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Conserved domains on  [gi|50513519|pdb|1SCK|A]
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Chain A, (S)-acetone-cyanohydrin lyase

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02211 super family cl26328
methyl indole-3-acetate methyltransferase
5-235 2.50e-37

methyl indole-3-acetate methyltransferase


The actual alignment was detected with superfamily member PLN02211:

Pssm-ID: 215128  Cd Length: 273  Bit Score: 132.32  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         5 HFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGESCGGL 84
Cdd:PLN02211  20 HFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSLPENEKVILVGHSAGGL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        85 NIAIAADKYCEKIAAAVFhnsvLPDTEHCPSYVVDK-LMEVFPDWKD-----TTYFTYTKDGKEITG-LKLGFTllRENL 157
Cdd:PLN02211 100 SVTQAIHRFPKKICLAVY----VAATMLKLGFQTDEdMKDGVPDLSEfgdvyELGFGLGPDQPPTSAiIKKEFR--RKIL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A       158 YTLCGPEEYELAKMLTRKGSlfqnILAKRPFFTKEGYGSIKK---IYVWTDQDEIFLPEFQLWQIENYKPDKVYKVEgGD 234
Cdd:PLN02211 174 YQMSPQEDSTLAAMLLRPGP----ILALRSARFEEETGDIDKvprVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELE-SD 248

                 .
1SCK_A       235 H 235
Cdd:PLN02211 249 H 249
 
Name Accession Description Interval E-value
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
5-235 2.50e-37

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 132.32  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         5 HFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGESCGGL 84
Cdd:PLN02211  20 HFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSLPENEKVILVGHSAGGL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        85 NIAIAADKYCEKIAAAVFhnsvLPDTEHCPSYVVDK-LMEVFPDWKD-----TTYFTYTKDGKEITG-LKLGFTllRENL 157
Cdd:PLN02211 100 SVTQAIHRFPKKICLAVY----VAATMLKLGFQTDEdMKDGVPDLSEfgdvyELGFGLGPDQPPTSAiIKKEFR--RKIL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A       158 YTLCGPEEYELAKMLTRKGSlfqnILAKRPFFTKEGYGSIKK---IYVWTDQDEIFLPEFQLWQIENYKPDKVYKVEgGD 234
Cdd:PLN02211 174 YQMSPQEDSTLAAMLLRPGP----ILALRSARFEEETGDIDKvprVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELE-SD 248

                 .
1SCK_A       235 H 235
Cdd:PLN02211 249 H 249
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
5-242 3.58e-32

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 117.99  E-value: 3.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A          5 HFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIG-SFDEYSEPLLTFLEALPPgEKVILVGESCGG 83
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALGL-EKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         84 LNIAIAADKYCEKIAAAVFHNSVLPDTEHcpSYVVDKLMEVFPDWKDTTYF-TYTKDGKEITGLKLGFTLLRENLYTLCG 162
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHEL--DEADRFILALFPGFFDGFVAdFAPNPLGRLVAKLLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        163 P-------EEYELAKMLTRKGSLFQNILAKRPFFTKEGYGSIKKIYVWTDQDEIFlPEFQLWQIENYKPDK-VYKVEGGD 234
Cdd:pfam00561 159 LlnkrfpsGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLV-PPQALEKLAQLFPNArLVVIPDAG 237

                  ....*...
1SCK_A        235 HLLQLTKT 242
Cdd:pfam00561 238 HFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-128 6.32e-09

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 54.62  E-value: 6.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A       12 ICHG----AWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEAL--PPGEKVILVGESCGGLN 85
Cdd:COG2267  33 LVHGlgehSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALraRPGLPVVLLGHSMGGLI 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1SCK_A       86 IAIAADKYCEKIAAAVFHNsvlpdtehcPSYVVDKLMEVFPDW 128
Cdd:COG2267 113 ALLYAARYPDRVAGLVLLA---------PAYRADPLLGPSARW 146
 
Name Accession Description Interval E-value
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
5-235 2.50e-37

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 132.32  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         5 HFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGESCGGL 84
Cdd:PLN02211  20 HFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSLPENEKVILVGHSAGGL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        85 NIAIAADKYCEKIAAAVFhnsvLPDTEHCPSYVVDK-LMEVFPDWKD-----TTYFTYTKDGKEITG-LKLGFTllRENL 157
Cdd:PLN02211 100 SVTQAIHRFPKKICLAVY----VAATMLKLGFQTDEdMKDGVPDLSEfgdvyELGFGLGPDQPPTSAiIKKEFR--RKIL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A       158 YTLCGPEEYELAKMLTRKGSlfqnILAKRPFFTKEGYGSIKK---IYVWTDQDEIFLPEFQLWQIENYKPDKVYKVEgGD 234
Cdd:PLN02211 174 YQMSPQEDSTLAAMLLRPGP----ILALRSARFEEETGDIDKvprVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELE-SD 248

                 .
1SCK_A       235 H 235
Cdd:PLN02211 249 H 249
PLN02965 PLN02965
Probable pheophorbidase
1-235 1.20e-35

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 127.34  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         1 MAFAHFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGES 80
Cdd:PLN02965   1 MPEIHFVFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        81 CGGLNIAIAADKYCEKIAAAVFHNSVLPDTEHCPSYVVDKLMEVFPDWKDTTYFTYTKdgKEITGLKLGFTLLRENLYTL 160
Cdd:PLN02965  81 IGGGSVTEALCKFTDKISMAIYVAAAMVKPGSIISPRLKNVMEGTEKIWDYTFGEGPD--KPPTGIMMKPEFVRHYYYNQ 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1SCK_A       161 CGPEEYELAKMLTRKGSL--FQNILAKRPFFTKEgygSIKKIYVWTDQDEIFLPEFQLWQIENYKPDKVYKVEGGDH 235
Cdd:PLN02965 159 SPLEDYTLSSKLLRPAPVraFQDLDKLPPNPEAE---KVPRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSDH 232
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
5-242 3.58e-32

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 117.99  E-value: 3.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A          5 HFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIG-SFDEYSEPLLTFLEALPPgEKVILVGESCGG 83
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILEALGL-EKVNLVGHSMGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         84 LNIAIAADKYCEKIAAAVFHNSVLPDTEHcpSYVVDKLMEVFPDWKDTTYF-TYTKDGKEITGLKLGFTLLRENLYTLCG 162
Cdd:pfam00561  81 LIALAYAAKYPDRVKALVLLGALDPPHEL--DEADRFILALFPGFFDGFVAdFAPNPLGRLVAKLLALLLLRLRLLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        163 P-------EEYELAKMLTRKGSLFQNILAKRPFFTKEGYGSIKKIYVWTDQDEIFlPEFQLWQIENYKPDK-VYKVEGGD 234
Cdd:pfam00561 159 LlnkrfpsGDYALAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLV-PPQALEKLAQLFPNArLVVIPDAG 237

                  ....*...
1SCK_A        235 HLLQLTKT 242
Cdd:pfam00561 238 HFAFLEGP 245
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
12-128 6.32e-09

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 54.62  E-value: 6.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A       12 ICHG----AWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEAL--PPGEKVILVGESCGGLN 85
Cdd:COG2267  33 LVHGlgehSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAALDALraRPGLPVVLLGHSMGGLI 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1SCK_A       86 IAIAADKYCEKIAAAVFHNsvlpdtehcPSYVVDKLMEVFPDW 128
Cdd:COG2267 113 ALLYAARYPDRVAGLVLLA---------PAYRADPLLGPSARW 146
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
7-107 8.22e-08

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 51.54  E-value: 8.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        7 VLIHTICHGAWIWHKLKPLLEAlGHKVTALDL---AASGVDPRQIeeigSFDEYSEPLLTFLEALPpGEKVILVGESCGG 83
Cdd:COG0596  27 VLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLrghGRSDKPAGGY----TLDDLADDLAALLDALG-LERVVLVGHSMGG 100
                        90       100
                ....*....|....*....|....
1SCK_A       84 LNIAIAADKYCEKIAAAVFHNSVL 107
Cdd:COG0596 101 MVALELAARHPERVAGLVLVDEVL 124
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
7-102 1.54e-07

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 48.29  E-value: 1.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A        7 VLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGvdprqieeiGSFDEYSEPLLTFLEAL---PPGEKVILVGESCGG 83
Cdd:COG1075   9 VLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTN---------GSIEDSAEQLAAFVDAVlaaTGAEKVDLVGHSMGG 79
                        90       100
                ....*....|....*....|.
1SCK_A       84 LNI--AIAADKYCEKIAAAVF 102
Cdd:COG1075  80 LVAryYLKRLGGAAKVARVVT 100
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
12-101 7.81e-06

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 45.54  E-value: 7.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         12 ICHGAWiwHKLKPLLEALGHKVT--ALDLAASGVDPRQIEEIGSFDEYSEplltFLEALPPGEKVILVGESCGGLnIAIA 89
Cdd:pfam12697   3 LVHGAG--LSAAPLAALLAAGVAvlAPDLPGHGSSSPPPLDLADLADLAA----LLDELGAARPVVLVGHSLGGA-VALA 75
                          90
                  ....*....|..
1SCK_A         90 ADKYCEKIAAAV 101
Cdd:pfam12697  76 AAAAALVVGVLV 87
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
12-102 8.10e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.89  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1SCK_A         12 ICHG----AWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEAL---PPGEKVILVGESCGGL 84
Cdd:pfam12146   9 LVHGlgehSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIreeHPGLPLFLLGHSMGGL 88
                          90
                  ....*....|....*...
1SCK_A         85 NIAIAADKYCEKIAAAVF 102
Cdd:pfam12146  89 IAALYALRYPDKVDGLIL 106
 
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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