NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|642918051|ref|XP_972552|]
View 

uncharacterized protein LOC661288 [Tribolium castaneum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 309-423 2.49e-24

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: 98.04  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  309 LPSFLQLME-TNTEHGLGVWAKMDIEEFTQFGPLVGKVvkevdisedsnmrdiweifvdsknvyfstenletsNWMRFVR 387
Cdd:cd10534     1 LPAGLELVLsSIPEGGLGVFARRTIPAGTRFGPLEGVV-----------------------------------NWMRFVR 45

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 642918051  388 PAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd10534    46 PARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVW 81
FYVE_like_SF super family cl28890
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 435-495 8.86e-05

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


The actual alignment was detected with superfamily member cd15740:

Pssm-ID: 333710 [Multi-domain]  Cd Length: 54  Bit Score: 41.52  E-value: 8.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642918051  435 EKNSCGGCNMTFAhplyyrthcsvfhdirfSLTIRKYHCKVCGAAVLGKENIMKHAAELHN 495
Cdd:cd15740     4 EKQTCKGCNESFN-----------------SITKRRHHCKQCGAVICGKCSEFKDLASRHN 47
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 596-618 1.34e-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: 1.34e-03
                           10        20
                   ....*....|....*....|...
gi 642918051   596 CSCSRCGKHFQNKSNLKIHMLTH 618
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 309-423 2.49e-24

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: 98.04  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  309 LPSFLQLME-TNTEHGLGVWAKMDIEEFTQFGPLVGKVvkevdisedsnmrdiweifvdsknvyfstenletsNWMRFVR 387
Cdd:cd10534     1 LPAGLELVLsSIPEGGLGVFARRTIPAGTRFGPLEGVV-----------------------------------NWMRFVR 45

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 642918051  388 PAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd10534    46 PARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVW 81
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 321-423 6.86e-08

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: 52.34  E-value: 6.86e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051    321 EHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDIWEI----FVDSKNVYFStENLETSNWMRFVRPAPTRDDRN 396
Cdd:smart00317   10 GKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkafyLFDIDSDLCI-DARRKGNLARFINHSCEPNCEL 88

                            90       100
                    ....*....|....*....|....*...
gi 642918051    397 ITV-VAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:smart00317   89 LFVeVNGDDRIVIFALRDIKPGEELTID 116
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
 435-495 8.86e-05

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 41.52  E-value: 8.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642918051  435 EKNSCGGCNMTFAhplyyrthcsvfhdirfSLTIRKYHCKVCGAAVLGKENIMKHAAELHN 495
Cdd:cd15740     4 EKQTCKGCNESFN-----------------SITKRRHHCKQCGAVICGKCSEFKDLASRHN 47
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 323-423 1.45e-04

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: 42.51  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051   323 GLGVWAKMDIEEFTQFGPLVGK-VVKEVDISEDSNMRDIWEIFVDSKNVYFSTENLET----------SNWMRFVRPApt 391
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEycidaralyyGNWARFINHS-- 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 642918051   392 rDDRN----ITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:pfam00856   79 -CDPNcevrVVYVNGGPRIVIFALRDIKPGEELTID 113
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 596-618 1.34e-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: 1.34e-03
                           10        20
                   ....*....|....*....|...
gi 642918051   596 CSCSRCGKHFQNKSNLKIHMLTH 618
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 309-423 2.49e-24

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: 98.04  E-value: 2.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  309 LPSFLQLME-TNTEHGLGVWAKMDIEEFTQFGPLVGKVvkevdisedsnmrdiweifvdsknvyfstenletsNWMRFVR 387
Cdd:cd10534     1 LPAGLELVLsSIPEGGLGVFARRTIPAGTRFGPLEGVV-----------------------------------NWMRFVR 45

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 642918051  388 PAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd10534    46 PARNEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVW 81
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 305-423 2.50e-22

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: 94.07  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  305 AYVSLPSFLQLMETNTEHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISE--DSNMRDIWEIFVDSKNV-YFSTENLETSN 381
Cdd:cd19189     2 ARLSLPRQLYLRQSETGAEVGVWTKETIPVRTCFGPLIGQQSHSAEVADwtDKAAPHIWKIYHNDVLEfCIITTDENECN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 642918051  382 WMRFVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19189    82 WMMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFY 123
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 307-423 2.48e-20

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: 88.15  E-value: 2.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  307 VSLPSFLQLMETNT-EHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDIWEIFVDSKNVYF-STENLETSNWMR 384
Cdd:cd19187     1 ASLPRNLTLKYSSVgREVLGVWSSDYIPRGTRFGPLVGEIYTNDPVPKGANRKYFWRIYSNGEFYHYiDGFDPSKSNWMR 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 642918051  385 FVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19187    81 YVNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVW 119
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 305-423 1.06e-19

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: 86.25  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  305 AYVSLPSFLQLMETNtEHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDiWEIFVDSKNVYFSTENLETSNWMR 384
Cdd:cd19194     2 ARASLPLILQIFRFG-ETLGGVFAKRRIPKRTQFGPLEGPLVKKSELKDNKIHPL-ELEEDDGEDLYFDLSDENKCNWMM 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 642918051  385 FVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19194    80 FVRPAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVW 118
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 301-434 2.76e-18

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: 82.42  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  301 QFIFAYVSLPSFLQLMETNT-EHGLGVWAKMDIEEFTQFGPLVGKVVKEVdisedSNMRDIWEIFVDSKNVYFSTENLE- 378
Cdd:cd19200     2 VYIPEDIPIPPDFELRESAAvGAGLGVWTKVRIEVGEKFGPFVGVQRSSV-----KDPTYAWEIVDEFGKVKFWIDASEp 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 642918051  379 -TSNWMRFVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYWQDSSIPSKKKM 434
Cdd:cd19200    77 gTGNWMKYIRSAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMKAAVYPHETM 133
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 305-423 4.23e-16

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: 75.91  E-value: 4.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  305 AYVSLPSFLQLmeTNTEHGL-GVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRdiweIFV-DSKNVYFSTENLETSNW 382
Cdd:cd19199     3 ARSSLPDNLEI--RQLEDGSeGVFALVPLVKRTQFGPFEAKRVARLDGFAVFPLK----VFEkDGSVVYLDTSNEDDCNW 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 642918051  383 MRFVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19199    77 MMFVRPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVW 117
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 309-423 4.35e-16

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: 76.28  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  309 LPSFLQLMETN---TEHgLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDIWEIFVDSKNVYFSTENLETSNWMRF 385
Cdd:cd19198     3 LPEGLRVLQTSfggTPH-YGVFCKKTIPKGTRFGPFRGRVVNTSEIKTYDDNSFMWEIFEDGKLSHFIDGRGSTGNWMSY 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 642918051  386 VRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19198    82 VNCARYAEEQNLIAIQCQGQIFYESCKEILQGQELLVW 119
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 300-428 6.57e-16

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: 75.47  E-value: 6.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  300 NQFIFAYVSLPSflqlmetnteHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDIWEIFVDSKNV-YF---STE 375
Cdd:cd19196     3 SQVIIAQSSIPG----------AGLGVFSKTWIKEGTEMGPYTGRIVSPEDVDPCKNNNLMWEVFNEDGTVsHFidaSQE 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 642918051  376 NleTSNWMRFVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYWQDSSI 428
Cdd:cd19196    73 N--HRSWMTFVNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSY 123
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 308-423 1.24e-15

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: 74.30  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  308 SLPSFLQLMETNTEHGL--GVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNmrDIWEIFVDSKNvYFSTENLETSNWMRF 385
Cdd:cd19201     2 SLPGELELRKPSQDAGRsgGVWAKQPLPEGTRFGPYPGKLVKEPLDPSYEW--KVEAQGSKGGE-GLLLLTEDSGTWLKL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 642918051  386 VRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19201    79 VRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILV 116
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 322-423 4.70e-15

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: 73.04  E-value: 4.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  322 HGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMrdiWEIFVDSK-NVYFSTENLETSNWMRFVRPAPTRDDRNITVV 400
Cdd:cd19193    18 AGLGVWAEAPIPKGMVFGPYEGEIVEDEEAADSGYS---WQIYKGGKlSHYIDAKDESKSNWMRYVNCARNEEEQNLVAF 94

                          90       100
                  ....*....|....*....|...
gi 642918051  401 AKDSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19193    95 QYRGKIYYRTCKDIAPGTELLVW 117
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 324-423 4.71e-14

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: 70.16  E-value: 4.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  324 LGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMrdiWEIFVDSKNVY-FSTENLETSNWMRFVRPAPTRDDRNITVVAK 402
Cdd:cd19188    20 IGVWAKKSIPKGRKFGPFVGEKKKRSQVKNNVYM---WEIYGPKRGWMcVDASDPTKGNWLRYVNWARSGEEQNLFPLQI 96

                          90       100
                  ....*....|....*....|.
gi 642918051  403 DSSLYFVSIKAIKNGEELLYW 423
Cdd:cd19188    97 NRAIYYKTLKPIAPGEELLCW 117
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 323-427 3.79e-13

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: 67.50  E-value: 3.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  323 GLGVWAKMDIEEFTQFGPLVG-KVVKEVDISEDSNMRDIWEIFVDSKNV--YFSTENLETSNWMRFVRPAPTRDDRNITV 399
Cdd:cd19191    16 GYGICAAQRIPQGTWIGPFEGvLVSPEKQIGAVRNTQHLWEIYDQEGTLqhFIDGGDPSKSSWMRYIRCARHCGEQNLTV 95

                          90       100
                  ....*....|....*....|....*...
gi 642918051  400 VAKDSSLYFVSIKAIKNGEELLYWQDSS 427
Cdd:cd19191    96 VQYRGCIFYRACRDIPRGTELLVWYDDS 123
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 325-423 5.10e-12

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: 64.37  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  325 GVWAKMDIEEFTQFGPLVGkvvkevDISEDSNMRDIWEIFVDSKNVYF--------STENLETSNWMRFVRPAPTRDDRN 396
Cdd:cd19192    21 SVVTTTDIPAGTIFGPCVL------SFTLGYDIADIALKTTDKRVVPYifrvdtgaCNGSSEPSDWLRLVQPARDRHEQN 94

                          90       100
                  ....*....|....*....|....*...
gi 642918051  397 ITVVAKDSS-LYFVSIKAIKNGEELLYW 423
Cdd:cd19192    95 LEAFRKNEGqVYFRTLRRIRKGEELLVW 122
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 307-429 5.27e-12

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: 65.28  E-value: 5.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  307 VSLPSFLQLMETNTE-HGLGVWAKMDIEEFTQFGPLVG---KVVKEVDISEDSNMRD---------IWEIFVDSKNVYFS 373
Cdd:cd19213    18 IPIPSDFELRESSIPgAGLGVWAKRKIEAGERFGPYTGvqrSTLKDTNFGWEQILNDvevssqegcITKIVDDLGNEKFC 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 642918051  374 TENLE--TSNWMRFVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELL-YWQDSSIP 429
Cdd:cd19213    98 VDAGQagAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLvYVKDGVYP 156
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 309-421 9.83e-12

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: 63.47  E-value: 9.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  309 LPSFLQLMETNTEHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDIWEIFVDSKNVYF--STENLETSNWMRFV 386
Cdd:cd19190     5 VPDRFSLKSSKVQDGMGLYTARRVKKGEKFGPFAGEKRMPNELDESMDPRLMWEVRGSKGEVLYilDASNPRHSNWLRFV 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 642918051  387 RPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELL 421
Cdd:cd19190    85 HEAPSQEQKNLAAIQEGENIFYLAVDDIETDTELL 119
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 307-434 7.20e-11

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: 61.88  E-value: 7.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  307 VSLPSFLQLMETNTE-HGLGVWAKMDIEEFTQFGPLVGKvvkevdisEDSNMRDI---WEIFVDSKNVYFSTE--NLETS 380
Cdd:cd19214    28 IPIPSEFELRESNIPgTGLGIWTKRKIEVGEKFGPYVGE--------QRSNLKDPsygWEVLDEFGNVKFCIDasQPDVG 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 642918051  381 NWMRFVRPAPTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYWQDSSIPSKKKM 434
Cdd:cd19214   100 SWLKYIRFAGCYDQHNLVACQINDQIFYRAVADIDPGEELLLFMKSEDYSHETM 153
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 310-424 3.49e-09

PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 (also termed zinc finger protein 408 (ZNF408)) may be involved in transcriptional regulation.


Pssm-ID: 380918  Cd Length: 121  Bit Score: 55.89  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051  310 PSFLQlmetntEHGLGVWAKMD-IEEFTQFGPLVGKVVKEvDISEDSNMRdiweIFVDSKNVYFStENLETSNWMRFVRP 388
Cdd:cd10520    13 PSLAQ------EERLGVWCVGDaLQKGTFLGPLEEELESH-DLTEGGSPR----QEESGQSGDVL-ACEQSSKWMRFACR 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 642918051  389 APTRDDRNITVVAKDSSLYFVSIKAIKNGEELLYWQ 424
Cdd:cd10520    81 ARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLWP 116
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 321-423 6.86e-08

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: 52.34  E-value: 6.86e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051    321 EHGLGVWAKMDIEEFTQFGPLVGKVVKEVDISEDSNMRDIWEI----FVDSKNVYFStENLETSNWMRFVRPAPTRDDRN 396
Cdd:smart00317   10 GKGWGVRATEDIPKGEFIGEYVGEIITSEEAEERPKAYDTDGAkafyLFDIDSDLCI-DARRKGNLARFINHSCEPNCEL 88

                            90       100
                    ....*....|....*....|....*...
gi 642918051    397 ITV-VAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:smart00317   89 LFVeVNGDDRIVIFALRDIKPGEELTID 116
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
 435-495 8.86e-05

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 41.52  E-value: 8.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 642918051  435 EKNSCGGCNMTFAhplyyrthcsvfhdirfSLTIRKYHCKVCGAAVLGKENIMKHAAELHN 495
Cdd:cd15740     4 EKQTCKGCNESFN-----------------SITKRRHHCKQCGAVICGKCSEFKDLASRHN 47
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 323-423 1.45e-04

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: 42.51  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642918051   323 GLGVWAKMDIEEFTQFGPLVGK-VVKEVDISEDSNMRDIWEIFVDSKNVYFSTENLET----------SNWMRFVRPApt 391
Cdd:pfam00856    1 GRGLFATEDIPKGEFIGEYVEVlLITKEEADKRELLYYDKLELRLWGPYLFTLDEDSEycidaralyyGNWARFINHS-- 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 642918051   392 rDDRN----ITVVAKDSSLYFVSIKAIKNGEELLYW 423
Cdd:pfam00856   79 -CDPNcevrVVYVNGGPRIVIFALRDIKPGEELTID 113
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 596-618 1.34e-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: 1.34e-03
                           10        20
                   ....*....|....*....|...
gi 642918051   596 CSCSRCGKHFQNKSNLKIHMLTH 618
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH