|
Name |
Accession |
Description |
Interval |
E-value |
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
90-307 |
2.22e-74 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 400284 [Multi-domain] Cd Length: 208 Bit Score: 228.25 E-value: 2.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 90 VVFFHGGGFAFLSPNAYpyDNVCRRFARKLPAYVISVNYRLAPEHRYPAQYDDGFDALKYIEENhgsILPANADLSRCFF 169
Cdd:pfam07859 1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQ---AAELGADPSRIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 170 AGDSAGGNIAHNVAIRICREPRssftaVKLIGLISIQPffGGEERTEAEKQLVGA----PLVSPDRTDWCWKAM--GLNR 243
Cdd:pfam07859 76 AGDSAGGNLAAAVALRARDEGL-----PKPAGQVLIYP--GTDLRTESPSYLAREfadgPLLTRAAMDWFWRLYlpGADR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237783 244 DHEAVNVggPNAVDISGLdyPETMVVVAGFDPLKDWQRSYYEWLKLCGKKATLIEYPNMFHAFY 307
Cdd:pfam07859 149 DDPLASP--LFASDLSGL--PPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
76-331 |
4.59e-48 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 160.42 E-value: 4.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 76 RLYTPHVSGDKIPVVVFFHGGGFAFLSPNAYpyDNVCRRFARKLPAYVISVNYRLAPEHRYPAQYDDGFDALKYIEENHG 155
Cdd:COG0657 2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTH--DPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 156 SIlpaNADLSRCFFAGDSAGGNIAHNVAIRICREPRSsftavKLIGLISIQPFFGgeerteaekqlvgaPLVSPDRtdwc 235
Cdd:COG0657 80 EL---GIDPDRIAVAGDSAGGHLAAALALRARDRGGP-----RPAAQVLIYPVLD--------------LTASPLR---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 236 wkamglnrdheavnvggpnaVDISGLdyPETMVVVAGFDPLKDWQRSYYEWLKLCGKKATLIEYPNMFHAFYIFPELPEA 315
Cdd:COG0657 134 --------------------ADLAGL--PPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEA 191
|
250
....*....|....*.
gi 15237783 316 GQLIMRIKDFVDERVA 331
Cdd:COG0657 192 RAALAEIAAFLRRALA 207
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
76-306 |
5.36e-17 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 80.15 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 76 RLYTPHvsgDKIPVVVFF-HGGGFAFLSPNAYpyDNVCRRFARKLPAYVISVNYRLAPEHRYPAQYDDGFDALKYIEEnH 154
Cdd:PRK10162 72 RLYYPQ---PDSQATLFYlHGGGFILGNLDTH--DRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQ-H 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 155 GSILPANAdlSRCFFAGDSAGGNIAHNVAIRIcREPRSSftAVKLIGLISIQPFFGgeERTEAEKQLVGAPLVSPDRTDW 234
Cdd:PRK10162 146 AEDYGINM--SRIGFAGDSAGAMLALASALWL-RDKQID--CGKVAGVLLWYGLYG--LRDSVSRRLLGGVWDGLTQQDL 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15237783 235 -CWKAMGLNRDHEAVNvggpNAVDISGLDY----PETMVVVAGFDPLKDWQRSYYEWLKLCGKKATLIEYPNMFHAF 306
Cdd:PRK10162 219 qMYEEAYLSNDADRES----PYYCLFNNDLtrdvPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAF 291
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
77-132 |
3.53e-08 |
|
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.
Pssm-ID: 238191 [Multi-domain] Cd Length: 493 Bit Score: 54.65 E-value: 3.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15237783 77 LYTPHVS--GDKIPVVVFFHGGGFAFLSPNAYPYDNvcrrFARKLPAY-VISVNYRLAP 132
Cdd:cd00312 83 VYTPKNTkpGNSLPVMVWIHGGGFMFGSGSLYPGDG----LAREGDNViVVSINYRLGV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Abhydrolase_3 |
pfam07859 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
90-307 |
2.22e-74 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 400284 [Multi-domain] Cd Length: 208 Bit Score: 228.25 E-value: 2.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 90 VVFFHGGGFAFLSPNAYpyDNVCRRFARKLPAYVISVNYRLAPEHRYPAQYDDGFDALKYIEENhgsILPANADLSRCFF 169
Cdd:pfam07859 1 LVYFHGGGFVLGSADTH--DRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQ---AAELGADPSRIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 170 AGDSAGGNIAHNVAIRICREPRssftaVKLIGLISIQPffGGEERTEAEKQLVGA----PLVSPDRTDWCWKAM--GLNR 243
Cdd:pfam07859 76 AGDSAGGNLAAAVALRARDEGL-----PKPAGQVLIYP--GTDLRTESPSYLAREfadgPLLTRAAMDWFWRLYlpGADR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237783 244 DHEAVNVggPNAVDISGLdyPETMVVVAGFDPLKDWQRSYYEWLKLCGKKATLIEYPNMFHAFY 307
Cdd:pfam07859 149 DDPLASP--LFASDLSGL--PPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
76-331 |
4.59e-48 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 160.42 E-value: 4.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 76 RLYTPHVSGDKIPVVVFFHGGGFAFLSPNAYpyDNVCRRFARKLPAYVISVNYRLAPEHRYPAQYDDGFDALKYIEENHG 155
Cdd:COG0657 2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTH--DPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 156 SIlpaNADLSRCFFAGDSAGGNIAHNVAIRICREPRSsftavKLIGLISIQPFFGgeerteaekqlvgaPLVSPDRtdwc 235
Cdd:COG0657 80 EL---GIDPDRIAVAGDSAGGHLAAALALRARDRGGP-----RPAAQVLIYPVLD--------------LTASPLR---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 236 wkamglnrdheavnvggpnaVDISGLdyPETMVVVAGFDPLKDWQRSYYEWLKLCGKKATLIEYPNMFHAFYIFPELPEA 315
Cdd:COG0657 134 --------------------ADLAGL--PPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEA 191
|
250
....*....|....*.
gi 15237783 316 GQLIMRIKDFVDERVA 331
Cdd:COG0657 192 RAALAEIAAFLRRALA 207
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
76-306 |
5.36e-17 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 80.15 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 76 RLYTPHvsgDKIPVVVFF-HGGGFAFLSPNAYpyDNVCRRFARKLPAYVISVNYRLAPEHRYPAQYDDGFDALKYIEEnH 154
Cdd:PRK10162 72 RLYYPQ---PDSQATLFYlHGGGFILGNLDTH--DRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQ-H 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 155 GSILPANAdlSRCFFAGDSAGGNIAHNVAIRIcREPRSSftAVKLIGLISIQPFFGgeERTEAEKQLVGAPLVSPDRTDW 234
Cdd:PRK10162 146 AEDYGINM--SRIGFAGDSAGAMLALASALWL-RDKQID--CGKVAGVLLWYGLYG--LRDSVSRRLLGGVWDGLTQQDL 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15237783 235 -CWKAMGLNRDHEAVNvggpNAVDISGLDY----PETMVVVAGFDPLKDWQRSYYEWLKLCGKKATLIEYPNMFHAF 306
Cdd:PRK10162 219 qMYEEAYLSNDADRES----PYYCLFNNDLtrdvPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAF 291
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
77-179 |
1.56e-10 |
|
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.
Pssm-ID: 466583 [Multi-domain] Cd Length: 215 Bit Score: 59.89 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 77 LYTPHVSGDKIPVVVFFHGGGFAFLSPNAYP--YDNVCRRFARKLPAyVISVNYRLAPEHRYPAQYDDGFDALKYIEenh 154
Cdd:pfam20434 3 IYLPKNAKGPYPVVIWIHGGGWNSGDKEADMgfMTNTVKALLKAGYA-VASINYRLSTDAKFPAQIQDVKAAIRFLR--- 78
|
90 100 110
....*....|....*....|....*....|
gi 15237783 155 gsilpANAD---LSRCFFA--GDSAGGNIA 179
Cdd:pfam20434 79 -----ANAAkygIDTNKIAlmGFSAGGHLA 103
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
77-132 |
3.53e-08 |
|
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.
Pssm-ID: 238191 [Multi-domain] Cd Length: 493 Bit Score: 54.65 E-value: 3.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15237783 77 LYTPHVS--GDKIPVVVFFHGGGFAFLSPNAYPYDNvcrrFARKLPAY-VISVNYRLAP 132
Cdd:cd00312 83 VYTPKNTkpGNSLPVMVWIHGGGFMFGSGSLYPGDG----LAREGDNViVVSINYRLGV 137
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
71-330 |
4.09e-08 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 53.10 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 71 RDLWFRLYTPHVSGdKIPVVVFFHGGGFAFlspnAYPYDNVCRRFARKlpAY-VISVNYRLAPEHR---YPAQYDDGFDA 146
Cdd:COG1506 8 TTLPGWLYLPADGK-KYPVVVYVHGGPGSR----DDSFLPLAQALASR--GYaVLAPDYRGYGESAgdwGGDEVDDVLAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 147 LKYIEENHGsilpanADLSRCFFAGDSAGGNIAHNVAiriCREPRsSFTAVkliglISIQPFFGGEERTEAEKQLVGAPL 226
Cdd:COG1506 81 IDYLAARPY------VDPDRIGIYGHSYGGYMALLAA---ARHPD-RFKAA-----VALAGVSDLRSYYGTTREYTERLM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 227 VSPdrtdwcWKAMGLNRDHEAVNvggpnavDISGLDYPeTMVVVAGFDPLKDWQRS--YYEWLKLCGKKATLIEYPNMFH 304
Cdd:COG1506 146 GGP------WEDPEAYAARSPLA-------YADKLKTP-LLLIHGEADDRVPPEQAerLYEALKKAGKPVELLVYPGEGH 211
|
250 260
....*....|....*....|....*.
gi 15237783 305 AFYifpeLPEAGQLIMRIKDFVDERV 330
Cdd:COG1506 212 GFS----GAGAPDYLERILDFLDRHL 233
|
|
| COesterase |
pfam00135 |
Carboxylesterase family; |
54-132 |
1.29e-07 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 53.08 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 54 PKPVNIVSTSDFVVDQSRD-LWFRLYTP---HVSGDKIPVVVFFHGGGFAFLSPNAYPYDNvcrrFARKLPAYVISVNYR 129
Cdd:pfam00135 66 PQNGDLTSPGSSGLEGSEDcLYLNVYTPkelKENKNKLPVMVWIHGGGFMFGSGSLYDGSY----LAAEGDVIVVTINYR 141
|
...
gi 15237783 130 LAP 132
Cdd:pfam00135 142 LGP 144
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
78-130 |
2.21e-07 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 52.20 E-value: 2.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15237783 78 YTPHVS-GDKIPVVVFFHGGGFAFLSPNAYPYDnvCRRFARKLpAYVISVNYRL 130
Cdd:COG2272 95 WTPALAaGAKLPVMVWIHGGGFVSGSGSEPLYD--GAALARRG-VVVVTINYRL 145
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
75-185 |
2.23e-04 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 41.88 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 75 FRLYTPHV--SGDKIPVVVFFHGGG------FAFLSPNAYPYDNVCRRfaRKLPAYVISVNYrlaPEHRY---PAQYDDG 143
Cdd:COG4099 35 YRLYLPKGydPGKKYPLVLFLHGAGergtdnEKQLTHGAPKFINPENQ--AKFPAIVLAPQC---PEDDYwsdTKALDAV 109
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15237783 144 FDALKYIEENHgsilpaNADLSRCFFAGDSAGGNIAHNVAIR 185
Cdd:COG4099 110 LALLDDLIAEY------RIDPDRIYLTGLSMGGYGTWDLAAR 145
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
33-185 |
2.83e-04 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 42.15 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 33 RPDGTINRRFLRLFDFRAPPNPKPVNIVSTSDF---VVDQSRDLWfrLYTPH---VSGDKIPVVVFFHGGGFaflSPNAY 106
Cdd:COG2382 54 APVVAAAVVVLGGPPPATDDKDVPHGTVETVTYpskALGRTRRVW--VYLPPgydNPGKKYPVLYLLDGGGG---DEQDW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 107 P--------YDNVCRrfARKL-PAYVISVNYRLAPEHRYPAQYDDGF------DALKYIEENhgsiLPANADLSRCFFAG 171
Cdd:COG2382 129 FdqgrlptiLDNLIA--AGKIpPMIVVMPDGGDGGDRGTEGPGNDAFerflaeELIPFVEKN----YRVSADPEHRAIAG 202
|
170
....*....|....
gi 15237783 172 DSAGGNIAHNVAIR 185
Cdd:COG2382 203 LSMGGLAALYAALR 216
|
|
| Say1_Mug180 |
pfam10340 |
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ... |
69-177 |
9.91e-04 |
|
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) and fission yeast Mug180. Say1 is a a membrane-anchored deacetylase required for the deacetylation of acetylated sterols. It is involved in the resistance to eugenol and pregnenolone toxicity. Mug180 has a role in meiosis.
Pssm-ID: 313549 Cd Length: 374 Bit Score: 40.59 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 69 QSRDLWFRLyTPHVSGDKI-PVVVFFHGGGFAF-LSPNAYPYDNVCRRFARKLPAYVI--SVNYRLAPEHRYPAQYDDGF 144
Cdd:pfam10340 104 DSTKFWLRK-VPETFDPKVdPILLYYHGGGFALkLIPVTLVFLNNLGKYFPDMAILVSdyTVTANCPQSYTYPLQVLQCL 182
|
90 100 110
....*....|....*....|....*....|...
gi 15237783 145 DALKYIEENHGsilpanadLSRCFFAGDSAGGN 177
Cdd:pfam10340 183 AVYDYLTLTKG--------CKNVTLMGDSAGGN 207
|
|
| Chlorophyllase2 |
pfam12740 |
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC: ... |
78-210 |
2.78e-03 |
|
Chlorophyllase enzyme; This family consists of several chlorophyllase and chlorophyllase-2 (EC:3.1.1.14) enzymes. Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of an ester bond to yield chlorophyllide and phytol. The family includes both plant and Amphioxus members.
Pssm-ID: 432755 Cd Length: 254 Bit Score: 38.84 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237783 78 YTPHVSGDkIPVVVFFHGggfaFLSPNAYpYDNVCRRFARKlpAY-VISVN-YRLAPehRYPAQYDDGFDALKYIEENHG 155
Cdd:pfam12740 9 FTPTEAGT-YPVLLFLHG----YLLYNSF-YSQLLQHIASH--GFiVVAPQlYLVAG--PDGDEIKSAAKVANWLSNGLQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15237783 156 SILPAN--ADLSRCFFAGDSAGGNIAHNVAIRICReprssfTAVKLIGLISIQPFFG 210
Cdd:pfam12740 79 HVLPEGvePDLSKLALSGHSRGGKTAFALALGHAK------TSLKFSALIGIDPVAG 129
|
|
| |
