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Conserved domains on  [gi|29826321|ref|NP_054908|]
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alpha-adducin isoform b [Homo sapiens]

Protein Classification

class II aldolase/adducin head domain-containing protein( domain architecture ID 842)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 145-391 3.23e-98

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


The actual alignment was detected with superfamily member PRK07044:

Pssm-ID: 469663  Cd Length: 252  Bit Score: 304.46  E-value: 3.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGtgsppkwqIGEQEFEALMRM 383
Cdd:PRK07044 174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAG--------AGELAWPALLRK 242

                        250
                 ....*....|
gi 29826321  384 LD--NLGYRT 391
Cdd:PRK07044 243 LDriDPGYRD 252
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 616-739 7.85e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   616 GSEENLDEAREQKEKSPPDQPAVP-HPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSP--DEPSEALGFPMLEKE 692
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPaSPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasDAASSRQAALPLSSP 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 29826321   693 EEAHRPPSP--TEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSD 739
Cdd:PHA03307  180 EETARAPSSppAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 145-391 3.23e-98

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 304.46  E-value: 3.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGtgsppkwqIGEQEFEALMRM 383
Cdd:PRK07044 174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAG--------AGELAWPALLRK 242

                        250
                 ....*....|
gi 29826321  384 LD--NLGYRT 391
Cdd:PRK07044 243 LDriDPGYRD 252
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 142-352 7.52e-68

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 222.63  E-value: 7.52e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIV--DRGSTNLGvnqa 219
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 220 gftLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKVLIQKNLG-PKSK 295
Cdd:cd00398  75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 29826321 296 VLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGG--PDNLVLLNPEKYKAK 352
Cdd:cd00398 151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 145-341 2.87e-57

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 194.28  E-value: 2.87e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnlGVNQAGFTLH 224
Cdd:COG0235   6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKVLIQKNLGpKSKVLILRNH 302
Cdd:COG0235  80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 29826321 303 GLVSVGESVEEAFYYIHNLVVACEIQVRTLAsAGGPDNL 341
Cdd:COG0235 158 GVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 147-329 1.94e-55

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 188.14  E-value: 1.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   227 IYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKVLIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 29826321   305 VSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 149-329 6.13e-53

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 181.68  E-value: 6.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321    149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321    229 AARPDVKCVVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKV-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 29826321    302 HGLVSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 616-739 7.85e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   616 GSEENLDEAREQKEKSPPDQPAVP-HPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSP--DEPSEALGFPMLEKE 692
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPaSPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasDAASSRQAALPLSSP 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 29826321   693 EEAHRPPSP--TEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSD 739
Cdd:PHA03307  180 EETARAPSSppAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 634-733 3.58e-04

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 43.60  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  634 DQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEA-SPEP 712
Cdd:NF040712 212 ARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAeTPEA 291

                         90       100
                 ....*....|....*....|.
gi 29826321  713 APDPAPVAEEAAPSAVEEGAA 733
Cdd:NF040712 292 AEPPAPAPAAPAAPAAPEAEE 312
ZipA COG3115
Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 606-730 2.56e-03

Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442349 [Multi-domain]  Cd Length: 298  Bit Score: 40.45  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 606 YRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEED------LVPEPTTGDDSD--AATFKPTLPDLSP 677
Cdd:COG3115  29 ERRSSFRDKPSKRDVLLDDDGIGEVRVVAAEAPERVEPEASFDAEDEvrepdqEEVDPLLDDEADieAAPAEPVRWAGTA 108

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 29826321 678 DEPSEALGFPMLEKEEEAHRPPSPTEAPTEAsPEPAPDPAPVAEEAAPSAVEE 730
Cdd:COG3115 109 AAVEPAPEQEAYEEAGPAGESAEQEDAPAEE-PEAEAPAEEALAAELCAEPEE 160
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 145-391 3.23e-98

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 304.46  E-value: 3.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGtgsppkwqIGEQEFEALMRM 383
Cdd:PRK07044 174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAG--------AGELAWPALLRK 242

                        250
                 ....*....|
gi 29826321  384 LD--NLGYRT 391
Cdd:PRK07044 243 LDriDPGYRD 252
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 142-352 7.52e-68

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 222.63  E-value: 7.52e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIV--DRGSTNLGvnqa 219
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 220 gftLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKVLIQKNLG-PKSK 295
Cdd:cd00398  75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 29826321 296 VLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGG--PDNLVLLNPEKYKAK 352
Cdd:cd00398 151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 145-341 2.87e-57

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 194.28  E-value: 2.87e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnlGVNQAGFTLH 224
Cdd:COG0235   6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKVLIQKNLGpKSKVLILRNH 302
Cdd:COG0235  80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 29826321 303 GLVSVGESVEEAFYYIHNLVVACEIQVRTLAsAGGPDNL 341
Cdd:COG0235 158 GVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 147-329 1.94e-55

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 188.14  E-value: 1.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   227 IYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKVLIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 29826321   305 VSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 149-329 6.13e-53

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 181.68  E-value: 6.13e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321    149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321    229 AARPDVKCVVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKV-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 29826321    302 HGLVSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PRK06661 PRK06661
hypothetical protein; Provisional
 149-334 1.97e-43

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 156.92  E-value: 1.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  149 LAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLHSAIY 228
Cdd:PRK06661   7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  229 AARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGE-VAYHDYHGILVDEE-EKVLIQKNLGpKSKVLILRNHGLVS 306
Cdd:PRK06661  84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSLALDADkQSSRLVNDLK-QNYVMLLRNHGAIT 162

                        170       180
                 ....*....|....*....|....*...
gi 29826321  307 VGESVEEAFYYIHNLVVACEIQVRTLAS 334
Cdd:PRK06661 163 CGKTIHEAMFYTYHLEQACKTQCLLNST 190
PRK06208 PRK06208
class II aldolase/adducin family protein;
148-361 2.36e-41

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 152.45  E-value: 2.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  148 KLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgsTNLGVNQAGFTLHSAI 227
Cdd:PRK06208  46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  228 YAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGE--VAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHGLV 305
Cdd:PRK06208 123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEdhALFDDFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 29826321  306 SVGESVEEA-FYYIhNLVVACEIQVrtLASAGGPdnLVLLNPEKYKAKSRSPGSPVG 361
Cdd:PRK06208 202 TVGPSVDAAaWWFI-ALERACQTQL--LAEAAGP--PQPIDHETARHTRSQVGSEYG 253
PRK06486 PRK06486
aldolase;
114-385 1.47e-26

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 109.42  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  114 MA-ALNMSLGMVTPVNDLRGSDSIAYdkgeklLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEV 192
Cdd:PRK06486   1 MAhSLTTDSAPPAGNRPLLDSDAVAQ------ARVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  193 TASSLVKINLQGDIVD-RGStnlgVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMK-CGLLPISPEALSL-GEVA 269
Cdd:PRK06486  75 TASDLLICDFDGNVLAgRGE----PEATAFFIHARIHRAIPRAKAAFHTHMPYATALSLTEgRPLTTLGQTALKFyGRTA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  270 Y-HDYHGILVDEEEKVLIQKNLGPKSkVLILRNHGLVSVGESVEEAF---YYihnLVVACEIQVRTLaSAGGPdnLVLLN 345
Cdd:PRK06486 151 VdEDYNGLALDAAEGDRIARAMGDAD-IVFLKNHGVMVCGPRIAEAWddlYY---LERACEVQVLAM-STGRP--LVPVD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 29826321  346 PEKYKAKSRspgspvgegtgsppKWQIGEQE-----FEALMRMLD 385
Cdd:PRK06486 224 PAIAAAVAR--------------QMREGDREsarlhLEALRRTLD 254
PRK07490 PRK07490
hypothetical protein; Provisional
 135-385 2.78e-20

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 90.93  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  135 SIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINlqGDIVDRGSTNL 214
Cdd:PRK07490   1 MTMALSDEEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD--ADDPSTAERPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  215 GVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCG-LLPISPE-ALSLGEVAYHDYHGILVDEEEKVLIQKNLGP 292
Cdd:PRK07490  79 VPDATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNtARFFNRVAVDTLYGGMALEEEGERLAGLLGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  293 KSkVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASaGGPdnLVLLNPEkykaksrspgspVGEGTGSppKWQ- 371
Cdd:PRK07490 159 KR-RLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALST-GQP--LRVLSDA------------VAEKTAR--DWEd 220

                        250
                 ....*....|....*..
gi 29826321  372 ---IGEQEFEALMRMLD 385
Cdd:PRK07490 221 ypgFSRQHFAELKALLD 237
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 145-338 5.40e-19

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 87.38  E-value: 5.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  145 LRCKLAAFYRLADLFGWSQLIYNHITTRvnSEQEH-FLIVPFGLLYSEVTASSLVKINLQGDIVD-RGSTNlGVNQagft 222
Cdd:PRK07090  31 LRQKLALTCRILFDAGHDSGLAGQITAR--AEAPGtYYTQRLGLGFDEITASNLLLVDEDLNVLDgEGMPN-PANR---- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  223 LHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAY-HDYHGILVDEEEKVLIQKNLGPKSKVLiLR 300
Cdd:PRK07090 104 FHSWIYRARPDVNCIIHTHPPHVAALSMLEVPLVVSHMDTCPLyDDCAFlKDWPGVPVGNEEGEIISAALGDKRAIL-LS 182

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 29826321  301 NHGLVSVGESVEEAFYYIHNLVVACEIQVrtLASAGGP 338
Cdd:PRK07090 183 HHGQLVAGKSIEEACVLALLIERAARLQL--LAMAAGP 218
PRK08333 PRK08333
aldolase;
143-316 2.15e-13

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 69.08  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  143 KLLRCKLAAFYRLADLFGWSQLIYNHITTRVNseqEHFLIVPFGLLYSEVTASSLVKINLQGDIVD--RGSTNlgvnqag 220
Cdd:PRK08333   2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSE------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  221 FTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLP-ISPEA-LSLGEVAYHDYHGI----LVDEEEKVLIQKNlgpks 294
Cdd:PRK08333  72 YRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPiITPEAeLYLKKIPILPFRPAgsveLAEQVAEAMKEYD----- 146

                        170       180
                 ....*....|....*....|..
gi 29826321  295 kVLILRNHGLVSVGESVEEAFY 316
Cdd:PRK08333 147 -AVIMERHGIVTVGRSLREAFY 167
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 176-314 4.48e-12

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 66.18  E-value: 4.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  176 EQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrGSTNLGVNQAGftlHSAIYAARPDVKCVVHIHTPAGAAVSA----M 251
Cdd:PRK06557  41 GTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDTAS---HLYVYRHMPDVGGVVHTHSTYATAWAArgepI 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29826321  252 KCGLLPISPEAlsLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEA 314
Cdd:PRK06557 117 PCVLTAMADEF--GGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
PRK08130 PRK08130
putative aldolase; Validated
 179-316 1.91e-07

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 52.57  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  179 HFLIVPFGLLYSEVTASSLVKINLQGDIV--DRGSTNLgvnqagfTLHSAIYAARPDVKCVVHIHTPAGAAVSAM----- 251
Cdd:PRK08130  38 GWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLTALSCLggldp 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29826321  252 KCGLLPISPEAL-SLGEVAYHDYH--GilvDEEEKVLIQKnLGPKSKVLILRNHGLVSVGESVEEAFY 316
Cdd:PRK08130 111 TNVLPPFTPYYVmRVGHVPLIPYYrpG---DPAIAEALAG-LAARYRAVLLANHGPVVWGSSLEAAVN 174
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
174-338 3.71e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 51.67  E-value: 3.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  174 NSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrGSTnlgVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKC 253
Cdd:PRK06833  34 NREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGW 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  254 GLLPISPE-ALSLGEVAYHDYHGI----LVDEEEKVLIQKnlgpksKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQ 328
Cdd:PRK06833 110 ELPAVHYLiAVAGPNVRCAEYATFgtkeLAENAFEAMEDR------RAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIY 183

                        170
                 ....*....|
gi 29826321  329 VRTlASAGGP 338
Cdd:PRK06833 184 YQT-KSIGEP 192
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
177-333 3.96e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 48.58  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  177 QEHFLIVPFGLLYSEVTASSLVKINlqgdivDRGSTNLG-VNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGL 255
Cdd:PRK08087  35 QDGMLITPTGIPYEKLTESHIVFVD------GNGKHEEGkLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRPI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  256 --------------LPISPEAlSLG--EVAYHDYHGIlvdeeekvliqknlgPKSKVLILRNHGLVSVGESVEEAFYYIH 319
Cdd:PRK08087 109 paihymiaaaggnsIPCAPYA-TFGtrELSEHVALAL---------------KNRKATLLQHHGLIACEVNLEKALWLAH 172

                        170
                 ....*....|....
gi 29826321  320 NLVVACEIQVRTLA 333
Cdd:PRK08087 173 EVEVLAQLYLKTLA 186
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 616-739 7.85e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   616 GSEENLDEAREQKEKSPPDQPAVP-HPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSP--DEPSEALGFPMLEKE 692
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPaSPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasDAASSRQAALPLSSP 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 29826321   693 EEAHRPPSP--TEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSD 739
Cdd:PHA03307  180 EETARAPSSppAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 173-327 8.13e-05

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 44.79  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  173 VNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVD---RGSTNLGVnqagftlHSAIYAARPDVKCVVHIHTP------ 243
Cdd:PRK12348  31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSSDTAT-------HLELYRRYPSLGGIVHTHSThatawa 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  244 -AGAAVSAMKC-------GLLPISpEALSLGEVAyHDYHgilvDEEEKVLIQkNLGPKSKV----LILRNHGLVSVGESV 311
Cdd:PRK12348 104 qAGLAIPALGTthadyffGDIPCT-RGLSEEEVQ-GEYE----LNTGKVIIE-TLGNAEPLhtpgIVVYQHGPFAWGKDA 176

                        170
                 ....*....|....*.
gi 29826321  312 EEAfyyIHNLVVACEI 327
Cdd:PRK12348 177 HDA---VHNAVVMEEV 189
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 173-323 9.07e-05

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 44.82  E-value: 9.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  173 VNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrGSTNlgvNQAGFTLHSAIYAARPDVKCVVHIHTPAGA----AV 248
Cdd:PRK13145  33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVE-GDLN---PSSDLPTHVELYKAWPEVGGIVHTHSTEAVgwaqAG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  249 SAMKC----------GLLPISpEALSLGEV--AYHDYHGILVDEEEKvliQKNLGPKS-KVLILRNHGLVSVGESVEEAF 315
Cdd:PRK13145 109 RDIPFygtthadyfyGPIPCA-RSLTKDEVngAYEKETGSVIIEEFE---KRGLDPMAvPGIVVRNHGPFTWGKNPEQAV 184


                 ....*...
gi 29826321  316 YyiHNLVV 323
Cdd:PRK13145 185 Y--HSVVL 190
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 627-736 1.57e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   627 QKEKSPP----DQPAVPH------PPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAH 696
Cdd:PRK10263  376 APEGYPQqsqyAQPAVQYneplqqPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQST 455

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 29826321   697 RPPSPTEAPTEASPEPAPDPAPvaeEAAPSAVEEGAAADP 736
Cdd:PRK10263  456 FAPQSTYQTEQTYQQPAAQEPL---YQQPQPVEQQPVVEP 492
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
622-734 1.67e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.23  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  622 DEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAAtfkPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSP 701
Cdd:PRK07003 437 DRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPA---SDAPPDAAFEPAPRAAAPSAATPAAVPDARAP 513

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 29826321  702 TEAPTEASPEPAPDPAPVAEEAAPSAVEE-----GAAA 734
Cdd:PRK07003 514 AAASREDAPAAAAPPAPEARPPTPAAAAPaaragGAAA 551
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 634-733 3.58e-04

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 43.60  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  634 DQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEA-SPEP 712
Cdd:NF040712 212 ARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAeTPEA 291

                         90       100
                 ....*....|....*....|.
gi 29826321  713 APDPAPVAEEAAPSAVEEGAA 733
Cdd:NF040712 292 AEPPAPAPAAPAAPAAPEAEE 312
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 591-738 5.87e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   591 GPNPFTTLTdRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEpttgdDSDAATfkp 670
Cdd:PHA03307  259 RPAPITLPT-RIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE-----SSSSST--- 329

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29826321   671 tlpdLSPDEPSEALGFPmlekeeeahRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGS 738
Cdd:PHA03307  330 ----SSSSESSRGAAVS---------PGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGR 384
PHA03419 PHA03419
E4 protein; Provisional
 632-722 7.76e-04

E4 protein; Provisional


Pssm-ID: 223079 [Multi-domain]  Cd Length: 200  Bit Score: 41.47  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  632 PPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTL--------PDLSPDEPSEAlgfpmlEKEEEAHRPPSPTE 703
Cdd:PHA03419  63 PPPCPPSPGHPPQTNDTHEKDLALQPPPGGKKKEKKKKETEkpaqggekPDQGPEAKGEG------EGHEPEDPPPEDTP 136

                         90       100
                 ....*....|....*....|....*
gi 29826321  704 AP------TEASPEPAPDPAPVAEE 722
Cdd:PHA03419 137 PPpggegeVEGGPSPGPGPGPLDQE 161
PHA03169 PHA03169
hypothetical protein; Provisional
 588-739 1.11e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  588 STTGPNPFTTLTD--RELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIkLEEDLVPEPTTG--DDS 663
Cdd:PHA03169  52 TTSGPQVRAVAEQghRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEE-LASGLSPENTSGssPES 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  664 DAATFKPTLP-----DLSPDEPSEALGFP----MLEKEEEAHRPPSPTEAPTEASPEPAPDP--APVAEEAAPSAV---E 729
Cdd:PHA03169 131 PASHSPPPSPpshpgPHEPAPPESHNPSPnqqpSSFLQPSHEDSPEEPEPPTSEPEPDSPGPpqSETPTSSPPPQSppdE 210

                        170
                 ....*....|
gi 29826321  730 EGAAADPGSD 739
Cdd:PHA03169 211 PGEPQSPTPQ 220
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 631-737 1.22e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  631 SPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLS-PDEPSEALGFPMLEKEEEAHRPPSPTEAPTEAS 709
Cdd:PRK07764 695 GAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPlPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774

                         90       100
                 ....*....|....*....|....*...
gi 29826321  710 PEPAPDPAPVAEEAAPSAVEEGAAADPG 737
Cdd:PRK07764 775 PPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 627-738 1.64e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.84  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  627 QKEKSPPdQPAVPHPPPSTPIKLEEDL------VPEPTTGDDSDA----ATFKPTLPDL--SPDEPSEALGFPMLEKEEE 694
Cdd:PLN03209 355 PIEEEPP-QPKAVVPRPLSPYTAYEDLkpptspIPTPPSSSPASSksvdAVAKPAEPDVvpSPGSASNVPEVEPAQVEAK 433

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 29826321  695 AHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGS 738
Cdd:PLN03209 434 KTRPLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDT 477
PHA03247 PHA03247
large tegument protein UL36; Provisional
 624-757 2.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   624 AREQKEKSPPDQP---------------AVPHPPPSTPIKLEEDLVP--EPTTGDDSDAATFKPTLPDLSPDEPSEALGF 686
Cdd:PHA03247 2671 GRAAQASSPPQRPrrraarptvgsltslADPPPPPPTPEPAPHALVSatPLPPGPAAARQASPALPAAPAPPAVPAGPAT 2750

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29826321   687 PMLEKEEEAHR----PPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPS 757
Cdd:PHA03247 2751 PGGPARPARPPttagPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
633-739 2.21e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  633 PDQPAVPHPPPSTPikleedlvPEPTTGDDSDAATFKPTLPDLSPDEPSEAlgfpmleKEEEAHRPPSPTEAPTEASPEP 712
Cdd:PRK07003 417 AAAATRAEAPPAAP--------APPATADRGDDAADGDAPVPAKANARASA-------DSRCDERDAQPPADSGSASAPA 481

                         90       100
                 ....*....|....*....|....*..
gi 29826321  713 APDPAPVAEEAAPSAVEEGAAADPGSD 739
Cdd:PRK07003 482 SDAPPDAAFEPAPRAAAPSAATPAAVP 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
 622-737 2.26e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   622 DEAREQKEKSPPDQPAVPHPPPSTpiKLEEDLVPEPTtgdDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAhRPPSP 701
Cdd:PHA03247 2861 DVRRRPPSRSPAAKPAAPARPPVR--RLARPAVSRST---ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP-QPPPP 2934

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 29826321   702 TEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPG 737
Cdd:PHA03247 2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG 2970
ZipA COG3115
Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
 606-730 2.56e-03

Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442349 [Multi-domain]  Cd Length: 298  Bit Score: 40.45  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 606 YRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEED------LVPEPTTGDDSD--AATFKPTLPDLSP 677
Cdd:COG3115  29 ERRSSFRDKPSKRDVLLDDDGIGEVRVVAAEAPERVEPEASFDAEDEvrepdqEEVDPLLDDEADieAAPAEPVRWAGTA 108

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 29826321 678 DEPSEALGFPMLEKEEEAHRPPSPTEAPTEAsPEPAPDPAPVAEEAAPSAVEE 730
Cdd:COG3115 109 AAVEPAPEQEAYEEAGPAGESAEQEDAPAEE-PEAEAPAEEALAAELCAEPEE 160
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 632-738 2.66e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   632 PPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPE 711
Cdd:PHA03307   81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPA 160

                          90       100
                  ....*....|....*....|....*...
gi 29826321   712 PAPDPAPVAEEAA-PSAVEEGAAADPGS 738
Cdd:PHA03307  161 AVASDAASSRQAAlPLSSPEETARAPSS 188
PHA03169 PHA03169
hypothetical protein; Provisional
 604-756 3.63e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  604 EEYRREVERKQKGSEENL-DEAREQKEK-SPPDQPAVPHPPPSTPIKLE--EDLVPEPTTGDDSDAAT--FKPTLPDlSP 677
Cdd:PHA03169  97 SESVGSPTPSPSGSAEELaSGLSPENTSgSSPESPASHSPPPSPPSHPGphEPAPPESHNPSPNQQPSsfLQPSHED-SP 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  678 DEPSEALGFPMlEKEEEAHRPPSPTEAPTEASP--EPAPDPAPVAEEAapsavEEGAAADPGSDGSPGKSPSKKKKKFRT 755
Cdd:PHA03169 176 EEPEPPTSEPE-PDSPGPPQSETPTSSPPPQSPpdEPGEPQSPTPQQA-----PSPNTQQAVEHEDEPTEPEREGPPFPG 249


                 .
gi 29826321  756 P 756
Cdd:PHA03169 250 H 250
PHA03379 PHA03379
EBNA-3A; Provisional
 623-730 3.77e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 40.81  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  623 EAREQKEKSPPDQPA-VPHPPP---STPIKLEEDLVPEPTTGDDSDAATFKPTLP-DLSPDEPSEALGFPMLEKEEEAH- 696
Cdd:PHA03379 426 EVPQSLETATSHGSAqVPEPPPvhdLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPgDQLPGVVQDGRPACAPVPAPAGPi 505

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 29826321  697 -RP--PSPTEAPTEASPEPAPDPAPVAEEAAPSAVEE 730
Cdd:PHA03379 506 vRPweASLSQVPGVAFAPVMPQPMPVEPVPVPTVALE 542
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 594-738 4.07e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 40.43  E-value: 4.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 594 PFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLV--PEPTTGDDSDAATFKPT 671
Cdd:COG5180 188 PRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAASSPKVDPPSTSEARSRPATvdAQPEMRPPADAKERRRA 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321 672 lPDLSPDEPSEAlGFPMLEKEEE---------------------------------------AHRPPSPTEAPTeASPEP 712
Cdd:COG5180 268 -AIGDTPAAEPP-GLPVLEAGSEpqsdapeaetarpidvkgvasappatrpvrppggardpgTPRPGQPTERPA-GVPEA 344

                       170       180       190
                ....*....|....*....|....*....|..
gi 29826321 713 A------PDPAPVAEEAAPSAVEEGAAADPGS 738
Cdd:COG5180 345 AsdagqpPSAYPPAEEAVPGKPLEQGAPRPGS 376
rne PRK10811
ribonuclease E; Reviewed
 618-733 4.20e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.79  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321   618 EENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHR 697
Cdd:PRK10811  889 EAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEV 968

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 29826321   698 PPSPTEAPTE-ASPEPAPDPAPVAEEAAPSAVEEGAA 733
Cdd:PRK10811  969 VVAEPEVVAQpAAPVVAEVAAEVETVTAVEPEVAPAQ 1005
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
629-739 9.58e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 9.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  629 EKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDL----SPDEPSEALGFPMLEKEEEAHRP------ 698
Cdd:PRK12323 371 GAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARavaaAPARRSPAPEALAAARQASARGPggapap 450

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 29826321  699 ---PSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSD 739
Cdd:PRK12323 451 apaPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADD 494
PRK08660 PRK08660
aldolase;
224-327 9.73e-03

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 38.01  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29826321  224 HSAIYAaRPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALS-LGE--VAYHDYHGILVDEEEKVLIQKNlgpksKVLILR 300
Cdd:PRK08660  72 HRAIYR-RTSAKAIVHAHPPYAVALSLLEDEIVPLDSEGLYfLGTipVVGGDIGSGELAENVARALSEH-----KGVVVR 145

                         90       100
                 ....*....|....*....|....*..
gi 29826321  301 NHGLVSVGESVEEAFYYIHNLVVACEI 327
Cdd:PRK08660 146 GHGTFAIGKTLEEAYIYTSQLEHSCKV 172
 
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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