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Conserved domains on  [gi|33859678|ref|NP_060349|]
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zinc finger protein 416 isoform 1 [Homo sapiens]

Protein Classification

KRAB domain-containing zinc finger protein( domain architecture ID 12016853)

KRAB (Kruppel-associated box) domain-containing zinc finger protein (KRAB-ZFP) plays important roles in cell differentiation and organ development and in regulating viral replication and transcription

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-67 2.20e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


:

Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.14  E-value: 2.20e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 33859678    27 CVTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 67
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
77-506 2.72e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.79  E-value: 2.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678  77 ETPEQSVSVEGVPQVRTPEASPSTQKIQSCDMCvPFLTDILHLTDL------------PGQELYLTGAC-----AVFHQD 139
Cdd:COG5048   4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSC-PNCTDSFSRLEHltrhirshtgekPSQCSYSGCDKsfsrpLELSRH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 140 QKHHSAEKPLESDMDKASFVQcclFHESGMPFTSSEVGKDFLAPLGILQPQAIANYEKPNKISKCEeAFHVGISHYKWSQ 219
Cdd:COG5048  83 LRTHHNNPSDLNSKSLPLSNS---KASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 220 CRRESSHKHTFFHPRVCTGKRLYESSKcgkacccecSLVQLQRVHPGERPYECSECGKSFSQTSHLNDHRRIHTGErPYV 299
Cdd:COG5048 159 VNTPQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLP 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 300 CGQCGKSFSQRATL-------IKHHRVHTGERPYECGecGKSFSQSSNLIEHC-RIHTGER-PYECDECGKAFGSKSTLV 370
Cdd:COG5048 229 LTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGFSlPIKSKQCNISFSRSSPLT 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 371 RHQRT--HTGE--KPYECGE--CGKLFRQSFSLVVHQRIHTTARPYEC--GQCGKSFS-----LKCGLIQHQLIHSGARP 437
Cdd:COG5048 307 RHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKK 386

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33859678 438 FECD--ECGKSFSQRTTLNKHHKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTGERPFECSECGKFFRQS 506
Cdd:COG5048 387 SETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 490-573 2.72e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


The actual alignment was detected with superfamily member COG5189:

Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 490 GERPFECS--ECGKFFRQSYTLVEHqKIHtglrpydcGQCGKSFIQKSSLIQHQVVHTGERPYECGKCGKSFTQHSGLIL 567
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 33859678 568 HRKSHT 573
Cdd:COG5189 417 HRKHSH 422
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-67 2.20e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.14  E-value: 2.20e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 33859678    27 CVTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 67
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
28-67 3.72e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 3.72e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 33859678     28 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 28-61 1.37e-18

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.37e-18
                        10        20        30
                ....*....|....*....|....*....|....
gi 33859678  28 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENF 61
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENY 34
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
77-506 2.72e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.79  E-value: 2.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678  77 ETPEQSVSVEGVPQVRTPEASPSTQKIQSCDMCvPFLTDILHLTDL------------PGQELYLTGAC-----AVFHQD 139
Cdd:COG5048   4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSC-PNCTDSFSRLEHltrhirshtgekPSQCSYSGCDKsfsrpLELSRH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 140 QKHHSAEKPLESDMDKASFVQcclFHESGMPFTSSEVGKDFLAPLGILQPQAIANYEKPNKISKCEeAFHVGISHYKWSQ 219
Cdd:COG5048  83 LRTHHNNPSDLNSKSLPLSNS---KASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 220 CRRESSHKHTFFHPRVCTGKRLYESSKcgkacccecSLVQLQRVHPGERPYECSECGKSFSQTSHLNDHRRIHTGErPYV 299
Cdd:COG5048 159 VNTPQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLP 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 300 CGQCGKSFSQRATL-------IKHHRVHTGERPYECGecGKSFSQSSNLIEHC-RIHTGER-PYECDECGKAFGSKSTLV 370
Cdd:COG5048 229 LTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGFSlPIKSKQCNISFSRSSPLT 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 371 RHQRT--HTGE--KPYECGE--CGKLFRQSFSLVVHQRIHTTARPYEC--GQCGKSFS-----LKCGLIQHQLIHSGARP 437
Cdd:COG5048 307 RHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKK 386

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33859678 438 FECD--ECGKSFSQRTTLNKHHKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTGERPFECSECGKFFRQS 506
Cdd:COG5048 387 SETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 440-544 1.35e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 44.86  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678  440 CDECGKSFsQRTTLNKHHKVHtaERPYVCGeCGkAFMFKSKLVRHQRTHTGERPFECSECGKFFRQSYT----------L 509
Cdd:PLN03086 456 CEKCGQAF-QQGEMEKHMKVF--HEPLQCP-CG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVQAGGSamdvrdrlrgM 530

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 33859678  510 VEHQKIhTGLRPYDCGQCGKSFIQKSSLIQHQVVH 544
Cdd:PLN03086 531 SEHESI-CGSRTAPCDSCGRSVMLKEMDIHQIAVH 564
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-363 2.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.12e-04
                          10        20
                  ....*....|....*....|....
gi 33859678   340 NLIEHCRIHTGERPYECDECGKAF 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 490-573 2.72e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 490 GERPFECS--ECGKFFRQSYTLVEHqKIHtglrpydcGQCGKSFIQKSSLIQHQVVHTGERPYECGKCGKSFTQHSGLIL 567
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 33859678 568 HRKSHT 573
Cdd:COG5189 417 HRKHSH 422
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 547-582 2.44e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 40.62  E-value: 2.44e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33859678 547 ERPYECGKCGKSFTQHSGLILHRKS-HTVERPRDSSK 582
Cdd:cd23959 243 TPTHACTICGKAFSTHEGLRMHSKAkHGVELEKAKTA 279
 
Name Accession Description Interval E-value
KRAB pfam01352
KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc ...
 27-67 2.20e-21

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.


Pssm-ID: 460171  Cd Length: 42  Bit Score: 87.14  E-value: 2.20e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 33859678    27 CVTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 67
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
28-67 3.72e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 3.72e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 33859678     28 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 67
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 28-61 1.37e-18

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.


Pssm-ID: 143639  Cd Length: 40  Bit Score: 79.13  E-value: 1.37e-18
                        10        20        30
                ....*....|....*....|....*....|....
gi 33859678  28 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENF 61
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENY 34
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
77-506 2.72e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 62.79  E-value: 2.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678  77 ETPEQSVSVEGVPQVRTPEASPSTQKIQSCDMCvPFLTDILHLTDL------------PGQELYLTGAC-----AVFHQD 139
Cdd:COG5048   4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSC-PNCTDSFSRLEHltrhirshtgekPSQCSYSGCDKsfsrpLELSRH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 140 QKHHSAEKPLESDMDKASFVQcclFHESGMPFTSSEVGKDFLAPLGILQPQAIANYEKPNKISKCEeAFHVGISHYKWSQ 219
Cdd:COG5048  83 LRTHHNNPSDLNSKSLPLSNS---KASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 220 CRRESSHKHTFFHPRVCTGKRLYESSKcgkacccecSLVQLQRVHPGERPYECSECGKSFSQTSHLNDHRRIHTGErPYV 299
Cdd:COG5048 159 VNTPQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLP 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 300 CGQCGKSFSQRATL-------IKHHRVHTGERPYECGecGKSFSQSSNLIEHC-RIHTGER-PYECDECGKAFGSKSTLV 370
Cdd:COG5048 229 LTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGFSlPIKSKQCNISFSRSSPLT 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 371 RHQRT--HTGE--KPYECGE--CGKLFRQSFSLVVHQRIHTTARPYEC--GQCGKSFS-----LKCGLIQHQLIHSGARP 437
Cdd:COG5048 307 RHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKK 386

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33859678 438 FECD--ECGKSFSQRTTLNKHHKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTGERPFECSECGKFFRQS 506
Cdd:COG5048 387 SETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
268-592 4.02e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 268 RPYECSECGKSFSQTSHLNDHRRIHTGERPYVCGQ--CGKSFSQRATLIKHHRVHTGERP-------------------- 325
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSdlnskslplsnskassssls 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 326 -------YECGECGKSFSQSSNLIEHCRIHTGERPYECDE-------------------------CGKAFGSKSTLVRHQ 373
Cdd:COG5048 112 ssssnsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLpgnnsssvntpqsnslhpplpanslSKDPSSNLSLLISSN 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 374 RTHTGEKPYECGECGKLFRQSFSLVVHQRIHTTArPYECGQCGKSFSLKCGLIQHQLIHSGARPFECDECGKSFSQRTTL 453
Cdd:COG5048 192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 454 NKHHKVHTAER-------PYVCGECGKAFMFKSKLVRHQRT--HTGE--RPFECSE--CGKFFRQSYTLVEHQKIHTGLR 520
Cdd:COG5048 271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 521 PYDC--GQCGKSFIQKS-----SLIQHQVVHTGERPYEC--GKCGKSFTQHSGLILHRKSHTVERPR--DSSKCGKPYSP 589
Cdd:COG5048 351 PAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNR 430


                ...
gi 33859678 590 RSN 592
Cdd:COG5048 431 HYN 433
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
269-459 4.20e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 55.86  E-value: 4.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 269 PYECSECGKSFSQTSHLNDHRR--IHTGE--RPYVCG--QCGKSFSQRATLIKHHRVHTGERPYEC--GECGKSFSQSSN 340
Cdd:COG5048 289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLN 368

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 341 ------LIEHCRIHTgERPYECD--ECGKAFGSKSTLVRHQRTHTGEKPYECgecgklfrqsfslvvhqrihttarpyEC 412
Cdd:COG5048 369 neppqsLQQYKDLKN-DKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------KN 421

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 33859678 413 GQCGKSFSLKCGLIQHQLIHSGARPFECDECgKSFSQRTTLNKHHKV 459
Cdd:COG5048 422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
273-535 1.91e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 53.93  E-value: 1.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 273 SECGKSFSQTSHLNDHRRIHTGERPYVCGQCGKSFSQRATLIKHHRVHTGErPYECGECGKSFSQSSNLIEHCRIHTGER 352
Cdd:COG5048 175 SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 353 PYECDECGKAFGSKSTLVRHQRTHTGE-------KPYECGECGKLFRQSFSLVVHQR--IHT--TARPYECG--QCGKSF 419
Cdd:COG5048 254 SSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSgeSLKPFSCPysLCGKLF 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 420 SLKCGLIQHQLIHSGARPFEC--DECGKSFSQRTTLNKH-----HKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTG 490
Cdd:COG5048 334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPqslqqYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLS 413

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 33859678 491 ERP--FECSECGKFFRQSYTLVEHQKIHTGLRPYDCGQCGKSFIQKS 535
Cdd:COG5048 414 FRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 440-544 1.35e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 44.86  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678  440 CDECGKSFsQRTTLNKHHKVHtaERPYVCGeCGkAFMFKSKLVRHQRTHTGERPFECSECGKFFRQSYT----------L 509
Cdd:PLN03086 456 CEKCGQAF-QQGEMEKHMKVF--HEPLQCP-CG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVQAGGSamdvrdrlrgM 530

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 33859678  510 VEHQKIhTGLRPYDCGQCGKSFIQKSSLIQHQVVH 544
Cdd:PLN03086 531 SEHESI-CGSRTAPCDSCGRSVMLKEMDIHQIAVH 564
zf-H2C2_2 pfam13465
Zinc-finger double domain;
340-363 2.12e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.51  E-value: 2.12e-04
                          10        20
                  ....*....|....*....|....
gi 33859678   340 NLIEHCRIHTGERPYECDECGKAF 363
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 490-573 2.72e-04

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 43.55  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33859678 490 GERPFECS--ECGKFFRQSYTLVEHqKIHtglrpydcGQCGKSFIQKSSLIQHQVVHTGERPYECGKCGKSFTQHSGLIL 567
Cdd:COG5189 346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                ....*.
gi 33859678 568 HRKSHT 573
Cdd:COG5189 417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
481-505 3.33e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 3.33e-04
                          10        20
                  ....*....|....*....|....*
gi 33859678   481 LVRHQRTHTGERPFECSECGKFFRQ 505
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
369-393 6.11e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.35  E-value: 6.11e-04
                          10        20
                  ....*....|....*....|....*
gi 33859678   369 LVRHQRTHTGEKPYECGECGKLFRQ 393
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
284-309 8.04e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.04e-04
                          10        20
                  ....*....|....*....|....*.
gi 33859678   284 HLNDHRRIHTGERPYVCGQCGKSFSQ 309
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 547-582 2.44e-03

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 40.62  E-value: 2.44e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 33859678 547 ERPYECGKCGKSFTQHSGLILHRKS-HTVERPRDSSK 582
Cdd:cd23959 243 TPTHACTICGKAFSTHEGLRMHSKAkHGVELEKAKTA 279
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 270-292 3.56e-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: 34.97  E-value: 3.56e-03
                          10        20
                  ....*....|....*....|...
gi 33859678   270 YECSECGKSFSQTSHLNDHRRIH 292
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
313-337 4.15e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.04  E-value: 4.15e-03
                          10        20
                  ....*....|....*....|....*
gi 33859678   313 LIKHHRVHTGERPYECGECGKSFSQ 337
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 354-376 4.64e-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: 34.97  E-value: 4.64e-03
                          10        20
                  ....*....|....*....|...
gi 33859678   354 YECDECGKAFGSKSTLVRHQRTH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 438-460 7.66e-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: 34.20  E-value: 7.66e-03
                          10        20
                  ....*....|....*....|...
gi 33859678   438 FECDECGKSFSQRTTLNKHHKVH 460
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.
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