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Conserved domains on  [gi|301802901|emb|CBW35682|]
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serine protease [Streptococcus pneumoniae INV200]

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 ...
 101-384 1.97e-110

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: 324.41  E-value: 1.97e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 101 SEGSGVIYkknDKEAYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVtTVAEFGDSSKLTVGET 180
Cdd:COG0265    1 GLGSGVII---SPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 181 AIAIGSPLGseYANTVTQGIVSSLNRNVSLKSEDGQaisTKAIQTDTAINPGNSGGPLINIQGQVIGITSSKIATNGGts 260
Cdd:COG0265   77 VLAIGNPFG--LGQTVTAGIVSALGRSIGSSGGGTY---DDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGG-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 261 VEGLGFAIPANDAINIIEQLEKNGKVTRPALGIQMVNLSNVSTsdiRRLNIPsnVTSGVVVRSVQSNMPA-NGHLEKYDV 339
Cdd:COG0265  150 SQGIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELA---EALGLP--EPEGVLVARVEPGSPAaKAGLRPGDV 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 301802901 340 ITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:COG0265  225 ILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTL 269
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 101-384 1.97e-110

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: 324.41  E-value: 1.97e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 101 SEGSGVIYkknDKEAYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVtTVAEFGDSSKLTVGET 180
Cdd:COG0265    1 GLGSGVII---SPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 181 AIAIGSPLGseYANTVTQGIVSSLNRNVSLKSEDGQaisTKAIQTDTAINPGNSGGPLINIQGQVIGITSSKIATNGGts 260
Cdd:COG0265   77 VLAIGNPFG--LGQTVTAGIVSALGRSIGSSGGGTY---DDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGG-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 261 VEGLGFAIPANDAINIIEQLEKNGKVTRPALGIQMVNLSNVSTsdiRRLNIPsnVTSGVVVRSVQSNMPA-NGHLEKYDV 339
Cdd:COG0265  150 SQGIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELA---EALGLP--EPEGVLVARVEPGSPAaKAGLRPGDV 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 301802901 340 ITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:COG0265  225 ILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTL 269
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 59-390 7.22e-86

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: 267.17  E-value: 7.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901   59 NSTTQAVNKVKDAVVSV-ITYSANRQNSVFGNDD--------------TDTDSQRISSEGSGVIYkknDKEAYIVTNNHV 123
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNIsVEGTVKRRNRPPALPPffrqffgddmpdfpRQQREQKVRGLGSGVII---SADGYVLTNNHV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  124 INGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTTVAEFGDSSKLTVGETAIAIGSPLGseYANTVTQGIVSS 203
Cdd:TIGR02037  78 VDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFG--LGQTVTSGIVSA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  204 LNRNVSlksedGQAISTKAIQTDTAINPGNSGGPLINIQGQVIGITSSkIATNGGTSVeGLGFAIPANDAINIIEQLEKN 283
Cdd:TIGR02037 156 LGRSGL-----GIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTA-ILSPSGGNV-GIGFAIPSNMAKNVVDQLIEG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  284 GKVTRPALGIQMVNLsnvsTSDIRR-LNIPSnvTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNH 361
Cdd:TIGR02037 229 GKVKRGWLGVTIQEV----TSDLAKsLGLEK--QRGALVAQVLPGSPAeKAGLKAGDVITSVNGKPISSFADLRRAIGTL 302

                         330       340
                  ....*....|....*....|....*....
gi 301802901  362 SIGDTIKITYYRNGKEETTSIKLNKSSGD 390
Cdd:TIGR02037 303 KPGKKVTLGILRKGKEKTITVTLGASPEE 331
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 62-383 1.51e-80

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: 250.47  E-value: 1.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  62 TQAVNKVKDAVV-----SVITYSAN--------RQnsVFGNDDTDTDSQ--RISSEGSGVIYKKNDKeayIVTNNHVING 126
Cdd:NF041521   4 AAAVEKVGPAVVridaeRTVVTQVPpffndpffRR--FFGSDIPPPPPQerVERGTGSGFIISSDGI---ILTNAHVVDG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 127 ASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTTVaEFGDSSKLTVGETAIAIGSPLGSEyaNTVTQGIVSSLNR 206
Cdd:NF041521  79 ADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLPTV-PLGNSDQLQPGEWAIAIGNPLGLD--NTVTLGIISATGR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 207 NVSlksEDGqaISTKA---IQTDTAINPGNSGGPLINIQGQVIGITSSKIAtnggtSVEGLGFAIPANDAINIIEQLEKN 283
Cdd:NF041521 156 SSS---QVG--VPDKRvdfIQTDAAINPGNSGGPLLNARGEVIGINTAIRA-----GAQGLGFAIPINTAQRIADQLIAG 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 284 GKVTRPALGIQMVNLsnvsTSDIRR-------LNIPSNVTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQ 355
Cdd:NF041521 226 GKVEHPYLGIQMVTL----TPELKQeinsdpnSGFTVPEDEGVLIVRVVPNSPAaRAGLRAGDVIQKINGQPVTTAEQVQ 301

                        330       340
                 ....*....|....*....|....*...
gi 301802901 356 SALYNHSIGDTIKITYYRNGKEETTSIK 383
Cdd:NF041521 302 QIVENSQVGQTLQLEVQRNGQTQTLTVR 329
PRK10942 PRK10942
serine endoprotease DegP;
88-388 1.86e-49

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 173.41  E-value: 1.86e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  88 GNDDTDTDSQRISSEGSGVIYkkNDKEAYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTTVA 167
Cdd:PRK10942  98 QGGNGGGQQQKFMALGSGVII--DADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAI 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 168 EFGDSSKLTVGETAIAIGSPLGseYANTVTQGIVSSLNRNvSLKSEDGQaistKAIQTDTAINPGNSGGPLINIQGQVIG 247
Cdd:PRK10942 176 KMADSDALRVGDYTVAIGNPYG--LGETVTSGIVSALGRS-GLNVENYE----NFIQTDAAINRGNSGGALVNLNGELIG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 248 ITSSKIATNGGTSveGLGFAIPANDAINIIEQLEKNGKVTRPALGIQMVNLsnvsTSDIRRLnIPSNVTSGVVVRSVQSN 327
Cdd:PRK10942 249 INTAILAPDGGNI--GIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTEL----NSELAKA-MKVDAQRGAFVSQVLPN 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301802901 328 MPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKLNKSS 388
Cdd:PRK10942 322 SSAaKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVELQQSS 383
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 288-384 1.47e-39

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: 136.23  E-value: 1.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 288 RPALGIQMVNLSNVSTSDIRRLNIPSNVTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDT 366
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAeKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDT 80

                         90
                 ....*....|....*...
gi 301802901 367 IKITYYRNGKEETTSIKL 384
Cdd:cd06781   81 VKVTIYRDGKEKTLNIKL 98
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 103-248 8.04e-29

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 109.43  E-value: 8.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  103 GSGVIYkknDKEAYIVTNNHVINGA-----SKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVT-TVAEFGDSSKLT 176
Cdd:pfam13365   1 GTGFVV---SSDGLVLTNAHVVDDAeeaavELVSVVLADGREYPATVVARDPDLDLALLRVSGDGRGlPPLPLGDSEPLV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301802901  177 VGETAIAIGSPLGSEyANTVTQGIVSSLNRNVSLKSEDgqaistKAIQTDTAINPGNSGGPLINIQGQVIGI 248
Cdd:pfam13365  78 GGERVYAVGYPLGGE-KLSLSEGIVSGVDEGRDGGDDG------RVIQTDAALSPGSSGGPVFDADGRVVGI 142
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 100-289 7.28e-12

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 66.36  E-value: 7.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 100 SSEGSGVIYKKNdkeaYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTtVAEFGDSSKLTvGE 179
Cdd:NF033740 210 ALEGSGFVVAPD----RVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVPGLGLP-PLPFADEPAET-GD 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 180 TAIAIGSPLGSEYanTVTQGIVsslnRNVS-LKSED--GQAISTKAIQTDTA-INPGNSGGPLINIQGQVIGITSSKIAT 255
Cdd:NF033740 284 DAIVLGYPEGGPF--TATPARV----RERIaLSGPDiyGSGTVTREVYTLRGtVRPGNSGGPLLDPDGRVLGVVFAAAVD 357

                        170       180       190
                 ....*....|....*....|....*....|....
gi 301802901 256 NGGTsveglGFAIPANDainIIEQLEKNGKVTRP 289
Cdd:NF033740 358 DSDT-----GYALTADE---VRPDLAAAAALTTP 383
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 101-384 1.97e-110

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: 324.41  E-value: 1.97e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 101 SEGSGVIYkknDKEAYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVtTVAEFGDSSKLTVGET 180
Cdd:COG0265    1 GLGSGVII---SPDGYILTNNHVVEGADEITVTLADGREYPAKVVGRDPLTDLAVLKIDAKDL-PAAPLGDSDKLRVGDW 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 181 AIAIGSPLGseYANTVTQGIVSSLNRNVSLKSEDGQaisTKAIQTDTAINPGNSGGPLINIQGQVIGITSSKIATNGGts 260
Cdd:COG0265   77 VLAIGNPFG--LGQTVTAGIVSALGRSIGSSGGGTY---DDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISRSGG-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 261 VEGLGFAIPANDAINIIEQLEKNGKVTRPALGIQMVNLSNVSTsdiRRLNIPsnVTSGVVVRSVQSNMPA-NGHLEKYDV 339
Cdd:COG0265  150 SQGIGFAIPINLAKRVVEQLIETGRVRRGWLGVTIQPVTPELA---EALGLP--EPEGVLVARVEPGSPAaKAGLRPGDV 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 301802901 340 ITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:COG0265  225 ILAVDGKPVTSARDLQRLLASLKPGDTVTLTVLRGGKELTVTVTL 269
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 59-390 7.22e-86

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: 267.17  E-value: 7.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901   59 NSTTQAVNKVKDAVVSV-ITYSANRQNSVFGNDD--------------TDTDSQRISSEGSGVIYkknDKEAYIVTNNHV 123
Cdd:TIGR02037   1 PSFAPLVEKVAPAVVNIsVEGTVKRRNRPPALPPffrqffgddmpdfpRQQREQKVRGLGSGVII---SADGYVLTNNHV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  124 INGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTTVAEFGDSSKLTVGETAIAIGSPLGseYANTVTQGIVSS 203
Cdd:TIGR02037  78 VDGADEITVTLSDGREFKAKLVGKDPRTDIAVLKIDAKKNLPVIKLGDSDKLRVGDWVLAIGNPFG--LGQTVTSGIVSA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  204 LNRNVSlksedGQAISTKAIQTDTAINPGNSGGPLINIQGQVIGITSSkIATNGGTSVeGLGFAIPANDAINIIEQLEKN 283
Cdd:TIGR02037 156 LGRSGL-----GIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGINTA-ILSPSGGNV-GIGFAIPSNMAKNVVDQLIEG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  284 GKVTRPALGIQMVNLsnvsTSDIRR-LNIPSnvTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNH 361
Cdd:TIGR02037 229 GKVKRGWLGVTIQEV----TSDLAKsLGLEK--QRGALVAQVLPGSPAeKAGLKAGDVITSVNGKPISSFADLRRAIGTL 302

                         330       340
                  ....*....|....*....|....*....
gi 301802901  362 SIGDTIKITYYRNGKEETTSIKLNKSSGD 390
Cdd:TIGR02037 303 KPGKKVTLGILRKGKEKTITVTLGASPEE 331
HhoA_HhoB_HtrA NF041521
HhoA/HhoB/HtrA family serine endopeptidase; Members of this family include the paralogous ...
 62-383 1.51e-80

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: 250.47  E-value: 1.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  62 TQAVNKVKDAVV-----SVITYSAN--------RQnsVFGNDDTDTDSQ--RISSEGSGVIYKKNDKeayIVTNNHVING 126
Cdd:NF041521   4 AAAVEKVGPAVVridaeRTVVTQVPpffndpffRR--FFGSDIPPPPPQerVERGTGSGFIISSDGI---ILTNAHVVDG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 127 ASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTTVaEFGDSSKLTVGETAIAIGSPLGSEyaNTVTQGIVSSLNR 206
Cdd:NF041521  79 ADTVTVTLKDGRTFEGKVLGTDPVTDVAVVKIEAKNLPTV-PLGNSDQLQPGEWAIAIGNPLGLD--NTVTLGIISATGR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 207 NVSlksEDGqaISTKA---IQTDTAINPGNSGGPLINIQGQVIGITSSKIAtnggtSVEGLGFAIPANDAINIIEQLEKN 283
Cdd:NF041521 156 SSS---QVG--VPDKRvdfIQTDAAINPGNSGGPLLNARGEVIGINTAIRA-----GAQGLGFAIPINTAQRIADQLIAG 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 284 GKVTRPALGIQMVNLsnvsTSDIRR-------LNIPSNVTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQ 355
Cdd:NF041521 226 GKVEHPYLGIQMVTL----TPELKQeinsdpnSGFTVPEDEGVLIVRVVPNSPAaRAGLRAGDVIQKINGQPVTTAEQVQ 301

                        330       340
                 ....*....|....*....|....*...
gi 301802901 356 SALYNHSIGDTIKITYYRNGKEETTSIK 383
Cdd:NF041521 302 QIVENSQVGQTLQLEVQRNGQTQTLTVR 329
PRK10942 PRK10942
serine endoprotease DegP;
88-388 1.86e-49

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 173.41  E-value: 1.86e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  88 GNDDTDTDSQRISSEGSGVIYkkNDKEAYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTTVA 167
Cdd:PRK10942  98 QGGNGGGQQQKFMALGSGVII--DADKGYVVTNNHVVDNATKIKVQLSDGRKFDAKVVGKDPRSDIALIQLQNPKNLTAI 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 168 EFGDSSKLTVGETAIAIGSPLGseYANTVTQGIVSSLNRNvSLKSEDGQaistKAIQTDTAINPGNSGGPLINIQGQVIG 247
Cdd:PRK10942 176 KMADSDALRVGDYTVAIGNPYG--LGETVTSGIVSALGRS-GLNVENYE----NFIQTDAAINRGNSGGALVNLNGELIG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 248 ITSSKIATNGGTSveGLGFAIPANDAINIIEQLEKNGKVTRPALGIQMVNLsnvsTSDIRRLnIPSNVTSGVVVRSVQSN 327
Cdd:PRK10942 249 INTAILAPDGGNI--GIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTEL----NSELAKA-MKVDAQRGAFVSQVLPN 321

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301802901 328 MPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKLNKSS 388
Cdd:PRK10942 322 SSAaKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKPVNVNVELQQSS 383
PRK10139 PRK10139
serine endoprotease DegQ;
67-388 5.09e-49

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 172.05  E-value: 5.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  67 KVKDAVVSV-ITYSANRQNSV-------FGNDDTDTDSQRISSEGSGVIYkkNDKEAYIVTNNHVINGASKVDIRLSDGT 138
Cdd:PRK10139  48 KVLPAVVSVrVEGTASQGQKIpeefkkfFGDDLPDQPAQPFEGLGSGVII--DAAKGYVLTNNHVINQAQKISIQLNDGR 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 139 KVPGEIVGADTFSDIAVVKISSEKVTTVAEFGDSSKLTVGETAIAIGSPLGseYANTVTQGIVSSLNRNvSLKSEDGQAI 218
Cdd:PRK10139 126 EFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFG--LGQTATSGIISALGRS-GLNLEGLENF 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 219 stkaIQTDTAINPGNSGGPLINIQGQVIGITSSKIATNGGTSveGLGFAIPANDAINIIEQLEKNGKVTRPALGIQMVNL 298
Cdd:PRK10139 203 ----IQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSV--GIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEM 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 299 SnvstSDI-RRLNIpsNVTSGVVVRSVQSNM-PANGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGK 376
Cdd:PRK10139 277 S----ADIaKAFNL--DVQRGAFVSEVLPNSgSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGK 350

                        330
                 ....*....|..
gi 301802901 377 EETTSIKLNKSS 388
Cdd:PRK10139 351 PLEVEVTLDTST 362
PRK10898 PRK10898
serine endoprotease DegS;
60-379 5.09e-43

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 153.62  E-value: 5.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  60 STTQAVNKVKDAVVSVITYSANRQNsvfgnddtdtDSQR-ISSEGSGVIYkknDKEAYIVTNNHVINGASKVDIRLSDGT 138
Cdd:PRK10898  46 SYNQAVRRAAPAVVNVYNRSLNSTS----------HNQLeIRTLGSGVIM---DQRGYILTNKHVINDADQIIVALQDGR 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 139 KVPGEIVGADTFSDIAVVKISSEKVTTVAEfgDSSKLT-VGETAIAIGSP--LGseyaNTVTQGIVSSLNRnVSLKSEDG 215
Cdd:PRK10898 113 VFEALLVGSDSLTDLAVLKINATNLPVIPI--NPKRVPhIGDVVLAIGNPynLG----QTITQGIISATGR-IGLSPTGR 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 216 QAIstkaIQTDTAINPGNSGGPLINIQGQVIGI-TSSKIATNGGTSVEGLGFAIPANDAINIIEQLEKNGKVTRPALGIQ 294
Cdd:PRK10898 186 QNF----LQTDASINHGNSGGALVNSLGELMGInTLSFDKSNDGETPEGIGFAIPTQLATKIMDKLIRDGRVIRGYIGIG 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 295 MVNLSNVSTSD--IRRLnipsnvtSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITY 371
Cdd:PRK10898 262 GREIAPLHAQGggIDQL-------QGIVVNEVSPDGPAaKAGIQVNDLIISVNNKPAISALETMDQVAEIRPGSVIPVVV 334


                 ....*...
gi 301802901 372 YRNGKEET 379
Cdd:PRK10898 335 MRDDKQLT 342
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 288-384 1.47e-39

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: 136.23  E-value: 1.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 288 RPALGIQMVNLSNVSTSDIRRLNIPSNVTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDT 366
Cdd:cd06781    1 RPSLGISMVDLSDVPEYEQQSLKLPSNVNKGVYVAQVQSNSPAeKAGLKKGDVITKLDGKKVESSSDLRQILYSHKVGDT 80

                         90
                 ....*....|....*...
gi 301802901 367 IKITYYRNGKEETTSIKL 384
Cdd:cd06781   81 VKVTIYRDGKEKTLNIKL 98
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 103-248 8.04e-29

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 109.43  E-value: 8.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  103 GSGVIYkknDKEAYIVTNNHVINGA-----SKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVT-TVAEFGDSSKLT 176
Cdd:pfam13365   1 GTGFVV---SSDGLVLTNAHVVDDAeeaavELVSVVLADGREYPATVVARDPDLDLALLRVSGDGRGlPPLPLGDSEPLV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301802901  177 VGETAIAIGSPLGSEyANTVTQGIVSSLNRNVSLKSEDgqaistKAIQTDTAINPGNSGGPLINIQGQVIGI 248
Cdd:pfam13365  78 GGERVYAVGYPLGGE-KLSLSEGIVSGVDEGRDGGDDG------RVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 288-382 4.42e-21

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: 86.96  E-value: 4.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 288 RPALGIQMVNLSNVSTSDIrrlniPSNVTSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDT 366
Cdd:cd06779    1 RPYLGIEMENISPLLAKEL-----GLPVNRGVLVAEVIPGSPAaKAGLKEGDVILSVNGKPVTSFNDLRAALDTKKPGDS 75

                         90
                 ....*....|....*.
gi 301802901 367 IKITYYRNGKEETTSI 382
Cdd:cd06779   76 LNLTILRDGKTLTVTV 91
PDZ_2 pfam13180
PDZ domain;
313-384 2.23e-20

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 84.25  E-value: 2.23e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301802901  313 SNVTSGVVVRSVQSNMPANGH-LEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:pfam13180   2 VDLEGGVVVVSVKSSGPAAKAgLKAGDVILSIDGRKINDLTDLESALYGHKPGDTVTLQVYRDGKLLTVEVKL 74
SdrC COG3480
Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];
307-390 7.74e-19

Predicted secreted protein YlbL, contains PDZ domain [Signal transduction mechanisms];


Pssm-ID: 442703 [Multi-domain]  Cd Length: 344  Bit Score: 86.79  E-value: 7.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 307 RRLNIPsnVTSGVVVRSVQSNMPANGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKLNK 386
Cdd:COG3480  130 RAAGYP--VTEGVYVASVLEGSPADGVLQPGDVITAVDGKPVTTAEDLRDALAAKKPGDTVTLTVTRDGKEKTVTVTLVK 207


                 ....
gi 301802901 387 SSGD 390
Cdd:COG3480  208 LPDD 211
Trypsin pfam00089
Trypsin;
105-277 3.82e-15

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 74.02  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  105 GVIYKKNdkeaYIVTNNHVINGASKVDIRL-------SDGTK--------VPGEIVGADTFS-DIAVVKIS-----SEKV 163
Cdd:pfam00089  29 GSLISEN----WVLTAAHCVSGASDVKVVLgahnivlREGGEqkfdvekiIVHPNYNPDTLDnDIALLKLEspvtlGDTV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901  164 TTVAEFGDSSKLTVGETAIAIGSPLGSE--YANTVTQGIVSSLNRNVSlKSEDGQAISTKAIQTDT---AINPGNSGGPL 238
Cdd:pfam00089 105 RPICLPDASSDLPVGTTCTVSGWGNTKTlgPSDTLQEVTVPVVSRETC-RSAYGGTVTDTMICAGAggkDACQGDSGGPL 183

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 301802901  239 INIQGQVIGITSSKIATNGGtsvEGLGFAIPANDAINII 277
Cdd:pfam00089 184 VCSDGELIGIVSWGYGCASG---NYPGVYTPVSSYLDWI 219
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 289-383 6.33e-13

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: 64.65  E-value: 6.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 289 PALGIQMVNLSNVSTSDIRRlNIPSNV----TSGVVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHSI 363
Cdd:cd10838    2 PYLGIQMTTLTPELAQQNNR-NPNSPVripeVDGVLIMQVLPNSPAaRAGLRRGDVIQAVDGQPVTTADDVQRIVEQAGV 80

                         90       100
                 ....*....|....*....|
gi 301802901 364 GDTIKITYYRNGKEETTSIK 383
Cdd:cd10838   81 GEELELTVLRGDRRQTLAVK 100
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 286-384 5.34e-12

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: 61.82  E-value: 5.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 286 VTRPALGIQMVnlsnvSTSDIRRLNIPSnvtsGVVVRSVQSNMPA------------NGHLEKYDVITKVDDKEIASSTD 353
Cdd:cd00990    1 VVRPGLGISFA-----PDQVARQLGVRS----GVLVLDVPPGGPAakaglrgtkrdeFGRIVLGDVIVAVDGKPVKNESD 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 301802901 354 LQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:cd00990   72 LYRALDEYKVGDVVTLKVLRGGTKVDLKVTL 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 100-289 7.28e-12

MarP family serine protease; The founding member of this family of membrane-spanning serine proteases, which is restricted to Actinobacteria, is the acid resistance periplasmic serine protease MarP of Mycobacterium tuberculosis. Recent work shows that MarP is required to cleave and activate the peptidoglycan hydrolase RipA, and loss of RipA activity creates a defect in progeny separation during cell division. Therefore, the requirement for MarP in order to survive acidic conditions may be a consequence of peptidoglycan hydrolysis requirements, explaining why MarP family members are distributed more broadly in the Actinobacteria than the subset of species capable of surviving intracellularly as pathogens.


Pssm-ID: 468161 [Multi-domain]  Cd Length: 390  Bit Score: 66.36  E-value: 7.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 100 SSEGSGVIYKKNdkeaYIVTNNHVINGASKVDIRLSDGTKVPGEIVGADTFSDIAVVKISSEKVTtVAEFGDSSKLTvGE 179
Cdd:NF033740 210 ALEGSGFVVAPD----RVMTNAHVVAGTDEVTVETVGGGTLDARVVYYDPDRDIAVLAVPGLGLP-PLPFADEPAET-GD 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 180 TAIAIGSPLGSEYanTVTQGIVsslnRNVS-LKSED--GQAISTKAIQTDTA-INPGNSGGPLINIQGQVIGITSSKIAT 255
Cdd:NF033740 284 DAIVLGYPEGGPF--TATPARV----RERIaLSGPDiyGSGTVTREVYTLRGtVRPGNSGGPLLDPDGRVLGVVFAAAVD 357

                        170       180       190
                 ....*....|....*....|....*....|....
gi 301802901 256 NGGTsveglGFAIPANDainIIEQLEKNGKVTRP 289
Cdd:NF033740 358 DSDT-----GYALTADE---VRPDLAAAAALTTP 383
cpPDZ_BsYlbL-like cd23080
circularly permuted PDZ domain of Bacillus subtilis YlbL and related domains; Permuted PDZ ...
 318-384 2.87e-11

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: 59.05  E-value: 2.87e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301802901 318 GVVVRSVQSNMPANGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:cd23080    1 GVYVLSVVENMPAKGILEAGDKITAIDGQNFQSSEKLIDYISSKKAGDKVKVKYERDEKEKEAELKL 67
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 314-382 1.08e-09

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: 54.80  E-value: 1.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 314 NVTSGVVVRSVQSNMPAN-GHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSI 382
Cdd:cd10839   22 KEPKGALVAQVLPDSPAAkAGLKAGDVILSLNGKPITSSADLRNRVATTKPGTKVELKILRDGKEKTLTV 91
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 288-380 1.00e-06

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: 46.69  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 288 RPALGIQMVNLSNVSTSDI--RRLNIPsNVTSGVVVRSVQSNMPAN-GHLEKYDVITKVDDKEIASSTDLQSALYNHsIG 364
Cdd:cd23085    1 RPWLGMKMLELNEHIIAQLkeRDPMFP-DVKAGVLVPQVIPGSPAErAGLRPGDVIVEFDGKPVDSTKQIIDALGDK-VG 78

                         90
                 ....*....|....*.
gi 301802901 365 DTIKITYYRNGKEETT 380
Cdd:cd23085   79 KPFKVVVKRANKVQVT 94
cpPDZ_RseP_YlbL-like cd10824
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), ...
 319-384 1.44e-06

circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP), Bacillus subtilis YlbL protease, 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), Bacillus subtilis YlbL, and related domains, including archaeal and chloroplast PDZ domains. RseP participates in the regulation of an extracytoplasmic stress response through the cleavage of membrane-spanning anti-stress-response transcription factor (anti-sigmaE) protein RseA. YlbL is an S16 protease which participates with another unrelated S41 protease (CtpA) in a dual protease mechanism that promotes DNA damage checkpoint recovery. 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 beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This RseP-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: 467636 [Multi-domain]  Cd Length: 82  Bit Score: 45.64  E-value: 1.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301802901 319 VVVRSVQSNMPANGHLEKYDVITKVDDKEIASSTDLQSALYNHSIGDTIKITYYRNGKEETTSIKL 384
Cdd:cd10824    1 VVVLSVKPNSPAAKALHAGDLITEIDGQPTKSWQTFIDYIHDKKVGESVKITYKHGNKNEEASLKL 66
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 116-261 1.71e-05

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 45.05  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 116 YIVTNNHVI----NGASKVDIRLSDG--------------TKVPGEIVGADTFSDIAVVKISSEKVTTVAEFG--DSSKL 175
Cdd:COG3591   23 LVLTAGHCVydgaGGGWATNIVFVPGynggpygtatatrfRVPPGWVASGDAGYDYALLRLDEPLGDTTGWLGlaFNDAP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 176 TVGETAIAIGSPLGSEYANTVTQ-GIVSSLNRNVslksedgqaistkaIQTDTAINPGNSGGPLINI---QGQVIGITSS 251
Cdd:COG3591  103 LAGEPVTIIGYPGDRPKDLSLDCsGRVTGVQGNR--------------LSYDCDTTGGSSGSPVLDDsdgGGRVVGVHSA 168

                        170
                 ....*....|
gi 301802901 252 KIATNGGTSV 261
Cdd:COG3591  169 GGADRANTGV 178
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 319-387 2.36e-05

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: 42.18  E-value: 2.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 319 VVVRSVQSNMPA-NGHLEKYDVITKVDDKEIASSTDLQSALYNHsIGDTIKITYYRNGKEETTSIKLNKS 387
Cdd:cd23081    1 PVVGEVVANSPAaEAGLKPGDRILKIDGQKVRTWEDIVRIVREN-PGKPLTLKIERDGKILTVTVTPELV 69
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 109-275 5.57e-05

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 43.45  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 109 KKNDKEAYIVTNNHVINGASKVDIRLSDGTKVpGEIVGAD-TFSDIAVVKISSEKVTTVAEFGDSSKLTV---GETAIAI 184
Cdd:cd21112   22 TDGSGTPYFLTAGHCGNGGGTVYADGALGVPI-GTVVASSfPGNDYALVRVTNPGWTPPPEVRTYGGGTVpitGSAEPVV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 185 GSPL---GSeyaNT-VTQGIVSSLNRNVSLksedGQAISTKAIQTDTAINPGNSGGPLINiQGQVIGITSSkiATNGGTS 260
Cdd:cd21112  101 GAPVcksGR---TTgWTCGTVTAVNVTVNY----PGGTVTGLTRTNACAEPGDSGGPVFS-GTQALGITSG--GSGNCGS 170

                        170
                 ....*....|....*
gi 301802901 261 VEGLGFAIPANDAIN 275
Cdd:cd21112  171 GGGTSYFQPVNPVLS 185
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 291-378 6.43e-05

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: 41.33  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301802901 291 LGIQMVNLsnvsTSDI------RRLNIPsNVTSGVVVRSVQSNMPAN-GHLEKYDVITKVDDKEIASSTDLQSALYNhsi 363
Cdd:cd06785    4 IGIRMLTL----TPSLleelkqRNPDFP-DVSSGVYVHKVIPGSPAQrAGLKDGDVIISINGKPVKSSSDVYEAVKS--- 75

                         90
                 ....*....|....*
gi 301802901 364 GDTIKITYYRnGKEE 378
Cdd:cd06785   76 GSSLLVVVRR-GNED 89
cpPDZ1_ScNma111-like cd06786
circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine ...
 316-383 7.55e-04

circularly permuted first PDZ domain (PDZ1) of Saccharomyces cerevisiae pro-apoptotic serine protease Nma111p and related domains; First PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the HtrA-type protease Saccharomyces cerevisiae Nma111p (also known as Ynm3p), and related domains. Nma111p is a nuclear serine protease which mediates apoptosis through proteolysis of the apoptotic inhibitor Bir1p. Nma111p is composed of 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. 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 ScNma111-like PDZ1 domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation places both beta-strands A and B on the C-terminus.


Pssm-ID: 467625 [Multi-domain]  Cd Length: 89  Bit Score: 38.33  E-value: 7.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301802901 316 TSGVVVRSVQSNMPANGHLEKYDVITKVDDKEIASSTDLQSALyNHSIGDTIKITYYRNGKEETTSIK 383
Cdd:cd06786   22 TGMLVAETVLPEGPADGKLEEGDVLISVNGELITQFIRLEEIL-DENVGKTVELVVQRGGEEITVTIT 88
 
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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