leucine rich region;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285     49 PERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLL 128
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 17738285    129 EYLERQLDEPAPQVPVGDQGQELLCCKMALLT 160
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLG 112

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 374 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKAFRRNS 445
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 446 HLLRHQRIHgdkNVQNPEHGESWESQGrtesqwenteapvsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 523
Cdd:COG5048 368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427

                       170       180
                ....*....|....*....|.
gi 17738285 524 FTRTSYLVQHQRSHVGKKTLS 544
Cdd:COG5048 428 FNRHYNLIPHKKIHTNHAPLL 448

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.

                          10        20
                  ....*....|....*....|...
gi 17738285   320 HYCHECGKSFAQSSGLTKHRRIH 342
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

leucine rich region;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285     49 PERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLL 128
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 17738285    129 EYLERQLDEPAPQVPVGDQGQELLCCKMALLT 160
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLG 112

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285  49 PERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLL 128
Cdd:cd07936   1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80

                .
gi 17738285 129 E 129
Cdd:cd07936  81 E 81

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 374 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKAFRRNS 445
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 446 HLLRHQRIHgdkNVQNPEHGESWESQGrtesqwenteapvsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 523
Cdd:COG5048 368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427

                       170       180
                ....*....|....*....|.
gi 17738285 524 FTRTSYLVQHQRSHVGKKTLS 544
Cdd:COG5048 428 FNRHYNLIPHKKIHTNHAPLL 448

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17738285 221 LKMEDVALTLTP-GWTQLDSSQVNLYRDEKQENHSSLVSL 259
Cdd:cd07765   1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|...
gi 17738285   335 LTKHRRIHTGEKPYECEDCGKTF 357
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSF 24

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.

                          10        20
                  ....*....|....*....|...
gi 17738285   348 YECEDCGKTFIGSSALVIHQRVH 370
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

leucine rich region;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285     49 PERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLL 128
Cdd:smart00431   1 PEIFRQRFRQFRYQETSGPREALSRLRELCRQWLRPELHTKEQILELLVLEQFLTILPGELQAWVREHHPESGEEAVTLL 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 17738285    129 EYLERQLDEPAPQVPVGDQGQELLCCKMALLT 160
Cdd:smart00431  81 EDLERELDEPGQQVSAHVHGQEVLLEKMVPLG 112

SCAN oligomerization domain; The SCAN domain (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several vertebrate proteins that contain C2H2 zinc finger motifs, many of which may be transcription factors playing roles in cell survival and differentiation. This protein-interaction domain is able to mediate homo- and hetero-oligomerization of SCAN-containing proteins. Some SCAN-containing proteins, including those of lower vertebrates, do not contain zinc finger motifs. It has been noted that the SCAN domain resembles a domain-swapped version of the C-terminal domain of the HIV capsid protein. This domain model features elements common to the three general groups of SCAN domains (SCAN-A1, SCAN-A2, and SCAN-B). The SCAND1 protein is truncated at the C-terminus with respect to this model, the SCAND2 protein appears to have a truncated central helix.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285  49 PERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLL 128
Cdd:cd07936   1 PETYRQRFRAFQYQEASGPREALQRLRELCRQWLRPEIHTKEQILELLVLEQFLIILPPEVQAWVRERKPESGEEAATLA 80

                .
gi 17738285 129 E 129
Cdd:cd07936  81 E 81

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 374 KPYECEECGKVFSHSSNLIKHQRT--HTGE--KPYECD--DCGKTFSQSCSLLEHHKIHTGEKPYQCNM--CGKAFRRNS 445
Cdd:COG5048 288 LPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPysLCGKLFSRNDALKRHILLHTSISPAKEKLlnSSSKFSPLL 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 446 HLLRHQRIHgdkNVQNPEHGESWESQGrtesqwenteapvsykcNECERSFTRNRSLIEHQKIHTGEKPYQCD--TCGKG 523
Cdd:COG5048 368 NNEPPQSLQ---QYKDLKNDKKSETLS-----------------NSCIRNFKRDSNLSLHIITHLSFRPYNCKnpPCSKS 427

                       170       180
                ....*....|....*....|.
gi 17738285 524 FTRTSYLVQHQRSHVGKKTLS 544
Cdd:COG5048 428 FNRHYNLIPHKKIHTNHAPLL 448

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17738285 221 LKMEDVALTLTP-GWTQLDSSQVNLYRDEKQENHSSLVSL 259
Cdd:cd07765   1 VTFEDVAVYFSQeEWELLDPAQRDLYRDVMLENYENLVSL 40

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 470 SQGRTESQWENTEAPVSYKCNECERSFTRNRSLIEHQKIHTGEKPYQC--DTCGKGFTRTSYLVQHQRSH 537
Cdd:COG5048  17 SSTPKSTLKSLSNAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTH 86

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17738285 374 KPYECEECGKVFSHSSNLIKHQRTHTGEKPYEC--DDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGK 439
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCsySGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLP 99

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 307 LQRKQKNAIGSRR-HYCHECGKSFAQSSGLTKHRRIHTGEKPYECED--CGKTFIGSSALVIHQRVHTGEKPYECE---- 379
Cdd:COG5048  20 PKSTLKSLSNAPRpDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSkslp 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 380 ----------------------------------------------------------------------------ECGK 383
Cdd:COG5048 100 lsnskasssslsssssnsndnnllsshslppssrdpqlpdllsisnlrnnplpgnnsssvntpqsnslhpplpansLSKD 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 384 VFSHSSNLIKHQRTHTGEKPYECDDCGKTFSQScSLLEHHKIHTGEKPYQCNMCGKAFRRNSHLLRHQRIHG-DKNVQNP 462
Cdd:COG5048 180 PSSNLSLLISSNVSTSIPSSSENSPLSSSYSIP-SSSSDQNLENSSSSLPLTTNSQLSPKSLLSQSPSSLSSsDSSSSAS 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 463 EHGES----WESQGRTESQWENTE---APVSYKCNECERSFTRNRSLIEHQ--KIHTGE--KPYQCD--TCGKGFTRTSY 529
Cdd:COG5048 259 ESPRSslptASSQSSSPNESDSSSekgFSLPIKSKQCNISFSRSSPLTRHLrsVNHSGEslKPFSCPysLCGKLFSRNDA 338

                       330
                ....*....|..
gi 17738285 530 LVQHQRSHVGKK 541
Cdd:COG5048 339 LKRHILLHTSIS 350

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 17738285   501 SLIEHQKIHTGEKPYQCDTCGKGFTR 526
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 17738285   362 ALVIHQRVHTGEKPYECEECGKVFSH 387
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

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.

                          10        20
                  ....*....|....*....|...
gi 17738285   320 HYCHECGKSFAQSSGLTKHRRIH 342
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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.

                          10        20
                  ....*....|....*....|...
gi 17738285   515 YQCDTCGKGFTRTSYLVQHQRSH 537
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17738285 372 GEKPYECE--ECGKVFShSSNLIKHQRTHtgekpyecDDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKAFrRNSHLLR 449
Cdd:COG5189 346 DGKPYKCPveGCNKKYK-NQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-KNLNGLK 415

                ....*
gi 17738285 450 HQRIH 454
Cdd:COG5189 416 YHRKH 420

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.

                          10        20
                  ....*....|....*....|...
gi 17738285   404 YECDDCGKTFSQSCSLLEHHKIH 426
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

N-terminal domain of Oryza sativa transcription factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana SUF4 (AtSUF4), and similar proteins; Oryza sativa SUPPRESSOR OF FRI 4 (OsSUF4) is a C2H2-type zinc finger transcription factor which interacts with the major H3K36 methyltransferase SDG725 to promote H3K36me3 (tri-methylation at H3K9) establishment. The transcription factor OsSUF4 recognizes a specific 7-bp DNA element (5'-CGGAAAT-3'), which is contained in the promoter regions of many genes throughout the rice genome. Through interaction with OsSUF4, SDG725 is recruited to the promoters of key florigen genes, RICE FLOWERING LOCUS T1 (RFT1) and Heading date 3a (Hd3a), for H3K36 deposition to promote gene activation and rice plant flowering. OsSUF4 target genes include a number of genes involved in many biological processes. Flowering plant Arabidopsis SUF4 binds to a 15bp DNA element (5'-CCAAATTTTAAGTTT-3') within the promoter of the floral repressor gene FLOWERING LOCUS C (FLC) and recruits the FRI-C transcription activator complex to the FLC promoter. Although the DNA-binding element and target genes of AtSUF4 are different from those of OsSUF4, AtSUF4 is known to interact with the Arabidopsis H3K36 methyltransferase SDG8 (also known as ASHH2/EFS/SET8), and the methylation deposition mechanism mediated by the SUF4 transcription factor and H3K36 methyltransferase may be conserved in Arabidopsis and rice. Proteins in this family have two conserved C2H2-type zinc finger motifs at the N-terminus (included in this model), and a large proline-rich domain at the C-terminus; for OsSUF4, it has been shown that the N-terminal zinc-finger domain is responsible for DNA binding, and that the C-terminal domain interacts with SDG725.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17738285 319 RHYCHECGKSFAQSSGLTKHRRIHTgekpYECEDCGKTFIGSSALVIH-QRVH 370
Cdd:cd20908   1 KPWCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVH 49