|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
1-222 |
2.08e-129 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 363.70 E-value: 2.08e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 1 MLPNGLIVSCQALPDEPLHSSFIMSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEV 80
Cdd:PRK01130 2 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 81 DELIESGCEVIALDATTQTRPK-ESLEELVHYIREKaPHVAIMADISTVEEAINADHLNFDYIGTTLRGYTSYTKghILF 159
Cdd:PRK01130 82 DALAAAGADIIALDATLRPRPDgETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETK--KPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092700774 160 ENDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAITRPKQITERFIEAVQQ 222
Cdd:PRK01130 159 EPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
|
|
| NanE |
COG3010 |
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism]; |
2-223 |
4.14e-125 |
|
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 442247 Cd Length: 226 Bit Score: 352.87 E-value: 4.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 2 LPNGLIVSCQALPDEPLHSSFIMSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEVD 81
Cdd:COG3010 7 LKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITPTLEEVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 82 ELIESGCEVIALDATTQTRPK-ESLEELVHYIREKaPHVAIMADISTVEEAINADHLNFDYIGTTLRGYTSYTKGHILfe 160
Cdd:COG3010 87 ALAEAGADIIALDATRRPRPDgETLAELIARIHEE-PGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTDG-- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092700774 161 NDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAITRPKQITERFIEAVQQK 223
Cdd:COG3010 164 PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKKA 226
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
1-216 |
9.69e-109 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 311.43 E-value: 9.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 1 MLPNGLIVSCQALPDEPLHSSFIMSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEV 80
Cdd:cd04729 6 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITPTIEEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 81 DELIESGCEVIALDATTQTRPK-ESLEELVHYIREKApHVAIMADISTVEEAINADHLNFDYIGTTLRGYTSYTKGhiLF 159
Cdd:cd04729 86 DALAAAGADIIALDATDRPRPDgETLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAK--TE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092700774 160 ENDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAITRPKQITERF 216
Cdd:cd04729 163 DPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
|
|
| NanE |
pfam04131 |
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ... |
24-222 |
6.85e-72 |
|
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ManNAc-6-P-to-GlcNAc-6P epimerase in the N-acetylmannosamine (ManNAc) utilization pathway found mainly in pathogenic bacteria.
Pssm-ID: 427732 Cd Length: 192 Bit Score: 216.92 E-value: 6.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 24 MSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEVDELIESGCEVIALDATTQTRPkE 103
Cdd:pfam04131 1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRP-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 104 SLEELVHYIREKapHVAIMADISTVEEAINADHLNFDYIGTTLRGytsYTKGHILFENDFEFLKEVLEKvNAKVIAEGNV 183
Cdd:pfam04131 80 TIEDFIKRIKEK--GCLAMADCSTFEEGLNADKLGVDIIGTTLSG---YTGGENPAEPDFQLVKTLSEA-GCFVIAEGRY 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092700774 184 ITPEMYKKVSDLGVHCTVVGGAITRPKQITERFIEAVQQ 222
Cdd:pfam04131 154 NTPELAKKAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
1-222 |
2.08e-129 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 363.70 E-value: 2.08e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 1 MLPNGLIVSCQALPDEPLHSSFIMSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEV 80
Cdd:PRK01130 2 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 81 DELIESGCEVIALDATTQTRPK-ESLEELVHYIREKaPHVAIMADISTVEEAINADHLNFDYIGTTLRGYTSYTKghILF 159
Cdd:PRK01130 82 DALAAAGADIIALDATLRPRPDgETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETK--KPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092700774 160 ENDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAITRPKQITERFIEAVQQ 222
Cdd:PRK01130 159 EPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
|
|
| NanE |
COG3010 |
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism]; |
2-223 |
4.14e-125 |
|
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 442247 Cd Length: 226 Bit Score: 352.87 E-value: 4.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 2 LPNGLIVSCQALPDEPLHSSFIMSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEVD 81
Cdd:COG3010 7 LKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITPTLEEVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 82 ELIESGCEVIALDATTQTRPK-ESLEELVHYIREKaPHVAIMADISTVEEAINADHLNFDYIGTTLRGYTSYTKGHILfe 160
Cdd:COG3010 87 ALAEAGADIIALDATRRPRPDgETLAELIARIHEE-PGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTDG-- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092700774 161 NDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAITRPKQITERFIEAVQQK 223
Cdd:COG3010 164 PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKKA 226
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
1-216 |
9.69e-109 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 311.43 E-value: 9.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 1 MLPNGLIVSCQALPDEPLHSSFIMSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEV 80
Cdd:cd04729 6 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITPTIEEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 81 DELIESGCEVIALDATTQTRPK-ESLEELVHYIREKApHVAIMADISTVEEAINADHLNFDYIGTTLRGYTSYTKGhiLF 159
Cdd:cd04729 86 DALAAAGADIIALDATDRPRPDgETLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAK--TE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092700774 160 ENDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAITRPKQITERF 216
Cdd:cd04729 163 DPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
|
|
| NanE |
pfam04131 |
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ... |
24-222 |
6.85e-72 |
|
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ManNAc-6-P-to-GlcNAc-6P epimerase in the N-acetylmannosamine (ManNAc) utilization pathway found mainly in pathogenic bacteria.
Pssm-ID: 427732 Cd Length: 192 Bit Score: 216.92 E-value: 6.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 24 MSKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGSNVFITATSKEVDELIESGCEVIALDATTQTRPkE 103
Cdd:pfam04131 1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRP-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 104 SLEELVHYIREKapHVAIMADISTVEEAINADHLNFDYIGTTLRGytsYTKGHILFENDFEFLKEVLEKvNAKVIAEGNV 183
Cdd:pfam04131 80 TIEDFIKRIKEK--GCLAMADCSTFEEGLNADKLGVDIIGTTLSG---YTGGENPAEPDFQLVKTLSEA-GCFVIAEGRY 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1092700774 184 ITPEMYKKVSDLGVHCTVVGGAITRPKQITERFIEAVQQ 222
Cdd:pfam04131 154 NTPELAKKAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
6-204 |
1.00e-06 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 47.58 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 6 LIVSCQALPDEPLHSsfimsKMALAAFQGGAVGIRANTKEDILAIREEVSLPVIGIVKRDYEGS---NVFITATSKEVDE 82
Cdd:cd04722 1 VILALLAGGPSGDPV-----ELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPlgvQLAINDAAAAVDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 83 L----IESGCEVIALDATTQTRPKESLEeLVHYIREKAPHVAIMADIS--TVEEAINADHLNFDYIGTTLRGYTSYtkGH 156
Cdd:cd04722 76 AaaaaRAAGADGVEIHGAVGYLAREDLE-LIRELREAVPDVKVVVKLSptGELAAAAAEEAGVDEVGLGNGGGGGG--GR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1092700774 157 ILFENDFEFLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGG 204
Cdd:cd04722 153 DAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
127-222 |
2.79e-05 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 43.25 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 127 TVEEAINADHLNFDYIGTtlrG--YTSYTKGHILFENDFEFLKEVLEKVNAKVIAEGNvITPEMYKKVSDLGVHCTVVGG 204
Cdd:COG0352 109 SLEEALRAEEAGADYVGF---GpvFPTPTKPGAPPPLGLEGLAWWAELVEIPVVAIGG-ITPENAAEVLAAGADGVAVIS 184
|
90 100
....*....|....*....|.
gi 1092700774 205 AITR---PKQITERFIEAVQQ 222
Cdd:COG0352 185 AIWGapdPAAAARELRAALEA 205
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
125-218 |
1.18e-04 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 41.35 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 125 ISTVEEAINADHLNFDYIGTtlrG--YTSYTK---GHILfenDFEFLKEVLEKVNAKVIAEGNvITPEMYKKVSDLGVHC 199
Cdd:cd00564 102 THSLEEALRAEELGADYVGF---GpvFPTPTKpgaGPPL---GLELLREIAELVEIPVVAIGG-ITPENAAEVLAAGADG 174
|
90 100
....*....|....*....|..
gi 1092700774 200 TVVGGAITR---PKQITERFIE 218
Cdd:cd00564 175 VAVISAITGaddPAAAARELLA 196
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
101-216 |
1.78e-03 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 37.95 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 101 PKESLEELVHYIREKAPHVAI-MADISTVEEAINADHLNFDYIGTTlRGYTSYTKGHILFENDfefLKEVLEKVNAKV-I 178
Cdd:cd04726 88 PLSTIKKAVKAAKKYGKEVQVdLIGVEDPEKRAKLLKLGVDIVILH-RGIDAQAAGGWWPEDD---LKKVKKLLGVKVaV 163
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1092700774 179 AEGnvITPEMYKKVSDLGVHCTVVGGAITR---PKQITERF 216
Cdd:cd04726 164 AGG--ITPDTLPEFKKAGADIVIVGRAITGaadPAEAAREF 202
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
30-206 |
3.60e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.46 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 30 AAFQGgavgiRANTKEDILAIREEVSLPVI---GIvkRDYEgsnvfitatskEVDELIESGCEVIALDATTQTRPkESLE 106
Cdd:pfam00977 53 AAKEG-----RPVNLDVVEEIAEEVFIPVQvggGI--RSLE-----------DVERLLSAGADRVIIGTAAVKNP-ELIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 107 ELVHYIREKAPHVAI--------------MADISTVEEAINADHLNFDYI--------GTtLRGYtsytkghilfenDFE 164
Cdd:pfam00977 114 EAAEKFGSQCIVVAIdarrgkvaingwreDTGIDAVEWAKELEELGAGEIlltdidrdGT-LSGP------------DLE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1092700774 165 FLKEVLEKVNAKVIAEGNVITPEMYKKVSDLGVHCTVVGGAI 206
Cdd:pfam00977 181 LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
119-220 |
5.05e-03 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 37.31 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092700774 119 VAIMAD-IST---VEEAINADHLNFDYIGTTLrGYTSYTKGhilfENDFEFLKEVLEKVNAKVIAEGNvITPEMYKKVSD 194
Cdd:PRK07028 108 VRLMADlINVpdpVKRAVELEELGVDYINVHV-GIDQQMLG----KDPLELLKEVSEEVSIPIAVAGG-LDAETAAKAVA 181
|
90 100
....*....|....*....|....*....
gi 1092700774 195 LGVHCTVVGGAITRPKQITE---RFIEAV 220
Cdd:PRK07028 182 AGADIVIVGGNIIKSADVTEaarKIREAI 210
|
|
| |
