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Conserved domains on  [gi|785039|emb|CAA88907|]
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alpha-adducin, normotensive phenotype [Rattus norvegicus]

Protein Classification

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 3.55e-97

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: 300.61  E-value: 3.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    225 SAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKILIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    304 LVSVGESVEEAFFYIHNLVVACEIQVRTLaSAGGPdnLVLLDPGKYKAKSRSPGTPAGEGSgsppkwqiGEQEFEALMRM 383
Cdd:PRK07044 174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAGA--------GELAWPALLRK 242

                        250
                 ....*....|
gi 785039    384 LD--NLGYRT 391
Cdd:PRK07044 243 LDriDPGYRD 252
PHA03169 super family cl27451
hypothetical protein; Provisional
 557-706 3.64e-04

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    557 STTGP--NPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPT--SRDGS 632
Cdd:PHA03169  52 TTSGPqvRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSgsSPESP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    633 GCHASKPTPP----DLSPDEPSEALAFPTVAEE------AHASPDTTQPlAEADPEPASASAPGAEEV------ASPATE 696
Cdd:PHA03169 132 ASHSPPPSPPshpgPHEPAPPESHNPSPNQQPSsflqpsHEDSPEEPEP-PTSEPEPDSPGPPQSETPtsspppQSPPDE 210

                        170
                 ....*....|
gi 785039    697 EGSPMDPGSD 706
Cdd:PHA03169 211 PGEPQSPTPQ 220
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 145-391 3.55e-97

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 300.61  E-value: 3.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    225 SAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKILIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    304 LVSVGESVEEAFFYIHNLVVACEIQVRTLaSAGGPdnLVLLDPGKYKAKSRSPGTPAGEGSgsppkwqiGEQEFEALMRM 383
Cdd:PRK07044 174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAGA--------GELAWPALLRK 242

                        250
                 ....*....|
gi 785039    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 1.86e-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: 223.78  E-value: 1.86e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIV--DRGSTNLGvnqa 219
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   220 gftLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKILIQKNLG-PKSK 295
Cdd:cd00398  75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 785039   296 VLILRNHGLVSVGESVEEAFFYIHNLVVACEIQVRTLASAGG--PDNLVLLDPGKYKAK 352
Cdd:cd00398 151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 145-341 6.59e-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: 192.74  E-value: 6.59e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGstnlGVNQAGFTLH 224
Cdd:COG0235   6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   225 SAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKILIQKNLGpKSKVLILRNH 302
Cdd:COG0235  80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 785039   303 GLVSVGESVEEAFFYIHNLVVACEIQVRTLAsAGGPDNL 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 3.36e-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: 186.98  E-value: 3.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039     147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039     227 IYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKILIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 785039     305 VSVGESVEEAFFYIHNLVVACEIQV 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 1.68e-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: 182.84  E-value: 1.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039      149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039      229 AARPDAKCIVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKI-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 785039      302 HGLVSVGESVEEAFFYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PHA03169 PHA03169
hypothetical protein; Provisional
 557-706 3.64e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    557 STTGP--NPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPT--SRDGS 632
Cdd:PHA03169  52 TTSGPqvRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSgsSPESP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    633 GCHASKPTPP----DLSPDEPSEALAFPTVAEE------AHASPDTTQPlAEADPEPASASAPGAEEV------ASPATE 696
Cdd:PHA03169 132 ASHSPPPSPPshpgPHEPAPPESHNPSPNQQPSsflqpsHEDSPEEPEP-PTSEPEPDSPGPPQSETPtsspppQSPPDE 210

                        170
                 ....*....|
gi 785039    697 EGSPMDPGSD 706
Cdd:PHA03169 211 PGEPQSPTPQ 220
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 567-700 5.01e-03

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: 39.75  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    567 LTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPTSRDGSGCHASKPTPPDLSP 646
Cdd:NF040712 187 LIDPDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAP 266

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 785039    647 DEPSEALAFPTVAEEAHASPDTTQPLAEADPEPASASAPGAEEVASPATEEGSP 700
Cdd:NF040712 267 AAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPP 320
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 145-391 3.55e-97

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 300.61  E-value: 3.55e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    225 SAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKILIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    304 LVSVGESVEEAFFYIHNLVVACEIQVRTLaSAGGPdnLVLLDPGKYKAKSRSPGTPAGEGSgsppkwqiGEQEFEALMRM 383
Cdd:PRK07044 174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAGA--------GELAWPALLRK 242

                        250
                 ....*....|
gi 785039    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 1.86e-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: 223.78  E-value: 1.86e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIV--DRGSTNLGvnqa 219
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   220 gftLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKILIQKNLG-PKSK 295
Cdd:cd00398  75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 785039   296 VLILRNHGLVSVGESVEEAFFYIHNLVVACEIQVRTLASAGG--PDNLVLLDPGKYKAK 352
Cdd:cd00398 151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 145-341 6.59e-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: 192.74  E-value: 6.59e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGstnlGVNQAGFTLH 224
Cdd:COG0235   6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039   225 SAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKILIQKNLGpKSKVLILRNH 302
Cdd:COG0235  80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 785039   303 GLVSVGESVEEAFFYIHNLVVACEIQVRTLAsAGGPDNL 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 3.36e-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: 186.98  E-value: 3.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039     147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039     227 IYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKILIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 785039     305 VSVGESVEEAFFYIHNLVVACEIQV 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 1.68e-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: 182.84  E-value: 1.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039      149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039      229 AARPDAKCIVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKI-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 785039      302 HGLVSVGESVEEAFFYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PRK06661 PRK06661
hypothetical protein; Provisional
 149-334 5.42e-44

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 158.07  E-value: 5.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    149 LAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrgSTNLGVNQAGFTLHSAIY 228
Cdd:PRK06661   7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    229 AARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGE-VAYHDYHGILVDE--EEKILIQkNLGpKSKVLILRNHGLV 305
Cdd:PRK06661  84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSLALDAdkQSSRLVN-DLK-QNYVMLLRNHGAI 161

                        170       180
                 ....*....|....*....|....*....
gi 785039    306 SVGESVEEAFFYIHNLVVACEIQVRTLAS 334
Cdd:PRK06661 162 TCGKTIHEAMFYTYHLEQACKTQCLLNST 190
PRK06208 PRK06208
class II aldolase/adducin family protein;
148-371 2.95e-40

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 148.98  E-value: 2.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    148 KLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrgsTNLGVNQAGFTLHSAI 227
Cdd:PRK06208  46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    228 YAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSLGE--VAYHDYHGILVDEEEKILIQKNLGPKsKVLILRNHGLV 305
Cdd:PRK06208 123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEdhALFDDFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 785039    306 SVGESVEEAFFYIHNLVVACEIQVrtLASAGGPdnLVLLDPGKYKAKSRSPGTPAGEGSGSPPKWQ 371
Cdd:PRK06208 202 TVGPSVDAAAWWFIALERACQTQL--LAEAAGP--PQPIDHETARHTRSQVGSEYGGWFNFQPLYQ 263
PRK06486 PRK06486
aldolase;
114-385 5.40e-26

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 107.88  E-value: 5.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    114 MA-ALNMSLGMVTPVNDLRGSDSIAYdkgeklLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEV 192
Cdd:PRK06486   1 MAhSLTTDSAPPAGNRPLLDSDAVAQ------ARVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    193 TASSLVKVNLQGDIVD-RGStnlgVNQAGFTLHSAIYAARPDAKCIVHIHTPAGAAVSAMK-CGLLPISPEALSL-GEVA 269
Cdd:PRK06486  75 TASDLLICDFDGNVLAgRGE----PEATAFFIHARIHRAIPRAKAAFHTHMPYATALSLTEgRPLTTLGQTALKFyGRTA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    270 Y-HDYHGILVDEEEKILIQKNLGPKSkVLILRNHGLVSVGESVEEAFFYIHNLVVACEIQVRTLaSAGGPdnLVLLDPGK 348
Cdd:PRK06486 151 VdEDYNGLALDAAEGDRIARAMGDAD-IVFLKNHGVMVCGPRIAEAWDDLYYLERACEVQVLAM-STGRP--LVPVDPAI 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 785039    349 YKAKSRspgtpagegsgsppKWQIGEQE-----FEALMRMLD 385
Cdd:PRK06486 227 AAAVAR--------------QMREGDREsarlhLEALRRTLD 254
PRK07490 PRK07490
hypothetical protein; Provisional
 135-334 2.26e-19

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 88.24  E-value: 2.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    135 SIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKVNlqGDIVDRGSTNL 214
Cdd:PRK07490   1 MTMALSDEEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD--ADDPSTAERPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    215 GVNQAGFTLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCG-LLPISPE-ALSLGEVAYHDYHGILVDEEEKILIQKNLGP 292
Cdd:PRK07490  79 VPDATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNtARFFNRVAVDTLYGGMALEEEGERLAGLLGD 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 785039    293 KSkVLILRNHGLVSVGESVEEAFFYIHNLVVACEIQVRTLAS 334
Cdd:PRK07490 159 KR-RLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALST 199
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 145-338 1.18e-18

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 86.23  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    145 LRCKLAAFYRLADLFGWSQLIYNHITTRvnSEQEH-FLIVPFGLLYSEVTASSLVKVNLQGDIVD-RGSTNlGVNQagft 222
Cdd:PRK07090  31 LRQKLALTCRILFDAGHDSGLAGQITAR--AEAPGtYYTQRLGLGFDEITASNLLLVDEDLNVLDgEGMPN-PANR---- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    223 LHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAY-HDYHGILVDEEEKILIQKNLGPKSKVLiLR 300
Cdd:PRK07090 104 FHSWIYRARPDVNCIIHTHPPHVAALSMLEVPLVVSHMDTCPLyDDCAFlKDWPGVPVGNEEGEIISAALGDKRAIL-LS 182

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 785039    301 NHGLVSVGESVEEAFFYIHNLVVACEIQVrtLASAGGP 338
Cdd:PRK07090 183 HHGQLVAGKSIEEACVLALLIERAARLQL--LAMAAGP 218
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 176-314 1.07e-11

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 65.03  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    176 EQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrGSTNLGVNQAGftlHSAIYAARPDAKCIVHIHTPAGAAVSA----M 251
Cdd:PRK06557  41 GTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDTAS---HLYVYRHMPDVGGVVHTHSTYATAWAArgepI 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 785039    252 KCGLLPISPEAlsLGEVAYHDYHGILVDEEEKILIQKNLGPKSKVLILRNHGLVSVGESVEEA 314
Cdd:PRK06557 117 PCVLTAMADEF--GGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
PRK08333 PRK08333
aldolase;
143-316 1.17e-11

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 64.07  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    143 KLLRCKLAAFYRLADLFGWSQLIYNHITTRVNseqEHFLIVPFGLLYSEVTASSLVKVNLQGDIVD--RGSTNlgvnqag 220
Cdd:PRK08333   2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSE------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    221 FTLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGLLP-ISPEA-LSLGEVAYHDYHGI----LVDEEEKILIQKNlgpks 294
Cdd:PRK08333  72 YRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPiITPEAeLYLKKIPILPFRPAgsveLAEQVAEAMKEYD----- 146

                        170       180
                 ....*....|....*....|..
gi 785039    295 kVLILRNHGLVSVGESVEEAFF 316
Cdd:PRK08333 147 -AVIMERHGIVTVGRSLREAFY 167
PRK08130 PRK08130
putative aldolase; Validated
 179-316 1.19e-08

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 56.04  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    179 HFLIVPFGLLYSEVTASSLVKVNLQGDIV--DRGSTNLgvnqagfTLHSAIYAARPDAKCIVHIHTPAGAAVSAM----- 251
Cdd:PRK08130  38 GWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLTALSCLggldp 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 785039    252 KCGLLPISPEAL-SLGEVAYHDYH--GilvDEEEKILIQKnLGPKSKVLILRNHGLVSVGESVEEAFF 316
Cdd:PRK08130 111 TNVLPPFTPYYVmRVGHVPLIPYYrpG---DPAIAEALAG-LAARYRAVLLANHGPVVWGSSLEAAVN 174
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
177-333 3.30e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 48.58  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    177 QEHFLIVPFGLLYSEVTASSLVKVNlqgdivDRGSTNLG-VNQAGFTLHSAIYAARPDAKCIVHIHTPAGAAVSAMKCGL 255
Cdd:PRK08087  35 QDGMLITPTGIPYEKLTESHIVFVD------GNGKHEEGkLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRPI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    256 --------------LPISPEAlSLG--EVAYHDYHGIlvdeeekiliqknlgPKSKVLILRNHGLVSVGESVEEAFFYIH 319
Cdd:PRK08087 109 paihymiaaaggnsIPCAPYA-TFGtrELSEHVALAL---------------KNRKATLLQHHGLIACEVNLEKALWLAH 172

                        170
                 ....*....|....
gi 785039    320 NLVVACEIQVRTLA 333
Cdd:PRK08087 173 EVEVLAQLYLKTLA 186
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
174-338 4.01e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 48.59  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    174 NSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVDrGSTnlgVNQAGFTLHSAIYAARPDAKCIVHIHTPAGAAVSAMKC 253
Cdd:PRK06833  34 NREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGW 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    254 GLLPISPE-ALSLGEVAYHDYHGI----LVDEEEKILIQKnlgpksKVLILRNHGLVSVGESVEEAFFYIHNLVVACEIQ 328
Cdd:PRK06833 110 ELPAVHYLiAVAGPNVRCAEYATFgtkeLAENAFEAMEDR------RAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIY 183

                        170
                 ....*....|
gi 785039    329 VRTlASAGGP 338
Cdd:PRK06833 184 YQT-KSIGEP 192
PRK08660 PRK08660
aldolase;
180-327 1.65e-04

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 43.02  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    180 FLIVPFGLLYSEVTASSLVKVNLQG-DIVDRG-STNLGVnqagftlHSAIYAaRPDAKCIVHIHTPAGAAVSAMKCGLLP 257
Cdd:PRK08660  33 LLITRTGSMLDEITEGDVIEVGIDDdGSVDPLaSSETPV-------HRAIYR-RTSAKAIVHAHPPYAVALSLLEDEIVP 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 785039    258 ISPEALS-LGE--VAYHDYHGILVDEEEKILIQKNlgpksKVLILRNHGLVSVGESVEEAFFYIHNLVVACEI 327
Cdd:PRK08660 105 LDSEGLYfLGTipVVGGDIGSGELAENVARALSEH-----KGVVVRGHGTFAIGKTLEEAYIYTSQLEHSCKV 172
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 173-327 2.64e-04

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 43.25  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    173 VNSEQEHFLIVPFGLLYSEVTASSLVKVNLQGDIVD---RGSTNLGVnqagftlHSAIYAARPDAKCIVHIHTP------ 243
Cdd:PRK12348  31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSSDTAT-------HLELYRRYPSLGGIVHTHSThatawa 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    244 -AGAAVSAMKC-------GLLPISpEALSLGEVAyHDYHgilvDEEEKILIQkNLGPKSKV----LILRNHGLVSVGESV 311
Cdd:PRK12348 104 qAGLAIPALGTthadyffGDIPCT-RGLSEEEVQ-GEYE----LNTGKVIIE-TLGNAEPLhtpgIVVYQHGPFAWGKDA 176

                        170
                 ....*....|....*.
gi 785039    312 EEAffyIHNLVVACEI 327
Cdd:PRK12348 177 HDA---VHNAVVMEEV 189
PHA03169 PHA03169
hypothetical protein; Provisional
 557-706 3.64e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.42  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    557 STTGP--NPFNTLTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPT--SRDGS 632
Cdd:PHA03169  52 TTSGPqvRAVAEQGHRQTESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSgsSPESP 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    633 GCHASKPTPP----DLSPDEPSEALAFPTVAEE------AHASPDTTQPlAEADPEPASASAPGAEEV------ASPATE 696
Cdd:PHA03169 132 ASHSPPPSPPshpgPHEPAPPESHNPSPNQQPSsflqpsHEDSPEEPEP-PTSEPEPDSPGPPQSETPtsspppQSPPDE 210

                        170
                 ....*....|
gi 785039    697 EGSPMDPGSD 706
Cdd:PHA03169 211 PGEPQSPTPQ 220
PHA03247 PHA03247
large tegument protein UL36; Provisional
 601-724 1.15e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039     601 PPDQsavPNTPPSTPVKLEGGLPQEPTSRDGSGchASKPTPPDLSPDEPSEALAFPtVAEEAHASPDTTQ-------PLA 673
Cdd:PHA03247 2701 PPPP---PPTPEPAPHALVSATPLPPGPAAARQ--ASPALPAAPAPPAVPAGPATP-GGPARPARPPTTAgppapapPAA 2774

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 785039     674 EADPEPASASAPGAEEVASPATEEGSPMDPGSDGSPGKSPSKKKKKFRTPS 724
Cdd:PHA03247 2775 PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA 2825
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 585-706 1.28e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039     585 GSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPTSRDGSGCHASKPTPPDLSPDE------PSEALAFPTV 658
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVAsdaassRQAALPLSSP 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 785039     659 AEEAHASPDTTQPLA-EADPEPASASAPGAEEVASPATEEGSPMDPGSD 706
Cdd:PHA03307  180 EETARAPSSPPAEPPpSTPPAAASPRPPRRSSPISASASSPAPAPGRSA 228
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 600-704 4.95e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    600 SPPDQSAVPNTPPSTPVKLEGGLPQEPTSRDGSGCHASKPTPPDLSPDEPSEALAFPTVAEEAHASPDTTQPLAEADPEP 679
Cdd:PRK07764 397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP 476

                         90       100
                 ....*....|....*....|....*
gi 785039    680 ASASAPGAEEVASPATEEGSPMDPG 704
Cdd:PRK07764 477 TAAPAPAPPAAPAPAAAPAAPAAPA 501
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 567-700 5.01e-03

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: 39.75  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    567 LTDRELEEYRREVERKQKGSEENLDETREQKEKSPPDQSAVPNTPPSTPVKLEGGLPQEPTSRDGSGCHASKPTPPDLSP 646
Cdd:NF040712 187 LIDPDFGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAP 266

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 785039    647 DEPSEALAFPTVAEEAHASPDTTQPLAEADPEPASASAPGAEEVASPATEEGSP 700
Cdd:NF040712 267 AAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPP 320
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
591-700 6.39e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 785039    591 DETREQKEKSPPDQSAVPNtpPSTPVKLEGGLPQEPTSRDGSGCHASKPTPPDlSPDEPSEALAFPTVAEEAHASPDTTQ 670
Cdd:PRK07003 437 DRGDDAADGDAPVPAKANA--RASADSRCDERDAQPPADSGSASAPASDAPPD-AAFEPAPRAAAPSAATPAAVPDARAP 513

                         90       100       110
                 ....*....|....*....|....*....|
gi 785039    671 PLAEADPEPASASAPgAEEVASPATEEGSP 700
Cdd:PRK07003 514 AAASREDAPAAAAPP-APEARPPTPAAAAP 542
 
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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