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Conserved domains on  [gi|488987810|ref|WP_002898590|]
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MULTISPECIES: HTH-type transcriptional regulator PuuR [Klebsiella]

Protein Classification

PRK09943 family protein( domain architecture ID 11484529)

PRK09943 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
1-185 8.45e-136

HTH-type transcriptional regulator PuuR;


:

Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 376.83  E-value: 8.45e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810   1 MSDDGLAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVVI 80
Cdd:PRK09943   1 MSDEGLAPGKRLSEIRQQQGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  81 NQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINT 160
Cdd:PRK09943  81 NQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAINT 160

                        170       180
                 ....*....|....*....|....*
gi 488987810 161 GIPHSFSNTSAGICRIISAHTPTTF 185
Cdd:PRK09943 161 GIPHSFSNTSAGICRIISAHTPTTF 185
 
Name Accession Description Interval E-value
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
1-185 8.45e-136

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 376.83  E-value: 8.45e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810   1 MSDDGLAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVVI 80
Cdd:PRK09943   1 MSDEGLAPGKRLSEIRQQQGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  81 NQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINT 160
Cdd:PRK09943  81 NQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAINT 160

                        170       180
                 ....*....|....*....|....*
gi 488987810 161 GIPHSFSNTSAGICRIISAHTPTTF 185
Cdd:PRK09943 161 GIPHSFSNTSAGICRIISAHTPTTF 185
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 92-181 2.82e-24

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 90.64  E-value: 2.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  92 GVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSA 171
Cdd:cd02209    1 GYTYELLSPGLPGRKMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGD 80

                         90
                 ....*....|
gi 488987810 172 GICRIISAHT 181
Cdd:cd02209   81 EPARVLWVIT 90
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
79-183 6.70e-20

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 80.45  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  79 VINQDDLIEMGSqGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQ-GEEIGTILEGEIVLTINGQSYHLVAGQSYA 157
Cdd:COG3837    1 IVNLDDLPGPEA-GRRYRRLGDALGLTRLGVNLITLPPGASSSPYHAHSaEEEFVYVLEGELTLRIGGEEYVLEPGDSVG 79

                         90       100
                 ....*....|....*....|....*.
gi 488987810 158 INTGIPHSFSNTSAGICRIISAHTPT 183
Cdd:COG3837   80 FPAGVPHRLRNRGDEPARYLVVGTRA 105
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
11-66 6.25e-15

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 65.62  E-value: 6.25e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 488987810    11 RLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEF 66
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 111-180 7.22e-15

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 66.13  E-value: 7.22e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987810  111 FETYQPGTTtGERIKHQGE-EIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGICRIISAH 180
Cdd:pfam07883   2 LVTLPPGES-SPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
CxxCG_CxxCG_HTH TIGR03830
putative zinc finger/helix-turn-helix protein, YgiT family; This model describes a family of ...
 4-58 5.61e-08

putative zinc finger/helix-turn-helix protein, YgiT family; This model describes a family of predicted regulatory proteins with a conserved zinc finger/HTH architecture. The amino-terminal region contains a novel domain, featuring two CXXC motifs and occuring in a number of small bacterial proteins as well as in the present family. The carboxyl-terminal region consists of a helix-turn-helix domain, modeled by pfam01381. The predicted function is DNA binding and transcriptional regulation.


Pssm-ID: 274805 [Multi-domain]  Cd Length: 127  Bit Score: 49.17  E-value: 5.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488987810    4 DGLAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAIStLQKLLKV 58
Cdd:TIGR03830  62 DGLLTGPEIRRIRKKLGLSQREAAELLGGGVNAFSRYERGEVRPSKA-LDKLLRL 115
 
Name Accession Description Interval E-value
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
1-185 8.45e-136

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 376.83  E-value: 8.45e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810   1 MSDDGLAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVVI 80
Cdd:PRK09943   1 MSDEGLAPGKRLSEIRQQQGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVVI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  81 NQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINT 160
Cdd:PRK09943  81 NQDDLIEMGSQGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAINT 160

                        170       180
                 ....*....|....*....|....*
gi 488987810 161 GIPHSFSNTSAGICRIISAHTPTTF 185
Cdd:PRK09943 161 GIPHSFSNTSAGICRIISAHTPTTF 185
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 92-181 2.82e-24

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 90.64  E-value: 2.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  92 GVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSA 171
Cdd:cd02209    1 GYTYELLSPGLPGRKMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGD 80

                         90
                 ....*....|
gi 488987810 172 GICRIISAHT 181
Cdd:cd02209   81 EPARVLWVIT 90
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
79-183 6.70e-20

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 80.45  E-value: 6.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  79 VINQDDLIEMGSqGVSMKLVHNGNPNRTLAMIFETYQPGTTTGERIKHQ-GEEIGTILEGEIVLTINGQSYHLVAGQSYA 157
Cdd:COG3837    1 IVNLDDLPGPEA-GRRYRRLGDALGLTRLGVNLITLPPGASSSPYHAHSaEEEFVYVLEGELTLRIGGEEYVLEPGDSVG 79

                         90       100
                 ....*....|....*....|....*.
gi 488987810 158 INTGIPHSFSNTSAGICRIISAHTPT 183
Cdd:COG3837   80 FPAGVPHRLRNRGDEPARYLVVGTRA 105
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-79 8.11e-20

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 79.27  E-value: 8.11e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987810   1 MSDDGLAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEKPDEPQVV 79
Cdd:COG1396    1 MSTLKKALGERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDELLGGADEELPEALL 79
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
84-182 2.29e-16

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 70.65  E-value: 2.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  84 DLIEMGSQGVSMKLVHNGNPNRTLAMIfeTYQPGTTTGERiKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIP 163
Cdd:COG1917    2 RLAEIALTGVSVRVLADGEDELEVVRV--TFEPGARTPWH-SHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVP 78

                         90
                 ....*....|....*....
gi 488987810 164 HSFSNTSAGICRIISAHTP 182
Cdd:COG1917   79 HAFRNLGDEPAVLLVVFSP 97
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 9-66 1.45e-15

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 67.19  E-value: 1.45e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488987810   9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEF 66
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
94-185 1.68e-15

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 69.01  E-value: 1.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  94 SMKLVHNGNPNRTLAMIfeTYQPGTTTGERIKHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGI 173
Cdd:COG0662   16 SYEVLGEGGERLSVKRI--TVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEP 93

                         90
                 ....*....|..
gi 488987810 174 CRIISAHTPTTF 185
Cdd:COG0662   94 LELLEVQAPAYL 105
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
11-66 6.25e-15

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 65.62  E-value: 6.25e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 488987810    11 RLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEF 66
Cdd:smart00530   1 RLKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
9-71 6.89e-15

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 66.02  E-value: 6.89e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987810   9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPE 71
Cdd:COG1476    6 GNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELALKIARALGVSLEELFSLEE 68
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 111-180 7.22e-15

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 66.13  E-value: 7.22e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987810  111 FETYQPGTTtGERIKHQGE-EIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGICRIISAH 180
Cdd:pfam07883   2 LVTLPPGES-SPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 12-66 3.04e-13

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 61.40  E-value: 3.04e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488987810   12 LSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEF 66
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 9-65 5.27e-12

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 58.41  E-value: 5.27e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488987810   9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSE 65
Cdd:COG1813   14 GERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISLAE 70
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 9-87 2.72e-10

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 54.64  E-value: 2.72e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987810   9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFFSEPEkpDEPQVVINQDDLIE 87
Cdd:COG3620   19 GEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALGKELSAVLVVDD--GKLVGIITRRDLLK 95
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 103-178 6.95e-10

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 53.74  E-value: 6.95e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987810 103 PNRTLAMIFETYQPGTTTGeRIKHQGEEIGTILEGEIVLTINGQ-SYHLVAGQSYAINTGIPHSFSNTSAGICRIIS 178
Cdd:cd02235   15 PGREVVQVRVEIPPGAVAG-RHTHPGEESGYVLEGSLELEVDGQpPVTLKAGDSFFIPAGTVHNAKNVGSGPAKLLA 90
HTH_31 pfam13560
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.
 9-65 5.17e-09

Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433309 [Multi-domain]  Cd Length: 64  Bit Score: 50.22  E-value: 5.17e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488987810    9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVS-PAISTLQKLLKVYGLSLSE 65
Cdd:pfam13560   3 GARLRRLRERAGLSQEALARRLGVSRSTLSRLETGRRGrPSPAVVERLARALGVDGAE 60
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 9-67 3.56e-08

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.


Pssm-ID: 463728 [Multi-domain]  Cd Length: 64  Bit Score: 48.05  E-value: 3.56e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488987810    9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLSEFF 67
Cdd:pfam12844   1 GERLRKAREERGLTQEELAERLGISRSQLSAIENGKSVPPAETLYKIAELLGVPANWLL 59
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 79-166 3.80e-08

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 49.00  E-value: 3.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  79 VINQDDL--IEMGsQGVSMKLVHNGNpnrTLAMIFETYQPGTTTGERiKHQGEEIGTILEGEIVLTINGQSYHLVAGQSY 156
Cdd:cd02238    1 FVKWDELpwEELG-PGVRRKILAGGE---KLMLVEVRFEKGAVVPLH-SHPHEQIGYVLSGRFEFTIGGETRILKPGDSY 75

                         90
                 ....*....|
gi 488987810 157 AINTGIPHSF 166
Cdd:cd02238   76 YIPPNVPHGA 85
CxxCG_CxxCG_HTH TIGR03830
putative zinc finger/helix-turn-helix protein, YgiT family; This model describes a family of ...
 4-58 5.61e-08

putative zinc finger/helix-turn-helix protein, YgiT family; This model describes a family of predicted regulatory proteins with a conserved zinc finger/HTH architecture. The amino-terminal region contains a novel domain, featuring two CXXC motifs and occuring in a number of small bacterial proteins as well as in the present family. The carboxyl-terminal region consists of a helix-turn-helix domain, modeled by pfam01381. The predicted function is DNA binding and transcriptional regulation.


Pssm-ID: 274805 [Multi-domain]  Cd Length: 127  Bit Score: 49.17  E-value: 5.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488987810    4 DGLAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAIStLQKLLKV 58
Cdd:TIGR03830  62 DGLLTGPEIRRIRKKLGLSQREAAELLGGGVNAFSRYERGEVRPSKA-LDKLLRL 115
PRK09706 PRK09706
transcriptional repressor DicA; Reviewed
 9-77 4.27e-07

transcriptional repressor DicA; Reviewed


Pssm-ID: 182039 [Multi-domain]  Cd Length: 135  Bit Score: 47.16  E-value: 4.27e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987810   9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSLS--EFFSEPEKPDEPQ 77
Cdd:PRK09706   7 GQRIRYRRKQLKLSQRSLAKAVKVSHVSISQWERDETEPTGKNLFALAKALQCSPTwlLFGDEDKQPTPPV 77
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 113-177 6.71e-07

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 45.17  E-value: 6.71e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987810 113 TYQPGTTTGERIKHQGEEIGTILEGEIVLTIN-GQSYHLVAGQSYAINTGIPHSFSNTSAGICRII 177
Cdd:cd02208    5 TLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 117-177 2.99e-06

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 44.43  E-value: 2.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987810 117 GTTTGERikhqGEEIGT---ILEGEIVLTINGQSYHLVAGqSYA-INTGIPHSFSNTSAGICRII 177
Cdd:cd02211   37 GSTAPEG----GEGIERflyVLEGEVELTVGGETHTLTAG-GYAyLPPGTKHSLRNAGDEPARLL 96
YiaG COG2944
DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];
1-58 4.55e-06

DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];


Pssm-ID: 442187 [Multi-domain]  Cd Length: 64  Bit Score: 42.61  E-value: 4.55e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488987810   1 MSDDGLAPgKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLqKLLKV 58
Cdd:COG2944    1 MTKKPLTP-EEIRALRERLGLSQAEFAALLGVSVSTVRRWEQGRRKPSGAAL-KLLRL 56
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 117-182 7.44e-06

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 43.05  E-value: 7.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987810 117 GTTT---GERIKHQ----GEEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGICRIISAHTP 182
Cdd:cd06991   22 GTLTlapGERVSEHyhpySEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARLVFHLSP 94
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 112-177 9.50e-06

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 42.47  E-value: 9.50e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987810 112 ETYQPGTTTGERIKH-QGEEIGTILEGEIVLTINGQSYHLVAGQSYA--INTGIPHSFSNTSAGICRII 177
Cdd:cd02224   22 ERLPPGARSSPRHWHsAEEEFVYVLSGEGTLRLDGEEVLPRPGDFVGfpAGTGVAHQLINRSDEPLVYL 90
couple_hipB TIGR03070
transcriptional regulator, y4mF family; Members of this family belong to a clade of ...
 16-63 9.75e-06

transcriptional regulator, y4mF family; Members of this family belong to a clade of helix-turn-helix DNA-binding proteins, among the larger family pfam01381 (HTH_3; Helix-turn-helix). Members are similar in sequence to the HipB protein of E. coli. Genes for members of the seed alignment for this protein family were found to be closely linked to genes encoding proteins related to HipA. The HibBA operon appears to have some features in common with toxin-antitoxin post-segregational killing systems. [Regulatory functions, DNA interactions]


Pssm-ID: 213767 [Multi-domain]  Cd Length: 58  Bit Score: 41.49  E-value: 9.75e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 488987810   16 RQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSL 63
Cdd:TIGR03070  11 RKALGLTQADLADLAGVGLRFIRDLENGKPTVRLDKVLRVLDALGLEL 58
RodZ COG1426
Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell ...
 8-67 1.42e-05

Cytoskeletal protein RodZ, contains Xre-like HTH and DUF4115 domains [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441035 [Multi-domain]  Cd Length: 71  Bit Score: 41.33  E-value: 1.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987810   8 PGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVS------PAISTLQKLLKVYGLSLSEFF 67
Cdd:COG1426    6 IGELLRQAREAKGLSLEDVAERTKISVSYLEAIEEGDFDalpgpvYVRGFLRSYARALGLDPEELL 71
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 125-171 3.02e-05

Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 41.03  E-value: 3.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488987810 125 KHQGEEIGTILEGEIVLTINGQSYHLVA-GQSYAINTGIPHSFSNTSA 171
Cdd:cd06975   36 QHREEQIGMILNGELEMTVGGEEQELEPlGDVYYAPPNVPHGAVNPSD 83
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 99-182 1.02e-04

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810  99 HNGNPNRTLAMIfeTYQPGTTTgERIKHQG-EEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGICRII 177
Cdd:cd02214   13 NDGDPRYSLAHA--RVPPGEST-LPHRLKGsEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIENTGEEDLVFL 89


                 ....*
gi 488987810 178 SAHTP 182
Cdd:cd02214   90 CICSP 94
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
 11-67 2.88e-04

Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433211 [Multi-domain]  Cd Length: 63  Bit Score: 37.52  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488987810   11 RLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKV-SPAISTLQKLLKVYGLSLSEFF 67
Cdd:pfam13443   1 KLRKLMADRGISKSDLARATGISRATLSRLRKGKPkRVSLDTLDKICDALGCQPGDLL 58
COG1395 COG1395
Predicted transcriptional regulator [Transcription];
9-96 3.69e-04

Predicted transcriptional regulator [Transcription];


Pssm-ID: 441005 [Multi-domain]  Cd Length: 313  Bit Score: 39.82  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987810   9 GKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAISTLQKLLKVYGLSL----------SEFFSEPEKPDEPQV 78
Cdd:COG1395  129 GEKLRELREERGLSLGELASELGVSRRTISKYERGEMDASIEVALKLEEILGEPIvkpidilegaEDLEEAEPTPEDPEE 208

                         90
                 ....*....|....*...
gi 488987810  79 VINQDDLIEMGSQGVSMK 96
Cdd:COG1395  209 EEILEVLSRLGFDVHPTK 226
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 127-165 4.33e-04

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 37.49  E-value: 4.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488987810 127 QGEEIGT----------ILEGEIVLTINGQSYHLVAGQSYAINTGIPHS 165
Cdd:cd02230   20 AGQELSEhtapgdatvqVLEGEAEFTIGGETVTLKAGELIVMPANVPHA 68
PRK10856 PRK10856
cytoskeleton protein RodZ;
6-48 5.43e-04

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 39.62  E-value: 5.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488987810   6 LAPGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKvSPA 48
Cdd:PRK10856  13 LTTGERLRQAREQLGLTQQAVAERLCLKVSTVRDIEEDK-APA 54
MqsA_antitoxin pfam15731
Antitoxin component of bacterial toxin-antitoxin system, MqsA; MqsA_antitoxin is a family of ...
 15-58 5.44e-04

Antitoxin component of bacterial toxin-antitoxin system, MqsA; MqsA_antitoxin is a family of prokaryotic proteins that act as antidotes to the mRNA interferase MqsR. It has a zinc-binding at the very N-terminus indicating its DNA-binding capacity. MqsR is the gene most highly upregulated in E. Colo MqsR_toxin is a family of bacterial toxins that act as an mRNA interferase. MqsR is the gene most highly upregulated in E. coli persister cells and it plays an essential role in biofilm regulation and cell signalling. It forms part of a bacterial toxin-antitoxin TA system, and as expected for a TA system, the expression of the MqsR toxin leads to growth arrest, while co-expression with its antitoxin, MqsA, rescues the growth arrest phenotype. In addition, MqsR associates with MqsA to form a tight, non-toxic complex and both MqsA alone and the MqsR:MqsA2:MqsR complex bind and regulate the mqsR promoter. The structure of MqsR shows that is is a member of the RelE/YoeB family of bacterial RNases that are structurally and functionally characterized bacterial toxins.


Pssm-ID: 292359 [Multi-domain]  Cd Length: 131  Bit Score: 38.13  E-value: 5.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 488987810   15 IRQQLGLSQRRAAELSGLTHSAISTIEQDKVSPAIStLQKLLKV 58
Cdd:pfam15731  77 VRKKLGLDQREAAEIFGGGVNAFSRYENGKTRPPLA-LVKLLRL 119
cupin_BacB_C cd10547
Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model ...
 125-170 5.64e-04

Bacillus subtilis bacilysin and related proteins, C-terminal cupin domain; This model represents the C-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380415 [Multi-domain]  Cd Length: 92  Bit Score: 37.63  E-value: 5.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488987810 125 KHQGEEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTS 170
Cdd:cd10547   36 QHRGEQIGIILNGKYDMTVGGEEQELGYGKIYYAPPNVSHSGYNDS 81
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
134-177 1.16e-03

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 38.34  E-value: 1.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488987810 134 ILEGEIVLTINGQSYHLVAGqSYA-INTGIPHSFSNTSAGICRII 177
Cdd:PRK11171  89 VVEGEITLTLEGKTHALSEG-GYAyLPPGSDWTLRNAGAEDARFH 132
cupin_BacB_N cd20307
Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model ...
 126-171 1.45e-03

Bacillus subtilis bacilysin and related proteins, N-terminal cupin domain; This model represents the N-terminal domain of bacilysin (BacB, also known as AerE in Microcystis aeruginosa), a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. Bacilysin is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF Aeruginosin biosynthesis gene cluster in Microcystis aeruginosa. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380441 [Multi-domain]  Cd Length: 100  Bit Score: 36.47  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488987810 126 HQGEEIGTILEGEIVLTINGQSYHLVAGQS-YAINTGIPHSFSNTSA 171
Cdd:cd20307   42 HPESQIGMVLSGELEMNVGGVKKVMEPLQDvYVAPPNVPHGAVNPSS 88
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 126-182 2.11e-03

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 35.90  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488987810 126 HQG-EEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGICRIISAHTP 182
Cdd:cd06979   36 HEDwEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVHGFVNRSGGPTCRLCVLAP 93
HTH_37 pfam13744
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain.
 7-46 2.67e-03

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain.


Pssm-ID: 433449 [Multi-domain]  Cd Length: 80  Bit Score: 35.28  E-value: 2.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 488987810    7 APGKRLSEIRQQLGLSQRRAAELSGLTHSAISTIEQDKVS 46
Cdd:pfam13744  18 QLARAIARLIEGRGLSQQEAAALLGIAQPKVSALLKGKLS 57
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 121-177 6.43e-03

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 35.22  E-value: 6.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987810 121 GERI---KHQG-EEIGTILEGEIVLTINGQSYHLVAGQSYAINTGIPHSFSNTSAGICRII 177
Cdd:cd02213   50 GKRLslqRHHHrSEHWVVVSGTAEVTLDGKEKLLKEGESIYIPKGTKHRLENPGKIPLEII 110
 
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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