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Conserved domains on  [gi|446464788|ref|WP_000542642|]
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MULTISPECIES: S1C family serine protease [Bacillus]

Protein Classification

S1C family serine protease( domain architecture ID 11415729)

S1C family serine protease containing a C-terminal PDZ domain, similar to the Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins

CATH:  2.40.10.10|2.30.42.10
EC:  3.4.21.-
Gene Ontology:  GO:0006508|GO:0004252|GO:0005515
MEROPS:  S1C
PubMed:  12408815|30712672|11158544|11283303|9383148
SCOP:  4001790

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 122-406 1.38e-114

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 335.97  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 122 GSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVnKVATLGDSSKLRAGEK 201
Cdd:COG0265    1 GLGSGVIISPDG---YILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 202 AIAIGNPLGFDGSVTEGIISSKEREIPVDiDGDKRPDwqaqVIQTDAAINPGNSGGALFNQNGEIIGINSSKIAQQE-VE 280
Cdd:COG0265   77 VLAIGNPFGLGQTVTAGIVSALGRSIGSS-GGGTYDD----FIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGgSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 281 GIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAVNqLKVPKevtnGVVLGKIYPISPAEKAGLEQYDIVV 360
Cdd:COG0265  152 GIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALG-LPEPE----GVLVARVEPGSPAAKAGLRPGDVIL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446464788 361 ALDDQKVENSLQFRKYLYEkKKVGEKVEVTFYRNGQKMTKTATLAD 406
Cdd:COG0265  227 AVDGKPVTSARDLQRLLAS-LKPGDTVTLTVLRGGKELTVTVTLGE 271
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 122-406 1.38e-114

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 335.97  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 122 GSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVnKVATLGDSSKLRAGEK 201
Cdd:COG0265    1 GLGSGVIISPDG---YILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 202 AIAIGNPLGFDGSVTEGIISSKEREIPVDiDGDKRPDwqaqVIQTDAAINPGNSGGALFNQNGEIIGINSSKIAQQE-VE 280
Cdd:COG0265   77 VLAIGNPFGLGQTVTAGIVSALGRSIGSS-GGGTYDD----FIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGgSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 281 GIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAVNqLKVPKevtnGVVLGKIYPISPAEKAGLEQYDIVV 360
Cdd:COG0265  152 GIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALG-LPEPE----GVLVARVEPGSPAAKAGLRPGDVIL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446464788 361 ALDDQKVENSLQFRKYLYEkKKVGEKVEVTFYRNGQKMTKTATLAD 406
Cdd:COG0265  227 AVDGKPVTSARDLQRLLAS-LKPGDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 109-404 2.41e-88

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 274.48  E-value: 2.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  109 PFAMQPTGQEQQAGSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVNKVA 188
Cdd:TIGR02037  45 PDFPRQQREQKVRGLGSGVIISADG---YVLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVI 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  189 TLGDSSKLRAGEKAIAIGNPLGFDGSVTEGIISSKEReipVDIDGDKRPDWqaqvIQTDAAINPGNSGGALFNQNGEIIG 268
Cdd:TIGR02037 122 KLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR---SGLGIGDYENF----IQTDAAINPGNSGGPLVNLRGEVIG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  269 INSSKIAQ-QEVEGIGFAIPINIAKPVIESLEKDGVVKRPALGvgvVSLEDVQAYAVNQLKVPKevTNGVVLGKIYPISP 347
Cdd:TIGR02037 195 INTAILSPsGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLG---VTIQEVTSDLAKSLGLEK--QRGALVAQVLPGSP 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446464788  348 AEKAGLEQYDIVVALDDQKVENSLQFRKYLYEkKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:TIGR02037 270 AEKAGLKAGDVITSVNGKPISSFADLRRAIGT-LKPGKKVTLGILRKGKEKTITVTL 325
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 108-405 1.75e-83

HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous serine proteases HhoA, HhoB, and HtrA of the model cyanobacterial isolate Synechocystis sp. PCC 6803. They resemble the paralogous trio of serine proteases DegQ, DegP, and DegS of Escherichia coli.


Pssm-ID: 469406 [Multi-domain]  Cd Length: 334  Bit Score: 258.56  E-value: 1.75e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 108 DPFAMQPTGQEQQAGSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVnKV 187
Cdd:NF041521  42 SDIPPPPPQERVERGTGSGFIISSDG---IILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNL-PT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 188 ATLGDSSKLRAGEKAIAIGNPLGFDGSVTEGIISSKER---EIPVdidGDKRPDWqaqvIQTDAAINPGNSGGALFNQNG 264
Cdd:NF041521 118 VPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRsssQVGV---PDKRVDF----IQTDAAINPGNSGGPLLNARG 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 265 EIIGINSSKIaqQEVEGIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSL-----EDVQAYAVNQLKVPkeVTNGVVL 339
Cdd:NF041521 191 EVIGINTAIR--AGAQGLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLtpelkQEINSDPNSGFTVP--EDEGVLI 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446464788 340 GKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKyLYEKKKVGEKVEVTFYRNGQKMTKTATLA 405
Cdd:NF041521 267 VRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQVQQ-IVENSQVGQTLQLEVQRNGQTQTLTVRPG 331
PRK10942 PRK10942
serine endoprotease DegP;
117-411 6.94e-56

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 191.13  E-value: 6.94e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 117 QEQQAGSGSGVIYKKAgnKAYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVNKVATLGDSSKL 196
Cdd:PRK10942 106 QQKFMALGSGVIIDAD--KGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDAL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 197 RAGEKAIAIGNPLGFDGSVTEGIISSKEREipvdidGDKRPDWQaQVIQTDAAINPGNSGGALFNQNGEIIGINSSKIAQ 276
Cdd:PRK10942 184 RVGDYTVAIGNPYGLGETVTSGIVSALGRS------GLNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTAILAP 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 277 QEVE-GIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAvnqLKVpkEVTNGVVLGKIYPISPAEKAGLEQ 355
Cdd:PRK10942 257 DGGNiGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKA---MKV--DAQRGAFVSQVLPNSSAAKAGIKA 331

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446464788 356 YDIVVALDDQKVENSLQFRKYLyEKKKVGEKVEVTFYRNGQKMTKTATLADNSATK 411
Cdd:PRK10942 332 GDVITSLNGKPISSFAALRAQV-GTMPVGSKLTLGLLRDGKPVNVNVELQQSSQNQ 386
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 124-269 3.51e-31

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 115.98  E-value: 3.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  124 GSGVIYKKAGnkaYIVTNNHVVDGANKLAVK-----LSDGKKVDAKLVGKDPWLDLAVVEIDGANVN-KVATLGDSSKLR 197
Cdd:pfam13365   1 GTGFVVSSDG---LVLTNAHVVDDAEEAAVElvsvvLADGREYPATVVARDPDLDLALLRVSGDGRGlPPLPLGDSEPLV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446464788  198 AGEKAIAIGNPLGFDG-SVTEGIISSKEREIPVDIDGDkrpdwqaqVIQTDAAINPGNSGGALFNQNGEIIGI 269
Cdd:pfam13365  78 GGERVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGR--------VIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 306-404 6.04e-28

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This BsHtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 105.79  E-value: 6.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 306 RPALGVGVVSLEDVQAYAVNQLKVPKEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYeKKKVGE 385
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILY-SHKVGD 79

                         90
                 ....*....|....*....
gi 446464788 386 KVEVTFYRNGQKMTKTATL 404
Cdd:cd06781   80 TVKVTIYRDGKEKTLNIKL 98
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 326-395 6.06e-06

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 44.29  E-value: 6.06e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788   326 QLKVPKEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYeKKKVGEKVEVTFYRNG 395
Cdd:smart00228  17 SLVGGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDL-LKKAGGKVTLTVLRGG 85
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 122-406 1.38e-114

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 335.97  E-value: 1.38e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 122 GSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVnKVATLGDSSKLRAGEK 201
Cdd:COG0265    1 GLGSGVIISPDG---YILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 202 AIAIGNPLGFDGSVTEGIISSKEREIPVDiDGDKRPDwqaqVIQTDAAINPGNSGGALFNQNGEIIGINSSKIAQQE-VE 280
Cdd:COG0265   77 VLAIGNPFGLGQTVTAGIVSALGRSIGSS-GGGTYDD----FIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGgSQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 281 GIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAVNqLKVPKevtnGVVLGKIYPISPAEKAGLEQYDIVV 360
Cdd:COG0265  152 GIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELAEALG-LPEPE----GVLVARVEPGSPAAKAGLRPGDVIL 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446464788 361 ALDDQKVENSLQFRKYLYEkKKVGEKVEVTFYRNGQKMTKTATLAD 406
Cdd:COG0265  227 AVDGKPVTSARDLQRLLAS-LKPGDTVTLTVLRGGKELTVTVTLGE 271
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 109-404 2.41e-88

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 274.48  E-value: 2.41e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  109 PFAMQPTGQEQQAGSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVNKVA 188
Cdd:TIGR02037  45 PDFPRQQREQKVRGLGSGVIISADG---YVLTNNHVVDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVI 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  189 TLGDSSKLRAGEKAIAIGNPLGFDGSVTEGIISSKEReipVDIDGDKRPDWqaqvIQTDAAINPGNSGGALFNQNGEIIG 268
Cdd:TIGR02037 122 KLGDSDKLRVGDWVLAIGNPFGLGQTVTSGIVSALGR---SGLGIGDYENF----IQTDAAINPGNSGGPLVNLRGEVIG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  269 INSSKIAQ-QEVEGIGFAIPINIAKPVIESLEKDGVVKRPALGvgvVSLEDVQAYAVNQLKVPKevTNGVVLGKIYPISP 347
Cdd:TIGR02037 195 INTAILSPsGGNVGIGFAIPSNMAKNVVDQLIEGGKVKRGWLG---VTIQEVTSDLAKSLGLEK--QRGALVAQVLPGSP 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446464788  348 AEKAGLEQYDIVVALDDQKVENSLQFRKYLYEkKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:TIGR02037 270 AEKAGLKAGDVITSVNGKPISSFADLRRAIGT-LKPGKKVTLGILRKGKEKTITVTL 325
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 108-405 1.75e-83

HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous serine proteases HhoA, HhoB, and HtrA of the model cyanobacterial isolate Synechocystis sp. PCC 6803. They resemble the paralogous trio of serine proteases DegQ, DegP, and DegS of Escherichia coli.


Pssm-ID: 469406 [Multi-domain]  Cd Length: 334  Bit Score: 258.56  E-value: 1.75e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 108 DPFAMQPTGQEQQAGSGSGVIYKKAGnkaYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVnKV 187
Cdd:NF041521  42 SDIPPPPPQERVERGTGSGFIISSDG---IILTNAHVVDGADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNL-PT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 188 ATLGDSSKLRAGEKAIAIGNPLGFDGSVTEGIISSKER---EIPVdidGDKRPDWqaqvIQTDAAINPGNSGGALFNQNG 264
Cdd:NF041521 118 VPLGNSDQLQPGEWAIAIGNPLGLDNTVTLGIISATGRsssQVGV---PDKRVDF----IQTDAAINPGNSGGPLLNARG 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 265 EIIGINSSKIaqQEVEGIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSL-----EDVQAYAVNQLKVPkeVTNGVVL 339
Cdd:NF041521 191 EVIGINTAIR--AGAQGLGFAIPINTAQRIADQLIAGGKVEHPYLGIQMVTLtpelkQEINSDPNSGFTVP--EDEGVLI 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446464788 340 GKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKyLYEKKKVGEKVEVTFYRNGQKMTKTATLA 405
Cdd:NF041521 267 VRVVPNSPAARAGLRAGDVIQKINGQPVTTAEQVQQ-IVENSQVGQTLQLEVQRNGQTQTLTVRPG 331
PRK10942 PRK10942
serine endoprotease DegP;
117-411 6.94e-56

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 191.13  E-value: 6.94e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 117 QEQQAGSGSGVIYKKAgnKAYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVNKVATLGDSSKL 196
Cdd:PRK10942 106 QQKFMALGSGVIIDAD--KGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAIKMADSDAL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 197 RAGEKAIAIGNPLGFDGSVTEGIISSKEREipvdidGDKRPDWQaQVIQTDAAINPGNSGGALFNQNGEIIGINSSKIAQ 276
Cdd:PRK10942 184 RVGDYTVAIGNPYGLGETVTSGIVSALGRS------GLNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTAILAP 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 277 QEVE-GIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAvnqLKVpkEVTNGVVLGKIYPISPAEKAGLEQ 355
Cdd:PRK10942 257 DGGNiGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKA---MKV--DAQRGAFVSQVLPNSSAAKAGIKA 331

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446464788 356 YDIVVALDDQKVENSLQFRKYLyEKKKVGEKVEVTFYRNGQKMTKTATLADNSATK 411
Cdd:PRK10942 332 GDVITSLNGKPISSFAALRAQV-GTMPVGSKLTLGLLRDGKPVNVNVELQQSSQNQ 386
PRK10139 PRK10139
serine endoprotease DegQ;
114-410 2.59e-49

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 173.21  E-value: 2.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 114 PTGQEQQ-AGSGSGVIYKKAgnKAYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANVNKVATLGD 192
Cdd:PRK10139  81 PDQPAQPfEGLGSGVIIDAA--KGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIAD 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 193 SSKLRAGEKAIAIGNPLGFDGSVTEGIISSKEREiPVDIDGDKrpdwqaQVIQTDAAINPGNSGGALFNQNGEIIGINSS 272
Cdd:PRK10139 159 SDKLRVGDFAVAVGNPFGLGQTATSGIISALGRS-GLNLEGLE------NFIQTDASINRGNSGGALLNLNGELIGINTA 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 273 KIAQQEVE-GIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAVNQlkvpkEVTNGVVLGKIYPISPAEKA 351
Cdd:PRK10139 232 ILAPGGGSvGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNL-----DVQRGAFVSEVLPNSGSAKA 306

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446464788 352 GLEQYDIVVALDDQKVENSLQFRKYLYEKKKvGEKVEVTFYRNGQKMTKTATLADNSAT 410
Cdd:PRK10139 307 GVKAGDIITSLNGKPLNSFAELRSRIATTEP-GTKVKLGLLRNGKPLEVEVTLDTSTSS 364
PRK10898 PRK10898
serine endoprotease DegS;
111-410 1.19e-48

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 169.03  E-value: 1.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 111 AMQPTGQEQQAGS--GSGVIYKkagNKAYIVTNNHVVDGANKLAVKLSDGKKVDAKLVGKDPWLDLAVVEIDGANV---- 184
Cdd:PRK10898  65 SLNSTSHNQLEIRtlGSGVIMD---QRGYILTNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATNLpvip 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 185 ---NKVATLGDSsklragekAIAIGNPLGFDGSVTEGIISSKEReipVDIDGDKRPDWqaqvIQTDAAINPGNSGGALFN 261
Cdd:PRK10898 142 inpKRVPHIGDV--------VLAIGNPYNLGQTITQGIISATGR---IGLSPTGRQNF----LQTDASINHGNSGGALVN 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 262 QNGEIIGINS---SKIAQQEV-EGIGFAIPINIAKPVIESLEKDGVVKRPALGVGVVSLEDVQAYAVNQLKVPkevtnGV 337
Cdd:PRK10898 207 SLGELMGINTlsfDKSNDGETpEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQ-----GI 281

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446464788 338 VLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYEKKKvGEKVEVTFYRNGQKMTKTATLADNSAT 410
Cdd:PRK10898 282 VVNEVSPDGPAAKAGIQVNDLIISVNNKPAISALETMDQVAEIRP-GSVIPVVVMRDDKQLTLQVTIQEYPAT 353
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 124-269 3.51e-31

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 115.98  E-value: 3.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  124 GSGVIYKKAGnkaYIVTNNHVVDGANKLAVK-----LSDGKKVDAKLVGKDPWLDLAVVEIDGANVN-KVATLGDSSKLR 197
Cdd:pfam13365   1 GTGFVVSSDG---LVLTNAHVVDDAEEAAVElvsvvLADGREYPATVVARDPDLDLALLRVSGDGRGlPPLPLGDSEPLV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446464788  198 AGEKAIAIGNPLGFDG-SVTEGIISSKEREIPVDIDGDkrpdwqaqVIQTDAAINPGNSGGALFNQNGEIIGI 269
Cdd:pfam13365  78 GGERVYAVGYPLGGEKlSLSEGIVSGVDEGRDGGDDGR--------VIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 306-404 6.04e-28

circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and YyxA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis HtrA/YkdA, HtrB/YvtA and YyxA/YycK, and related domains. HtrA-type serine proteases participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. HtrA, HtrB, and YyxA have a single transmembrane domain at the N-terminus and a PDZ domain at the C-terminus. Expression of htrA and htrB genes is induced both by heat shock and by secretion stress (by a common) mechanism; yyxA is neither heat shock nor secretion stress inducible. HtrA and HtrB may have overlapping cellular functions; YyxA may have a cellular function distinct from the other two proteases or have the same function but under different conditions. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This BsHtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467622 [Multi-domain]  Cd Length: 98  Bit Score: 105.79  E-value: 6.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 306 RPALGVGVVSLEDVQAYAVNQLKVPKEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYeKKKVGE 385
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILY-SHKVGD 79

                         90
                 ....*....|....*....
gi 446464788 386 KVEVTFYRNGQKMTKTATL 404
Cdd:cd06781   80 TVKVTIYRDGKEKTLNIKL 98
Trypsin pfam00089
Trypsin;
134-295 1.61e-14

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 72.09  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  134 NKAYIVTNNHVVDGANKLAVKL-------SDGKKVDAKLV------GKDPW---LDLAVVEID-----GANVNKV--ATL 190
Cdd:pfam00089  33 SENWVLTAAHCVSGASDVKVVLgahnivlREGGEQKFDVEkiivhpNYNPDtldNDIALLKLEspvtlGDTVRPIclPDA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788  191 GDSSKLRAGEKAIAIGNP--LGFDGSVTEGIISSKEREipvDIDGDKRPDWQAQVIQTDA---AINPGNSGGALFNQNGE 265
Cdd:pfam00089 113 SSDLPVGTTCTVSGWGNTktLGPSDTLQEVTVPVVSRE---TCRSAYGGTVTDTMICAGAggkDACQGDSGGPLVCSDGE 189

                         170       180       190
                  ....*....|....*....|....*....|
gi 446464788  266 IIGINSSKIAQQEVEGIGFAIPINIAKPVI 295
Cdd:pfam00089 190 LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 307-406 3.44e-12

circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB, and HtrA and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the cyanobacterial Synechocystis sp. PCC 6803 putative serine proteases HhoA, HhoB and HtrA, and related domains. These three proteases are functionally overlapping, and are involved in a number of key physiological responses, ranging from protection against light and heat stresses to phototaxis. HhoA assembles into trimers, mediated by its protease domain and further into a hexamer by a novel interaction between the PDZ domains of opposing trimers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HhoA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467629 [Multi-domain]  Cd Length: 104  Bit Score: 62.34  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 307 PALGVGVVSLEDVQAYAVNQL-----KVPkeVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLyEKK 381
Cdd:cd10838    2 PYLGIQMTTLTPELAQQNNRNpnspvRIP--EVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIV-EQA 78

                         90       100
                 ....*....|....*....|....*
gi 446464788 382 KVGEKVEVTFYRNGQKMTKTATLAD 406
Cdd:cd10838   79 GVGEELELTVLRGDRRQTLAVKPGD 103
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 306-399 6.73e-12

permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Deg/HtrA-type serine proteases that participate in folding and degradation of aberrant proteins, and in processing and maturation of native proteins. Typically, these proteases have an N-terminal serine protease domain and at least one C-terminal PDZ domain that recognizes substrates, and in some cases activates the protease function. An exception is yeast Nma11p which has two protease domains and four PDZ domains; its N-terminal half is comprised of a protease domain, followed by two PDZ domains, and its C-terminal half has a similar domain arrangement. HtrA-type proteases include the human HtrA1-4 and MBTPS2, tricorn protease, DegS, DegP and C-terminal processing peptidase, cyanobacterial serine proteases Hhoa, HhoB, and HtrA, and yeast Nma11p. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-termini of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This Deg/HtrA family PDZ domain is a circularly permuted PDZ domain which places beta-strand A at the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467621 [Multi-domain]  Cd Length: 91  Bit Score: 61.15  E-value: 6.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 306 RPALGVgvvSLEDVQAYAVNQLKVPkeVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYEkKKVGE 385
Cdd:cd06779    1 RPYLGI---EMENISPLLAKELGLP--VNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDT-KKPGD 74

                         90
                 ....*....|....
gi 446464788 386 KVEVTFYRNGQKMT 399
Cdd:cd06779   75 SLNLTILRDGKTLT 88
PDZ_2 pfam13180
PDZ domain;
331-404 2.61e-11

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 59.21  E-value: 2.61e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446464788  331 KEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYeKKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:pfam13180   2 VDLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALY-GHKPGDTVTLQVYRDGKLLTVEVKL 74
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 332-399 4.26e-11

circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do) and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 1 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 59.03  E-value: 4.26e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446464788 332 EVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKyLYEKKKVGEKVEVTFYRNGQKMT 399
Cdd:cd10839   22 KEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADLRN-RVATTKPGTKVELKILRDGKEKT 88
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 338-411 3.26e-10

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 61.26  E-value: 3.26e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446464788 338 VLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYEKKkvGEKVEVTFYRNGQKMTKTATLADNSATK 411
Cdd:COG0750  131 VVGEVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRASP--GKPLTLTVERDGEELTLTVTPRLVEEDG 202
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 337-411 3.93e-10

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ResP (also known as Site-2 protease RseP, and YaeL), and related domains. RseP is involved in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmE) protein RseA; it cleaves the peptide bond between the critical alanine and cysteine in the transmembrane region of RseA, releasing the cytoplasmic domain of RseA with its associated sigmaE. RseP contains two tandem-arranged periplasmic PDZ domains (PDZ-N/PDZ1 and PDZ-C/PDZ2) which act to negatively regulate protease action on intact RseA; they serve as a size-exclusion filter which prevents the access of an intact RseA into the active site of RseP. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467638 [Multi-domain]  Cd Length: 83  Bit Score: 56.05  E-value: 3.93e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446464788 337 VVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYEKKkvGEKVEVTFYRNGQKMTKTATLADNSATK 411
Cdd:cd23081    1 PVVGEVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRENP--GKPLTLKIERDGKILTVTVTPELVEVEG 73
COG3975 COG3975
Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];
331-411 5.06e-10

Predicted metalloprotease, contains C-terminal PDZ domain [General function prediction only];


Pssm-ID: 443174 [Multi-domain]  Cd Length: 591  Bit Score: 61.38  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 331 KEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSlQFRKYLyEKKKVGEKVEVTFYRNGQKMTKTATLADNSAT 410
Cdd:COG3975  490 SADGGGLVVTSVLWGSPAYKAGLSAGDELLAIDGLRVTAD-NLDDAL-AAYKPGDPIELLVFRRDELRTVTVTLAAAPAD 567


                 .
gi 446464788 411 K 411
Cdd:COG3975  568 T 568
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 304-404 9.49e-09

circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana DEGP1 (also known as protease Do-like 1, chloroplastic, protein DEGRADATION OF PERIPLASMIC PROTEINS 1, DEGP PROTEASE 1 and DEG1), and related domains. DEGP1 is a serine protease that is required at high temperature and may be involved in the degradation of damaged proteins. This family also includes Arabidopsis protease DEGP8/Do-like 8 (chloroplastic), a probable serine protease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467618 [Multi-domain]  Cd Length: 102  Bit Score: 52.58  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 304 VKRPALGVGVvsLEDVQAyavNQLKVPKEVtngVVLGkIYPISPAEKAGL-----------EQYDIVVALDDQKVENSLQ 372
Cdd:cd00990    1 VVRPGLGISF--APDQVA---RQLGVRSGV---LVLD-VPPGGPAAKAGLrgtkrdefgriVLGDVIVAVDGKPVKNESD 71

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446464788 373 FRKYLyEKKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:cd00990   72 LYRAL-DEYKVGDVVTLKVLRGGTKVDLKVTL 102
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 332-404 3.53e-06

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 48.71  E-value: 3.53e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446464788 332 EVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVE--NSLQFRKYLyeKKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:COG0793   68 EEDGKVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAglTLDDAVKLL--RGKAGTKVTLTIKRPGEGEPITVTL 140
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 326-395 6.06e-06

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 44.29  E-value: 6.06e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788   326 QLKVPKEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYeKKKVGEKVEVTFYRNG 395
Cdd:smart00228  17 SLVGGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDL-LKKAGGKVTLTVLRGG 85
Peptidase_M50 pfam02163
Peptidase family M50;
337-403 7.59e-06

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 47.49  E-value: 7.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446464788  337 VVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLyeKKKVGEKVEVTFYRNGQKMTKTAT 403
Cdd:pfam02163  95 PVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEAL--AKSPGKPITLTVERGGQTLTVTIT 159
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 172-282 8.77e-05

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 43.13  E-value: 8.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 172 LDLAVVEIDGANVNKVATLG--DSSKLRAGEKAIAIGNPLGFDGSVT---EGIISskereipvdidgdkrpDWQAQVIQT 246
Cdd:COG3591   76 YDYALLRLDEPLGDTTGWLGlaFNDAPLAGEPVTIIGYPGDRPKDLSldcSGRVT----------------GVQGNRLSY 139

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446464788 247 DAAINPGNSGGALFNQN---GEIIGINSSKIAQQEVEGI 282
Cdd:COG3591  140 DCDTTGGSSGSPVLDDSdggGRVVGVHSAGGADRANTGV 178
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 335-401 1.97e-04

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 42.28  E-value: 1.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446464788 335 NGVVLG-KIYPISPAE---KAGLEQYDIVVALDDQKVENSLQFRKyLYEKKKVGEKVEVTFYRNGQKMTKT 401
Cdd:COG3031  147 DGKLVGyRVNPGRPGSlfsKLGLQPGDVITSINGQDLTDPAQALE-LLQQLRDASEVTLTVERNGQPVTLT 216
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 346-404 4.19e-04

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 39.00  E-value: 4.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446464788 346 SPAEKAGLEQYDIVVALDDQKVENslqfrKYLYE-----KKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:cd06782   25 GPAEKAGIKPGDVIVAVDGESVRG-----MSLDEvvkllRGPKGTKVKLTIRRGGEGEPRDVTL 83
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 332-399 6.52e-04

circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine proteases and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of HtrA family serine proteases including human HtrA1, HtrA2 (mitochondrial), HtrA3, and HtrA4, and related domains. These proteases are key enzymes associated with pregnancy. Their diverse biological functions include cell growth proliferation, migration and apoptosis. They are also implicated in disorders including Alzheimer's, Parkinson's, arthritis and cancer. HtrA1 (also known as high-temperature requirement A serine peptidase 1, L56, and serine protease 11) substrates include extracellular matrix proteins, proteoglycans, and insulin-like growth factor (IGF)-binding proteins. HtrA1 also inhibits signaling by members of the transforming growth factor beta (TGF-beta) family. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This HtrA-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467624 [Multi-domain]  Cd Length: 98  Bit Score: 38.63  E-value: 6.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446464788 332 EVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQfrkyLYEKKKVGEKVEVTFYRNGQKMT 399
Cdd:cd06785   28 DVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSD----VYEAVKSGSSLLVVVRRGNEDLL 91
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 342-393 6.96e-04

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 37.51  E-value: 6.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446464788  342 IYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLyeKKKVGEKVEVTFYR 393
Cdd:pfam17820   5 VVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLL--QGSAGESVTLTVRR 54
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 336-413 1.04e-03

circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Bacillus subtilis YlbL and related domains. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. Deletion of both proteases leads to accumulation of the cell division inhibitor YneA. PDZ domains usually bind in sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This YlbL family PDZ domain is a circularly permuted PDZ domain which places both beta-strands A and B at the C-terminus. Another permutation exists in the PDZ superfamily which places beta-strand A at the C-terminus.


Pssm-ID: 467637 [Multi-domain]  Cd Length: 83  Bit Score: 37.86  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446464788 336 GVVLGKIYPISPAeKAGLEQYDIVVALDDQKVENSLQFRKYLYEkKKVGEKVEVTFYRNGQKMTKTATLADNSATKNQ 413
Cdd:cd23080    1 GVYVLSVVENMPA-KGILEAGDKITAIDGQNFQSSEKLIDYISS-KKAGDKVKVKYERDEKEKEAELKLKQFPDEKNR 76
cpPDZ_DegS cd06777
circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density ...
 334-404 1.33e-03

circularly permuted PDZ domain of DegS serine endoprotease; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Escherichia coli DegS and related domains. DegS (also known as Site-1 protease DegS, S1P protease DegS, and Site-1-type intramembrane protease) participates in the activation of the sigma(E) extracytoplasmic stress response. Initially, there is an accumulation of misfolded membrane proteins (OMPs) in the periplasm which bind by their YXF motif to the DegS PDZ domain, activating DegS-catalyzed cleavage of the RseA periplasmic domain and making RseA a substrate for cleavage by another membrane protease RseP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegS family PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467620 [Multi-domain]  Cd Length: 93  Bit Score: 37.76  E-value: 1.33e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446464788 334 TNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKyLYEKKKVGEKVEVTFYRNGQKMTKTATL 404
Cdd:cd06777   24 LQGALVKGVSPDSPAAKAGIQVGDIILQFDNKPVISVLELMD-LVAEIRPGTVIPVVVLRDGKQLTLEVTI 93
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 330-383 1.46e-03

circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine endoprotease DegP and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Escherichia coli DegP (also known as heat shock protein DegP and Protease Do), and related domains. DegP belongs to the HtrA family of housekeeping proteases. It acts as a protease, degrading transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions, and as a molecular chaperone at low temperatures. DegP has two PDZ domains in addition to the protease domain; its PDZ1 domain is responsible for the identifying the distinct substrate sequences that affect degradation (degron) of the substrate sequence, and its PDZ2 domain is responsible for the combining with other DegP monomers to form a stable oligomer structure. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This DegP family PDZ domain 2 is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467631 [Multi-domain]  Cd Length: 83  Bit Score: 37.22  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446464788 330 PKEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYEKKKV 383
Cdd:cd23084   13 DEDGGKGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKSKPSA 66
PDZ_RGS3-like cd06711
PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 ...
 337-370 2.41e-03

PDZ domain of regulator of G-protein signaling 3 (RGS3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS3, and related domains. RGS3 down-regulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. It downregulates G-protein-mediated release of inositol phosphates and activation of MAP kinases. In Eph/ephrin signaling, RGS3 binds via its PDZ domain to the cytoplasmic C terminus of Eph receptor tyrosine kinase EphB. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467195 [Multi-domain]  Cd Length: 77  Bit Score: 36.60  E-value: 2.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446464788 337 VVLGKIYPISPAEKAGLEQYDIVVALDDQKVENS 370
Cdd:cd06711   22 VRVQAVDPGGPAEQAGLQQGDTVLQINGQPVERS 55
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 306-390 4.22e-03

circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Arabidopsis thaliana putative protease DEGP14 and related domains. DEGP14 is a putative protease belonging to the HtrA family of housekeeping proteases. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This AtDEGP14-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467632 [Multi-domain]  Cd Length: 101  Bit Score: 36.67  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446464788 306 RPALGVGVVSLEDVQayaVNQLK-----VPkEVTNGVVLGKIYPISPAEKAGLEQYDIVVALDDQKVENSLQFRKYLYEK 380
Cdd:cd23085    1 RPWLGMKMLELNEHI---IAQLKerdpmFP-DVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALGDK 76

                         90
                 ....*....|....*...
gi 446464788 381 --------KKVGEKVEVT 390
Cdd:cd23085   77 vgkpfkvvVKRANKVQVT 94
 
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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