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Conserved domains on  [gi|119610601|gb|EAW90195|]
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neuroligin 2, isoform CRA_a [Homo sapiens]

Protein Classification

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, ...
 11-90 1.29e-20

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 pfam00135:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 513  Bit Score: 93.53  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610601   11 NFSKNDVMLSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFW 90
Cdd:pfam00135 448 LFTEEDEKLSRKMMTYWTNFAKTGNPNGP--------------EGLPKWPPYTDENGQYLSIDLEPRVKQGLKAERCAFW 513
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
11-90 1.29e-20

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 93.53  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610601   11 NFSKNDVMLSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFW 90
Cdd:pfam00135 448 LFTEEDEKLSRKMMTYWTNFAKTGNPNGP--------------EGLPKWPPYTDENGQYLSIDLEPRVKQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
19-94 1.60e-06

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 49.89  E-value: 1.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119610601  19 LSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrfEEVVWSKFNSKEKQYLHIGLKPRV-RDNYRANKVAFWLELV 94
Cdd:COG2272  439 LSDQMQAYWVNFARTGDPNGP---------------GLPEWPAYDPEDRAVMVFDAEPRVvNDPDAEERLDLWDGVV 500
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 1-76 9.28e-06

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: 47.71  E-value: 9.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119610601   1 MVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrFEEVVWSKFNSKEKQYLHIGLKP 76
Cdd:cd00312  427 FVFGNPLLKEGLREEEEKLSRTMMKYWANFAKTGNPNTE--------------GNLVVWPAYTSESEKYLDINIEG 488
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
11-90 1.29e-20

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 93.53  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119610601   11 NFSKNDVMLSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFW 90
Cdd:pfam00135 448 LFTEEDEKLSRKMMTYWTNFAKTGNPNGP--------------EGLPKWPPYTDENGQYLSIDLEPRVKQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
19-94 1.60e-06

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 49.89  E-value: 1.60e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119610601  19 LSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrfEEVVWSKFNSKEKQYLHIGLKPRV-RDNYRANKVAFWLELV 94
Cdd:COG2272  439 LSDQMQAYWVNFARTGDPNGP---------------GLPEWPAYDPEDRAVMVFDAEPRVvNDPDAEERLDLWDGVV 500
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 1-76 9.28e-06

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: 47.71  E-value: 9.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119610601   1 MVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPvpqdtkfihtkpnrFEEVVWSKFNSKEKQYLHIGLKP 76
Cdd:cd00312  427 FVFGNPLLKEGLREEEEKLSRTMMKYWANFAKTGNPNTE--------------GNLVVWPAYTSESEKYLDINIEG 488
 
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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