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Conserved domains on  [gi|2462566208|ref|XP_054177385|]
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zinc finger protein 416 isoform X1 [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 ...
 7-47 2.12e-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: 2.12e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462566208   7 CVTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
57-486 8.66e-10

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


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208  57 ETPEQSVSVEGVPQVRTPEASPSTQKIQSCDMCvPFLTDILHLTDL------------PGQELYLTGAC-----AVFHQD 119
Cdd:COG5048     4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSC-PNCTDSFSRLEHltrhirshtgekPSQCSYSGCDKsfsrpLELSRH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 120 QKHHSAEKPLESDMDKASFVQcclFHESGMPFTSSEVGKDFLAPLGILQPQAIANYEKPNKISKCEeAFHVGISHYKWSQ 199
Cdd:COG5048    83 LRTHHNNPSDLNSKSLPLSNS---KASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 200 CRRESSHKHTFFHPRVCTGKRLYESSKcgkacccecSLVQLQRVHPGERPYECSECGKSFSQTSHLNDHRRIHTGErPYV 279
Cdd:COG5048   159 VNTPQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 280 CGQCGKSFSQRATL-------IKHHRVHTGERPYECGecGKSFSQSSNLIEHC-RIHTGER-PYECDECGKAFGSKSTLV 350
Cdd:COG5048   229 LTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGFSlPIKSKQCNISFSRSSPLT 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 351 RHQRT--HTGE--KPYECGE--CGKLFRQSFSLVVHQRIHTTARPYEC--GQCGKSFS-----LKCGLIQHQLIHSGARP 417
Cdd:COG5048   307 RHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKK 386

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462566208 418 FECD--ECGKSFSQRTTLNKHHKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTGERPFECSECGKFFRQS 486
Cdd:COG5048   387 SETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
SFP1 super family cl25788
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 470-553 2.59e-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: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 470 GERPFECS--ECGKFFRQSYTLVEHqKIHtglrpydcGQCGKSFIQKSSLIQHQVVHTGERPYECGKCGKSFTQHSGLIL 547
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 2462566208 548 HRKSHT 553
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 ...
 7-47 2.12e-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: 2.12e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462566208   7 CVTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
8-47 3.58e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 3.58e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462566208    8 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 47
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-41 1.33e-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: 1.33e-18
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462566208   8 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENF 41
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENY 34
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
57-486 8.66e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208  57 ETPEQSVSVEGVPQVRTPEASPSTQKIQSCDMCvPFLTDILHLTDL------------PGQELYLTGAC-----AVFHQD 119
Cdd:COG5048     4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSC-PNCTDSFSRLEHltrhirshtgekPSQCSYSGCDKsfsrpLELSRH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 120 QKHHSAEKPLESDMDKASFVQcclFHESGMPFTSSEVGKDFLAPLGILQPQAIANYEKPNKISKCEeAFHVGISHYKWSQ 199
Cdd:COG5048    83 LRTHHNNPSDLNSKSLPLSNS---KASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 200 CRRESSHKHTFFHPRVCTGKRLYESSKcgkacccecSLVQLQRVHPGERPYECSECGKSFSQTSHLNDHRRIHTGErPYV 279
Cdd:COG5048   159 VNTPQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 280 CGQCGKSFSQRATL-------IKHHRVHTGERPYECGecGKSFSQSSNLIEHC-RIHTGER-PYECDECGKAFGSKSTLV 350
Cdd:COG5048   229 LTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGFSlPIKSKQCNISFSRSSPLT 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 351 RHQRT--HTGE--KPYECGE--CGKLFRQSFSLVVHQRIHTTARPYEC--GQCGKSFS-----LKCGLIQHQLIHSGARP 417
Cdd:COG5048   307 RHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKK 386

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462566208 418 FECD--ECGKSFSQRTTLNKHHKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTGERPFECSECGKFFRQS 486
Cdd:COG5048   387 SETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 420-524 1.38e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 44.86  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 420 CDECGKSFsQRTTLNKHHKVHtaERPYVCGeCGkAFMFKSKLVRHQRTHTGERPFECSECGKFFRQSYT----------L 489
Cdd:PLN03086  456 CEKCGQAF-QQGEMEKHMKVF--HEPLQCP-CG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVQAGGSamdvrdrlrgM 530

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462566208 490 VEHQKIhTGLRPYDCGQCGKSFIQKSSLIQHQVVH 524
Cdd:PLN03086  531 SEHESI-CGSRTAPCDSCGRSVMLKEMDIHQIAVH 564
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 470-553 2.59e-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: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 470 GERPFECS--ECGKFFRQSYTLVEHqKIHtglrpydcGQCGKSFIQKSSLIQHQVVHTGERPYECGKCGKSFTQHSGLIL 547
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 2462566208 548 HRKSHT 553
Cdd:COG5189   417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-343 2.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|....
gi 2462566208 320 NLIEHCRIHTGERPYECDECGKAF 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 527-562 2.33e-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: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462566208 527 ERPYECGKCGKSFTQHSGLILHRKS-HTVERPRDSSK 562
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 ...
 7-47 2.12e-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: 2.12e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2462566208   7 CVTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 47
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSL 41
KRAB smart00349
krueppel associated box;
8-47 3.58e-19

krueppel associated box;


Pssm-ID: 214630 [Multi-domain]  Cd Length: 61  Bit Score: 81.48  E-value: 3.58e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462566208    8 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENFALITAL 47
Cdd:smart00349   1 VTFEDVAVYFTQEEWEQLDPAQKNLYRDVMLENYSNLVSL 40
KRAB_A-box cd07765
KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression ...
 8-41 1.33e-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: 1.33e-18
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462566208   8 VTFEDVAIYFSQEEWGLLDEAQRLLYRDVMLENF 41
Cdd:cd07765     1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENY 34
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
57-486 8.66e-10

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 61.25  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208  57 ETPEQSVSVEGVPQVRTPEASPSTQKIQSCDMCvPFLTDILHLTDL------------PGQELYLTGAC-----AVFHQD 119
Cdd:COG5048     4 TSSQSSSSNNSVLSSTPKSTLKSLSNAPRPDSC-PNCTDSFSRLEHltrhirshtgekPSQCSYSGCDKsfsrpLELSRH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 120 QKHHSAEKPLESDMDKASFVQcclFHESGMPFTSSEVGKDFLAPLGILQPQAIANYEKPNKISKCEeAFHVGISHYKWSQ 199
Cdd:COG5048    83 LRTHHNNPSDLNSKSLPLSNS---KASSSSLSSSSSNSNDNNLLSSHSLPPSSRDPQLPDLLSISN-LRNNPLPGNNSSS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 200 CRRESSHKHTFFHPRVCTGKRLYESSKcgkacccecSLVQLQRVHPGERPYECSECGKSFSQTSHLNDHRRIHTGErPYV 279
Cdd:COG5048   159 VNTPQSNSLHPPLPANSLSKDPSSNLS---------LLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 280 CGQCGKSFSQRATL-------IKHHRVHTGERPYECGecGKSFSQSSNLIEHC-RIHTGER-PYECDECGKAFGSKSTLV 350
Cdd:COG5048   229 LTTNSQLSPKSLLSqspsslsSSDSSSSASESPRSSL--PTASSQSSSPNESDsSSEKGFSlPIKSKQCNISFSRSSPLT 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 351 RHQRT--HTGE--KPYECGE--CGKLFRQSFSLVVHQRIHTTARPYEC--GQCGKSFS-----LKCGLIQHQLIHSGARP 417
Cdd:COG5048   307 RHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSpllnnEPPQSLQQYKDLKNDKK 386

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462566208 418 FECD--ECGKSFSQRTTLNKHHKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTGERPFECSECGKFFRQS 486
Cdd:COG5048   387 SETLsnSCIRNFKRDSNLSLHIITHLSFRPYNCknPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDL 459
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
249-439 8.81e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 8.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 249 PYECSECGKSFSQTSHLNDHRR--IHTGE--RPYVCG--QCGKSFSQRATLIKHHRVHTGERPYEC--GECGKSFSQSSN 320
Cdd:COG5048   289 PIKSKQCNISFSRSSPLTRHLRsvNHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEklLNSSSKFSPLLN 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 321 ------LIEHCRIHTgERPYECD--ECGKAFGSKSTLVRHQRTHTGEKPYECgecgklfrqsfslvvhqrihttarpyEC 392
Cdd:COG5048   369 neppqsLQQYKDLKN-DKKSETLsnSCIRNFKRDSNLSLHIITHLSFRPYNC--------------------------KN 421

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462566208 393 GQCGKSFSLKCGLIQHQLIHSGARPFECDECgKSFSQRTTLNKHHKV 439
Cdd:COG5048   422 PPCSKSFNRHYNLIPHKKIHTNHAPLLCSIL-KSFRRDLDLSNHGKD 467
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
248-572 9.36e-08

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 54.70  E-value: 9.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 248 RPYECSECGKSFSQTSHLNDHRRIHTGERPYVCGQ--CGKSFSQRATLIKHHRVHTGERP-------------------- 305
Cdd:COG5048    32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSdlnskslplsnskassssls 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 306 -------YECGECGKSFSQSSNLIEHCRIHTGERPYECDE-------------------------CGKAFGSKSTLVRHQ 353
Cdd:COG5048   112 ssssnsnDNNLLSSHSLPPSSRDPQLPDLLSISNLRNNPLpgnnsssvntpqsnslhpplpanslSKDPSSNLSLLISSN 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 354 RTHTGEKPYECGECGKLFRQSFSLVVHQRIHTTArPYECGQCGKSFSLKCGLIQHQLIHSGARPFECDECGKSFSQRTTL 433
Cdd:COG5048   192 VSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDSSSSASESPRSSLPTASS 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 434 NKHHKVHTAER-------PYVCGECGKAFMFKSKLVRHQRT--HTGE--RPFECSE--CGKFFRQSYTLVEHQKIHTGLR 500
Cdd:COG5048   271 QSSSPNESDSSsekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILLHTSIS 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 501 PYDC--GQCGKSFIQKS-----SLIQHQVVHTGERPYEC--GKCGKSFTQHSGLILHRKSHTVERPR--DSSKCGKPYSP 569
Cdd:COG5048   351 PAKEklLNSSSKFSPLLnneppQSLQQYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLSFRPYncKNPPCSKSFNR 430


                  ...
gi 2462566208 570 RSN 572
Cdd:COG5048   431 HYN 433
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
253-515 3.94e-07

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


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 52.78  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 253 SECGKSFSQTSHLNDHRRIHTGERPYVCGQCGKSFSQRATLIKHHRVHTGErPYECGECGKSFSQSSNLIEHCRIHTGER 332
Cdd:COG5048   175 SLSKDPSSNLSLLISSNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENSSS-SLPLTTNSQLSPKSLLSQSPSSLSSSDS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 333 PYECDECGKAFGSKSTLVRHQRTHTGE-------KPYECGECGKLFRQSFSLVVHQR--IHT--TARPYECG--QCGKSF 399
Cdd:COG5048   254 SSSASESPRSSLPTASSQSSSPNESDSssekgfsLPIKSKQCNISFSRSSPLTRHLRsvNHSgeSLKPFSCPysLCGKLF 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 400 SLKCGLIQHQLIHSGARPFEC--DECGKSFSQRTTLNKH-----HKVHTAERPYVC--GECGKAFMFKSKLVRHQRTHTG 470
Cdd:COG5048   334 SRNDALKRHILLHTSISPAKEklLNSSSKFSPLLNNEPPqslqqYKDLKNDKKSETlsNSCIRNFKRDSNLSLHIITHLS 413

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2462566208 471 ERP--FECSECGKFFRQSYTLVEHQKIHTGLRPYDCGQCGKSFIQKS 515
Cdd:COG5048   414 FRPynCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCSILKSFRRDLD 460
PLN03086 PLN03086
PRLI-interacting factor K; Provisional
 420-524 1.38e-04

PRLI-interacting factor K; Provisional


Pssm-ID: 178635 [Multi-domain]  Cd Length: 567  Bit Score: 44.86  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 420 CDECGKSFsQRTTLNKHHKVHtaERPYVCGeCGkAFMFKSKLVRHQRTHTGERPFECSECGKFFRQSYT----------L 489
Cdd:PLN03086  456 CEKCGQAF-QQGEMEKHMKVF--HEPLQCP-CG-VVLEKEQMVQHQASTCPLRLITCRFCGDMVQAGGSamdvrdrlrgM 530

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462566208 490 VEHQKIhTGLRPYDCGQCGKSFIQKSSLIQHQVVH 524
Cdd:PLN03086  531 SEHESI-CGSRTAPCDSCGRSVMLKEMDIHQIAVH 564
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 470-553 2.59e-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: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462566208 470 GERPFECS--ECGKFFRQSYTLVEHqKIHtglrpydcGQCGKSFIQKSSLIQHQVVHTGERPYECGKCGKSFTQHSGLIL 547
Cdd:COG5189   346 DGKPYKCPveGCNKKYKNQNGLKYH-MLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416


                  ....*.
gi 2462566208 548 HRKSHT 553
Cdd:COG5189   417 HRKHSH 422
zf-H2C2_2 pfam13465
Zinc-finger double domain;
320-343 2.80e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 38.12  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|....
gi 2462566208 320 NLIEHCRIHTGERPYECDECGKAF 343
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 24
zf-H2C2_2 pfam13465
Zinc-finger double domain;
461-485 4.40e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 37.74  E-value: 4.40e-04
                          10        20
                  ....*....|....*....|....*
gi 2462566208 461 LVRHQRTHTGERPFECSECGKFFRQ 485
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
349-373 8.01e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 8.01e-04
                          10        20
                  ....*....|....*....|....*
gi 2462566208 349 LVRHQRTHTGEKPYECGECGKLFRQ 373
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-H2C2_2 pfam13465
Zinc-finger double domain;
264-289 1.07e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 1.07e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462566208 264 HLNDHRRIHTGERPYVCGQCGKSFSQ 289
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 527-562 2.33e-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: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462566208 527 ERPYECGKCGKSFTQHSGLILHRKS-HTVERPRDSSK 562
Cdd:cd23959   243 TPTHACTICGKAFSTHEGLRMHSKAkHGVELEKAKTA 279
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 250-272 4.76e-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: 34.58  E-value: 4.76e-03
                          10        20
                  ....*....|....*....|...
gi 2462566208 250 YECSECGKSFSQTSHLNDHRRIH 272
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-H2C2_2 pfam13465
Zinc-finger double domain;
293-317 5.28e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 34.65  E-value: 5.28e-03
                          10        20
                  ....*....|....*....|....*
gi 2462566208 293 LIKHHRVHTGERPYECGECGKSFSQ 317
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 334-356 5.91e-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: 34.58  E-value: 5.91e-03
                          10        20
                  ....*....|....*....|...
gi 2462566208 334 YECDECGKAFGSKSTLVRHQRTH 356
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 418-440 9.95e-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: 33.81  E-value: 9.95e-03
                          10        20
                  ....*....|....*....|...
gi 2462566208 418 FECDECGKSFSQRTTLNKHHKVH 440
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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