|
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. |
78-285 |
2.25e-70 |
|
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: 217.46 E-value: 2.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 78 LLWIHGGGYILGSIDDNDDTCMRFAKEAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIADNAKSLNIDSNRIGVAGVSA 157
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 158 GGGLTAALSLLARDRKYPSICLQMPLYPMIDDRNDTPS--ANEIKEGFVWNQKANEAGWKMYLGEMYGTDqipAYAAPSR 235
Cdd:pfam07859 81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSylAREFADGPLLTRAAMDWFWRLYLPGADRDD---PLASPLF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446780678 236 AEDYSDLPYTYTFVGQLDPFRSETLTYVSKLAQAGVDVEFHLYPNAYHWF 285
Cdd:pfam07859 158 ASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
64-311 |
2.89e-66 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 206.65 E-value: 2.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 64 RIYRPKSNHESLPVLLWIHGGGYILGSIDDNDDTCMRFAKEAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIADNAKSL 143
Cdd:COG0657 2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 144 NIDSNRIgvagvsagggLTAALSLLARDRKYPSICLQMPLYPMIDDRndtpsaneikegfvwnqkaneagwkmylgemyg 223
Cdd:COG0657 82 GIDPDRIavagdsagghLAAALALRARDRGGPRPAAQVLIYPVLDLT--------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 224 tdqipayAAPSRAeDYSDLPYTYTFVGQLDPFRSETLTYVSKLAQAGVDVEFHLYPNAYHWFeGLNPNADVSIYAVNEIV 303
Cdd:COG0657 129 -------ASPLRA-DLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGF-GLLAGLPEARAALAEIA 199
|
....*...
gi 446780678 304 QAIKTGFK 311
Cdd:COG0657 200 AFLRRALA 207
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
60-285 |
2.71e-27 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 108.65 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 60 PLPLRIYRPKSNheSLPVLLWIHGGGYILGSIDDNDDTCMRFAKEAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIADN 139
Cdd:PRK10162 68 QVETRLYYPQPD--SQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 140 AKSLNIDSNRIGVAGVSAGGGLTAALSLLARDRKYP-----SICLQMPLYPMIDdrndtpSANEIKEGFVWNqKANEAGW 214
Cdd:PRK10162 146 AEDYGINMSRIGFAGDSAGAMLALASALWLRDKQIDcgkvaGVLLWYGLYGLRD------SVSRRLLGGVWD-GLTQQDL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 215 KMYLgEMYGTDqipayaAPSRAEDYSDL---------PYTYTFVGQLDPFRSETLTYVSKLAQAGVDVEFHLYPNAYHWF 285
Cdd:PRK10162 219 QMYE-EAYLSN------DADRESPYYCLfnndltrdvPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAF 291
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
61-150 |
1.57e-10 |
|
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: 61.58 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 61 LPLRIYRPK--SNHESLPVLLWIHGGGYILGS-IDDNDDTCMRFAKEAgcVVVSVDYRLAP---------EHPYPAPIED 128
Cdd:cd00312 79 LYLNVYTPKntKPGNSLPVMVWIHGGGFMFGSgSLYPGDGLAREGDNV--IVVSINYRLGVlgflstgdiELPGNYGLKD 156
|
90 100
....*....|....*....|..
gi 446780678 129 CYSALKWIADNAKSLNIDSNRI 150
Cdd:cd00312 157 QRLALKWVQDNIAAFGGDPDSV 178
|
|
| |
|
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. |
78-285 |
2.25e-70 |
|
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: 217.46 E-value: 2.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 78 LLWIHGGGYILGSIDDNDDTCMRFAKEAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIADNAKSLNIDSNRIGVAGVSA 157
Cdd:pfam07859 1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 158 GGGLTAALSLLARDRKYPSICLQMPLYPMIDDRNDTPS--ANEIKEGFVWNQKANEAGWKMYLGEMYGTDqipAYAAPSR 235
Cdd:pfam07859 81 GGNLAAAVALRARDEGLPKPAGQVLIYPGTDLRTESPSylAREFADGPLLTRAAMDWFWRLYLPGADRDD---PLASPLF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446780678 236 AEDYSDLPYTYTFVGQLDPFRSETLTYVSKLAQAGVDVEFHLYPNAYHWF 285
Cdd:pfam07859 158 ASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGF 207
|
|
| Aes |
COG0657 |
Acetyl esterase/lipase [Lipid transport and metabolism]; |
64-311 |
2.89e-66 |
|
Acetyl esterase/lipase [Lipid transport and metabolism];
Pssm-ID: 440422 [Multi-domain] Cd Length: 207 Bit Score: 206.65 E-value: 2.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 64 RIYRPKSNHESLPVLLWIHGGGYILGSIDDNDDTCMRFAKEAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIADNAKSL 143
Cdd:COG0657 2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 144 NIDSNRIgvagvsagggLTAALSLLARDRKYPSICLQMPLYPMIDDRndtpsaneikegfvwnqkaneagwkmylgemyg 223
Cdd:COG0657 82 GIDPDRIavagdsagghLAAALALRARDRGGPRPAAQVLIYPVLDLT--------------------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 224 tdqipayAAPSRAeDYSDLPYTYTFVGQLDPFRSETLTYVSKLAQAGVDVEFHLYPNAYHWFeGLNPNADVSIYAVNEIV 303
Cdd:COG0657 129 -------ASPLRA-DLAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGF-GLLAGLPEARAALAEIA 199
|
....*...
gi 446780678 304 QAIKTGFK 311
Cdd:COG0657 200 AFLRRALA 207
|
|
| PRK10162 |
PRK10162 |
acetyl esterase; |
60-285 |
2.71e-27 |
|
acetyl esterase;
Pssm-ID: 236660 [Multi-domain] Cd Length: 318 Bit Score: 108.65 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 60 PLPLRIYRPKSNheSLPVLLWIHGGGYILGSIDDNDDTCMRFAKEAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIADN 139
Cdd:PRK10162 68 QVETRLYYPQPD--SQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 140 AKSLNIDSNRIGVAGVSAGGGLTAALSLLARDRKYP-----SICLQMPLYPMIDdrndtpSANEIKEGFVWNqKANEAGW 214
Cdd:PRK10162 146 AEDYGINMSRIGFAGDSAGAMLALASALWLRDKQIDcgkvaGVLLWYGLYGLRD------SVSRRLLGGVWD-GLTQQDL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 215 KMYLgEMYGTDqipayaAPSRAEDYSDL---------PYTYTFVGQLDPFRSETLTYVSKLAQAGVDVEFHLYPNAYHWF 285
Cdd:PRK10162 219 QMYE-EAYLSN------DADRESPYYCLfnndltrdvPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAF 291
|
|
| BD-FAE |
pfam20434 |
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ... |
63-150 |
1.78e-24 |
|
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: 98.41 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 63 LRIYRPKSNHESLPVLLWIHGGGYILGS----IDDNDDTCMRFAKeAGCVVVSVDYRLAPEHPYPAPIEDCYSALKWIAD 138
Cdd:pfam20434 1 LDIYLPKNAKGPYPVVIWIHGGGWNSGDkeadMGFMTNTVKALLK-AGYAVASINYRLSTDAKFPAQIQDVKAAIRFLRA 79
|
90
....*....|..
gi 446780678 139 NAKSLNIDSNRI 150
Cdd:pfam20434 80 NAAKYGIDTNKI 91
|
|
| COesterase |
pfam00135 |
Carboxylesterase family; |
20-150 |
5.31e-12 |
|
Carboxylesterase family;
Pssm-ID: 395084 [Multi-domain] Cd Length: 513 Bit Score: 66.18 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 20 DLR------PENLQSIREGiAQMRPPTVVDDSLSLKDKVIVGPDDNPLPLRIYRPKSNHES---LPVLLWIHGGGYILGS 90
Cdd:pfam00135 40 ELRfqppepPEPWTGVRDA-TKFGPRCPQNGDLTSPGSSGLEGSEDCLYLNVYTPKELKENknkLPVMVWIHGGGFMFGS 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446780678 91 IDDNDDTcmRFAKEAGCVVVSVDYRLAP---------EHPYPAPIEDCYSALKWIADNAKSLNIDSNRI 150
Cdd:pfam00135 119 GSLYDGS--YLAAEGDVIVVTINYRLGPlgflstgddEAPGNYGLLDQVLALRWVQENIASFGGDPNRV 185
|
|
| PnbA |
COG2272 |
Carboxylesterase type B [Lipid transport and metabolism]; |
65-140 |
6.77e-12 |
|
Carboxylesterase type B [Lipid transport and metabolism];
Pssm-ID: 441873 Cd Length: 500 Bit Score: 65.68 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 65 IYRP-KSNHESLPVLLWIHGGGYILGS--IDDNDDTcmRFAKEaGCVVVSVDYRLAPE----HP------YPAP----IE 127
Cdd:COG2272 94 VWTPaLAAGAKLPVMVWIHGGGFVSGSgsEPLYDGA--ALARR-GVVVVTINYRLGALgflaLPalsgesYGASgnygLL 170
|
90
....*....|...
gi 446780678 128 DCYSALKWIADNA 140
Cdd:COG2272 171 DQIAALRWVRDNI 183
|
|
| Esterase_lipase |
cd00312 |
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ... |
61-150 |
1.57e-10 |
|
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: 61.58 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 61 LPLRIYRPK--SNHESLPVLLWIHGGGYILGS-IDDNDDTCMRFAKEAgcVVVSVDYRLAP---------EHPYPAPIED 128
Cdd:cd00312 79 LYLNVYTPKntKPGNSLPVMVWIHGGGFMFGSgSLYPGDGLAREGDNV--IVVSINYRLGVlgflstgdiELPGNYGLKD 156
|
90 100
....*....|....*....|..
gi 446780678 129 CYSALKWIADNAKSLNIDSNRI 150
Cdd:cd00312 157 QRLALKWVQDNIAAFGGDPDSV 178
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
53-285 |
5.22e-10 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 58.49 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 53 IVGPDDNPLPLRIYRPKSNhESLPVLLWIHGGGYilGSIDDNDDTCMRFAkEAGCVVVSVDYR---LAPEHPYPAPIEDC 129
Cdd:COG1506 2 FKSADGTTLPGWLYLPADG-KKYPVVVYVHGGPG--SRDDSFLPLAQALA-SRGYAVLAPDYRgygESAGDWGGDEVDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 130 YSALKWIADNAkslNIDSNRIGVAGvsaggglTAALSLLARD-RKYPSICLQMPLYPMIDDRNDTPSANEIKEGFVWNQK 208
Cdd:COG1506 78 LAAIDYLAARP---YVDPDRIGIYGhsy--ggYMALLAAARHpDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446780678 209 ANeagwkmyLGEMYGTDQIPAYAAPsraedysdlpyTYTFVGQLDPF--RSETLTYVSKLAQAGVDVEFHLYPNAYHWF 285
Cdd:COG1506 153 EA-------YAARSPLAYADKLKTP-----------LLLIHGEADDRvpPEQAERLYEALKKAGKPVELLVYPGEGHGF 213
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
53-294 |
3.70e-05 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 44.19 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 53 IVGPDDNPLPLRIYRPKSNhESLPVLLWIHGggyILGSIDDNDDTCMRFAkEAGCVVVSVDY--------------RLAP 118
Cdd:COG0412 8 IPTPDGVTLPGYLARPAGG-GPRPGVVVLHE---IFGLNPHIRDVARRLA-AAGYVVLAPDLygrggpgddpdearALMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 119 EHPYPAPIEDCYSALKWIADNAkslNIDSNRIGvagvsagggLT-------AALsLLARDRKypsiclqmplypmiddrn 191
Cdd:COG0412 83 ALDPELLAADLRAALDWLKAQP---EVDAGRVG---------VVgfcfgggLAL-LAAARGP------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 192 dtpsanEIKEGFVWnqkaneagwkmylgemYG---TDQIPAYAAPSRAEdysdlpyTYTFVGQLDPF--RSETLTYVSKL 266
Cdd:COG0412 132 ------DLAAAVSF----------------YGglpADDLLDLAARIKAP-------VLLLYGEKDPLvpPEQVAALEAAL 182
|
250 260
....*....|....*....|....*...
gi 446780678 267 AQAGVDVEFHLYPNAYHWFEglNPNADV 294
Cdd:COG0412 183 AAAGVDVELHVYPGAGHGFT--NPGRPR 208
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
57-284 |
5.93e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 37.64 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 57 DDNPLPLRIYRPKS--NHESLPVLLWIHGGGyilGSIDDNDDT---------CMRFAKEAGCVVVSVdyrLAPEHPYPAP 125
Cdd:COG4099 29 DGDTLPYRLYLPKGydPGKKYPLVLFLHGAG---ERGTDNEKQlthgapkfiNPENQAKFPAIVLAP---QCPEDDYWSD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 126 IEDCYSALKWIADNAKSLNIDSNRIgvagvsaggGLT-------AALSLLARdrkYP-------SIClqmplypmiddrn 191
Cdd:COG4099 103 TKALDAVLALLDDLIAEYRIDPDRI---------YLTglsmggyGTWDLAAR---YPdlfaaavPIC------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446780678 192 dtpsaneikegfvwnqkaneagwkmylgemygtdqipAYAAPSRAEDYSDLPyTYTFVGQLDP--FRSETLTYVSKLAQA 269
Cdd:COG4099 158 -------------------------------------GGGDPANAANLKKVP-VWIFHGAKDDvvPVEESRAMVEALKAA 199
|
250
....*....|....*
gi 446780678 270 GVDVEFHLYPNAYHW 284
Cdd:COG4099 200 GADVKYTEYPGVGHN 214
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
248-298 |
9.54e-03 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 36.82 E-value: 9.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446780678 248 FVGQLD---PFrSETLTYVSKLAQAGVDVEFHLYPNAYHWFegLNPNADVSIYA 298
Cdd:pfam00326 150 IHGLLDdrvPP-WQSLKLVAALQRKGVPFLLLIFPDEGHGI--GKPRNKVEEYA 200
|
|
| |
