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Conserved domains on  [gi|2459607088|gb|KAJ6892952|]
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hypothetical protein NC651_025997 [Populus alba x Populus x berolinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 283-412 6.79e-29

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


The actual alignment was detected with superfamily member cd01838:

Pssm-ID: 470049  Cd Length: 199  Bit Score: 113.50  E-value: 6.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 283 TRGVLSRFSiKFFQRKLLCKPSLVIVYFGGNDS-------------------DGASLVwPGPSYTTRIIFLSCPPVDETI 343
Cdd:cd01838    45 TRWALKVLP-KIFLEEKLAQPDLVTIFFGANDAalpgqpqhvpldeykenlrKIVSHL-KSLSPKTKVILITPPPVDEEA 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2459607088 344 VGSGLSGILSELIRTNELCQNYSNACIKLCQEMGVEVVDLFSAFQKRDDWTKACFT--------GNKIVVEEILKVL 412
Cdd:cd01838   123 WEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTdglhfsskGYELLFEEIVKVI 199
GINS_A_psf3 cd11713
Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of ...
 461-523 2.10e-11

Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


:

Pssm-ID: 212551  Cd Length: 109  Bit Score: 60.74  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 461 RMEIQADAACVDLRSRCPYFYEFGCKLAPLC--DKTIGLLLPYAF------------------------------RIIYE 508
Cdd:cd11713    15 RNALKADPTSVDLHKLSPYFYELGLKLLSLFpeDEELAEVLLETFkerfreimdhaqnasnednseflrkldeleRKLFR 94

                          90
                  ....*....|....*
gi 2459607088 509 AAQSSMAAFKKWRMG 523
Cdd:cd11713    95 AGQESLKDFKKWLKG 109
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 283-412 6.79e-29

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 113.50  E-value: 6.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 283 TRGVLSRFSiKFFQRKLLCKPSLVIVYFGGNDS-------------------DGASLVwPGPSYTTRIIFLSCPPVDETI 343
Cdd:cd01838    45 TRWALKVLP-KIFLEEKLAQPDLVTIFFGANDAalpgqpqhvpldeykenlrKIVSHL-KSLSPKTKVILITPPPVDEEA 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2459607088 344 VGSGLSGILSELIRTNELCQNYSNACIKLCQEMGVEVVDLFSAFQKRDDWTKACFT--------GNKIVVEEILKVL 412
Cdd:cd01838   123 WEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTdglhfsskGYELLFEEIVKVI 199
GINS_A_psf3 cd11713
Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of ...
 461-523 2.10e-11

Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212551  Cd Length: 109  Bit Score: 60.74  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 461 RMEIQADAACVDLRSRCPYFYEFGCKLAPLC--DKTIGLLLPYAF------------------------------RIIYE 508
Cdd:cd11713    15 RNALKADPTSVDLHKLSPYFYELGLKLLSLFpeDEELAEVLLETFkerfreimdhaqnasnednseflrkldeleRKLFR 94

                          90
                  ....*....|....*
gi 2459607088 509 AAQSSMAAFKKWRMG 523
Cdd:cd11713    95 AGQESLKDFKKWLKG 109
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 281-413 1.03e-07

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 52.34  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 281 DGTRGVLSRFsikffQRKLL-CKPSLVIVYFGGNDSdGASLVWPGPSYT----------------TRIIFLSCPPVDETI 343
Cdd:COG2755    53 ATTADLLARL-----DRDLLaLKPDLVVIELGTNDL-LRGLGVSPEEFRanlealidrlraagpgARVVLVTPPPRLRPN 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2459607088 344 VGSGLSGILSELIRtnelcqnysnaciKLCQEMGVEVVDLFSAFQKRDDWTKACFT--------GNKIVVEEILKVLR 413
Cdd:COG2755   127 YLNERIEAYNAAIR-------------ELAAEYGVPLVDLYAALRDAGDLPDLLTAdglhpnaaGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 295-393 1.09e-04

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 42.92  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 295 FQRKLLCKPSLVIVYFGGNDSD-GASLVWPGPSYT------------TRIIFLSCPPVdetivgsgLSGILSELIRTNEL 361
Cdd:pfam13472  54 LDDVLRLKPDLVVILLGTNDLGrGVSAARAAANLEalidalraagpdARVLLIGPLPV--------GPPPPLDERRLNAR 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2459607088 362 CQNYSNACIKLCQEMGVEVVDLFSAFQKRDDW 393
Cdd:pfam13472 126 IAEYNAAIREVAAERGVPYVDLWDALRDDGGW 157
 
Name Accession Description Interval E-value
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 283-412 6.79e-29

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 113.50  E-value: 6.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 283 TRGVLSRFSiKFFQRKLLCKPSLVIVYFGGNDS-------------------DGASLVwPGPSYTTRIIFLSCPPVDETI 343
Cdd:cd01838    45 TRWALKVLP-KIFLEEKLAQPDLVTIFFGANDAalpgqpqhvpldeykenlrKIVSHL-KSLSPKTKVILITPPPVDEEA 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2459607088 344 VGSGLSGILSELIRTNELCQNYSNACIKLCQEMGVEVVDLFSAFQKRDDWTKACFT--------GNKIVVEEILKVL 412
Cdd:cd01838   123 WEKSLEDGGSQPGRTNELLKQYAEACVEVAEELGVPVIDLWTAMQEEAGWLESLLTdglhfsskGYELLFEEIVKVI 199
GINS_A_psf3 cd11713
Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of ...
 461-523 2.10e-11

Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212551  Cd Length: 109  Bit Score: 60.74  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 461 RMEIQADAACVDLRSRCPYFYEFGCKLAPLC--DKTIGLLLPYAF------------------------------RIIYE 508
Cdd:cd11713    15 RNALKADPTSVDLHKLSPYFYELGLKLLSLFpeDEELAEVLLETFkerfreimdhaqnasnednseflrkldeleRKLFR 94

                          90
                  ....*....|....*
gi 2459607088 509 AAQSSMAAFKKWRMG 523
Cdd:cd11713    95 AGQESLKDFKKWLKG 109
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 281-413 1.03e-07

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 52.34  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 281 DGTRGVLSRFsikffQRKLL-CKPSLVIVYFGGNDSdGASLVWPGPSYT----------------TRIIFLSCPPVDETI 343
Cdd:COG2755    53 ATTADLLARL-----DRDLLaLKPDLVVIELGTNDL-LRGLGVSPEEFRanlealidrlraagpgARVVLVTPPPRLRPN 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2459607088 344 VGSGLSGILSELIRtnelcqnysnaciKLCQEMGVEVVDLFSAFQKRDDWTKACFT--------GNKIVVEEILKVLR 413
Cdd:COG2755   127 YLNERIEAYNAAIR-------------ELAAEYGVPLVDLYAALRDAGDLPDLLTAdglhpnaaGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 295-393 1.09e-04

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 42.92  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 295 FQRKLLCKPSLVIVYFGGNDSD-GASLVWPGPSYT------------TRIIFLSCPPVdetivgsgLSGILSELIRTNEL 361
Cdd:pfam13472  54 LDDVLRLKPDLVVILLGTNDLGrGVSAARAAANLEalidalraagpdARVLLIGPLPV--------GPPPPLDERRLNAR 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2459607088 362 CQNYSNACIKLCQEMGVEVVDLFSAFQKRDDW 393
Cdd:pfam13472 126 IAEYNAAIREVAAERGVPYVDLWDALRDDGGW 157
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 281-387 3.50e-04

NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.


Pssm-ID: 238879  Cd Length: 174  Bit Score: 41.55  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 281 DGTRGVLSRFSIKFFQRKLLCK-PSLVIVYFGGNDsdgasLVWPGPS------------------YTTRIIFLSCPPVde 341
Cdd:cd01841    29 LGIAGISSRQYLEHIEPQLIQKnPSKVFLFLGTND-----IGKEVSSnqfikwyrdiieqireefPNTKIYLLSVLPV-- 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2459607088 342 tivgsglSGILSELIRTNELCQNYSNACIKLCQEMGVEVVDLFSAF 387
Cdd:cd01841   102 -------LEEDEIKTRSNTRIQRLNDAIKELAPELGVTFIDLNDVL 140
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 281-399 2.06e-03

sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238866  Cd Length: 169  Bit Score: 39.18  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459607088 281 DGTRGVLSRFsikffQRKLLCKPSLVIVYFGGND-SDGASL------------VWPGPSYTTRIIFLSCPPVdetivgSG 347
Cdd:cd01828    32 DTTRGLLARL-----DEDVALQPKAIFIMIGINDlAQGTSDedivanyrtileKLRKHFPNIKIVVQSILPV------GE 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2459607088 348 LSGILSELIRtnELCQNYsnacIKLCQEMGVEVVDLFSAFQKRDDWTKACFT 399
Cdd:cd01828   101 LKSIPNEQIE--ELNRQL----AQLAQQEGVTFLDLWAVFTNADGDLKNEFT 146
 
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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