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Conserved domains on  [gi|964126932|ref|XP_014762863|]
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hormone-sensitive lipase [Drosophila ananassae]

Protein Classification

HSL_N and Abhydrolase domain-containing protein( domain architecture ID 12070005)

protein containing domains HSL_N, Abhydrolase, and Aes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
57-382 2.91e-158

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


:

Pssm-ID: 461882  Cd Length: 306  Bit Score: 464.81  E-value: 2.91e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932   57 YGSLFSACQEHASFFAKDNTEYGQRLHAAHIAWQDFIVLANRLVLQIQAFAHEYDFDEQTPGNGYRSFIYVTNACISHGS 136
Cdd:pfam06350   2 FETLRSLCEDNAAYFEGDSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLHII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  137 NICRQLLAFRSTLFFRKKFYMKEVEACSQLLSSLCTCMQYLLILRQWSvNTGDLFACGNHTAEQLFELGDTINQYCFYGR 216
Cdd:pfam06350  82 KLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWS-EPGDLFPSEDHSSEELLREYETINQYCFYGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  217 CLGFQYGDSIRGVLRFLGISMASYSESFYSQegDGAIVKTTRSLWTSGKYLMNPELRARRIVNISQNAKIDFCKSFWFLA 296
Cdd:pfam06350 161 CLGFQFCPSLRPILKTISISMASFSEGYYNN--GGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  297 ESELMLKLPSIVGSSIKVNRLIELPAEPLKLPRRKgfkpkensssdvnqnvgDDEFVDIPVPTAHLGPGlPVSVRLLSAR 376
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLPLSD-----------------DGEMVTIPPPSAHIGPG-PVHVRLISYE 300

                  ....*.
gi 964126932  377 RRSGML 382
Cdd:pfam06350 301 LREGQD 306
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
401-545 2.35e-33

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam07859:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 208  Bit Score: 127.71  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  401 LFHCHGGGFVAQSSKSHELYLRDWAVSLDCPILSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAERIVCAGDSA 480
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 964126932  481 GANLSIGVALKCIEQGVRVPDGLFLaYCP--TLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPA 545
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVL-IYPgtDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
772-856 5.17e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.03  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 772 DPFLSPYWASdewLSQMPETKILTLNMDPCLDDCVMFAKKLKRLGRDVQLEILEGLPHGFLNFTMLSnEAMEGSKHCIES 851
Cdd:COG0657  126 DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP-EARAALAEIAAF 201

                 ....*
gi 964126932 852 LKKLL 856
Cdd:COG0657  202 LRRAL 206
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
57-382 2.91e-158

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 464.81  E-value: 2.91e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932   57 YGSLFSACQEHASFFAKDNTEYGQRLHAAHIAWQDFIVLANRLVLQIQAFAHEYDFDEQTPGNGYRSFIYVTNACISHGS 136
Cdd:pfam06350   2 FETLRSLCEDNAAYFEGDSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLHII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  137 NICRQLLAFRSTLFFRKKFYMKEVEACSQLLSSLCTCMQYLLILRQWSvNTGDLFACGNHTAEQLFELGDTINQYCFYGR 216
Cdd:pfam06350  82 KLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWS-EPGDLFPSEDHSSEELLREYETINQYCFYGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  217 CLGFQYGDSIRGVLRFLGISMASYSESFYSQegDGAIVKTTRSLWTSGKYLMNPELRARRIVNISQNAKIDFCKSFWFLA 296
Cdd:pfam06350 161 CLGFQFCPSLRPILKTISISMASFSEGYYNN--GGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  297 ESELMLKLPSIVGSSIKVNRLIELPAEPLKLPRRKgfkpkensssdvnqnvgDDEFVDIPVPTAHLGPGlPVSVRLLSAR 376
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLPLSD-----------------DGEMVTIPPPSAHIGPG-PVHVRLISYE 300

                  ....*.
gi 964126932  377 RRSGML 382
Cdd:pfam06350 301 LREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
401-545 2.35e-33

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: 127.71  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  401 LFHCHGGGFVAQSSKSHELYLRDWAVSLDCPILSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAERIVCAGDSA 480
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 964126932  481 GANLSIGVALKCIEQGVRVPDGLFLaYCP--TLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPA 545
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVL-IYPgtDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
392-556 4.05e-32

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 124.21  E-value: 4.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 392 KPPPPSRSILFHCHGGGFVAQSSKSHELYLRDWAVSLDCPILSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAE 471
Cdd:COG0657    7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 472 RIVCAGDSAGANLSIGVALKCIEQGVRVPDGLFLAYCPTLVSFVPSPARLLCL---------MDPLLPFGFMM-RCLRAY 541
Cdd:COG0657   87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTASPLRADLAGLpptlivtgeADPLVDESEALaAALRAA 166
                        170
                 ....*....|....*
gi 964126932 542 AAPAQETLRENARHV 556
Cdd:COG0657  167 GVPVELHVYPGGGHG 181
PRK10162 PRK10162
acetyl esterase;
353-490 8.78e-21

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 94.40  E-value: 8.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 353 VDIPVPTAHlgpGlPVSVRLLSarrrsgmlgegryrgwhkPPPPSRSILFHCHGGGFVAQSSKSHELYLRDWAVSLDCPI 432
Cdd:PRK10162  58 RAYMVPTPY---G-QVETRLYY------------------PQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTV 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 964126932 433 LSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAERIVCAGDSAGANLSIGVAL 490
Cdd:PRK10162 116 IGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLALASAL 173
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
772-856 5.17e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.03  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 772 DPFLSPYWASdewLSQMPETKILTLNMDPCLDDCVMFAKKLKRLGRDVQLEILEGLPHGFLNFTMLSnEAMEGSKHCIES 851
Cdd:COG0657  126 DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP-EARAALAEIAAF 201

                 ....*
gi 964126932 852 LKKLL 856
Cdd:COG0657  202 LRRAL 206
 
Name Accession Description Interval E-value
HSL_N pfam06350
Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian ...
57-382 2.91e-158

Hormone-sensitive lipase (HSL) N-terminus; This family consists of several mammalian hormone-sensitive lipase (HSL) proteins (EC:3.1.1.-). Hormone-sensitive lipase, a key enzyme in fatty acid mobilization, overall energy homeostasis, and possibly steroidogenesis, is acutely controlled through reversible phosphorylation by catecholamines and insulin.


Pssm-ID: 461882  Cd Length: 306  Bit Score: 464.81  E-value: 2.91e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932   57 YGSLFSACQEHASFFAKDNTEYGQRLHAAHIAWQDFIVLANRLVLQIQAFAHEYDFDEQTPGNGYRSFIYVTNACISHGS 136
Cdd:pfam06350   2 FETLRSLCEDNAAYFEGDSSENGQRLVAAFVGIQDHIDALEPLVKGIAAVAHHFDFDEETPGNGYRSLVKVVDSCLLHII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  137 NICRQLLAFRSTLFFRKKFYMKEVEACSQLLSSLCTCMQYLLILRQWSvNTGDLFACGNHTAEQLFELGDTINQYCFYGR 216
Cdd:pfam06350  82 KLCRYIASNRDSLFFRKSHYVKELEAYSQLLASLRACLQHLQTLLSWS-EPGDLFPSEDHSSEELLREYETINQYCFYGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  217 CLGFQYGDSIRGVLRFLGISMASYSESFYSQegDGAIVKTTRSLWTSGKYLMNPELRARRIVNISQNAKIDFCKSFWFLA 296
Cdd:pfam06350 161 CLGFQFCPSLRPILKTISISMASFSEGYYNN--GGGLGRAASSLFTSGKYALDPELRARRIVNITQNADVDFCKAFWNLT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  297 ESELMLKLPSIVGSSIKVNRLIELPAEPLKLPRRKgfkpkensssdvnqnvgDDEFVDIPVPTAHLGPGlPVSVRLLSAR 376
Cdd:pfam06350 239 ESELLSSLPSIVSPSVAVNRVISIPPEPLTLPLSD-----------------DGEMVTIPPPSAHIGPG-PVHVRLISYE 300

                  ....*.
gi 964126932  377 RRSGML 382
Cdd:pfam06350 301 LREGQD 306
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
401-545 2.35e-33

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: 127.71  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  401 LFHCHGGGFVAQSSKSHELYLRDWAVSLDCPILSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAERIVCAGDSA 480
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 964126932  481 GANLSIGVALKCIEQGVRVPDGLFLaYCP--TLVSFVPSPARLLCLMDPLLPFGFMMRCLRAYAAPA 545
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVL-IYPgtDLRTESPSYLAREFADGPLLTRAAMDWFWRLYLPGA 146
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
392-556 4.05e-32

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 124.21  E-value: 4.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 392 KPPPPSRSILFHCHGGGFVAQSSKSHELYLRDWAVSLDCPILSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAE 471
Cdd:COG0657    7 AGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAELGIDPD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 472 RIVCAGDSAGANLSIGVALKCIEQGVRVPDGLFLAYCPTLVSFVPSPARLLCL---------MDPLLPFGFMM-RCLRAY 541
Cdd:COG0657   87 RIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLTASPLRADLAGLpptlivtgeADPLVDESEALaAALRAA 166
                        170
                 ....*....|....*
gi 964126932 542 AAPAQETLRENARHV 556
Cdd:COG0657  167 GVPVELHVYPGGGHG 181
PRK10162 PRK10162
acetyl esterase;
353-490 8.78e-21

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 94.40  E-value: 8.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 353 VDIPVPTAHlgpGlPVSVRLLSarrrsgmlgegryrgwhkPPPPSRSILFHCHGGGFVAQSSKSHELYLRDWAVSLDCPI 432
Cdd:PRK10162  58 RAYMVPTPY---G-QVETRLYY------------------PQPDSQATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTV 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 964126932 433 LSVDYSLAPEAPFPRALQEVYYAYCWMLNNTELLGTTAERIVCAGDSAGANLSIGVAL 490
Cdd:PRK10162 116 IGIDYTLSPEARFPQAIEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLALASAL 173
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
392-485 1.20e-07

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: 53.34  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  392 KPPPPsrsILFHCHGGGFVAQSSKS---------HELYLRDWAVSldcpilSVDYSLAPEAPFPRALQEVYYAYCWMLNN 462
Cdd:pfam20434  10 KGPYP---VVIWIHGGGWNSGDKEAdmgfmtntvKALLKAGYAVA------SINYRLSTDAKFPAQIQDVKAAIRFLRAN 80
                          90       100
                  ....*....|....*....|...
gi 964126932  463 TELLGTTAERIVCAGDSAGANLS 485
Cdd:pfam20434  81 AAKYGIDTNKIALMGFSAGGHLA 103
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
772-856 5.17e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.03  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932 772 DPFLSPYWASdewLSQMPETKILTLNMDPCLDDCVMFAKKLKRLGRDVQLEILEGLPHGFLNFTMLSnEAMEGSKHCIES 851
Cdd:COG0657  126 DLTASPLRAD---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP-EARAALAEIAAF 201

                 ....*
gi 964126932 852 LKKLL 856
Cdd:COG0657  202 LRRAL 206
Say1_Mug180 pfam10340
Steryl acetyl hydrolase; This entry includes budding yeast steryl acetyl hydrolase 1 (Say1) ...
391-492 5.99e-03

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: 39.82  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964126932  391 HKPPPPSRSILFHCHGGGFVAQSSKSHELYLRDWAVSL-DCPILSVDYSLAPEAP----FPRALQEVYYAYCWMlnnTEL 465
Cdd:pfam10340 115 ETFDPKVDPILLYYHGGGFALKLIPVTLVFLNNLGKYFpDMAILVSDYTVTANCPqsytYPLQVLQCLAVYDYL---TLT 191
                          90       100
                  ....*....|....*....|....*..
gi 964126932  466 LGTTaeRIVCAGDSAGANLSIGVALKC 492
Cdd:pfam10340 192 KGCK--NVTLMGDSAGGNLVLNILLYL 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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