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Conserved domains on  [gi|1696187464|ref|XP_029598667|]
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zinc finger protein 2 homolog isoform X1 [Salmo trutta]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 11589988)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIN2_N cd11657
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ...
34-212 6.69e-85

N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres.


:

Pssm-ID: 240667  Cd Length: 188  Bit Score: 265.70  E-value: 6.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464  34 SAAMWQVAQRRDVMDYEKLEEFVGLVTATVPDLLNEKQRAKLLLRLRTRVILELCSADHTADIQIIQPHLDRIRPPGHTG 113
Cdd:cd11657     8 SAAMWQVVQRRDVKHYGKVEEFVSLVTETVPELLTFRQRAKLILGLRARVILELCRNEKAADLAALNPHLPRLLPPYPNK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 114 S--GDAEVDAEEAIFLELIQTLLKDPAEREHFFQEVFPAEYGASYDTDMQLLVWEFLSKLEKILPVPDLGQTVSWLSSAP 191
Cdd:cd11657    88 CqrEDALMEEPQLNFLQLVQSLLKDPEEREHFFQEVFPVEYGEEFDQALEKLLWEFLSRLEKLLPVPDLKQTVSWLSTSP 167
                         170       180
                  ....*....|....*....|.
gi 1696187464 192 SVLEECLQALSQPEDLKSLLQ 212
Cdd:cd11657   168 SVLEECLDSVSDPDDLKSLLQ 188
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-636 9.58e-15

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.43  E-value: 9.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 298 YACHECGKTFTRSSDVTRHQRIHTGERPYTC--KECDKGFKNSWDLTRHQRIHTGERPYICPQCG------KGFTQLGLL 369
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLSSS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 370 SLHFTRT------PCGQS-----ADPPLQSTEQQEEPNDKGSGQYKCQKCGASFDTVLER--------------LKHRQT 424
Cdd:COG5048   114 SSNSNDNnllsshSLPPSsrdpqLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAnslskdpssnlsllISSNVS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 425 HVVNRHYKCSQCEKIYGRPSDLrRHQMKHTGERPFPCAECGKGFTHVWLLNKHRQIHTKERPYPCPECGKSFTQLQILNR 504
Cdd:COG5048   194 TSIPSSSENSPLSSSYSIPSSS-SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQS 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 505 HQLIHNGQR-------PFQCSFCEKSFTQLAGLTRHER--IHTGE--RPYLCTV--CQKTFLTHGELVRHQRSHSDFRPF 571
Cdd:COG5048   273 SSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 572 SC-------------------------------------SQCPKSFKTKRAQSEHMNTHTGERP--FSCAHCGKEFAKST 612
Cdd:COG5048   353 KEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHY 432
                         410       420
                  ....*....|....*....|....
gi 1696187464 613 SLIRHNLMHTGERPHQCAQCGKTF 636
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
669-694 2.85e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.85e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 669 DLTMHLRTHTGERPYSCMLCKKCFST 694
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
641-666 5.51e-03

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 641 ELLLHRRIHTGERPYPCSVCERRFRC 666
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
TIN2_N cd11657
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ...
34-212 6.69e-85

N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres.


Pssm-ID: 240667  Cd Length: 188  Bit Score: 265.70  E-value: 6.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464  34 SAAMWQVAQRRDVMDYEKLEEFVGLVTATVPDLLNEKQRAKLLLRLRTRVILELCSADHTADIQIIQPHLDRIRPPGHTG 113
Cdd:cd11657     8 SAAMWQVVQRRDVKHYGKVEEFVSLVTETVPELLTFRQRAKLILGLRARVILELCRNEKAADLAALNPHLPRLLPPYPNK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 114 S--GDAEVDAEEAIFLELIQTLLKDPAEREHFFQEVFPAEYGASYDTDMQLLVWEFLSKLEKILPVPDLGQTVSWLSSAP 191
Cdd:cd11657    88 CqrEDALMEEPQLNFLQLVQSLLKDPEEREHFFQEVFPVEYGEEFDQALEKLLWEFLSRLEKLLPVPDLKQTVSWLSTSP 167
                         170       180
                  ....*....|....*....|.
gi 1696187464 192 SVLEECLQALSQPEDLKSLLQ 212
Cdd:cd11657   168 SVLEECLDSVSDPDDLKSLLQ 188
TINF2_N pfam14973
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ...
38-182 3.37e-61

TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting nuclear factor 2. It is required for the formation of the shelterin complex. The shelterin complex is involved in the protection and maintenance of telomeres.


Pssm-ID: 464415  Cd Length: 148  Bit Score: 201.74  E-value: 3.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464  38 WQVAQRRDVMDYEKLEEFVGLVTATVPDLLNEKQRAKLLLRLRTRVILELCSADHTADIQIIQPHLDRIRPPGHTGSG-- 115
Cdd:pfam14973   1 WQVVQQRDVEHYGKVEEFVSLVTEAVPGLLSYRHHAQLIMGLRAKLILELCRGERPQDLKAIQSHLDRLGPTVSPKATkq 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696187464 116 -DAEVDAEEAIFLELIQTLLKDPAEREHFFQEVFPAEYGASYDTDMQLLVWEFLSKLEKILPVPDLGQ 182
Cdd:pfam14973  81 dDVKVEEAQENFLQLVQSLLEDPVEREHFFQEVFPVEYGPKFDAALEKLVWEFLSRLEQLLPVPDLQQ 148
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-636 9.58e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.43  E-value: 9.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 298 YACHECGKTFTRSSDVTRHQRIHTGERPYTC--KECDKGFKNSWDLTRHQRIHTGERPYICPQCG------KGFTQLGLL 369
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLSSS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 370 SLHFTRT------PCGQS-----ADPPLQSTEQQEEPNDKGSGQYKCQKCGASFDTVLER--------------LKHRQT 424
Cdd:COG5048   114 SSNSNDNnllsshSLPPSsrdpqLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAnslskdpssnlsllISSNVS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 425 HVVNRHYKCSQCEKIYGRPSDLrRHQMKHTGERPFPCAECGKGFTHVWLLNKHRQIHTKERPYPCPECGKSFTQLQILNR 504
Cdd:COG5048   194 TSIPSSSENSPLSSSYSIPSSS-SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQS 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 505 HQLIHNGQR-------PFQCSFCEKSFTQLAGLTRHER--IHTGE--RPYLCTV--CQKTFLTHGELVRHQRSHSDFRPF 571
Cdd:COG5048   273 SSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 572 SC-------------------------------------SQCPKSFKTKRAQSEHMNTHTGERP--FSCAHCGKEFAKST 612
Cdd:COG5048   353 KEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHY 432
                         410       420
                  ....*....|....*....|....
gi 1696187464 613 SLIRHNLMHTGERPHQCAQCGKTF 636
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFR 456
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-470 2.57e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.57e-04
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 445 DLRRHQMKHTGERPFPCAECGKGFTH 470
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
669-694 2.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.85e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 669 DLTMHLRTHTGERPYSCMLCKKCFST 694
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
641-666 5.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 641 ELLLHRRIHTGERPYPCSVCERRFRC 666
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
Name Accession Description Interval E-value
TIN2_N cd11657
N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; ...
34-212 6.69e-85

N-terminal domain of TRF-interacting nuclear factor 2; shelterin complex protein of telomeres; TIN2 is one of the six proteins of shelterin complex, which acts to protect telomeres from DNA damage repair machinery. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) region and the N-terminus, while the far C-terminal region has lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a negative regulatory function of this region. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of Skp1-Cul1-Rbx1-F- box (SCF) protein complexes. Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds PIP1, which recruits POT1 to telomeres.


Pssm-ID: 240667  Cd Length: 188  Bit Score: 265.70  E-value: 6.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464  34 SAAMWQVAQRRDVMDYEKLEEFVGLVTATVPDLLNEKQRAKLLLRLRTRVILELCSADHTADIQIIQPHLDRIRPPGHTG 113
Cdd:cd11657     8 SAAMWQVVQRRDVKHYGKVEEFVSLVTETVPELLTFRQRAKLILGLRARVILELCRNEKAADLAALNPHLPRLLPPYPNK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 114 S--GDAEVDAEEAIFLELIQTLLKDPAEREHFFQEVFPAEYGASYDTDMQLLVWEFLSKLEKILPVPDLGQTVSWLSSAP 191
Cdd:cd11657    88 CqrEDALMEEPQLNFLQLVQSLLKDPEEREHFFQEVFPVEYGEEFDQALEKLLWEFLSRLEKLLPVPDLKQTVSWLSTSP 167
                         170       180
                  ....*....|....*....|.
gi 1696187464 192 SVLEECLQALSQPEDLKSLLQ 212
Cdd:cd11657   168 SVLEECLDSVSDPDDLKSLLQ 188
TINF2_N pfam14973
TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting ...
38-182 3.37e-61

TERF1-interacting nuclear factor 2 N-terminus; This is the N-terminus of TERF1-interacting nuclear factor 2. It is required for the formation of the shelterin complex. The shelterin complex is involved in the protection and maintenance of telomeres.


Pssm-ID: 464415  Cd Length: 148  Bit Score: 201.74  E-value: 3.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464  38 WQVAQRRDVMDYEKLEEFVGLVTATVPDLLNEKQRAKLLLRLRTRVILELCSADHTADIQIIQPHLDRIRPPGHTGSG-- 115
Cdd:pfam14973   1 WQVVQQRDVEHYGKVEEFVSLVTEAVPGLLSYRHHAQLIMGLRAKLILELCRGERPQDLKAIQSHLDRLGPTVSPKATkq 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1696187464 116 -DAEVDAEEAIFLELIQTLLKDPAEREHFFQEVFPAEYGASYDTDMQLLVWEFLSKLEKILPVPDLGQ 182
Cdd:pfam14973  81 dDVKVEEAQENFLQLVQSLLEDPVEREHFFQEVFPVEYGPKFDAALEKLVWEFLSRLEQLLPVPDLQQ 148
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
298-636 9.58e-15

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 77.43  E-value: 9.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 298 YACHECGKTFTRSSDVTRHQRIHTGERPYTC--KECDKGFKNSWDLTRHQRIHTGERPYICPQCG------KGFTQLGLL 369
Cdd:COG5048    34 DSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLplsnskASSSSLSSS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 370 SLHFTRT------PCGQS-----ADPPLQSTEQQEEPNDKGSGQYKCQKCGASFDTVLER--------------LKHRQT 424
Cdd:COG5048   114 SSNSNDNnllsshSLPPSsrdpqLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPAnslskdpssnlsllISSNVS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 425 HVVNRHYKCSQCEKIYGRPSDLrRHQMKHTGERPFPCAECGKGFTHVWLLNKHRQIHTKERPYPCPECGKSFTQLQILNR 504
Cdd:COG5048   194 TSIPSSSENSPLSSSYSIPSSS-SDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASSQS 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 505 HQLIHNGQR-------PFQCSFCEKSFTQLAGLTRHER--IHTGE--RPYLCTV--CQKTFLTHGELVRHQRSHSDFRPF 571
Cdd:COG5048   273 SSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPA 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 572 SC-------------------------------------SQCPKSFKTKRAQSEHMNTHTGERP--FSCAHCGKEFAKST 612
Cdd:COG5048   353 KEkllnssskfspllnneppqslqqykdlkndkksetlsNSCIRNFKRDSNLSLHIITHLSFRPynCKNPPCSKSFNRHY 432
                         410       420
                  ....*....|....*....|....
gi 1696187464 613 SLIRHNLMHTGERPHQCAQCGKTF 636
Cdd:COG5048   433 NLIPHKKIHTNHAPLLCSILKSFR 456
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
230-582 5.96e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.02  E-value: 5.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 230 SSQVFACSQCPFFHMQESYLLQHIERNHPEEYSKLQKTEE-NPALPRKKFPRPEFPKPFPIHASSEPgayacHECGKTFT 308
Cdd:COG5048   107 SSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISNLrNNPLPGNNSSSVNTPQSNSLHPPLPA-----NSLSKDPS 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 309 RSSDVTRHQRIHTGERPYTCKECDKGFKNSWDLTRHQRIHTGERPYICPQCGKGFTQLGLLSLHftrtpcgQSADPPLQS 388
Cdd:COG5048   182 SNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSP-------SSLSSSDSS 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 389 TEQQEEPNdkgSGQYKCQKCGASFDTVLERLKHRQTHvvnrHYKCSQCEKIYGRPSDLRRHQ--MKHTGE--RPFPCAE- 463
Cdd:COG5048   255 SSASESPR---SSLPTASSQSSSPNESDSSSEKGFSL----PIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPYs 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 464 -CGKGFTHVWLLNKHRQIHTKERPYPCPECGKSFTQLQILN-------RHQLIHNGQRPFQC--SFCEKSFTQLAGLTRH 533
Cdd:COG5048   328 lCGKLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNneppqslQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLH 407
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1696187464 534 ERIHTGERPYLCT--VCQKTFLTHGELVRHQRSHSDFRPFSCSQCPKSFKT 582
Cdd:COG5048   408 IITHLSFRPYNCKnpPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRD 458
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
476-627 2.93e-05

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 47.00  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 476 KHRQIHTKERPYPCPECGKSFTQLQILNRHQLIHNGQRPFQCSF--CEKSFTQLAGLTRHERIHTGERPYLC--TVCQKT 551
Cdd:COG5048    23 TLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNskSLPLSN 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 552 FLTHGELVRHQRSHSDFrPFSCSQCPKSFKTKRAQ--SEHMNTHTGERPFS-CAHCGKEFAKSTSLI-RHNLMHTGERPH 627
Cdd:COG5048   103 SKASSSSLSSSSSNSND-NNLLSSHSLPPSSRDPQlpDLLSISNLRNNPLPgNNSSSVNTPQSNSLHpPLPANSLSKDPS 181
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
378-708 1.26e-04

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.07  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 378 CGQSADPPLQSTEQQEEPNDKgsgQYKCQKCGASFDTVLERLKHRQTHVVNRHYKCSQ--CEKIYGRPSDLRRHQMKHTG 455
Cdd:COG5048    12 NNSVLSSTPKSTLKSLSNAPR---PDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 456 ERPFPCAecgKGFTHVWLLNKHRQIH--TKERPYPCPECGKSFTQLQilnRHQLIHNGQRPfqCSFCEKSFTQLAGLTRH 533
Cdd:COG5048    89 NPSDLNS---KSLPLSNSKASSSSLSssSSNSNDNNLLSSHSLPPSS---RDPQLPDLLSI--SNLRNNPLPGNNSSSVN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 534 ERIHTGERPYLCTVCQKTFLTHGELVR-HQRSHSDFRPFSCSQCPKSFKTKRAQSEHMNTHTGERPFSCAHCGKEFAK-S 611
Cdd:COG5048   161 TPQSNSLHPPLPANSLSKDPSSNLSLLiSSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSSSLPLTTNSQLSPKsL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1696187464 612 TSLIRHNLMHTGERPHQCAQCGKTFLTSGE---------LLLHRRIHTgerPYPCSVCERRFRCSSDLTMHLRT--HTGE 680
Cdd:COG5048   241 LSQSPSSLSSSDSSSSASESPRSSLPTASSqssspnesdSSSEKGFSL---PIKSKQCNISFSRSSPLTRHLRSvnHSGE 317
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1696187464 681 --RPYSC--MLCKKCFSTSTRLKRHLRTHIGK 708
Cdd:COG5048   318 slKPFSCpySLCGKLFSRNDALKRHILLHTSI 349
zf-H2C2_2 pfam13465
Zinc-finger double domain;
445-470 2.57e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.57e-04
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 445 DLRRHQMKHTGERPFPCAECGKGFTH 470
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
315-337 3.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|...
gi 1696187464 315 RHQRIHTGERPYTCKECDKGFKN 337
Cdd:pfam13465   4 RHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
474-498 3.74e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.74e-04
                          10        20
                  ....*....|....*....|....*
gi 1696187464 474 LNKHRQIHTKERPYPCPECGKSFTQ 498
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-365 8.86e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.86e-04
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 340 DLTRHQRIHTGERPYICPQCGKGFTQ 365
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
298-320 1.44e-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: 36.51  E-value: 1.44e-03
                          10        20
                  ....*....|....*....|...
gi 1696187464 298 YACHECGKTFTRSSDVTRHQRIH 320
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
669-694 2.85e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 2.85e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 669 DLTMHLRTHTGERPYSCMLCKKCFST 694
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
326-348 2.89e-03

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


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 35.74  E-value: 2.89e-03
                          10        20
                  ....*....|....*....|...
gi 1696187464 326 YTCKECDKGFKNSWDLTRHQRIH 348
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
641-666 5.51e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 641 ELLLHRRIHTGERPYPCSVCERRFRC 666
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
613-638 6.32e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 6.32e-03
                          10        20
                  ....*....|....*....|....*.
gi 1696187464 613 SLIRHNLMHTGERPHQCAQCGKTFLT 638
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
 
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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