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Conserved domains on  [gi|1804891976|ref|NP_071398|]
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PR domain zinc finger protein 15 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 107-232 6.67e-82

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: 263.12  E-value: 6.67e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  107 AQGRSSLPPNLEIRRLEDGAEGVFAITQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLV 186
Cdd:cd19199      1 SRARSSLPDNLEIRQLEDGSEGVFALVPLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGSVVYLDTSNEDDCNWMMFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1804891976  187 RPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 232
Cdd:cd19199     81 RPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
429-891 7.62e-08

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 7.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  429 KQLGEHKRVYQCNICSKIFQNSSNLSRHVRSH-GDKLFKC--EECAKLFSRKESLKQHVSYKHSRNEVDGEyryrcgtce 505
Cdd:COG5048     25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHtGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS--------- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  506 ktfrIESALEFHNCRTDDKTFQCEMCFRFFSTNSNLskhkkkhgdkkfacevCSKMFYRKDVMLDHQRRHLegvrrvkre 585
Cdd:COG5048     96 ----KSLPLSNSKASSSSLSSSSSNSNDNNLLSSHS----------------LPPSSRDPQLPDLLSISNL--------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  586 dleaggenlvrYKKEPSGCpvcgkvFSCRSNMNKHLLTHGDKKYTCEICGRKFFRVDVLrdHIHVHFKDIALMDDHQREE 665
Cdd:COG5048    147 -----------RNNPLPGN------NSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSS 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  666 FIGKIGISSEENDDNSDESADSePHKYSCKRCQLTFGRGKEYLKHIMEVHkekgygCSICNRRFALKATYHAHMVIHREN 745
Cdd:COG5048    208 SYSIPSSSSDQNLENSSSSLPL-TTNSQLSPKSLLSQSPSSLSSSDSSSS------ASESPRSSLPTASSQSSSPNESDS 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  746 LPdPNVQKYIHPCEICGRIFNSIGNLERHK--LIHTG--VKSHAC--EQCGKSFARKDMLKEHMRVHDNVREYLC--AEC 817
Cdd:COG5048    281 SS-EKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNS 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  818 GKGMKTK-----HALRHHMKLHKGIKEYEC--KECHRRFAQKVNMLKHCKRHT--GIKDFMCELCGKTFSERNTMETHKL 888
Cdd:COG5048    360 SSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKK 439


                   ...
gi 1804891976  889 IHT 891
Cdd:COG5048    440 IHT 442
PRK10819 super family cl35954
transport protein TonB; Provisional
 293-377 9.28e-04

transport protein TonB; Provisional


The actual alignment was detected with superfamily member PRK10819:

Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 42.36  E-value: 9.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  293 PPgsQSEAAAPEKEQDtPRGEPPAVPESENVA-----TKEQKKKPRRGRKPKVSKAEQPLVIVEDKEPTEQVAEIITEVP 367
Cdd:PRK10819    60 PP--QAVQPPPEPVVE-PEPEPEPIPEPPKEApvvipKPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTA 136

                           90
                   ....*....|
gi 1804891976  368 PDEPVSATPD 377
Cdd:PRK10819   137 PARPTSSTAT 146
zf_PR_Knuckle super family cl39781
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 12-37 1.67e-03

PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, SC-1), a member of the PR protein family. PRDM4 is a transcriptional regulator that has been implied in transduction of nerve growth factor signals via the p75 neurotrophin receptor and in cell growth arrest. The short motif is also present in several other PR proteins including human PRDM6 (PRISM), PRDM7, PRDM9 (meisetz), PRDM10 (tristanin), PRDM11, and PRDM15. The conservation of cysteine and histidine residues suggested that this 20 amino acid motif binds zinc, hence the name 'PR zinc knuckle' to distinguish it from the longer (30 amino acid) C2H2-like zinc fingers that are located C-terminally of the PR domain. The PR zinc knuckle fold is similar to that of Gag-knuckles (a beta-hairpin providing two zinc ligands followed by a short helix or a loop providing the other two zinc ligands) and zinc ribbons (two beta-hairpins, each providing two zinc ligands).


The actual alignment was detected with superfamily member pfam18445:

Pssm-ID: 375871  Cd Length: 38  Bit Score: 37.27  E-value: 1.67e-03
                           10        20
                   ....*....|....*....|....*.
gi 1804891976   12 IWCEDCSQYHDSECPELGPVVMVKDS 37
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDT 36
 
Name Accession Description Interval E-value
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 107-232 6.67e-82

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: 263.12  E-value: 6.67e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  107 AQGRSSLPPNLEIRRLEDGAEGVFAITQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLV 186
Cdd:cd19199      1 SRARSSLPDNLEIRQLEDGSEGVFALVPLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGSVVYLDTSNEDDCNWMMFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1804891976  187 RPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 232
Cdd:cd19199     81 RPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
429-891 7.62e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 7.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  429 KQLGEHKRVYQCNICSKIFQNSSNLSRHVRSH-GDKLFKC--EECAKLFSRKESLKQHVSYKHSRNEVDGEyryrcgtce 505
Cdd:COG5048     25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHtGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS--------- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  506 ktfrIESALEFHNCRTDDKTFQCEMCFRFFSTNSNLskhkkkhgdkkfacevCSKMFYRKDVMLDHQRRHLegvrrvkre 585
Cdd:COG5048     96 ----KSLPLSNSKASSSSLSSSSSNSNDNNLLSSHS----------------LPPSSRDPQLPDLLSISNL--------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  586 dleaggenlvrYKKEPSGCpvcgkvFSCRSNMNKHLLTHGDKKYTCEICGRKFFRVDVLrdHIHVHFKDIALMDDHQREE 665
Cdd:COG5048    147 -----------RNNPLPGN------NSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSS 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  666 FIGKIGISSEENDDNSDESADSePHKYSCKRCQLTFGRGKEYLKHIMEVHkekgygCSICNRRFALKATYHAHMVIHREN 745
Cdd:COG5048    208 SYSIPSSSSDQNLENSSSSLPL-TTNSQLSPKSLLSQSPSSLSSSDSSSS------ASESPRSSLPTASSQSSSPNESDS 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  746 LPdPNVQKYIHPCEICGRIFNSIGNLERHK--LIHTG--VKSHAC--EQCGKSFARKDMLKEHMRVHDNVREYLC--AEC 817
Cdd:COG5048    281 SS-EKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNS 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  818 GKGMKTK-----HALRHHMKLHKGIKEYEC--KECHRRFAQKVNMLKHCKRHT--GIKDFMCELCGKTFSERNTMETHKL 888
Cdd:COG5048    360 SSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKK 439


                   ...
gi 1804891976  889 IHT 891
Cdd:COG5048    440 IHT 442
zf-H2C2_2 pfam13465
Zinc-finger double domain;
770-795 1.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 1.18e-04
                           10        20
                   ....*....|....*....|....*.
gi 1804891976  770 NLERHKLIHTGVKSHACEQCGKSFAR 795
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 115-231 2.41e-04

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: 41.94  E-value: 2.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976   115 PNLEIRRLEDGAEGVFAITQLVKRTQFGPF---------ESRRVAKWEKESAFPLKVFQKDGHPVCfDTSNEDdcNWMML 185
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYvgeiitseeAEERPKAYDTDGAKAFYLFDIDSDLCI-DARRKG--NLARF 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1804891976   186 VRPAAEAEHQNLTAYQHG-SDVYFTTSRDIPPGTELRVWYAAFYAKK 231
Cdd:smart00317   78 INHSCEPNCELLFVEVNGdDRIVIFALRDIKPGEELTIDYGSDYANE 124
PRK10819 PRK10819
transport protein TonB; Provisional
 293-377 9.28e-04

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 42.36  E-value: 9.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  293 PPgsQSEAAAPEKEQDtPRGEPPAVPESENVA-----TKEQKKKPRRGRKPKVSKAEQPLVIVEDKEPTEQVAEIITEVP 367
Cdd:PRK10819    60 PP--QAVQPPPEPVVE-PEPEPEPIPEPPKEApvvipKPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTA 136

                           90
                   ....*....|
gi 1804891976  368 PDEPVSATPD 377
Cdd:PRK10819   137 PARPTSSTAT 146
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 128-224 1.11e-03

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: 39.81  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  128 GVFAITQLVKRTQFGPF-ESRRVAKWEKESAFPLKVFQKDGH-------------PVCFDTSNEDDCNWMMLV----RPA 189
Cdd:pfam00856    3 GLFATEDIPKGEFIGEYvEVLLITKEEADKRELLYYDKLELRlwgpylftldedsEYCIDARALYYGNWARFInhscDPN 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1804891976  190 AEAEHQNLTAYQHgsdVYFTTSRDIPPGTELRVWY 224
Cdd:pfam00856   83 CEVRVVYVNGGPR---IVIFALRDIKPGEELTIDY 114
zf_PR_Knuckle pfam18445
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 12-37 1.67e-03

PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, SC-1), a member of the PR protein family. PRDM4 is a transcriptional regulator that has been implied in transduction of nerve growth factor signals via the p75 neurotrophin receptor and in cell growth arrest. The short motif is also present in several other PR proteins including human PRDM6 (PRISM), PRDM7, PRDM9 (meisetz), PRDM10 (tristanin), PRDM11, and PRDM15. The conservation of cysteine and histidine residues suggested that this 20 amino acid motif binds zinc, hence the name 'PR zinc knuckle' to distinguish it from the longer (30 amino acid) C2H2-like zinc fingers that are located C-terminally of the PR domain. The PR zinc knuckle fold is similar to that of Gag-knuckles (a beta-hairpin providing two zinc ligands followed by a short helix or a loop providing the other two zinc ligands) and zinc ribbons (two beta-hairpins, each providing two zinc ligands).


Pssm-ID: 375871  Cd Length: 38  Bit Score: 37.27  E-value: 1.67e-03
                           10        20
                   ....*....|....*....|....*.
gi 1804891976   12 IWCEDCSQYHDSECPELGPVVMVKDS 37
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDT 36
 
Name Accession Description Interval E-value
PR-SET_PRDM15 cd19199
PR-SET domain found in PR domain zinc finger protein 15 (PRDM15) and similar proteins; PRDM15 ...
 107-232 6.67e-82

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: 263.12  E-value: 6.67e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  107 AQGRSSLPPNLEIRRLEDGAEGVFAITQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLV 186
Cdd:cd19199      1 SRARSSLPDNLEIRQLEDGSEGVFALVPLVKRTQFGPFEAKRVARLDGFAVFPLKVFEKDGSVVYLDTSNEDDCNWMMFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1804891976  187 RPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 232
Cdd:cd19199     81 RPATDVEHQNLTAYQQGEDIYFTTSRDIQPGAELRVWYAAFYAKKM 126
PR-SET_PRDM10 cd19194
PR-SET domain found in PR domain zinc finger protein 10 (PRDM10) and similar proteins; PRDM10 ...
 110-232 2.17e-47

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: 165.22  E-value: 2.17e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  110 RSSLPPNLEIRRLEDGAEGVFAITQLVKRTQFGPFESRRVAKWEK--ESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVR 187
Cdd:cd19194      3 RASLPLILQIFRFGETLGGVFAKRRIPKRTQFGPLEGPLVKKSELkdNKIHPLELEEDDGEDLYFDLSDENKCNWMMFVR 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1804891976  188 PAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 232
Cdd:cd19194     83 PAQNHLEQNLVAYQYGQEIYFTTIKNIEPKQELKVWYAASYAEFL 127
PR-SET_PRDM4 cd19189
PR-SET domain found in PR domain zinc finger protein 4 (PRDM4) and similar proteins; PRDM4 ...
 110-232 1.13e-31

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: 120.65  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  110 RSSLPPNLEIRRLEDGAE-GVFAITQLVKRTQFGPF-----ESRRVAKWEKESAFPL-KVFQKDGHPVCFDTSNEDDCNW 182
Cdd:cd19189      3 RLSLPRQLYLRQSETGAEvGVWTKETIPVRTCFGPLigqqsHSAEVADWTDKAAPHIwKIYHNDVLEFCIITTDENECNW 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1804891976  183 MMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 232
Cdd:cd19189     83 MMFVRKARTREEQNLVAYPHDGKIYFCTSRDIPPDQELLFYYSRDYARQL 132
PR-SET_PRDM-like cd10534
PR-SET domain found in PRDM (PRDI-BF1 and RIZ homology domain) family of proteins; PRDM family ...
 113-224 3.38e-28

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: 108.82  E-value: 3.38e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  113 LPPNLEIRRLED--GAEGVFAITQLVKRTQFGPFESRRvakwekesafplkvfqkdghpvcfdtsneddcNWMMLVRPAA 190
Cdd:cd10534      1 LPAGLELVLSSIpeGGLGVFARRTIPAGTRFGPLEGVV--------------------------------NWMRFVRPAR 48

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1804891976  191 EAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 224
Cdd:cd10534     49 NEEEQNLVAYQHGGQIYFRTTRDIPPGEELLVWY 82
PR-SET_PRDM7_9 cd19193
PR-SET domain found in PR domain zinc finger protein 7 (PRDM7) and 9 (PRDM9) and similar ...
 110-230 2.43e-24

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: 99.62  E-value: 2.43e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  110 RSSLPPNLEIRR--LEDGAEGVFAITQLVKRTQFGPFESRRVAKWE-KESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLV 186
Cdd:cd19193      1 RLTLPPGLSIKRssIPGAGLGVWAEAPIPKGMVFGPYEGEIVEDEEaADSGYSWQIYKGGKLSHYIDAKDESKSNWMRYV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1804891976  187 RPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAK 230
Cdd:cd19193     81 NCARNEEEQNLVAFQYRGKIYYRTCKDIAPGTELLVWYGDEYAK 124
PR-SET_PRDM1 cd19187
PR-SET domain found in PR domain zinc finger protein 1 (PRDM1) and similar proteins; PRDM1 ...
 112-231 7.61e-22

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: 92.39  E-value: 7.61e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  112 SLPPNLEIRRLEDGAE--GVFAITQLVKRTQFGPFESRRVAKWEKESAFPLKVF---QKDGHPVCF-DTSNEDDCNWMML 185
Cdd:cd19187      2 SLPRNLTLKYSSVGREvlGVWSSDYIPRGTRFGPLVGEIYTNDPVPKGANRKYFwriYSNGEFYHYiDGFDPSKSNWMRY 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1804891976  186 VRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKK 231
Cdd:cd19187     82 VNPAHSLQEQNLVACQIGMNIYFYTVKPIPPNQELLVWYCREFARR 127
PR-SET_PRDM12 cd19196
PR-SET domain found in PR domain zinc finger protein 12 (PRDM12) and similar proteins; PRDM12 ...
 113-235 3.10e-19

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: 85.10  E-value: 3.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  113 LPPNLEIRR--LEDGAEGVFAITQLVKRTQFGPFESRRVAK----WEKESAFPLKVFQKDGHPVCF-DTSNEDDCNWMML 185
Cdd:cd19196      1 LPSQVIIAQssIPGAGLGVFSKTWIKEGTEMGPYTGRIVSPedvdPCKNNNLMWEVFNEDGTVSHFiDASQENHRSWMTF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1804891976  186 VRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKMDKP 235
Cdd:cd19196     81 VNCARNEQEQNLEVVQIGESIYYRAIKDIPPDQELLVWYGNSYNTFLGIP 130
PR-SET_PRDM14 cd19198
PR-SET domain found in PR domain zinc finger protein 14 (PRDM14) and similar proteins; PRDM14 ...
 128-236 8.17e-18

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: 80.91  E-value: 8.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  128 GVFAITQLVKRTQFGPFESRRV----AKWEKESAFPLKVFQkDGHPVCFDTSNEDDCNWMMLVRPAAEAEHQNLTAYQHG 203
Cdd:cd19198     21 GVFCKKTIPKGTRFGPFRGRVVntseIKTYDDNSFMWEIFE-DGKLSHFIDGRGSTGNWMSYVNCARYAEEQNLIAIQCQ 99

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1804891976  204 SDVYFTTSRDIPPGTELRVWYAAFYAKKMDKPM 236
Cdd:cd19198    100 GQIFYESCKEILQGQELLVWYGDCYLQFMGIPV 132
PR-SET_PRDM11 cd19195
PR-SET domain found in PR domain zinc finger protein 11 (PRDM11) and similar proteins; PRDM11 ...
 112-232 9.83e-18

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: 80.67  E-value: 9.83e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  112 SLPPNLEIRRLEDGAEGVFAITQLVKRTQ-FGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVRPAA 190
Cdd:cd19195      4 TAPQGIEVVKDTSGESDVRCVDEVIPKGHiFGPYEGQICTQDKSSGFFSWLIVDKNNRYKSIDGSDETKANWMRYVVISR 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1804891976  191 EAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWYAAFYAKKM 232
Cdd:cd19195     84 EEREQNLLAFQHSEQIYFRACRDIRPGEKLRVWYSEDYMKRL 125
PR-SET_ZFPM cd19201
PR-SET domain found in zinc finger protein ZFPM1, ZFPM2 and similar proteins; ZFPM1 (also ...
 111-224 1.85e-17

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: 79.70  E-value: 1.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  111 SSLPPNLEIRR---LEDGAEGVFAITQLVKRTQFGPFEsrrvAKWEKESAFP---LKVFQKDG-HPVCFDTSNEDDCNWM 183
Cdd:cd19201      1 LSLPGELELRKpsqDAGRSGGVWAKQPLPEGTRFGPYP----GKLVKEPLDPsyeWKVEAQGSkGGEGLLLLTEDSGTWL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1804891976  184 MLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 224
Cdd:cd19201     77 KLVRSADDEDEANLILYFKGGQIWCEVTKDIPPGEELILVL 117
PR-SET_PRDM2 cd19188
PR-SET domain found in PR domain zinc finger protein 2 (PRDM2) and similar proteins; PRDM2 ...
 113-224 9.00e-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: 69.01  E-value: 9.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  113 LPPNLEIRR--LEDGAEGVFAITQLVKRTQFGPFESRRVAKWE-KESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVRPA 189
Cdd:cd19188      4 LPEELELKPsaVDKTRIGVWAKKSIPKGRKFGPFVGEKKKRSQvKNNVYMWEIYGPKRGWMCVDASDPTKGNWLRYVNWA 83

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1804891976  190 AEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 224
Cdd:cd19188     84 RSGEEQNLFPLQINRAIYYKTLKPIAPGEELLCWY 118
PR-SET_PRDM16_PRDM3 cd19200
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16), MDS1 and EVI1 complex locus ...
 112-229 5.43e-12

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: 64.31  E-value: 5.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  112 SLPPNLEIR--RLEDGAEGVFAITQLVKRTQFGPFES-RRVAKweKESAFPLKVFQKDGH-PVCFDTSNEDDCNWMMLVR 187
Cdd:cd19200      9 PIPPDFELResAAVGAGLGVWTKVRIEVGEKFGPFVGvQRSSV--KDPTYAWEIVDEFGKvKFWIDASEPGTGNWMKYIR 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1804891976  188 PAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY-AAFYA 229
Cdd:cd19200     87 SAPSCEQQNLMACQIDEQIYYKVVRDIQPGEELLLYMkAAVYP 129
PR-SET_PRDM6 cd19191
PR-SET domain found in PR domain zinc finger protein 6 (PRDM6) and similar proteins; PRDM6 ...
 128-224 5.34e-11

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: 61.34  E-value: 5.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  128 GVFAITQLVKRTQFGPFESRRV-----AKWEKESAFPLKVFQKDGHPVCF-DTSNEDDCNWMMLVRPAAEAEHQNLTAYQ 201
Cdd:cd19191     18 GICAAQRIPQGTWIGPFEGVLVspekqIGAVRNTQHLWEIYDQEGTLQHFiDGGDPSKSSWMRYIRCARHCGEQNLTVVQ 97

                           90       100
                   ....*....|....*....|...
gi 1804891976  202 HGSDVYFTTSRDIPPGTELRVWY 224
Cdd:cd19191     98 YRGCIFYRACRDIPRGTELLVWY 120
PR-SET_PRDM8 cd19192
PR-SET domain found in PR domain zinc finger protein 8 (PRDM8) and similar proteins; PRDM8 ...
 122-224 2.28e-09

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: 56.67  E-value: 2.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  122 LEDGAEGVFAITQLVKRTQFGP----FESRRVAKWEKESAFPLK-VFQKDGHPVCFDTSNEDDCNWMMLVRPAAEAEHQN 196
Cdd:cd19192     15 LTDIFTSVVTTTDIPAGTIFGPcvlsFTLGYDIADIALKTTDKRvVPYIFRVDTGACNGSSEPSDWLRLVQPARDRHEQN 94

                           90       100
                   ....*....|....*....|....*....
gi 1804891976  197 LTAYQHG-SDVYFTTSRDIPPGTELRVWY 224
Cdd:cd19192     95 LEAFRKNeGQVYFRTLRRIRKGEELLVWY 123
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
429-891 7.62e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 56.24  E-value: 7.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  429 KQLGEHKRVYQCNICSKIFQNSSNLSRHVRSH-GDKLFKC--EECAKLFSRKESLKQHVSYKHSRNEVDGEyryrcgtce 505
Cdd:COG5048     25 KSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHtGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNS--------- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  506 ktfrIESALEFHNCRTDDKTFQCEMCFRFFSTNSNLskhkkkhgdkkfacevCSKMFYRKDVMLDHQRRHLegvrrvkre 585
Cdd:COG5048     96 ----KSLPLSNSKASSSSLSSSSSNSNDNNLLSSHS----------------LPPSSRDPQLPDLLSISNL--------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  586 dleaggenlvrYKKEPSGCpvcgkvFSCRSNMNKHLLTHGDKKYTCEICGRKFFRVDVLrdHIHVHFKDIALMDDHQREE 665
Cdd:COG5048    147 -----------RNNPLPGN------NSSSVNTPQSNSLHPPLPANSLSKDPSSNLSLLI--SSNVSTSIPSSSENSPLSS 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  666 FIGKIGISSEENDDNSDESADSePHKYSCKRCQLTFGRGKEYLKHIMEVHkekgygCSICNRRFALKATYHAHMVIHREN 745
Cdd:COG5048    208 SYSIPSSSSDQNLENSSSSLPL-TTNSQLSPKSLLSQSPSSLSSSDSSSS------ASESPRSSLPTASSQSSSPNESDS 280

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  746 LPdPNVQKYIHPCEICGRIFNSIGNLERHK--LIHTG--VKSHAC--EQCGKSFARKDMLKEHMRVHDNVREYLC--AEC 817
Cdd:COG5048    281 SS-EKGFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGesLKPFSCpySLCGKLFSRNDALKRHILLHTSISPAKEklLNS 359

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  818 GKGMKTK-----HALRHHMKLHKGIKEYEC--KECHRRFAQKVNMLKHCKRHT--GIKDFMCELCGKTFSERNTMETHKL 888
Cdd:COG5048    360 SSKFSPLlnnepPQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLsfRPYNCKNPPCSKSFNRHYNLIPHKK 439


                   ...
gi 1804891976  889 IHT 891
Cdd:COG5048    440 IHT 442
PR-SET_PRDM5 cd19190
PR-SET domain found in PR domain zinc finger protein 5 (PRDM5) and similar proteins; PRDM5 ...
 117-224 1.18e-07

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: 51.91  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  117 LEIRRLEDGAeGVFAITQLVKRTQFGPFE-SRRVAKWEKESAFPLKVFQKDGHP----VCFDTSNEDDCNWMMLVRPAAE 191
Cdd:cd19190     11 LKSSKVQDGM-GLYTARRVKKGEKFGPFAgEKRMPNELDESMDPRLMWEVRGSKgevlYILDASNPRHSNWLRFVHEAPS 89

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1804891976  192 AEHQNLTAYQHGSDVYFTTSRDIPPGTELRVWY 224
Cdd:cd19190     90 QEQKNLAAIQEGENIFYLAVDDIETDTELLIGY 122
PR-SET_PRDM16 cd19213
PR-SET domain found in PR domain zinc finger protein 16 (PRDM16) and similar proteins; PRDM16, ...
 113-223 1.69e-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: 52.19  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  113 LPPNLEIRR--LEDGAEGVFAITQLVKRTQFGPFES--RRVAK-----WEK-----ESAFPLKVFQKDGHPV-----CFD 173
Cdd:cd19213     20 IPSDFELREssIPGAGLGVWAKRKIEAGERFGPYTGvqRSTLKdtnfgWEQilndvEVSSQEGCITKIVDDLgnekfCVD 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1804891976  174 TSNEDDCNWMMLVRPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVW 223
Cdd:cd19213    100 AGQAGAGSWLKYIRVACSCDEQNLTACQINEQIYYKVIKDIEPGEELLVY 149
PR-SET_PRDM13 cd19197
PR-SET domain found in PR domain zinc finger protein 13 (PRDM13) and similar proteins; PRDM13 ...
 173-225 1.72e-07

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: 50.59  E-value: 1.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1804891976  173 DTSNEDDCNWMMLVRPAAEAEHQNLTAYQ--HGSDVYFTTSRDIPPGTELRVWYA 225
Cdd:cd19197     42 DESGSPATEWIGLVRAARNNQEQNLEAIAdlPGGQIFYRALRDIQPGEELTVWYS 96
PR-SET_PRDM3 cd19214
PR-SET domain found in MDS1 and EVI1 complex locus protein and similar proteins; PRDM3 (also ...
 113-220 7.69e-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: 44.54  E-value: 7.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  113 LPPNLEIRR--LEDGAEGVFAITQLVKRTQFGPFESRRVAKWeKESAFPLKVFQKDGH-PVCFDTSNEDDCNWMMLVRPA 189
Cdd:cd19214     30 IPSEFELREsnIPGTGLGIWTKRKIEVGEKFGPYVGEQRSNL-KDPSYGWEVLDEFGNvKFCIDASQPDVGSWLKYIRFA 108

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1804891976  190 AEAEHQNLTAYQHGSDVYFTTSRDIPPGTEL 220
Cdd:cd19214    109 GCYDQHNLVACQINDQIFYRAVADIDPGEEL 139
zf-H2C2_2 pfam13465
Zinc-finger double domain;
770-795 1.18e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 40.05  E-value: 1.18e-04
                           10        20
                   ....*....|....*....|....*.
gi 1804891976  770 NLERHKLIHTGVKSHACEQCGKSFAR 795
Cdd:pfam13465    1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
SET smart00317
SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain; Putative methyl transferase, based on ...
 115-231 2.41e-04

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: 41.94  E-value: 2.41e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976   115 PNLEIRRLEDGAEGVFAITQLVKRTQFGPF---------ESRRVAKWEKESAFPLKVFQKDGHPVCfDTSNEDdcNWMML 185
Cdd:smart00317    1 NKLEVFKSPGKGWGVRATEDIPKGEFIGEYvgeiitseeAEERPKAYDTDGAKAFYLFDIDSDLCI-DARRKG--NLARF 77

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1804891976   186 VRPAAEAEHQNLTAYQHG-SDVYFTTSRDIPPGTELRVWYAAFYAKK 231
Cdd:smart00317   78 INHSCEPNCELLFVEVNGdDRIVIFALRDIKPGEELTIDYGSDYANE 124
PRK10819 PRK10819
transport protein TonB; Provisional
 293-377 9.28e-04

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 42.36  E-value: 9.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  293 PPgsQSEAAAPEKEQDtPRGEPPAVPESENVA-----TKEQKKKPRRGRKPKVSKAEQPLVIVEDKEPTEQVAEIITEVP 367
Cdd:PRK10819    60 PP--QAVQPPPEPVVE-PEPEPEPIPEPPKEApvvipKPEPKPKPKPKPKPKPVKKVEEQPKREVKPVEPRPASPFENTA 136

                           90
                   ....*....|
gi 1804891976  368 PDEPVSATPD 377
Cdd:PRK10819   137 PARPTSSTAT 146
SET pfam00856
SET domain; SET domains are protein lysine methyltransferase enzymes. SET domains appear to be ...
 128-224 1.11e-03

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: 39.81  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  128 GVFAITQLVKRTQFGPF-ESRRVAKWEKESAFPLKVFQKDGH-------------PVCFDTSNEDDCNWMMLV----RPA 189
Cdd:pfam00856    3 GLFATEDIPKGEFIGEYvEVLLITKEEADKRELLYYDKLELRlwgpylftldedsEYCIDARALYYGNWARFInhscDPN 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1804891976  190 AEAEHQNLTAYQHgsdVYFTTSRDIPPGTELRVWY 224
Cdd:pfam00856   83 CEVRVVYVNGGPR---IVIFALRDIKPGEELTIDY 114
PR-SET_PRDM17 cd10520
PR-SET domain found in PR domain zinc finger protein 17 (PRDM17) and similar proteins; PRDM17 ...
 112-223 1.27e-03

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: 40.09  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804891976  112 SLPPNLEI--RRLEDGAEGVFAI-TQLVKRTQFGPFE--SRRVAKWEKESAFPLKVFQKDGHPVCFDTSNeddcnWMMLV 186
Cdd:cd10520      4 SLPPGLALgpSLAQEERLGVWCVgDALQKGTFLGPLEeeLESHDLTEGGSPRQEESGQSGDVLACEQSSK-----WMRFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1804891976  187 RPAAEAEHQNLTAYQHGSDVYFTTSRDIPPGTELRVW 223
Cdd:cd10520     79 CRARSEEESNVAVVRLSGRLHLRVCKDIEPGSELLLW 115
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 784-806 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 1804891976  784 HACEQCGKSFARKDMLKEHMRVH 806
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf_PR_Knuckle pfam18445
PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, ...
 12-37 1.67e-03

PR zinc knuckle motif; This is a zinc knuckle motif found in PRDM4 (Schwann cell factor 1, SC-1), a member of the PR protein family. PRDM4 is a transcriptional regulator that has been implied in transduction of nerve growth factor signals via the p75 neurotrophin receptor and in cell growth arrest. The short motif is also present in several other PR proteins including human PRDM6 (PRISM), PRDM7, PRDM9 (meisetz), PRDM10 (tristanin), PRDM11, and PRDM15. The conservation of cysteine and histidine residues suggested that this 20 amino acid motif binds zinc, hence the name 'PR zinc knuckle' to distinguish it from the longer (30 amino acid) C2H2-like zinc fingers that are located C-terminally of the PR domain. The PR zinc knuckle fold is similar to that of Gag-knuckles (a beta-hairpin providing two zinc ligands followed by a short helix or a loop providing the other two zinc ligands) and zinc ribbons (two beta-hairpins, each providing two zinc ligands).


Pssm-ID: 375871  Cd Length: 38  Bit Score: 37.27  E-value: 1.67e-03
                           10        20
                   ....*....|....*....|....*.
gi 1804891976   12 IWCEDCSQYHDSECPELGPVVMVKDS 37
Cdd:pfam18445   11 IWCTLCERSYPSDCPEHGPVTFIPDT 36
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
 288-357 2.46e-03

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 41.82  E-value: 2.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1804891976  288 QAKSLPPGSQSEAAAPEKEQDTPRGEPPAVPES----ENVATKEQKKKPRRGRKPKVSKAEQPlvivED--KEPTE 357
Cdd:PRK01297    13 EAEQPAPAPPSPAAAPAPPPPAKTAAPATKAAApaaaAPRAEKPKKDKPRRERKPKPASLWKL----EDfvVEPQE 84
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 438-460 3.33e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 3.33e-03
                           10        20
                   ....*....|....*....|...
gi 1804891976  438 YQCNICSKIFQNSSNLSRHVRSH 460
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
746-808 4.87e-03

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 4.87e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1804891976  746 LPDPNVQKYIHPCEICGRIFNSIGNLERHKLIHTGVKSHACEQCGKSFARKDM--LKEHMRVHDN 808
Cdd:COG5048     24 LKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPleLSRHLRTHHN 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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