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Conserved domains on  [gi|485929911|gb|EOD53161|]
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putative expansin-like protein 1 protein [Neofusicoccum parvum UCRNP2]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YoaJ super family cl27618
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
451-657 1.32e-41

Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG4305:

Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 150.90  E-value: 1.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 451 AGLIGTVGGTVTSLTEAVTGEATYYTGDvSAGTCSFTgySLPASIFGTALSDSNWDDASNCGACVNIKGPSGSsITAMIV 530
Cdd:COG4305   17 ACGAAGPAAAAAPPGATHSGEATYYDAD-GGGNCSFD--PIPADLLVAALNPTDYANSAACGACLEVTGPKGS-VTVRVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 531 DQCPGCGDNHLDLFQEAFTELSALATGVIDVTWEIVECGISTPLTLANKDGASEYWFSMQVVNSNLPVKSLSVSVDGGst 610
Cdd:COG4305   93 DRCPECAPGDLDLSPEAFAKIADLEAGRVPITWRLVSCPVSGNVSYRFKEGSSQWWTAVQVRNHRNPIAKLEVRSGGQ-- 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 485929911 611 WTETTRTTYNFFEYEQGFGTTTVDVKITSSTGKEVIQKNVTVGSSTS 657
Cdd:COG4305  171 WVALPREDYNYFVAESGMGPGPFTIRVTDVYGQVLEDTLPPLSPGVV 217
rne super family cl35953
ribonuclease E; Reviewed
 297-445 1.20e-04

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 45.42  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  297 TPVYTPAPVEPSSSSVAVDTPVYTPAPVESSSVSVAVDTPVYTPAPVAAST---PAIAAGVDgASGASSSVAVDTPVYTP 373
Cdd:PRK10811  874 PVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVteqPQVITESD-VAVAQEVAEHAEPVVEP 952

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485929911  374 VYTPSVAVDTPIYTPAPVVETPsvAVDTPVYTPAPSSSAPAVSVESVASSSSIVTPSSSVAQSTFVTS---SAPA 445
Cdd:PRK10811  953 QDETADIEEAAETAEVVVAEPE--VVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATApmtRAPA 1025
 
Name Accession Description Interval E-value
YoaJ COG4305
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
451-657 1.32e-41

Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 150.90  E-value: 1.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 451 AGLIGTVGGTVTSLTEAVTGEATYYTGDvSAGTCSFTgySLPASIFGTALSDSNWDDASNCGACVNIKGPSGSsITAMIV 530
Cdd:COG4305   17 ACGAAGPAAAAAPPGATHSGEATYYDAD-GGGNCSFD--PIPADLLVAALNPTDYANSAACGACLEVTGPKGS-VTVRVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 531 DQCPGCGDNHLDLFQEAFTELSALATGVIDVTWEIVECGISTPLTLANKDGASEYWFSMQVVNSNLPVKSLSVSVDGGst 610
Cdd:COG4305   93 DRCPECAPGDLDLSPEAFAKIADLEAGRVPITWRLVSCPVSGNVSYRFKEGSSQWWTAVQVRNHRNPIAKLEVRSGGQ-- 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 485929911 611 WTETTRTTYNFFEYEQGFGTTTVDVKITSSTGKEVIQKNVTVGSSTS 657
Cdd:COG4305  171 WVALPREDYNYFVAESGMGPGPFTIRVTDVYGQVLEDTLPPLSPGVV 217
expansin_EXLX1 NF041144
expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of ...
 470-657 1.30e-36

expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of Bacillus subtilis, a cellulose-binding bacterial expansin, and similar domains in related bacteirial proteins. Expansins, which are small and non-catalytic, have the ability to loosen plant cell wall material and improve enzyme access, but an expansin domain can occur as an auxiliary domain in cellulases such as CelA of Clavibacter michiganensis, a bacterial pathogen of tomato plants. Pfam model PF01357 (expansin C-terminal domain), somewhat less than half the size, is related but is oriented toward plant expansin and hits relatively few members of this family above cutoffs (as of version PF01357.23).


Pssm-ID: 469065 [Multi-domain]  Cd Length: 192  Bit Score: 135.80  E-value: 1.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 470 GEATYYTGDVSAGTCSFTgySLPASIFGTALSDSNWDDASNCGACVNIKGPSGSsITAMIVDQCPGCGDNHLDLFQEAFT 549
Cdd:NF041144   1 GEATFYGAGYGGGACSLD--PIPADMMIAALNPADYNGAAACGAYLEVTGPKGT-VTVRVTDRCPECAPGHLDLSPQAFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 550 ELSALATGVIDVTWEIV-ECGISTPLTLANKDGASEYWFSMQVVNSNLPVKSLSVSVDGGstWTETTRTTYNFFEYEQGF 628
Cdd:NF041144  78 KIADPVAGIVPITWRLVsAPSGPGPVSYRIKEGSSQYWAAIQVRNHRNPVAKLEYRKGGT--WVALPRTDYNYFVSESGM 155

                        170       180
                 ....*....|....*....|....*....
gi 485929911 629 GTTTVDVKITSSTGKEVIQKNVTVGSSTS 657
Cdd:NF041144 156 GTGPLTIRVTDIYGQVLTDTGIPLPPGVV 184
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 468-568 2.78e-31

N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439251 [Multi-domain]  Cd Length: 109  Bit Score: 117.86  E-value: 2.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 468 VTGEATYYTG-DVSAGTCSFTGYSL-PASIFGTALSDSNWDDASNCGACVNIKGP-----SGSSITAMIVDQCPGCGD-N 539
Cdd:cd22271    1 STGRATFYGGpDLSGGACGYGPLPPpPGGGFVAALNPALYDNGAGCGACYEVTCPgspccSGGSVVVMVTDSCPECGDaG 80

                         90       100
                 ....*....|....*....|....*....
gi 485929911 540 HLDLFQEAFTELSALATGVIDVTWEIVEC 568
Cdd:cd22271   81 HFDLSPDAFAALADPSGGIVPVTWRRVPC 109
PLN03024 PLN03024
Putative EG45-like domain containing protein 1; Provisional
 456-563 3.18e-07

Putative EG45-like domain containing protein 1; Provisional


Pssm-ID: 178595  Cd Length: 125  Bit Score: 49.64  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 456 TVGGTVTSLTEAVTGEATYYTGDVSAGTCSFTGYSlpasIFGTALSDSNWDDASNCGACVNIK--GP--------SGSSI 525
Cdd:PLN03024  10 TVLVFLFSVSYATPGIATFYTSYTPSACYRGTSFG----VMIAAASDSLWNNGRVCGKMFTVKckGPrnavphpcTGKSV 85

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 485929911 526 TAMIVDQCPGCGDNHLDLFQEAFTELSALATGVIDVTW 563
Cdd:PLN03024  86 TVKIVDHCPSGCASTLDLSREAFAQIANPVAGIINIDY 123
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 498-563 2.99e-06

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 45.66  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  498 TALSDSNWDDASNCGACVNIK----------------GPSGSSITAMIVDQCPGCGDNHLDLFQEAFTELSALATGVIDV 561
Cdd:pfam03330   1 AAGSASLYNNGTACGECYDVRcltaahptlpfgtycrVLSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAMPRAGIVPV 80


                  ..
gi 485929911  562 TW 563
Cdd:pfam03330  81 QY 82
rne PRK10811
ribonuclease E; Reviewed
 297-445 1.20e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 45.42  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  297 TPVYTPAPVEPSSSSVAVDTPVYTPAPVESSSVSVAVDTPVYTPAPVAAST---PAIAAGVDgASGASSSVAVDTPVYTP 373
Cdd:PRK10811  874 PVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVteqPQVITESD-VAVAQEVAEHAEPVVEP 952

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485929911  374 VYTPSVAVDTPIYTPAPVVETPsvAVDTPVYTPAPSSSAPAVSVESVASSSSIVTPSSSVAQSTFVTS---SAPA 445
Cdd:PRK10811  953 QDETADIEEAAETAEVVVAEPE--VVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATApmtRAPA 1025
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
222-414 5.73e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 39.74  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 222 TVTVDPEPVTVTVTPSASASGAADGVVGAAAYEPSSSSLISVAVDTPVYTPAPVAAATAGVDGASGASSSSVAVDTPVYT 301
Cdd:COG3469   24 GAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTAS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 302 PAPVEPSSSSVAVDTPVYTPAPVESSSVSVAVDTPVYTPAPVAASTPAIAAGVDGASGASSSVAVDTPVYTPVYTPSVAV 381
Cdd:COG3469  104 GANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATT 183

                        170       180       190
                 ....*....|....*....|....*....|...
gi 485929911 382 DTPIYTPAPVveTPSVAVDTPVYTPAPSSSAPA 414
Cdd:COG3469  184 TATATTASGA--TTPSATTTATTTGPPTPGLPK 214
 
Name Accession Description Interval E-value
YoaJ COG4305
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
451-657 1.32e-41

Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 150.90  E-value: 1.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 451 AGLIGTVGGTVTSLTEAVTGEATYYTGDvSAGTCSFTgySLPASIFGTALSDSNWDDASNCGACVNIKGPSGSsITAMIV 530
Cdd:COG4305   17 ACGAAGPAAAAAPPGATHSGEATYYDAD-GGGNCSFD--PIPADLLVAALNPTDYANSAACGACLEVTGPKGS-VTVRVV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 531 DQCPGCGDNHLDLFQEAFTELSALATGVIDVTWEIVECGISTPLTLANKDGASEYWFSMQVVNSNLPVKSLSVSVDGGst 610
Cdd:COG4305   93 DRCPECAPGDLDLSPEAFAKIADLEAGRVPITWRLVSCPVSGNVSYRFKEGSSQWWTAVQVRNHRNPIAKLEVRSGGQ-- 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 485929911 611 WTETTRTTYNFFEYEQGFGTTTVDVKITSSTGKEVIQKNVTVGSSTS 657
Cdd:COG4305  171 WVALPREDYNYFVAESGMGPGPFTIRVTDVYGQVLEDTLPPLSPGVV 217
expansin_EXLX1 NF041144
expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of ...
 470-657 1.30e-36

expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of Bacillus subtilis, a cellulose-binding bacterial expansin, and similar domains in related bacteirial proteins. Expansins, which are small and non-catalytic, have the ability to loosen plant cell wall material and improve enzyme access, but an expansin domain can occur as an auxiliary domain in cellulases such as CelA of Clavibacter michiganensis, a bacterial pathogen of tomato plants. Pfam model PF01357 (expansin C-terminal domain), somewhat less than half the size, is related but is oriented toward plant expansin and hits relatively few members of this family above cutoffs (as of version PF01357.23).


Pssm-ID: 469065 [Multi-domain]  Cd Length: 192  Bit Score: 135.80  E-value: 1.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 470 GEATYYTGDVSAGTCSFTgySLPASIFGTALSDSNWDDASNCGACVNIKGPSGSsITAMIVDQCPGCGDNHLDLFQEAFT 549
Cdd:NF041144   1 GEATFYGAGYGGGACSLD--PIPADMMIAALNPADYNGAAACGAYLEVTGPKGT-VTVRVTDRCPECAPGHLDLSPQAFA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 550 ELSALATGVIDVTWEIV-ECGISTPLTLANKDGASEYWFSMQVVNSNLPVKSLSVSVDGGstWTETTRTTYNFFEYEQGF 628
Cdd:NF041144  78 KIADPVAGIVPITWRLVsAPSGPGPVSYRIKEGSSQYWAAIQVRNHRNPVAKLEYRKGGT--WVALPRTDYNYFVSESGM 155

                        170       180
                 ....*....|....*....|....*....
gi 485929911 629 GTTTVDVKITSSTGKEVIQKNVTVGSSTS 657
Cdd:NF041144 156 GTGPLTIRVTDIYGQVLTDTGIPLPPGVV 184
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 468-568 2.78e-31

N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439251 [Multi-domain]  Cd Length: 109  Bit Score: 117.86  E-value: 2.78e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 468 VTGEATYYTG-DVSAGTCSFTGYSL-PASIFGTALSDSNWDDASNCGACVNIKGP-----SGSSITAMIVDQCPGCGD-N 539
Cdd:cd22271    1 STGRATFYGGpDLSGGACGYGPLPPpPGGGFVAALNPALYDNGAGCGACYEVTCPgspccSGGSVVVMVTDSCPECGDaG 80

                         90       100
                 ....*....|....*....|....*....
gi 485929911 540 HLDLFQEAFTELSALATGVIDVTWEIVEC 568
Cdd:cd22271   81 HFDLSPDAFAALADPSGGIVPVTWRRVPC 109
DPBB_EXLX1-like cd22272
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ...
 469-564 1.46e-29

N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus subtilis EXLX1; This subfamily is composed of bacterial expansins including Bacillus subtilis EXLX1, also called expansin-YoaJ. Similar to plant expansins, EXLX1 contains an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. It strongly binds to crystalline cellulose via D2, and weakly binds soluble cellooligosaccharides. Bacterial expansins, which are present in some plant pathogens, have the ability to loosen plant cell walls, but with weaker activity compared to plant expansins. They may have a role in plant-bacterial interactions. This model represents the N-terminal domain of EXLX1 and similar bacterial expansins, which adopts a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439252 [Multi-domain]  Cd Length: 95  Bit Score: 112.28  E-value: 1.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 469 TGEATYYTGDVSAGTCSFTGysLPASIFGTALSDSNWDDASNCGACVNIKGPSGSsITAMIVDQCPGCGDNHLDLFQEAF 548
Cdd:cd22272    3 TGEATFYGAGAGGGNCSLDP--PPADRMIAALNTADYNGSAACGACLEVTGPKGT-VVVQVVDRCPECAPGDLDLSEEAF 79

                         90
                 ....*....|....*.
gi 485929911 549 TELSALATGVIDVTWE 564
Cdd:cd22272   80 AKIADPSAGRVPITWR 95
DPBB_RlpA_EXP_N-like cd22191
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ...
 470-563 2.47e-25

double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), the N-terminal domain of plant and bacterial expansins, GH45 family of endoglucanases, barwins, cerato-platanins, membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. Endoglucanases (EC 3.2.1.4) catalyze the endohydrolysis of (1-4)-beta-D-glucosidic linkages in cellulose, lichenin, and cereal beta-D-glucans. Animal cellulases, such as endoglucanase EG27II, have great potential for industrial applications such as bioethanol production. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Cerato-platanin is a phytotoxin which causes production of phytoalexin in platanus acerifolia, platanus occidentalis, and platanus orientalis. It also induces cell necrosis. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. YuiC is a Firmicute stationary phase survival (Sps) protein.


Pssm-ID: 439247 [Multi-domain]  Cd Length: 92  Bit Score: 100.04  E-value: 2.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 470 GEATYYTGDVSAGTCsftGYSLPASIFGTALSDSNWDDASNCGACVNIKGPSGSSITAMIVDQCPGCGDNHLDLFQEAFT 549
Cdd:cd22191    1 GRATYYDPSGGLGAC---GTTNSDSDLVVALSAALFDSGPLCGKCIRITYNDGKTVTATVVDECPGCGPGDLDLSPAAFQ 77

                         90
                 ....*....|....*
gi 485929911 550 ELSA-LATGVIDVTW 563
Cdd:cd22191   78 ALAGdLDGGVIPVTW 92
DPBB_SPI-like cd22273
double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins; ...
 469-565 1.47e-14

double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins; Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.


Pssm-ID: 439253  Cd Length: 101  Bit Score: 69.68  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 469 TGEATYYTgDVSAGTCSFTGY-------SLPASIFGTAlsdSNWDDASNCGACVNIKgPSGSSITAMIVDQCPGCGDNHL 541
Cdd:cd22273    2 NGDFTYYN-DAGYGACGTPINaatemlvAVSPAYWTTP---NPNNDPPCCNVCVKVT-YNGKTITVPVKDKCPSCGKNHI 76

                         90       100
                 ....*....|....*....|....*
gi 485929911 542 DLFQEAFTELSALATG-VIDVTWEI 565
Cdd:cd22273   77 DLSQPAFKQLAPLLVGgIIGATWKF 101
DPBB_EG45-like cd22269
double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains ...
 469-562 2.64e-09

double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold.


Pssm-ID: 439249 [Multi-domain]  Cd Length: 106  Bit Score: 54.94  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 469 TGEATYYTGDVSAGTCSFTGYSLPASIFGtALSDSNWDDASNCGACVNIK--GPS--------GSSITAMIVDQCPGCGD 538
Cdd:cd22269    2 VGTATFYTPPYTPSACYGNDPSPSGNLFA-AAGDALWDNGAACGRRYRVRciGGTnpgprpctGGSVVVKIVDYCPGCCG 80

                         90       100
                 ....*....|....*....|....
gi 485929911 539 NHLDLFQEAFTELSALATGVIDVT 562
Cdd:cd22269   81 ATFDLSQEAFAKIADPDAGRINIE 104
PLN03024 PLN03024
Putative EG45-like domain containing protein 1; Provisional
 456-563 3.18e-07

Putative EG45-like domain containing protein 1; Provisional


Pssm-ID: 178595  Cd Length: 125  Bit Score: 49.64  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 456 TVGGTVTSLTEAVTGEATYYTGDVSAGTCSFTGYSlpasIFGTALSDSNWDDASNCGACVNIK--GP--------SGSSI 525
Cdd:PLN03024  10 TVLVFLFSVSYATPGIATFYTSYTPSACYRGTSFG----VMIAAASDSLWNNGRVCGKMFTVKckGPrnavphpcTGKSV 85

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 485929911 526 TAMIVDQCPGCGDNHLDLFQEAFTELSALATGVIDVTW 563
Cdd:PLN03024  86 TVKIVDHCPSGCASTLDLSREAFAQIANPVAGIINIDY 123
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 498-563 2.99e-06

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 45.66  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  498 TALSDSNWDDASNCGACVNIK----------------GPSGSSITAMIVDQCPGCGDNHLDLFQEAFTELSALATGVIDV 561
Cdd:pfam03330   1 AAGSASLYNNGTACGECYDVRcltaahptlpfgtycrVLSGRSVIVRITDRGPFPPGRHFDLSGAAFEKLAMPRAGIVPV 80


                  ..
gi 485929911  562 TW 563
Cdd:pfam03330  81 QY 82
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 469-568 1.41e-05

N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins (EXPB, expansin-B) have cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. They also affect environmental stress responses. The EXPB subfamily is known in the allergen literature as group-1 grass pollen allergens. EXPB of Bermuda, Johnson, and Para grass pollens, is a major cross-reactive allergen for allergic rhinitis patients in subtropical climate. EXPB1 induces extension and stress relaxation of grass cell walls. Wheat TaEXPB7-B is a beta-expansin gene involved in low-temperature stress and abscisic acid responses. Beta-expansins belong to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of beta-expansins, which adopts a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439255  Cd Length: 121  Bit Score: 44.92  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 469 TGEATYY---TGDVS-AGTCSFTGYSL-PASIFGTALSDSNWDDASNCGACVNIK--GP---SGSSITAMIVDQCPGC-- 536
Cdd:cd22275    3 PARATWYgdpNGAGSnGGACGYKNVVQpPFSGMVSAGNPPIFKDGKGCGSCYEVKctGPpacSGKPVTVVITDECPGGpi 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 485929911 537 GDNHLDLFQEAFTelsALA----------TGVIDVTWEIVEC 568
Cdd:cd22275   83 APYHFDLSGTAFG---AMAkpgqedqlrnAGILDVQYRRVPC 121
rne PRK10811
ribonuclease E; Reviewed
 297-445 1.20e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 45.42  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  297 TPVYTPAPVEPSSSSVAVDTPVYTPAPVESSSVSVAVDTPVYTPAPVAAST---PAIAAGVDgASGASSSVAVDTPVYTP 373
Cdd:PRK10811  874 PVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVteqPQVITESD-VAVAQEVAEHAEPVVEP 952

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 485929911  374 VYTPSVAVDTPIYTPAPVVETPsvAVDTPVYTPAPSSSAPAVSVESVASSSSIVTPSSSVAQSTFVTS---SAPA 445
Cdd:PRK10811  953 QDETADIEEAAETAEVVVAEPE--VVAQPAAPVVAEVAAEVETVTAVEPEVAPAQVPEATVEHNHATApmtRAPA 1025
DPBB_kiwellin-like cd22270
double-psi beta-barrel fold of the kiwellin family; Kiwellin (KWL) proteins comprise a ...
 499-563 2.83e-04

double-psi beta-barrel fold of the kiwellin family; Kiwellin (KWL) proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. They are part of a spatio-temporally coordinated, plant-wide defense response comprising KWL proteins with overlapping activities. Zea mays KWL1 specifically inhibits the enzymatic activity of the secreted chorismate mutase Cmu1, a virulence-promoting effector of the smut fungus Ustilago maydis. KWL proteins adopt a double-psi beta-barrel (DPBB) fold, which provides a versatile scaffold that can specifically counteract pathogen effectors such as Cmu1.


Pssm-ID: 439250 [Multi-domain]  Cd Length: 128  Bit Score: 41.13  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 499 ALSDSNWDDASNCGACVNIKGPSGSSITAMIVDQC-------------PGCGDNHLDLFQEAFtelSALA----TGVIDV 561
Cdd:cd22270   48 ALSTGWYAGGSRCGRNIRITASNGRSVVAKVVDECdsrhgcdaehnyqPPCPNNIVDASKAVW---KALGldtdVGEVDI 124


                 ..
gi 485929911 562 TW 563
Cdd:cd22270  125 TW 126
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 470-568 4.66e-04

N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins (EXPA, expansin-A) have cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. They also affect environmental stress responses. Arabidopsis thaliana EXPA1 is a cell wall modifying enzyme that controls the divisions marking lateral root initiation. Nicotiana tabacum EXPA4 positively regulates abiotic stress tolerance, and negatively regulates pathogen resistance. Wheat TaEXPA2 is involved in conferring cadmium tolerance. Alpha-expansins belong to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of alpha-expansins, which adopts a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439254  Cd Length: 129  Bit Score: 40.66  E-value: 4.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 470 GEATYYTGDVSAGT----CsftGY-SLPASIFGT---ALSDSNWDDASNCGACVNIKG--------PSGSSITAMIVDQC 533
Cdd:cd22274    5 AHATFYGGSDASGTmggaC---GYgNLYSQGYGTntaALSTALFNDGASCGACYEIRCvddpspccPGGPSITVTATNFC 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 485929911 534 P----GCGDN---------HLDLFQEAFTELSALATGVIDVTWEIVEC 568
Cdd:cd22274   82 PpnyaLPSDNggwcnppreHFDLSQPAFLKIAQYKAGIVPVQYRRVPC 129
PHA03247 PHA03247
large tegument protein UL36; Provisional
 298-413 1.25e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  298 PVYTPAPVEPSSSSVAV----DTPVYTPAPVESSSVSVAVDTPVYTPAPVAASTPAIAAGVDGASGASSSVAVDTPVYTP 373
Cdd:PHA03247 2733 PALPAAPAPPAVPAGPAtpggPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 485929911  374 VYTPSVavdTPIYTPAPVVETPSVAVDTPVYTPAPSSSAP 413
Cdd:PHA03247 2813 APAAAL---PPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 317-472 1.29e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 317 PVYTPAPVESSSVSVAVDTPVYTPAPVAASTPAIAAGVDGASGASSSVavdtPVYTPVYTPSVAVDTPIYTPAPVVETPS 396
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASA----PAAPPAAAPPAPVAAPAAAAPAAAPAAA 441

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485929911 397 VAvdtpVYTPAPSSSAPAVSVESVASSSSIVTPSSSVAQSTfvTSSAPAATSSDAGLIGTV-GGTVTSLT--EAVTGEA 472
Cdd:PRK14951 442 PA----AVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPA--PAAAPAAARLTPTEEGDVwHATVQQLAaaEAITALA 514
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
298-413 1.58e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 298 PVYTPAPvePSSSSVAVDTPVYTPAPVESSSVSVAVDTPVYTPAPVAASTPAIAAGVDGASGASSSVAVDTPVYTPVYTP 377
Cdd:PRK12323 381 PVAQPAP--AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAP 458

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 485929911 378 SVAVDTPIYTPAPV--VETPSVAVDTPVYTPAPSSSAP 413
Cdd:PRK12323 459 AAAARPAAAGPRPVaaAAAAAPARAAPAAAPAPADDDP 496
PHA03247 PHA03247
large tegument protein UL36; Provisional
 297-461 1.78e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  297 TPVYTPAPVEPSSSSVAVDTPVYTPAPVESSSVSVAVDTPV-------YTPAPVAASTPAIAAGVDGASGASSSVAVDTP 369
Cdd:PHA03247 2684 RRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGpaaarqaSPALPAAPAPPAVPAGPATPGGPARPARPPTT 2763

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  370 VYTPVYTPSVAvdtPIYTPAPVVETPSVAVDTPVYTPAPSSSAPAVSVESVASSSSIVTPSSS----VAQSTFVTSSAPA 445
Cdd:PHA03247 2764 AGPPAPAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASpagpLPPPTSAQPTAPP 2840

                         170
                  ....*....|....*.
gi 485929911  446 ATSSDAGLIGTVGGTV 461
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSV 2856
PRK04654 PRK04654
sec-independent translocase; Provisional
 335-414 1.87e-03

sec-independent translocase; Provisional


Pssm-ID: 135173 [Multi-domain]  Cd Length: 214  Bit Score: 40.18  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 335 TPVYTPAPVAASTPAIAAGVDGASGASSSvAVDTPVYTPVYTPSVAVDTPIyTPAP---VVETPSVA-VDTPVYTPAPSS 410
Cdd:PRK04654 106 TPVATPLELAHADLSASAQVDAAAGAEPG-AGQAHTPVPAPAPVIAQAQPI-APAPhqtLVPAPHDTiVPAPHAAHLPSA 183


                 ....
gi 485929911 411 SAPA 414
Cdd:PRK04654 184 PATP 187
Barwin pfam00967
Barwin family;
486-568 2.01e-03

Barwin family;


Pssm-ID: 395772  Cd Length: 116  Bit Score: 38.39  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911  486 FTGYSLPASIFGTAlsdsnwddasNCGACVNIKGP-SGSSITAMIVDQCPGCGdnhLDLFQEAFTELSALATGV----ID 560
Cdd:pfam00967  42 WTAFCGPAGPRGQA----------SCGKCLRVTNTaTNAQVTVRIVDQCSNGG---LDLDVCVFNALDTNGAGYqqghLN 108


                  ....*...
gi 485929911  561 VTWEIVEC 568
Cdd:pfam00967 109 VDYQFVDC 116
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
222-414 5.73e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 39.74  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 222 TVTVDPEPVTVTVTPSASASGAADGVVGAAAYEPSSSSLISVAVDTPVYTPAPVAAATAGVDGASGASSSSVAVDTPVYT 301
Cdd:COG3469   24 GAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTAS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485929911 302 PAPVEPSSSSVAVDTPVYTPAPVESSSVSVAVDTPVYTPAPVAASTPAIAAGVDGASGASSSVAVDTPVYTPVYTPSVAV 381
Cdd:COG3469  104 GANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATT 183

                        170       180       190
                 ....*....|....*....|....*....|...
gi 485929911 382 DTPIYTPAPVveTPSVAVDTPVYTPAPSSSAPA 414
Cdd:COG3469  184 TATATTASGA--TTPSATTTATTTGPPTPGLPK 214
 
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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