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Conserved domains on  [gi|490246944|ref|WP_004145104|]
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MULTISPECIES: alpha/beta hydrolase-fold protein [Klebsiella]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
78-388 1.08e-77

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


:

Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 242.45  E-value: 1.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  78 AADGVWTWKSEPMKPNLYEYYFDVDGFRSVDTGSRYQK--PQRQVNTSLILVPGSILDDREVAHGDLRTLTYHSKALNAE 155
Cdd:COG2382   15 AALLLLAALAGAAPPGLLVASAVVVVRVLPAAAAAARLlaPVVAAAVVVLGGPPPATDDKDVPHGTVETVTYPSKALGRT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 156 RRLYVWTPPGYSGTGDPLPVLYFYHGFGDSGLSAIDQGRIPQIMDNLLAEGKIKPMLVVVPDTETDipeavaenfppqER 235
Cdd:COG2382   95 RRVWVYLPPGYDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILDNLIAAGKIPPMIVVMPDGGDG------------GD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 236 RKTFYPLNAQAAdKELMQDIIPLIDARFNVRKDADGRALAGLSQGGYQALVSGMNHLESFGWLATFSGVTTTTVPNA--- 312
Cdd:COG2382  163 RGTEGPGNDAFE-RFLAEELIPFVEKNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDAdrg 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246944 313 GVEAQLKQPdAINKQLRnFTVVVGEKDSVTgKDIAGLKSELEKQQIKFDYHQYPGlNHEMDVWRPAYAEFVQKLFK 388
Cdd:COG2382  242 GWAELLAAG-APKKPLR-FYLDVGTEDDLL-EANRALAAALKAKGYDVEYREFPG-GHDWAVWRAALPDFLPWLFK 313
E_set super family cl28984
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
39-114 3.37e-06

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


The actual alignment was detected with superfamily member cd02853:

Pssm-ID: 475140 [Multi-domain]  Cd Length: 84  Bit Score: 44.82  E-value: 3.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490246944  39 TQVNADKSITYRLFAPDARRVSIVTgatpDSFVSHDMTKAADGVWTWKSEPMKPNLyEYYFDVDGFRSV-DTGSRYQ 114
Cdd:cd02853    2 AELLGDGGVRFRVWAPAAESVELVL----EGGRRLPMQRDGDGWFEAEVAAAGAGT-RYRFRLDGGLPVpDPASRFQ 73
 
Name Accession Description Interval E-value
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
78-388 1.08e-77

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 242.45  E-value: 1.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  78 AADGVWTWKSEPMKPNLYEYYFDVDGFRSVDTGSRYQK--PQRQVNTSLILVPGSILDDREVAHGDLRTLTYHSKALNAE 155
Cdd:COG2382   15 AALLLLAALAGAAPPGLLVASAVVVVRVLPAAAAAARLlaPVVAAAVVVLGGPPPATDDKDVPHGTVETVTYPSKALGRT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 156 RRLYVWTPPGYSGTGDPLPVLYFYHGFGDSGLSAIDQGRIPQIMDNLLAEGKIKPMLVVVPDTETDipeavaenfppqER 235
Cdd:COG2382   95 RRVWVYLPPGYDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILDNLIAAGKIPPMIVVMPDGGDG------------GD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 236 RKTFYPLNAQAAdKELMQDIIPLIDARFNVRKDADGRALAGLSQGGYQALVSGMNHLESFGWLATFSGVTTTTVPNA--- 312
Cdd:COG2382  163 RGTEGPGNDAFE-RFLAEELIPFVEKNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDAdrg 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246944 313 GVEAQLKQPdAINKQLRnFTVVVGEKDSVTgKDIAGLKSELEKQQIKFDYHQYPGlNHEMDVWRPAYAEFVQKLFK 388
Cdd:COG2382  242 GWAELLAAG-APKKPLR-FYLDVGTEDDLL-EANRALAAALKAKGYDVEYREFPG-GHDWAVWRAALPDFLPWLFK 313
E_set_Esterase_like_N cd11294
N-terminal Early set domain associated with the catalytic domain of putative esterases; E or ...
45-128 5.38e-25

N-terminal Early set domain associated with the catalytic domain of putative esterases; E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199894 [Multi-domain]  Cd Length: 83  Bit Score: 97.25  E-value: 5.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  45 KSITYRLFAPDARRVSiVTGATPDSFVSHDMTKAADGVWTWKSEPMKPNLYEYYFDVDGFRSVDTGSRYQKPQRQVNTSL 124
Cdd:cd11294    1 GTVTFRLFAPKAKKVE-VTGDFLPGPGPVAMTKDDDGVWSVTTGPLAPEIYSYSFNVDGVKVLDPSNPYVKRDVSTVSSV 79

                 ....
gi 490246944 125 ILVP 128
Cdd:cd11294   80 FEVP 83
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
149-378 1.93e-16

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 78.27  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  149 SKALNAERRLYVWTPPGYSGTGdPLPVLYFYHGFGDSGLsaidqGRIPQIMDNLLAEGKIKP-MLVVVP-------DTET 220
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYPPGR-KYPVLYLLDGTGWFQN-----GPAKEGLDRLAASGEIPPvIIVGSPrggevsfYSDW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  221 DIPEAVAEnFPPQERRKTFyplnaqaadkeLMQDIIPLIDARFNVrkDADGRALAGLSQGGYQALVSGMNHLESFGWLAT 300
Cdd:pfam00756  75 DRGLNATE-GPGAYAYETF-----------LTQELPPLLDANFPT--APDGRALAGQSMGGLGALYLALKYPDLFGSVSS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  301 FSGVTTTTVPNAGVE--AQLKQPDAI---------NKQLRNFtVVVGEKDSVTGKDIAG-----------LKSELEKQQI 358
Cdd:pfam00756 141 FSPILNPSNSMWGPEddPAWQEGDPVllavalsanNTRLRIY-LDVGTREDFLGDQLPVeileelapnreLAEQLAYRGV 219
                         250       260
                  ....*....|....*....|
gi 490246944  359 KFDYHQYPGLNHEMDvWRPA 378
Cdd:pfam00756 220 GGYDHEYYGGHDWAY-WRAQ 238
E_set_MTHase_like_N cd02853
N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose ...
39-114 3.37e-06

N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (also called Glycosyltrehalose trehalohydrolase) and similar proteins; E or "early" set domains are associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (MTHase) and similar proteins at the N-terminal end. This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. Maltooligosyl trehalose synthase (MTSase) and MTHase work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The N-terminal domain of MTHase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199883 [Multi-domain]  Cd Length: 84  Bit Score: 44.82  E-value: 3.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490246944  39 TQVNADKSITYRLFAPDARRVSIVTgatpDSFVSHDMTKAADGVWTWKSEPMKPNLyEYYFDVDGFRSV-DTGSRYQ 114
Cdd:cd02853    2 AELLGDGGVRFRVWAPAAESVELVL----EGGRRLPMQRDGDGWFEAEVAAAGAGT-RYRFRLDGGLPVpDPASRFQ 73
CBM_48 pfam02922
Carbohydrate-binding module 48 (Isoamylase N-terminal domain); This domain is found in a range ...
41-101 3.41e-05

Carbohydrate-binding module 48 (Isoamylase N-terminal domain); This domain is found in a range of enzymes that act on branched substrates - isoamylase, pullulanase and branching enzyme. This family also contains the beta subunit of 5' AMP activated kinase.


Pssm-ID: 427056 [Multi-domain]  Cd Length: 80  Bit Score: 41.87  E-value: 3.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490246944   41 VNADKSITYRLFAPDARRVSIVtGATPD-SFVSHDMTKAADGVWTWKSEPMKPN-LYEYYFDV 101
Cdd:pfam02922   6 PDPDGGVNFRVWAPNAERVTLV-LDFNNwDGREIPMTRRTGGVWELFVPGDLPHgRYKYRVHG 67
PRK10439 PRK10439
enterobactin/ferric enterobactin esterase; Provisional
142-303 4.83e-03

enterobactin/ferric enterobactin esterase; Provisional


Pssm-ID: 236695 [Multi-domain]  Cd Length: 411  Bit Score: 38.84  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 142 LRTLTYHSKALNAERRLYVWTPPGYSGTGDPLPVLYfyhgfgDSGLSAIDQgRIPQIMDNLLAEGKIKP---MLVVVPDT 218
Cdd:PRK10439 180 AKEIIWKSERLGNSRRVWIYTTGDAAPEERPLAILL------DGQFWAESM-PVWPALDSLTHRGQLPPavyLLIDAIDT 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 219 EtdipeavaenfppqeRRKTFYPLNA---QAADKELmqdiIPLIDARFNVRKDADGRALAGLSQGGYQALVSGMNHLESF 295
Cdd:PRK10439 253 T---------------HRSQELPCNAdfwLAVQQEL----LPQVRAIAPFSDDADRTVVAGQSFGGLAALYAGLHWPERF 313

                 ....*...
gi 490246944 296 GWLATFSG 303
Cdd:PRK10439 314 GCVLSQSG 321
 
Name Accession Description Interval E-value
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
78-388 1.08e-77

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 242.45  E-value: 1.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  78 AADGVWTWKSEPMKPNLYEYYFDVDGFRSVDTGSRYQK--PQRQVNTSLILVPGSILDDREVAHGDLRTLTYHSKALNAE 155
Cdd:COG2382   15 AALLLLAALAGAAPPGLLVASAVVVVRVLPAAAAAARLlaPVVAAAVVVLGGPPPATDDKDVPHGTVETVTYPSKALGRT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 156 RRLYVWTPPGYSGTGDPLPVLYFYHGFGDSGLSAIDQGRIPQIMDNLLAEGKIKPMLVVVPDTETDipeavaenfppqER 235
Cdd:COG2382   95 RRVWVYLPPGYDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILDNLIAAGKIPPMIVVMPDGGDG------------GD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 236 RKTFYPLNAQAAdKELMQDIIPLIDARFNVRKDADGRALAGLSQGGYQALVSGMNHLESFGWLATFSGVTTTTVPNA--- 312
Cdd:COG2382  163 RGTEGPGNDAFE-RFLAEELIPFVEKNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDAdrg 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490246944 313 GVEAQLKQPdAINKQLRnFTVVVGEKDSVTgKDIAGLKSELEKQQIKFDYHQYPGlNHEMDVWRPAYAEFVQKLFK 388
Cdd:COG2382  242 GWAELLAAG-APKKPLR-FYLDVGTEDDLL-EANRALAAALKAKGYDVEYREFPG-GHDWAVWRAALPDFLPWLFK 313
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
140-378 6.90e-31

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 118.01  E-value: 6.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 140 GDLRTLTYHSKALNAERRLYVWTPPGYSGTgdPLPVLYFYHGFGDSGLSAIDQGRIPQIMDNllaegkiKPMLVVVPDTE 219
Cdd:COG0627    2 GRVVRVTVPSPALGREMPVSVYLPPGYDGR--PLPVLYLLHGLTGTHENWTRKTGAQRLAAE-------LGVIVVMPDGG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 220 TDipeavaenfppqerrkTFYpLNAQAADKE-------LMQDIIPLIDARFNVRKDADGRALAGLSQGGYQALVSGMNHL 292
Cdd:COG0627   73 QA----------------SFY-VDWTQGPAGhyrwetyLTEELPPLIEANFPVSADRERRAIAGLSMGGHGALTLALRHP 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 293 ESFGWLATFSGVTTTTVPNAGV-----------EAQLKQPDAIN--KQLRNFT---VVVGEKDSVTGKDIAGLKSELEKQ 356
Cdd:COG0627  136 DLFRAVAAFSGILDPSQPPWGEkafdayfgppdRAAWAANDPLAlaEKLRAGLplyIDCGTADPFFLEANRQLHAALRAA 215
                        250       260
                 ....*....|....*....|..
gi 490246944 357 QIKFDYHQYPGlNHEMDVWRPA 378
Cdd:COG0627  216 GIPHTYRERPG-GHSWYYWASF 236
E_set_Esterase_like_N cd11294
N-terminal Early set domain associated with the catalytic domain of putative esterases; E or ...
45-128 5.38e-25

N-terminal Early set domain associated with the catalytic domain of putative esterases; E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199894 [Multi-domain]  Cd Length: 83  Bit Score: 97.25  E-value: 5.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  45 KSITYRLFAPDARRVSiVTGATPDSFVSHDMTKAADGVWTWKSEPMKPNLYEYYFDVDGFRSVDTGSRYQKPQRQVNTSL 124
Cdd:cd11294    1 GTVTFRLFAPKAKKVE-VTGDFLPGPGPVAMTKDDDGVWSVTTGPLAPEIYSYSFNVDGVKVLDPSNPYVKRDVSTVSSV 79

                 ....
gi 490246944 125 ILVP 128
Cdd:cd11294   80 FEVP 83
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
149-378 1.93e-16

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 78.27  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  149 SKALNAERRLYVWTPPGYSGTGdPLPVLYFYHGFGDSGLsaidqGRIPQIMDNLLAEGKIKP-MLVVVP-------DTET 220
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYPPGR-KYPVLYLLDGTGWFQN-----GPAKEGLDRLAASGEIPPvIIVGSPrggevsfYSDW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  221 DIPEAVAEnFPPQERRKTFyplnaqaadkeLMQDIIPLIDARFNVrkDADGRALAGLSQGGYQALVSGMNHLESFGWLAT 300
Cdd:pfam00756  75 DRGLNATE-GPGAYAYETF-----------LTQELPPLLDANFPT--APDGRALAGQSMGGLGALYLALKYPDLFGSVSS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944  301 FSGVTTTTVPNAGVE--AQLKQPDAI---------NKQLRNFtVVVGEKDSVTGKDIAG-----------LKSELEKQQI 358
Cdd:pfam00756 141 FSPILNPSNSMWGPEddPAWQEGDPVllavalsanNTRLRIY-LDVGTREDFLGDQLPVeileelapnreLAEQLAYRGV 219
                         250       260
                  ....*....|....*....|
gi 490246944  359 KFDYHQYPGLNHEMDvWRPA 378
Cdd:pfam00756 220 GGYDHEYYGGHDWAY-WRAQ 238
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
137-386 3.82e-13

Predicted hydrolase of the alpha/beta superfamily [General function prediction only];


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 68.47  E-value: 3.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 137 VAHGDLRTLTYHSKALNAERRLYVWTPPGYSGTGDPLPVLY-------FYHGFGDSGLSAIDQGRIPqimdnllaegkik 209
Cdd:COG2819    2 IALGQTEYFTLESPILGEDRRIRVYLPPGYDAPEKRYPVLYmldgqnlFDALAGAVGTLSRLEGGIP------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 210 PMLVVVPDTETDIPEAVAE-NFPPQERRKTFYPLNAQAAD--KELMQDIIPLIDARFNVrkDADGRALAGLSQGGYQALV 286
Cdd:COG2819   69 PAIVVGIGNGDDGERRLRDyTPPPAPGYPGPGGPGGGADAflRFLEEELKPYIDKRYRT--DPERTGLIGHSLGGLFSLY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 287 SGMNHLESFGWLATFSgvTTTTVPNAGVEAQLKQPDAINKQLRNFTVVVGEKDSVTGKDIAG----LKSELEKQ---QIK 359
Cdd:COG2819  147 ALLKYPDLFGRYIAIS--PSLWWDDGALLDEAEALLKRSPLPKRLYLSVGTLEGDSMDGMVDdarrLAEALKAKgypGLN 224
                        250       260
                 ....*....|....*....|....*..
gi 490246944 360 FDYHQYPGLNHeMDVWRPAYAEFVQKL 386
Cdd:COG2819  225 VKFEVFPGETH-GSVAWAALPRALRFL 250
E_set_Esterase_N cd02858
N-terminal Early set domain associated with the catalytic domain of esterase; E or "early" set ...
46-113 1.26e-12

N-terminal Early set domain associated with the catalytic domain of esterase; E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199888 [Multi-domain]  Cd Length: 78  Bit Score: 62.60  E-value: 1.26e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490246944  46 SITYRLFAPDARRVSIVTGAtpdsfVSHDMTKAADGVWTWKSEPMKPNLYEYYFDVDGFRSVDTGSRY 113
Cdd:cd02858    2 RVRFRIKAPDAKSVQVDLGG-----GKYDMTKGADGVWTGTTGPLVPGFHYYFLIVDGVRVVDPASPT 64
COG4099 COG4099
Predicted peptidase [General function prediction only];
138-381 2.43e-09

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 57.28  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 138 AHGDLRTLTYHSKALNAERRLYVWTPPGYSGTGdPLPVLYFYHGFGDSG---LSAIDQGRIPQIMDnllAEGKIKPMLVV 214
Cdd:COG4099   15 AQDGFEARTFTDPSDGDTLPYRLYLPKGYDPGK-KYPLVLFLHGAGERGtdnEKQLTHGAPKFINP---ENQAKFPAIVL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 215 VPdtetdipeavaenfppQerrktfYPLNAQAADKELMQDIIPLID---ARFNVrkDADGRALAGLSQGGYQALVSGMNH 291
Cdd:COG4099   91 AP----------------Q------CPEDDYWSDTKALDAVLALLDdliAEYRI--DPDRIYLTGLSMGGYGTWDLAARY 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 292 LEsfgwlaTFSGVttttVPNAGveaqlkQPDAIN-KQLRN--FTVVVGEKDSVTGKD-----IAGLKSelEKQQIKFDYh 363
Cdd:COG4099  147 PD------LFAAA----VPICG------GGDPANaANLKKvpVWIFHGAKDDVVPVEesramVEALKA--AGADVKYTE- 207
                        250
                 ....*....|....*...
gi 490246944 364 qYPGLNHemDVWRPAYAE 381
Cdd:COG4099  208 -YPGVGH--NSWDPAYAN 222
E_set_MTHase_like_N cd02853
N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose ...
39-114 3.37e-06

N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (also called Glycosyltrehalose trehalohydrolase) and similar proteins; E or "early" set domains are associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (MTHase) and similar proteins at the N-terminal end. This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. Maltooligosyl trehalose synthase (MTSase) and MTHase work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The N-terminal domain of MTHase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.


Pssm-ID: 199883 [Multi-domain]  Cd Length: 84  Bit Score: 44.82  E-value: 3.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490246944  39 TQVNADKSITYRLFAPDARRVSIVTgatpDSFVSHDMTKAADGVWTWKSEPMKPNLyEYYFDVDGFRSV-DTGSRYQ 114
Cdd:cd02853    2 AELLGDGGVRFRVWAPAAESVELVL----EGGRRLPMQRDGDGWFEAEVAAAGAGT-RYRFRLDGGLPVpDPASRFQ 73
CBM_48 pfam02922
Carbohydrate-binding module 48 (Isoamylase N-terminal domain); This domain is found in a range ...
41-101 3.41e-05

Carbohydrate-binding module 48 (Isoamylase N-terminal domain); This domain is found in a range of enzymes that act on branched substrates - isoamylase, pullulanase and branching enzyme. This family also contains the beta subunit of 5' AMP activated kinase.


Pssm-ID: 427056 [Multi-domain]  Cd Length: 80  Bit Score: 41.87  E-value: 3.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490246944   41 VNADKSITYRLFAPDARRVSIVtGATPD-SFVSHDMTKAADGVWTWKSEPMKPN-LYEYYFDV 101
Cdd:pfam02922   6 PDPDGGVNFRVWAPNAERVTLV-LDFNNwDGREIPMTRRTGGVWELFVPGDLPHgRYKYRVHG 67
E_set_Pullulanase cd02860
Early set domain associated with the catalytic domain of pullulanase (also called dextrinase ...
44-108 6.83e-05

Early set domain associated with the catalytic domain of pullulanase (also called dextrinase and alpha-dextrin endo-1,6-alpha glucosidase); E or "early" set domains are associated with the catalytic domain of pullulanase at either the N-terminal or C-terminal end, and in a few instances at both ends. Pullulanase is an enzyme with activity similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. The E set domain of pullulanase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199890 [Multi-domain]  Cd Length: 97  Bit Score: 41.37  E-value: 6.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490246944  44 DKSITYRLFAPDARRVSIV---TGATPDSFVSHDMTKAADGVWTWKsepMKPNL------YEYYFDVDGFRSVD 108
Cdd:cd02860    9 PEKTTFKLWAPTAQKVKLLlydDGDDAKPAKTVPMKREEKGVWSVT---VDGDLkgkyytYEVTVYGETNEVVD 79
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
46-122 1.89e-04

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199878 [Multi-domain]  Cd Length: 82  Bit Score: 39.83  E-value: 1.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490246944  46 SITYRLFAPDARRVSIVTG-ATPDSFVSHDMTKAADGVWTWKsEPMKPNLYEYYFDVDGFRSVDTGSRYQKPQRQVNT 122
Cdd:cd02688    1 GVTFRIFAPGAKSVYLIGSfNGWWQAQALPMTKNGGGVWSAT-IPLPLGTYEYKYVIDGGKNVLPYFDPYYVAGDGNS 77
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
159-388 4.97e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.16  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 159 YVWTPPGysgtGDPLPVLYFYHGFGdsglSAIDQGRIPqIMDNLLAEGkikpMLVVVPDtetdipeavaenfppqerrKT 238
Cdd:COG1506   13 WLYLPAD----GKKYPVVVYVHGGP----GSRDDSFLP-LAQALASRG----YAVLAPD-------------------YR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 239 FYPLNAQAADKELMQDIIPLID---ARFNVrkDADGRALAGLSQGGYQALVSGMNHLESFGWLATFSGVT----TTTVPN 311
Cdd:COG1506   61 GYGESAGDWGGDEVDDVLAAIDylaARPYV--DPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSdlrsYYGTTR 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 312 AGVEAQLKQPDAINKQLRNFT-------------VVVGEKDSVTGKDIA-GLKSELEKQQIKFDYHQYPGLNHEM-DVWR 376
Cdd:COG1506  139 EYTERLMGGPWEDPEAYAARSplayadklktpllLIHGEADDRVPPEQAeRLYEALKKAGKPVELLVYPGEGHGFsGAGA 218
                        250
                 ....*....|..
gi 490246944 377 PAYAEFVQKLFK 388
Cdd:COG1506  219 PDYLERILDFLD 230
YpfH COG0400
Predicted esterase [General function prediction only];
169-373 2.45e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 169 TGDPLPVLYFYHGFGDSGLSAIdqgripQIMDNLLAEGkikpMLVVVPDtetdipeavAeNFPPQERRKTFYPLNA---- 244
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLL------PLAPELALPG----AAVLAPR---------A-PVPEGPGGRAWFDLSFlegr 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 245 --QAADKELMQDIIPLIDARFNVRKDADGR-ALAGLSQGGYQALVSGMNHLESFGWLATFSGvtttTVPNagvEAQLKQP 321
Cdd:COG0400   61 edEEGLAAAAEALAAFIDELEARYGIDPERiVLAGFSQGAAMALSLALRRPELLAGVVALSG----YLPG---EEALPAP 133
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490246944 322 DAINKQLRnFTVVVGEKDSVTGKDIA-GLKSELEKQQIKFDYHQYPGlNHEMD 373
Cdd:COG0400  134 EAALAGTP-VFLAHGTQDPVIPVERArEAAEALEAAGADVTYREYPG-GHEIS 184
PRK10439 PRK10439
enterobactin/ferric enterobactin esterase; Provisional
142-303 4.83e-03

enterobactin/ferric enterobactin esterase; Provisional


Pssm-ID: 236695 [Multi-domain]  Cd Length: 411  Bit Score: 38.84  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 142 LRTLTYHSKALNAERRLYVWTPPGYSGTGDPLPVLYfyhgfgDSGLSAIDQgRIPQIMDNLLAEGKIKP---MLVVVPDT 218
Cdd:PRK10439 180 AKEIIWKSERLGNSRRVWIYTTGDAAPEERPLAILL------DGQFWAESM-PVWPALDSLTHRGQLPPavyLLIDAIDT 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490246944 219 EtdipeavaenfppqeRRKTFYPLNA---QAADKELmqdiIPLIDARFNVRKDADGRALAGLSQGGYQALVSGMNHLESF 295
Cdd:PRK10439 253 T---------------HRSQELPCNAdfwLAVQQEL----LPQVRAIAPFSDDADRTVVAGQSFGGLAALYAGLHWPERF 313

                 ....*...
gi 490246944 296 GWLATFSG 303
Cdd:PRK10439 314 GCVLSQSG 321
 
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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