSC---------------KWVRIVGS-----GSKGWLDAShESRNWLKYIRSTASPHLVNLKHIL 228
Cdd:smart00317   15 VRATEDIPKGEFIGEYVGeiitseeaeerpkayDTDGAKAFylfdiDSDLCIDAR-RKGNLARFINHSCEPNCELLFVEV 93

                            90       100
                    ....*....|....*....|..
gi 954563610    229 IGGE-IIYETIRDIAIGEELFL 249
Cdd:smart00317   94 NGDDrIVIFALRDIKPGEELTI 115
ZnF_C2H2 smart00355
zinc finger;
840-862 8.33e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 8.33e-04
                            10        20
                    ....*....|....*....|...
gi 954563610    840 YSCKFCGKVFPRSANLTRHLRTH 862
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 415-437 1.19e-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: 37.28  E-value: 1.19e-03
                           10        20
                   ....*....|....*....|...
gi 954563610   415 FQCEVCFKAYTQFSNLCRHKRMH 437
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
840-891 1.51e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 954563610  840 YSCKFCGKVFPRSANLTRHLRTHTGEQPYKCKYCER--SFSISSNLQRHVRNIH 891
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 868-891 2.89e-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: 2.89e-03
                           10        20
                   ....*....|....*....|....
gi 954563610   868 YKCKYCERSFSISSNLQRHVRnIH 891
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
835-879 9.12e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 39.08  E-value: 9.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 954563610  835 KIKDRYSCKFCGkvfprSANLTRHLRTHTGEQPYKCKYCERSFSI 879
Cdd:COG3677    12 RWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51
 
Name Accession Description Interval E-value
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 148-256 5.90e-21

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: 89.33  E-value: 5.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  148 QEWVSLVPEVEVGGSAPGgpqVRARKDIPRGTRFGPFSCKWVR-------------IVGSGSKGWLDASHESRNWLKYIR 214
Cdd:cd19201     4 PGELELRKPSQDAGRSGG---VWAKQPLPEGTRFGPYPGKLVKepldpsyewkveaQGSKGGEGLLLLTEDSGTWLKLVR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 954563610  215 STASPHLVNLKHILIGGEIIYETIRDIAIGEELFLGLREPLQ 256
Cdd:cd19201    81 SADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVLREPLL 122
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 165-249 1.28e-16

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: 77.41  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  165 GGPQVRARKDIPRGTRFGPF-----------SCKWVRIVGSGS-KGWLDASH-ESRNWLKYIRSTASPHLVNLKHILIGG 231
Cdd:cd19200    24 AGLGVWTKVRIEVGEKFGPFvgvqrssvkdpTYAWEIVDEFGKvKFWIDASEpGTGNWMKYIRSAPSCEQQNLMACQIDE 103

                          90
                  ....*....|....*...
gi 954563610  232 EIIYETIRDIAIGEELFL 249
Cdd:cd19200   104 QIYYKVVRDIQPGEELLL 121
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 164-247 1.40e-13

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: 66.84  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  164 PGGPQVRARKDIPRGTRFGPFsckwvriVGSgskgwldashesRNWLKYIRSTASPHLVNLKHILIGGEIIYETIRDIAI 243
Cdd:cd10534    14 EGGLGVFARRTIPAGTRFGPL-------EGV------------VNWMRFVRPARNEEEQNLVAYQHGGQIYFRTTRDIPP 74


                  ....
gi 954563610  244 GEEL 247
Cdd:cd10534    75 GEEL 78
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 151-248 2.07e-10

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: 59.55  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  151 VSLVPEVEVGGSA-PG-GPQVRARKDIPRGTRFGPFSCK-------------WVRIVGSGSKGWLDASHESR-NWLKYIR 214
Cdd:cd19193     2 LTLPPGLSIKRSSiPGaGLGVWAEAPIPKGMVFGPYEGEivedeeaadsgysWQIYKGGKLSHYIDAKDESKsNWMRYVN 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 954563610  215 STASPHLVNLKHILIGGEIIYETIRDIAIGEELF 248
Cdd:cd19193    82 CARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELL 115
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 169-247 6.07e-10

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: 57.84  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  169 VRARKDIPRGTRFGPFSCKWVRI-----------VGSGSKGWL--DASHESR-NWLKYIRSTASPHLVNLKHILIGGEII 234
Cdd:cd19188    22 VWAKKSIPKGRKFGPFVGEKKKRsqvknnvymweIYGPKRGWMcvDASDPTKgNWLRYVNWARSGEEQNLFPLQINRAIY 101

                          90
                  ....*....|...
gi 954563610  235 YETIRDIAIGEEL 247
Cdd:cd19188   102 YKTLKPIAPGEEL 114
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 169-247 2.96e-09

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: 56.25  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  169 VRARKDIPRGTRFGPFSCKWVRIV-----GSGSKGW-----------LDASHESRNWLKYIRSTASPHLVNLKHILIGGE 232
Cdd:cd19198    22 VFCKKTIPKGTRFGPFRGRVVNTSeiktyDDNSFMWeifedgklshfIDGRGSTGNWMSYVNCARYAEEQNLIAIQCQGQ 101

                          90
                  ....*....|....*
gi 954563610  233 IIYETIRDIAIGEEL 247
Cdd:cd19198   102 IFYESCKEILQGQEL 116
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 175-248 7.35e-08

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: 51.94  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  175 IPRGTRFGPFSCK----------------WvRIVGSGSK-GWLDASHESR-NWLKYIRSTASPHLVNLKHILIGGEIIYE 236
Cdd:cd19187    27 IPRGTRFGPLVGEiytndpvpkganrkyfW-RIYSNGEFyHYIDGFDPSKsNWMRYVNPAHSLQEQNLVACQIGMNIYFY 105

                          90
                  ....*....|..
gi 954563610  237 TIRDIAIGEELF 248
Cdd:cd19187   106 TVKPIPPNQELL 117
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 162-253 2.31e-07

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: 51.41  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  162 SAPG-GPQVRARKDIPRGTRFGPFSCKWVRIVGSGSKGW-----------------------------LDASHE-SRNWL 210
Cdd:cd19213    30 SIPGaGLGVWAKRKIEAGERFGPYTGVQRSTLKDTNFGWeqilndvevssqegcitkivddlgnekfcVDAGQAgAGSWL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 954563610  211 KYIRSTASPHLVNLKHILIGGEIIYETIRDIAIGEELFLGLRE 253
Cdd:cd19213   110 KYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVYVKD 152
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 147-247 2.84e-06

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: 47.41  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  147 SQEWVSLVPEVEVGGSAPGGPQVRARKDIPRGTRFGPFSCKWV-----------RIVGS-GSKGWLDASHESR-NWLKYI 213
Cdd:cd19199     1 SRARSSLPDNLEIRQLEDGSEGVFALVPLVKRTQFGPFEAKRVarldgfavfplKVFEKdGSVVYLDTSNEDDcNWMMFV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 954563610  214 RSTASPHLVNLKHILIGGEIIYETIRDIAIGEEL 247
Cdd:cd19199    81 RPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAEL 114
zf-H2C2_2 pfam13465
Zinc-finger double domain;
854-878 2.94e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 44.67  E-value: 2.94e-06
                           10        20
                   ....*....|....*....|....*
gi 954563610   854 NLTRHLRTHTGEQPYKCKYCERSFS 878
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFK 25
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 840-862 8.47e-06

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: 43.06  E-value: 8.47e-06
                           10        20
                   ....*....|....*....|...
gi 954563610   840 YSCKFCGKVFPRSANLTRHLRTH 862
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 155-247 1.16e-05

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: 45.81  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  155 PEVEVGGSAPGGPQ--VRARKDIPRGTRFGPFSCkwvRIVGSG--------SKGW------------LDASHES-RNWLK 211
Cdd:cd19196     3 SQVIIAQSSIPGAGlgVFSKTWIKEGTEMGPYTG---RIVSPEdvdpcknnNLMWevfnedgtvshfIDASQENhRSWMT 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 954563610  212 YIRSTASPHLVNLKHILIGGEIIYETIRDIAIGEEL 247
Cdd:cd19196    80 FVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQEL 115
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 169-247 3.16e-05

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: 44.65  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  169 VRARKDIPRGTRFGPFSCKWVR--------------IVGSGSKGWLDASHESR-NWLKYIRStASPHL-VNLKHILIGGE 232
Cdd:cd19194    22 VFAKRRIPKRTQFGPLEGPLVKkselkdnkihplelEEDDGEDLYFDLSDENKcNWMMFVRP-AQNHLeQNLVAYQYGQE 100

                          90
                  ....*....|....*
gi 954563610  233 IIYETIRDIAIGEEL 247
Cdd:cd19194   101 IYFTTIKNIEPKQEL 115
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 468-648 3.97e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 47.76  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  468 STTP-TGPPGTMPQLpSSAPSPFLVYPRPPVSlpgGLPFY-PPSLMAPYPGI-FPNAPnFLNSPLIFPPKLDETEKPNRS 544
Cdd:PTZ00395  410 SNAGySNPGNSNPGY-NNAPNSNTPYNNPPNS---NTPYSnPPNSNPPYSNLpYSNTP-YSNAPLSNAPPSSAKDHHSAY 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  545 ESPRKERFTPPRIHSQHSKISPSA----GEEATSLFRPSPARPLVQQQQQQQPTSESEEDQS-KRRDNVGQQSNEKKMEI 619
Cdd:PTZ00395  485 HAAYQHRAANQPAANLPTANQPAAnnfhGAAGNSVGNPFASRPFGSAPYGGNAATTADPNGIaKREDHPEGGTNRQKYEQ 564

                         170       180       190
                  ....*....|....*....|....*....|.
gi 954563610  620 --ETSNNASSTEESTDQplDLRVQTKKQDVF 648
Cdd:PTZ00395  565 sdEESVESSSSENSSEN--ENEVTDKGEEIY 593
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 169-249 4.82e-05

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: 43.86  E-value: 4.82e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610    169 VRARKDIPRGTRFGPFSC---------------KWVRIVGS-----GSKGWLDAShESRNWLKYIRSTASPHLVNLKHIL 228
Cdd:smart00317   15 VRATEDIPKGEFIGEYVGeiitseeaeerpkayDTDGAKAFylfdiDSDLCIDAR-RKGNLARFINHSCEPNCELLFVEV 93

                            90       100
                    ....*....|....*....|..
gi 954563610    229 IGGE-IIYETIRDIAIGEELFL 249
Cdd:smart00317   94 NGDDrIVIFALRDIKPGEELTI 115
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 169-248 6.61e-05

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: 43.57  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  169 VRARKDIPRGTRFGPFSC------------------KWVRIVGSGSKGWLDASHESRNWLKYIRSTASPHLVNLKHILIG 230
Cdd:cd19192    22 VVTTTDIPAGTIFGPCVLsftlgydiadialkttdkRVVPYIFRVDTGACNGSSEPSDWLRLVQPARDRHEQNLEAFRKN 101

                          90
                  ....*....|....*....
gi 954563610  231 -GEIIYETIRDIAIGEELF 248
Cdd:cd19192   102 eGQVYFRTLRRIRKGEELL 120
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 164-252 9.26e-05

PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; 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) is a nuclear transcription factor, which is essential for the proliferation/maintenance of hematopoietic stem cells (HSCs). It is closely related to paralog PRDM16, both o fwhich are directly linked to various aspects of oncogenic transformation.


Pssm-ID: 380991  Cd Length: 158  Bit Score: 43.77  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 954563610  164 PG-GPQVRARKDIPRGTRFGPFSCKWVRIVGSGSKGW------------LDASH-ESRNWLKYIRSTASPHLVNLKHILI 229
Cdd:cd19214    42 PGtGLGIWTKRKIEVGEKFGPYVGEQRSNLKDPSYGWevldefgnvkfcIDASQpDVGSWLKYIRFAGCYDQHNLVACQI 121

                          90       100
                  ....*....|....*....|...
gi 954563610  230 GGEIIYETIRDIAIGEELFLGLR 252
Cdd:cd19214   122 NDQIFYRAVADIDPGEELLLFMK 144
SET_LegAS4-like cd10522
SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and ...
 194-249 2.37e-04

SET domain found in Legionella pneumophila type IV secretion system effector LegAS4 and similar proteins; LegAS4 is a type IV secretion system effector of Legionella pneumophila. It contains a SET domain that is involved in the modification of Lys4 of histone H3 (H3K4) in the nucleolus of the host cell, thereby enhancing heterochromatic rDNA transcription. It also contains an ankyrin repeat domain of unknown function at its C-terminal region.


Pssm-ID: 380920 [Multi-domain]  Cd Length: 122  Bit Score: 41.94  E-value: 2.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 954563610  194 SGSKGWLDASHeSRNWLKYIRSTASPHLvNLKHILIGGE--IIYETIRDIAIGEELFL 249
Cdd:cd10522    59 NGDILVIDAGK-KGNLTRFINHSDQPNL-ELIVRTLKGEqhIGFVAIRDIKPGEELFI 114
ZnF_C2H2 smart00355
zinc finger;
840-862 8.33e-04

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 37.45  E-value: 8.33e-04
                            10        20
                    ....*....|....*....|...
gi 954563610    840 YSCKFCGKVFPRSANLTRHLRTH 862
Cdd:smart00355    1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 415-437 1.19e-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: 37.28  E-value: 1.19e-03
                           10        20
                   ....*....|....*....|...
gi 954563610   415 FQCEVCFKAYTQFSNLCRHKRMH 437
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
840-891 1.51e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 954563610  840 YSCKFCGKVFPRSANLTRHLRTHTGEQPYKCKYCER--SFSISSNLQRHVRNIH 891
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCdkSFSRPLELSRHLRTHH 87
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 868-891 2.89e-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: 2.89e-03
                           10        20
                   ....*....|....*....|....
gi 954563610   868 YKCKYCERSFSISSNLQRHVRnIH 891
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLR-TH 23
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 840-862 7.04e-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: 7.04e-03
                           10        20
                   ....*....|....*....|...
gi 954563610   840 YSCKFCGKVFPRSANLTRHLRTH 862
Cdd:pfam13894    1 FKCPICGKSFSSKKSLKRHLKTH 23
InsA COG3677
Transposase InsA [Mobilome: prophages, transposons];
835-879 9.12e-03

Transposase InsA [Mobilome: prophages, transposons];


Pssm-ID: 442893 [Multi-domain]  Cd Length: 241  Bit Score: 39.08  E-value: 9.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 954563610  835 KIKDRYSCKFCGkvfprSANLTRHLRTHTGEQPYKCKYCERSFSI 879
Cdd:COG3677    12 RWPNGPVCPHCG-----STRIVKNGKTRNGRQRYRCKDCGRTFTV 51
 
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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