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Conserved domains on  [gi|1002292742|ref|XP_015650718|]
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putative methylesterase 14, chloroplastic [Oryza sativa Japonica Group]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
118-364 6.13e-65

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 PLN02965:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 255  Bit Score: 207.85  E-value: 6.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 118 VLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYSKPLIDYLNKLPENEKVILVGHSCGGASV 197
Cdd:PLN02965    7 VFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHSIGGGSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 198 SYALEQCPKKISKAIFLTATMVKDGQRPfdvfSEELASADVFLQESQLLIYGNGKDKPPTGLMFDKQQIKGLYFNTSPSK 277
Cdd:PLN02965   87 TEALCKFTDKISMAIYVAAAMVKPGSII----SPRLKNVMEGTEKIWDYTFGEGPDKPPTGIMMKPEFVRHYYYNQSPLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 278 DTVLAAVSMRPIPLAPI--MEKLSLTPENyGTVPRYFIQTLDDRMLSPDVQEKLVRENPPDGIFKIKGGDHCPFFSKPQS 355
Cdd:PLN02965  163 DYTLSSKLLRPAPVRAFqdLDKLPPNPEA-EKVPRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSDHSAFFSVPTT 241

                  ....*....
gi 1002292742 356 LNKILLEIA 364
Cdd:PLN02965  242 LFQYLLQAV 250
 
Name Accession Description Interval E-value
PLN02965 PLN02965
Probable pheophorbidase
118-364 6.13e-65

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 207.85  E-value: 6.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 118 VLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYSKPLIDYLNKLPENEKVILVGHSCGGASV 197
Cdd:PLN02965    7 VFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHSIGGGSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 198 SYALEQCPKKISKAIFLTATMVKDGQRPfdvfSEELASADVFLQESQLLIYGNGKDKPPTGLMFDKQQIKGLYFNTSPSK 277
Cdd:PLN02965   87 TEALCKFTDKISMAIYVAAAMVKPGSII----SPRLKNVMEGTEKIWDYTFGEGPDKPPTGIMMKPEFVRHYYYNQSPLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 278 DTVLAAVSMRPIPLAPI--MEKLSLTPENyGTVPRYFIQTLDDRMLSPDVQEKLVRENPPDGIFKIKGGDHCPFFSKPQS 355
Cdd:PLN02965  163 DYTLSSKLLRPAPVRAFqdLDKLPPNPEA-EKVPRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSDHSAFFSVPTT 241

                  ....*....
gi 1002292742 356 LNKILLEIA 364
Cdd:PLN02965  242 LFQYLLQAV 250
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
117-351 4.83e-15

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 73.66  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGegfgAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYskplIDYLNKLPENEKVILVGHSCGGAs 196
Cdd:pfam12697   1 VVLVHG----AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADL----AALLDELGAARPVVLVGHSLGGA- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 197 vsYALEQCPKKISKAIFLTATMVKDGQRPFDvfseelasadvflqesqLLIYGNGKDKPPTGLMFDKQQIKGLYFNTSPS 276
Cdd:pfam12697  72 --VALAAAAAALVVGVLVAPLAAPPGLLAAL-----------------LALLARLGAALAAPAWLAAESLARGFLDDLPA 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002292742 277 KDTVLAAVSmRPIPLAPIMekLSLTPENYGTVPR-YFIQTLDDRMLSPDVQEkLVRENPPDGIFKIKGGDHCPFFS 351
Cdd:pfam12697 133 DAEWAAALA-RLAALLAAL--ALLPLAAWRDLPVpVLVLAEEDRLVPELAQR-LLAALAGARLVVLPGAGHLPLDD 204
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
117-365 5.29e-13

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: 67.72  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWCWYKTISLLEEaGLDPIALDLTGSGiDNADTNSIATLADYSKPLIDYLNKLPEnEKVILVGHSCGGAS 196
Cdd:COG0596    26 VVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHG-RSDKPAGGYTLDDLADDLAALLDALGL-ERVVLVGHSMGGMV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 197 VSYALEQCPKKISKAIfLTATMVKDGQRPFDVFSEELASADVFLQesqlliygngkdkpptglmfdkqqikglyfntsps 276
Cdd:COG0596   103 ALELAARHPERVAGLV-LVDEVLAALAEPLRRPGLAPEALAALLR----------------------------------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 277 kdtvlaavSMRPIPLAPIMEKLsltpenygTVPRYFIQTLDDRMLSPDVQEKLVRENPPDGIFKIKGGDHCPFFSKPQSL 356
Cdd:COG0596   147 --------ALARTDLRERLARI--------TVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAF 210

                  ....*....
gi 1002292742 357 NKILLEIAQ 365
Cdd:COG0596   211 AAALRDFLA 219
 
Name Accession Description Interval E-value
PLN02965 PLN02965
Probable pheophorbidase
118-364 6.13e-65

Probable pheophorbidase


Pssm-ID: 178549 [Multi-domain]  Cd Length: 255  Bit Score: 207.85  E-value: 6.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 118 VLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYSKPLIDYLNKLPENEKVILVGHSCGGASV 197
Cdd:PLN02965    7 VFVHGASHGAWCWYKLATLLDAAGFKSTCVDLTGAGISLTDSNTVSSSDQYNRPLFALLSDLPPDHKVILVGHSIGGGSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 198 SYALEQCPKKISKAIFLTATMVKDGQRPfdvfSEELASADVFLQESQLLIYGNGKDKPPTGLMFDKQQIKGLYFNTSPSK 277
Cdd:PLN02965   87 TEALCKFTDKISMAIYVAAAMVKPGSII----SPRLKNVMEGTEKIWDYTFGEGPDKPPTGIMMKPEFVRHYYYNQSPLE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 278 DTVLAAVSMRPIPLAPI--MEKLSLTPENyGTVPRYFIQTLDDRMLSPDVQEKLVRENPPDGIFKIKGGDHCPFFSKPQS 355
Cdd:PLN02965  163 DYTLSSKLLRPAPVRAFqdLDKLPPNPEA-EKVPRVYIKTAKDNLFDPVRQDVMVENWPPAQTYVLEDSDHSAFFSVPTT 241

                  ....*....
gi 1002292742 356 LNKILLEIA 364
Cdd:PLN02965  242 LFQYLLQAV 250
PLN02211 PLN02211
methyl indole-3-acetate methyltransferase
110-364 7.65e-62

methyl indole-3-acetate methyltransferase


Pssm-ID: 215128  Cd Length: 273  Bit Score: 200.50  E-value: 7.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 110 ENLETKKIVLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYSKPLIDYLNKLPENEKVILVG 189
Cdd:PLN02211   14 PNRQPPHFVLIHGISGGSWCWYKIRCLMENSGYKVTCIDLKSAGIDQSDADSVTTFDEYNKPLIDFLSSLPENEKVILVG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 190 HSCGGASVSYALEQCPKKISKAIFLTATMVKDGQRPFDVFSEELASADVFlQESQLLIYGNGKDKPPTGLMFDKQQIKGL 269
Cdd:PLN02211   94 HSAGGLSVTQAIHRFPKKICLAVYVAATMLKLGFQTDEDMKDGVPDLSEF-GDVYELGFGLGPDQPPTSAIIKKEFRRKI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 270 YFNTSPSKDTVLAAVSMRPIPLAPIME-KLSLTPENYGTVPRYFIQTLDDRMLSPDVQEKLVRENPPDGIFKIKgGDHCP 348
Cdd:PLN02211  173 LYQMSPQEDSTLAAMLLRPGPILALRSaRFEEETGDIDKVPRVYIKTLHDHVVKPEQQEAMIKRWPPSQVYELE-SDHSP 251
                         250
                  ....*....|....*.
gi 1002292742 349 FFSKPQSLNKILLEIA 364
Cdd:PLN02211  252 FFSTPFLLFGLLIKAA 267
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
117-351 4.83e-15

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 73.66  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGegfgAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYskplIDYLNKLPENEKVILVGHSCGGAs 196
Cdd:pfam12697   1 VVLVHG----AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADL----AALLDELGAARPVVLVGHSLGGA- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 197 vsYALEQCPKKISKAIFLTATMVKDGQRPFDvfseelasadvflqesqLLIYGNGKDKPPTGLMFDKQQIKGLYFNTSPS 276
Cdd:pfam12697  72 --VALAAAAAALVVGVLVAPLAAPPGLLAAL-----------------LALLARLGAALAAPAWLAAESLARGFLDDLPA 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002292742 277 KDTVLAAVSmRPIPLAPIMekLSLTPENYGTVPR-YFIQTLDDRMLSPDVQEkLVRENPPDGIFKIKGGDHCPFFS 351
Cdd:pfam12697 133 DAEWAAALA-RLAALLAAL--ALLPLAAWRDLPVpVLVLAEEDRLVPELAQR-LLAALAGARLVVLPGAGHLPLDD 204
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
117-353 3.81e-14

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: 71.38  E-value: 3.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGID----NADTNSIATLADYskplIDY-LNKLPeNEKVILVGHS 191
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSsrpkAQDDYRTDDLAED----LEYiLEALG-LEKVNLVGHS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 192 CGGASVSYALEQCPKKISKAIFLTAT--------------MVKDGQRPFDVFSEELASADVFLQESQLLIYGNGKDKPPT 257
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGALdppheldeadrfilALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 258 GLMFDkqQIKGLYFNTSPSKDTVlAAVSMRPIPLAPIMEKLsltpeNYGTVPRYFIQTLDDRMLSPDVQEKLVRENPPDG 337
Cdd:pfam00561 158 PLLNK--RFPSGDYALAKSLVTG-ALLFIETWSTELRAKFL-----GRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNAR 229
                         250
                  ....*....|....*.
gi 1002292742 338 IFKIKGGDHCPFFSKP 353
Cdd:pfam00561 230 LVVIPDAGHFAFLEGP 245
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
117-365 5.29e-13

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: 67.72  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWCWYKTISLLEEaGLDPIALDLTGSGiDNADTNSIATLADYSKPLIDYLNKLPEnEKVILVGHSCGGAS 196
Cdd:COG0596    26 VVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHG-RSDKPAGGYTLDDLADDLAALLDALGL-ERVVLVGHSMGGMV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 197 VSYALEQCPKKISKAIfLTATMVKDGQRPFDVFSEELASADVFLQesqlliygngkdkpptglmfdkqqikglyfntsps 276
Cdd:COG0596   103 ALELAARHPERVAGLV-LVDEVLAALAEPLRRPGLAPEALAALLR----------------------------------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 277 kdtvlaavSMRPIPLAPIMEKLsltpenygTVPRYFIQTLDDRMLSPDVQEKLVRENPPDGIFKIKGGDHCPFFSKPQSL 356
Cdd:COG0596   147 --------ALARTDLRERLARI--------TVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAF 210

                  ....*....
gi 1002292742 357 NKILLEIAQ 365
Cdd:COG0596   211 AAALRDFLA 219
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
117-221 6.30e-11

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 61.56  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGIDNADTNSIATLADYS---KPLIDYLNKLPeNEKVILVGHSCG 193
Cdd:COG2267    31 VVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYVddlRAALDALRARP-GLPVVLLGHSMG 109
                          90       100
                  ....*....|....*....|....*...
gi 1002292742 194 GASVSYALEQCPKKISKAIFLTATMVKD 221
Cdd:COG2267   110 GLIALLYAARYPDRVAGLVLLAPAYRAD 137
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
117-214 5.03e-10

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 56.38  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWCWYKTISLLEEAGLDPIALDLtgsgidNADTNSIATLADYskpLIDYLNKLPEN---EKVILVGHSCG 193
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAGYPVYALNY------PSTNGSIEDSAEQ---LAAFVDAVLAAtgaEKVDLVGHSMG 78
                          90       100
                  ....*....|....*....|...
gi 1002292742 194 GASVSYALEQC--PKKISKAIFL 214
Cdd:COG1075    79 GLVARYYLKRLggAAKVARVVTL 101
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
117-212 2.72e-04

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.93  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWC-WYKTISLLEEAGLDPIALDLTGSGiDNADTNSIATLADYsKPLIDYLNKLPE--NEKVILVGHSCG 193
Cdd:COG1506    26 VVYVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYG-ESAGDWGGDEVDDV-LAAIDYLAARPYvdPDRIGIYGHSYG 103
                          90
                  ....*....|....*....
gi 1002292742 194 GASVSYALEQCPKKISKAI 212
Cdd:COG1506   104 GYMALLAAARHPDRFKAAV 122
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
117-195 1.36e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 40.70  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGegFGA----WcwyktisLLEEAGLDP----IALDLTGSG--IDNADTNSIATLADYskpLIDYLNKLPEnEKVI 186
Cdd:PRK14875  134 VVLIHG--FGGdlnnW-------LFNHAALAAgrpvIALDLPGHGasSKAVGAGSLDELAAA---VLAFLDALGI-ERAH 200

                  ....*....
gi 1002292742 187 LVGHSCGGA 195
Cdd:PRK14875  201 LVGHSMGGA 209
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
117-225 1.45e-03

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: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002292742 117 IVLVHGEGFGAWCWYKTISLLEEAGLDPIALDLTGSGI-DN--ADTNSIATLADYSKPLIDYLNKLPENEKVILVGHSCG 193
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRsDGkrGHVPSFDDYVDDLDTFVDKIREEHPGLPLFLLGHSMG 86
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1002292742 194 GASVSYALEQCPKKISKAIfLTATMVKDGQRP 225
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLI-LSAPALKIKPYL 117
 
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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