helix_turn_helix, mercury resistance;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489496909    13 FLISVAAELAGMHAQTLRTYDRLGLVSP-RRTSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRIIELT 82
Cdd:smart00422   1 YTIGEVAKLAGVSVRTLRYYERIGLLPPpIRTEGGYRLYSDEDLERLRFIKRL-KELGFSLEEIKELLELL 70

MerR HTH family regulatory protein;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489496909   15 ISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRII 79
Cdd:pfam13411   3 ISELARLLGVTPRTLRYWEREGLLPPPRTERGRRYYTDEDVERLRLIKAL-LERGLSLKEIKELL 66

Helix-Turn-Helix DNA binding domain of the HspR transcription regulator; Helix-turn-helix (HTH) transcription regulator HspR, N-terminal domain. Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  13 FLISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVELLRQVQHLSQDEGVNLAGIKRIIEltsqveaLQSRL 92
Cdd:cd04766    2 YVISVAAELSGMHPQTLRLYERLGLLSPSRTDGGTRRYSERDIERLRRIQRLTQELGVNLAGVKRILE-------LEEEL 74

                         90
                 ....*....|....*..
gi 489496909  93 QEMAEELAVLRANQRRE 109
Cdd:cd04766   75 AELRAELDELRARLRRE 91

DNA-binding transcriptional regulator, MerR family [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVSP-RRTSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRIIELTSQ-----VEAL 88
Cdd:COG0789    1 IGEVARLTGVSVRTLRYYERIGLLPPpERTEGGYRLYSEEDVERLRFIRRL-RELGFSLAEIRELLDLLDDgeeevRELL 79

                         90       100
                 ....*....|....*....|
gi 489496909  89 QSRLQEMAEELAVLRANQRR 108
Cdd:COG0789   80 EEHLAELEAQIAELQALRAE 99

Helix-Turn-Helix DNA binding domain of transcription regulators from the MerR superfamily; Helix-turn-helix (HTH) transcription regulator MerR superfamily, N-terminal domain. The MerR family transcription regulators have been shown to mediate responses to stress including exposure to heavy metals, drugs, or oxygen radicals in eubacterial and some archaeal species. They regulate transcription of multidrug/metal ion transporter genes and oxidative stress regulons by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489496909  13 FLISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVELLRQV 61
Cdd:cd04761    1 YTIGELAKLTGVSPSTLRYYERIGLLSPARTEGGYRLYSDADLERLRLI 49

Helix-Turn-Helix DNA binding domain of putative HspR-like transcription regulators; Putative helix-turn-helix (HTH) transcription regulator HspR-like proteins. Unlike the characterized HspR, these proteins have a C-terminal domain with putative metal binding cysteines (MBC). Heat shock protein regulators (HspR) have been shown to regulate expression of specific regulons in response to high temperature or high osmolarity in Streptomyces and Helicobacter, respectively. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489496909  13 FLISVAAELAGMHAQTLRTYDRLGLVSPRRtSGGGRRYSLHDVELLRQVQHLSQDEGVNLAGIKRII 79
Cdd:cd04767    2 YPIGVVAELLNIHPETLRIWERHGLIKPAR-RNGQRLYSNNDLKRLRFIKKLINEKGLNIAGVKQIL 67

Helix-Turn-Helix DNA binding domain of the MerR-like transcription regulators YyaN and YraB; Putative helix-turn-helix (HTH) MerR-like transcription regulators of Bacillus subtilis, YyaN and YraB, and related proteins; N-terminal domain. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVSP-RRTSGGGRRYSLHDVELLRQVQHLSQdEGVNLAGIKRIIELTSQVEA-LQSRL 92
Cdd:cd01109    3 IKEVAEKTGLSADTLRYYEKEGLLPPvKRDENGIRDFTEEDLEWLEFIKCLRN-TGMSIKDIKEYAELRREGDStIPERL 81

                         90
                 ....*....|....*
gi 489496909  93 QEMAEELAVLRANQR 107
Cdd:cd01109   82 ELLEEHREELEEQIA 96

Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA; Helix-turn-helix (HTH) TipAL, Mta, and SkgA transcription regulators, and related proteins, N-terminal domain. TipAL regulates resistance to and activation by numerous cyclic thiopeptide antibiotics, such as thiostrepton. Mta is a global transcriptional regulator; the N-terminal DNA-binding domain of Mta interacts directly with the promoters of mta, bmr, blt, and ydfK, and induces transcription of these multidrug-efflux transport genes. SkgA has been shown to control stationary-phase expression of catalase-peroxidase in Caulobacter crescentus. These proteins are comprised of distinct domains that harbor an N-terminal active (DNA-binding) site and a regulatory (effector-binding) site. The conserved N-terminal domain of these transcription regulators contains winged HTH motifs that mediate DNA binding. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Unique to this family, is a TipAL-like, lineage specific Bacilli subgroup, which has five conserved cysteines in the C-terminus of the protein.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRR-YSLHDVELLRQVQHLsQDEGVNLAGIKRIIE---------LTSQ 84
Cdd:cd01106    3 VGEVAKLTGVSVRTLHYYDEIGLLKPSRRTENGYRlYTEEDLERLQQILFL-KELGFSLKEIKELLKdpsedlleaLREQ 81

                         90       100
                 ....*....|....*....|..
gi 489496909  85 VEALQSRLQEMAEELAVLRANQ 106
Cdd:cd01106   82 KELLEEKKERLDKLIKTIDRTL 103

Helix-Turn-Helix DNA binding domain of the transcription regulators MlrA and CarA; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA- and CarA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYD-RLGLVSPRRTSGGGRRYSLHDVELLRQVQHLsQDEGVNlagIKRIIELTS 83
Cdd:cd01104    3 IGAVARLTGVSPDTLRAWErRYGLPAPQRTDGGHRLYSEADVARLRLIRRL-TSEGVR---ISQAAALAL 68

Helix-Turn-Helix DNA binding domain of BmrR-like transcription regulators; Helix-turn-helix (HTH) BmrR-like transcription regulators (TipAL, Mta, SkgA, BmrR, and BltR), N-terminal domain. These proteins have been shown to regulate expression of specific regulons in response to various toxic substances, antibiotics, or oxygen radicals in Bacillus subtilis, Streptomyces, and Caulobacter crescentus. They are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain HTH motifs that mediate DNA binding, while the C-terminal domains are often unrelated and bind specific coactivator molecules. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  13 FLISVAAELAGMHAQTLRTYDRLGLVSPRR-TSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRIIE---------LT 82
Cdd:cd04768    1 LTIGEFAKLAGVSIRTLRHYDDIGLFKPAKiAENGYRYYSYAQLYQLQFILFL-RELGFSLAEIKELLDtemeeltamLL 79

                         90
                 ....*....|....*
gi 489496909  83 SQVEALQSRLQEMAE 97
Cdd:cd04768   80 EKKQAIQQKIDRLQQ 94

Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator; Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  19 AELAGMHAQTLRTYDRLGLVSPRRTSG--GGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRIIELTSQVEA---LQSRLQ 93
Cdd:cd01107    7 AKLSNLSIKALRYYDKIGLLKPAYVDPdtGYRYYSAEQLERLNRIKYL-RDLGFPLEEIKEILDADNDDELrklLREKLA 85

                         90
                 ....*....|....*
gi 489496909  94 EMAEELAVLRANQRR 108
Cdd:cd01107   86 ELEAEIEELQRILRL 100

Helix-Turn-Helix DNA binding domain of putative Cfa-like transcription regulators; Putative helix-turn-helix (HTH) MerR-like transcription regulator; conserved, Cfa-like, unknown proteins (~172 a.a.). The N-terminal domain of these proteins appears to be related to the HTH domain of Cfa, a cyclopropane fatty acid synthase. These Cfa-like proteins have a unique C-terminal domain with conserved histidines (motif HXXFX7HXXF). Based on sequence similarity of the N-terminal domains, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVSP-RRTSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRIIElTSQVEA---LQS 90
Cdd:cd04790    4 ISQLARQFGLSRSTLLYYERIGLLSPsARSESNYRLYGERDLERLEQICAY-RSAGVSLEDIRSLLQ-QPGDDAtdvLRR 81

                         90
                 ....*....|....*..
gi 489496909  91 RLQEMAEELAVLRANQR 107
Cdd:cd04790   82 RLAELNREIQRLRQQQR 98

Helix-Turn-Helix DNA binding domain of MlrA-like transcription regulators; Helix-turn-helix (HTH) transcription regulator MlrA (merR-like regulator A) and related proteins, N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. Its close homolog, CarA from Myxococcus xanthus, is involved in activation of the carotenoid biosynthesis genes by light. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules. Many MlrA-like proteins in this group appear to lack the long dimerization helix seen in the N-terminal domains of typical MerR-like proteins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489496909  13 FLISVAAELAGMHAQTLRTYDR-LGLVSPRRTSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRII 79
Cdd:cd04763    1 YTIGEVALLTGIKPHVLRAWEReFGLLKPQRSDGGHRLFNDADIDRILEIKRW-IDNGVQVSKVKKLL 67

Helix-Turn-Helix DNA binding domain of the CadR- and PbrR-like transcription regulators; Helix-turn-helix (HTH) CadR- and PbrR-like transcription regulators. CadR and PbrR regulate expression of the cadmium and lead resistance operons, respectively. These proteins are comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the C-terminal domains have three conserved cysteines which comprise a putative metal binding site. Some members in this group have a histidine-rich C-terminal extension. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVS-PRRTSGGGRRYSLHDVELLRQVQHlSQDEGVNLAGIKRIIELT----------- 82
Cdd:cd04785    3 IGELARRTGVNVETIRYYESIGLLPePARTAGGYRLYGAAHVERLRFIRR-ARDLGFSLEEIRALLALSdrpdrscaead 81

                         90       100
                 ....*....|....*....|....*
gi 489496909  83 -------SQVEALQSRLQEMAEELA 100
Cdd:cd04785   82 aiarahlADVRARIADLRRLEAELK 106

Helix-Turn-Helix DNA binding domain of the Cfa transcription regulator; Putative helix-turn-helix (HTH) MerR-like transcription regulator; the N-terminal domain of Cfa, a cyclopropane fatty acid synthase and other related methyltransferases. Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  13 FLISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVELLRQVQHLsQDEGVNLAGIKRIIELTSQVEALQSRL 92
Cdd:cd04789    2 YTISELAEKAGISRSTLLYYEKLGLITGTRNANGYRLYPDSDLQRLLLIQQL-QAGGLSLKECLACLQGKLTRSLLLERL 80

                 ....*...
gi 489496909  93 QEMAEELA 100
Cdd:cd04789   81 SSLAEQIA 88

Predicted site-specific integrase-resolvase [Mobilome: prophages, transposons];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVE 56
Cdd:COG2452    3 PGEAAELLGVSPKTLRRWEKEGKLPAIRTPGGHRRYPESEVE 44

Helix-Turn-Helix DNA binding domain of putative transcription regulators from the MerR superfamily; Putative helix-turn-helix (HTH) MerR-like transcription regulators (subgroup 4). Based on sequence similarity, these proteins are predicted to function as transcription regulators that mediate responses to stress in eubacteria. They belong to the MerR superfamily of transcription regulators that promote transcription of various stress regulons by reconfiguring the operator sequence located between the -35 and -10 promoter elements. A typical MerR regulator is comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their N-terminal domains are homologous and contain a DNA-binding winged HTH motif, while the C-terminal domains are often dissimilar and bind specific coactivator molecules such as metal ions, drugs, and organic substrates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVSPRRTSGGGRRYSLHDVELLRQV-----QHLSQDE------------GVNLAGIKR 77
Cdd:cd04779    3 IGQLAHLAGVSKRTIDYYTNLGLLTPERSDSNYRYYDETALDRLQLIehlkgQRLSLAEikdqleevqrsdKEQREVAQE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489496909  78 IIELTSQVEALQSRLQEMAEELAVLRANQRRE--VAVVPKSTALV 120
Cdd:cd04779   83 VQLVCDQIDGLEHRLKQLKPIASQTDRAQRMKmtKELSQQVLTLI 127

First Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD contains the N-terminal or first repeat (rpt1) of these tandem MerR-like domain proteins.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489496909  19 AELAGMHAQTLRTYDRLGLVSP-RRTSGGGRRYSLHDVELLRQVQHLSQDEGVNLAG 74
Cdd:cd04772    7 ARAIGLSPQTVRNYESLGLIPPaERTANGYRIYTDKHIAALRAYRALLPGYGYRVAQ 63

mercuric resistance operon transcriptional regulator MerR;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  15 ISVAAELAGMHAQTLRTYDRLGLVS-PRRTSGGGRRYSLHDVELLRQVQHlSQDEGVNLAGIKRIIEL---TSQVEA--- 87
Cdd:PRK13752  10 IGVFAKAAGVNVETIRFYQRKGLLPePDKPYGSIRRYGEADVTRVRFVKS-AQRLGFSLDEIAELLRLedgTHCEEAssl 88

                         90
                 ....*....|....*
gi 489496909  88 LQSRLQEMAEELAVL 102
Cdd:PRK13752  89 AEHKLKDVREKMADL 103

Second Helix-Turn-Helix DNA binding domain of the regulatory protein TioE; Putative helix-turn-helix (HTH) regulatory protein, TioE, and related proteins. TioE is part of the thiocoraline gene cluster, which is involved in the biosynthesis of the antitumor thiocoraline from the marine actinomycete, Micromonospora. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Proteins in this family are unique within the MerR superfamily in that they are composed of just two adjacent MerR-like N-terminal domains; this CD mainly contains the C-terminal or second repeat (rpt2) of these tandem MerR-like domain proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489496909  14 LISVAAELAGMHAQTLRTYDRLGLVSP-RRTSGGGRRYSLHDVELLRqVQHLSQDEGVNLAGIKRIIEltsQVEALQSrl 92
Cdd:cd04773    2 TIGELAHLLGVPPSTLRHWEKEGLLSPdREPETGYRVYDPSDVRDAR-LIHLLRRGGYLLEQIATVVE---QLRHAGG-- 75

                         90       100
                 ....*....|....*....|
gi 489496909  93 qemAEELAVLRANQRREVAV 112
Cdd:cd04773   76 ---TEALAAALEQRRVALTQ 92