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Conserved domains on  [gi|2351297925|ref|WP_266457225|]
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alpha/beta hydrolase [Streptomyces sp. NBC_00620]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10411583)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
440-536 1.46e-33

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


:

Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 122.83  E-value: 1.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 440 PVFGEGLAWASLNCGYWPVKPTGEPHRIEAKGAAPILVVGTTRDPATPYPWAQGLASQLSSATLLTYVGDGHTAYGRGSD 519
Cdd:pfam08386   1 PVFGAYWAEGLLSCAGWPVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGNA 80
                          90
                  ....*....|....*...
gi 2351297925 520 CIDSTINRYLLKGT-PAT 536
Cdd:pfam08386  81 CVDKAVDAYLLTGTlPAD 98
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
128-315 1.36e-16

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 pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 79.47  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 128 LLVNPGGPGGSAVgylqaYAGIGYPAEvRARYDMVAVDPRGVARSEPvecltGREMDTYTqtdttpddgqetdqlvdayk 207
Cdd:pfam00561   3 VLLLHGLPGSSDL-----WRKLAPALA-RDGFRVIALDLRGFGKSSR-----PKAQDDYR-------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 208 qfaegcgqhspdllrhvsTVETARDMDMLRAVLGDKKLTYVGASYGTFLGATYAGLFPDRVGRLVLDGAMDPSLSARKLT 287
Cdd:pfam00561  52 ------------------TDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAD 113
                         170       180
                  ....*....|....*....|....*...
gi 2351297925 288 EGQTAGFETAFQSFAKDCVGRSDCPLGG 315
Cdd:pfam00561 114 RFILALFPGFFDGFVADFAPNPLGRLVA 141
 
Name Accession Description Interval E-value
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
440-536 1.46e-33

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 122.83  E-value: 1.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 440 PVFGEGLAWASLNCGYWPVKPTGEPHRIEAKGAAPILVVGTTRDPATPYPWAQGLASQLSSATLLTYVGDGHTAYGRGSD 519
Cdd:pfam08386   1 PVFGAYWAEGLLSCAGWPVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGNA 80
                          90
                  ....*....|....*...
gi 2351297925 520 CIDSTINRYLLKGT-PAT 536
Cdd:pfam08386  81 CVDKAVDAYLLTGTlPAD 98
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
128-315 1.36e-16

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: 79.47  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 128 LLVNPGGPGGSAVgylqaYAGIGYPAEvRARYDMVAVDPRGVARSEPvecltGREMDTYTqtdttpddgqetdqlvdayk 207
Cdd:pfam00561   3 VLLLHGLPGSSDL-----WRKLAPALA-RDGFRVIALDLRGFGKSSR-----PKAQDDYR-------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 208 qfaegcgqhspdllrhvsTVETARDMDMLRAVLGDKKLTYVGASYGTFLGATYAGLFPDRVGRLVLDGAMDPSLSARKLT 287
Cdd:pfam00561  52 ------------------TDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAD 113
                         170       180
                  ....*....|....*....|....*...
gi 2351297925 288 EGQTAGFETAFQSFAKDCVGRSDCPLGG 315
Cdd:pfam00561 114 RFILALFPGFFDGFVADFAPNPLGRLVA 141
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
212-312 2.89e-05

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: 45.38  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 212 GCGQhSPDLLRHVSTVETARDMDMLRAVLGDKKLTYVGASYGTFLGATYAGLFPDRVGRLVL-DGAMDPSLSARKLTEGQ 290
Cdd:COG0596    59 GHGR-SDKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLvDEVLAALAEPLRRPGLA 137
                          90       100
                  ....*....|....*....|....*.
gi 2351297925 291 TAGFETAFQSFAK----DCVGRSDCP 312
Cdd:COG0596   138 PEALAALLRALARtdlrERLARITVP 163
 
Name Accession Description Interval E-value
Abhydrolase_4 pfam08386
TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear ...
440-536 1.46e-33

TAP-like protein; This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.


Pssm-ID: 429964 [Multi-domain]  Cd Length: 98  Bit Score: 122.83  E-value: 1.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 440 PVFGEGLAWASLNCGYWPVKPTGEPHRIEAKGAAPILVVGTTRDPATPYPWAQGLASQLSSATLLTYVGDGHTAYGRGSD 519
Cdd:pfam08386   1 PVFGAYWAEGLLSCAGWPVPPVPPPDESTAKGAPPVLLVQGERDPATPYEGARELARALGGAVLVTVQGAGHGAYIGGNA 80
                          90
                  ....*....|....*...
gi 2351297925 520 CIDSTINRYLLKGT-PAT 536
Cdd:pfam08386  81 CVDKAVDAYLLTGTlPAD 98
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
128-315 1.36e-16

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: 79.47  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 128 LLVNPGGPGGSAVgylqaYAGIGYPAEvRARYDMVAVDPRGVARSEPvecltGREMDTYTqtdttpddgqetdqlvdayk 207
Cdd:pfam00561   3 VLLLHGLPGSSDL-----WRKLAPALA-RDGFRVIALDLRGFGKSSR-----PKAQDDYR-------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 208 qfaegcgqhspdllrhvsTVETARDMDMLRAVLGDKKLTYVGASYGTFLGATYAGLFPDRVGRLVLDGAMDPSLSARKLT 287
Cdd:pfam00561  52 ------------------TDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAD 113
                         170       180
                  ....*....|....*....|....*...
gi 2351297925 288 EGQTAGFETAFQSFAKDCVGRSDCPLGG 315
Cdd:pfam00561 114 RFILALFPGFFDGFVADFAPNPLGRLVA 141
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
212-312 2.89e-05

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: 45.38  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351297925 212 GCGQhSPDLLRHVSTVETARDMDMLRAVLGDKKLTYVGASYGTFLGATYAGLFPDRVGRLVL-DGAMDPSLSARKLTEGQ 290
Cdd:COG0596    59 GHGR-SDKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLvDEVLAALAEPLRRPGLA 137
                          90       100
                  ....*....|....*....|....*.
gi 2351297925 291 TAGFETAFQSFAK----DCVGRSDCP 312
Cdd:COG0596   138 PEALAALLRALARtdlrERLARITVP 163
 
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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