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 122937229  150 YICNECGKSFSQWSKLLRHQRIH 172
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 122937229  179 TCSECGKSFTQSSHLVQHQRTH 200
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 122937229  472 HLIQHRRTHTGEKPYKCPECGKSFSQ 497
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

104 kDa microneme/rhoptry antigen; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229   3 PETALWGPDLQGPEQSPNDAH---RGAESENEEESPRQESSGEEIIMGDPAQSPE-SKDSTEMSLERSSQDPSVPQNPPT 78
Cdd:PTZ00449 514 PEASGLPPKAPGDKEGEEGEHedsKESDEPKEGGKPGETKEGEVGKKPGPAKEHKpSKIPTLSKKPEFPKDPKHPKDPEE 593

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122937229  79 PLGHSNPLDHQIPLDPPAPEvVPTPSDWTKACEaswQWGALTTWNSPPvvPANEPSLRElvqgRPAGAEKP 149
Cdd:PTZ00449 594 PKKPKRPRSAQRPTRPKSPK-LPELLDIPKSPK---RPESPKSPKRPP--PPQRPSSPE----RPEGPKII 654

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 122937229  179 TCSECGKSFTQSSHLVQHQRTH 200
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 23

hypothetical protein

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 122937229 373 PFKCPVCGKTFTLSATLLRHQRthTGERPYKCPECGKSFSVSSNLINH 420
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 146 AEKPYICNECGKSFSQWSKLLRHQRIHTGERPNTCS--ECGKSFTQSSHLVQHQRTHTGEKPYKCPDC------------ 211
Cdd:COG5048   30 APRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSysGCDKSFSRPLELSRHLRTHHNNPSDLNSKSlplsnskassss 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 212 --GKCFSWSSN-------LVQHQRTHTGEKPYKCTECEKAFTQSTNLIKHQRSHTGEKPYKCG---ECRRAFYRSSDLIQ 279
Cdd:COG5048  110 lsSSSSNSNDNnllsshsLPPSSRDPQLPDLLSISNLRNNPLPGNNSSSVNTPQSNSLHPPLPansLSKDPSSNLSLLIS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 280 HQATHTGEKPYKCPECGKRFGQNHNLLKHQKIHAgEKPYRCTECgkSFIQSSELTQHQRTHTGeKPYECLECGKSFGHSS 359
Cdd:COG5048  190 SNVSTSIPSSSENSPLSSSYSIPSSSSDQNLENS-SSSLPLTTN--SQLSPKSLLSQSPSSLS-SSDSSSSASESPRSSL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 360 TLIKHQRTHLRED----------PFKCPVCGKTFTLSATLLRHQRT--HTGE--RPYKCPE--CGKSFSVSSNLINHQRI 423
Cdd:COG5048  266 PTASSQSSSPNESdsssekgfslPIKSKQCNISFSRSSPLTRHLRSvnHSGEslKPFSCPYslCGKLFSRNDALKRHILL 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 424 HRGERPYIC--ADCGKSFIMSST-----LIRHQRIHTGEKPYKCSD--CGKSFIRSSHLIQHRRTHTGEKP--YKCPECG 492
Cdd:COG5048  346 HTSISPAKEklLNSSSKFSPLLNneppqSLQQYKDLKNDKKSETLSnsCIRNFKRDSNLSLHIITHLSFRPynCKNPPCS 425

                        410       420
                 ....*....|....*....|....*....
gi 122937229 493 KSFSQSSNLITHVRTHMDENLFVCSDCGK 521
Cdd:COG5048  426 KSFNRHYNLIPHKKIHTNHAPLLCSILKS 454

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 230 GEKPYKC--TECEKAFTQSTNLiKHQRSHtgekpykcGECRRAFYRSSDLIQHQATHTGEKPYKCPECGKRFgQNHNLLK 307
Cdd:COG5189  346 DGKPYKCpvEGCNKKYKNQNGL-KYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRY-KNLNGLK 415

                 ....*
gi 122937229 308 HQKIH 312
Cdd:COG5189  416 YHRKH 420

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*.
gi 122937229  220 NLVQHQRTHTGEKPYKCTECEKAFTQ 245
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 122937229  192 HLVQHQRTHTGEKPYKCPDCGKCFS 216
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFK 25

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....
gi 122937229  276 DLIQHQATHTGEKPYKCPECGKRF 299
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSF 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 122937229  458 YKCSDCGKSFIRSSHLIQHRRTH 480
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 122937229  402 YKCPECGKSFSVSSNLINHQRIH 424
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 122937229  318 YRCTECGKSFIQSSELTQHQRTH 340
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 122937229  150 YICNECGKSFSQWSKLLRHQRIH 172
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

104 kDa microneme/rhoptry antigen; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229   3 PETALWGPDLQGPEQSPNDAH---RGAESENEEESPRQESSGEEIIMGDPAQSPE-SKDSTEMSLERSSQDPSVPQNPPT 78
Cdd:PTZ00449 514 PEASGLPPKAPGDKEGEEGEHedsKESDEPKEGGKPGETKEGEVGKKPGPAKEHKpSKIPTLSKKPEFPKDPKHPKDPEE 593

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122937229  79 PLGHSNPLDHQIPLDPPAPEvVPTPSDWTKACEaswQWGALTTWNSPPvvPANEPSLRElvqgRPAGAEKP 149
Cdd:PTZ00449 594 PKKPKRPRSAQRPTRPKSPK-LPELLDIPKSPK---RPESPKSPKRPP--PPQRPSSPE----RPEGPKII 654

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 122937229  179 TCSECGKSFTQSSHLVQHQRTH 200
Cdd:pfam00096   2 KCPDCGKSFSRKSNLKRHLRTH 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 122937229  234 YKCTECEKAFTQSTNLIKHQRSH 256
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 122937229  374 FKCPVCGKTFTLSATLLRHQRTH 396
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 122937229  165 LLRHQRIHTGERPNTCSECGKSFTQ 189
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

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
                 ....*....|....*....|....*....|....*....|....*
gi 122937229 180 CSECGKSFTQSSHLVQHQRTHTgekpYKCPDCGKCFSWSSNLVQH 224
Cdd:cd20908    4 CYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVH 44

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 122937229 375 KCPVCGKTFTLSATLLRHQRTHTgerpYKCPECGKSFSVSSNLINH-QRIHR 425
Cdd:cd20908    3 WCYYCDREFDDEKILIQHQKAKH----FKCHICHKKLYTAGGLAVHcLQVHK 50

IS1 family transposase; Proteins of this family are DDE transposases encoded by the IS1 family elements usually through a translational frameshift mechanism.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 122937229 292 CPECgkrfgQNHNLLKHQKIHAGEKPYRCTECGKSFI 328
Cdd:NF033558   1 CPRC-----QSDNVVKNGKSVRGKQRYRCKDCGRQFQ 32

hypothetical protein

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 122937229 345 PYECLECGKSFGHSSTLIKHQRthLREDPFKCPVCGKTFTLSATLLRH 392
Cdd:PHA00733  73 PYVCPLCLMPFSSSVSLKQHIR--YTEHSKVCPVCGKEFRNTDSTLDH 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 286 GEKPYKCP--ECGKRFgQNHNLLKHQKIHAgekpyrctecgksfiqsseltqHQRTHTGEKPYEclecgksfghsstlIK 363
Cdd:COG5189  346 DGKPYKCPveGCNKKY-KNQNGLKYHMLHG----------------------HQNQKLHENPSP--------------EK 388

                         90       100       110
                 ....*....|....*....|....*....|....
gi 122937229 364 HQRTHLREDPFKCPVCGKTFTlSATLLRHQRTHT 397
Cdd:COG5189  389 MNIFSAKDKPYRCEVCDKRYK-NLNGLKYHRKHS 421

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122937229 398 GERPYKCP--ECGKSFSvSSNLINHQRIHrgerpyicADCGKSFIMSSTLIRHQRIHTGEKPYKCSDCGKSFIRSSHLIQ 475
Cdd:COG5189  346 DGKPYKCPveGCNKKYK-NQNGLKYHMLH--------GHQNQKLHENPSPEKMNIFSAKDKPYRCEVCDKRYKNLNGLKY 416

                 ....*.
gi 122937229 476 HRRTHT 481
Cdd:COG5189  417 HRKHSH 422