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Conserved domains on  [gi|119583694|gb|EAW63290|]
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HtrA serine peptidase 4 [Homo sapiens]

Protein Classification

Kazal-type serine protease inhibitor family protein( domain architecture ID 13622476)

Kazal-type serine protease inhibitor family protein may function as a serine protease inhibitor

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 ...
 201-479 1.92e-72

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: 230.42  E-value: 1.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 201 SGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNG----AQAVHT-LWSILIVIcslpflsspslfgHVQAE-LPVLMLGRS 274
Cdd:COG0265    2 LGSGVIISPDGYILTNNHVVEGADEITVTLADGreypAKVVGRdPLTDLAVL-------------KIDAKdLPAAPLGDS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 275 SDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGkELGMKDSDMDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVT-- 352
Cdd:COG0265   69 DKLRVGDWVLAIGNPFGLGQTVTAGIVSALGRSI-GSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrs 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 353 ---DGISFAIPSDRVRQFLAEYHEHqmkGKAfsNKKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQS 429
Cdd:COG0265  148 ggsQGIGFAIPINLAKRVVEQLIET---GRV--RRGWLGVTIQPVTPELAEALGL------PEPEGVLVARVEPGSPAAK 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119583694 430 SGLRDHDVIVNINGKPITTTTDVVKALDS----DSLSMAVLRGKDNLLLTVIPE 479
Cdd:COG0265  217 AGLRPGDVILAVDGKPVTSARDLQRLLASlkpgDTVTLTVLRGGKELTVTVTLG 270
IGFBP pfam00219
Insulin-like growth factor binding protein;
40-94 1.43e-14

Insulin-like growth factor binding protein;


:

Pssm-ID: 459717  Cd Length: 53  Bit Score: 67.74  E-value: 1.43e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119583694   40 CPAVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCGGAQGqPCAPGLQC 94
Cdd:pfam00219   1 CPPPCDPERCPPPPpGCPAGVVL--DGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 104-152 3.13e-08

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


:

Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.80  E-value: 3.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 119583694  104 STCGCPTLGGA-VCGSDRRTYPSMCALRAENRAARRLGKVPAVpVQWGNC 152
Cdd:pfam07648   2 CNCQCPKTEYEpVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 201-479 1.92e-72

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: 230.42  E-value: 1.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 201 SGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNG----AQAVHT-LWSILIVIcslpflsspslfgHVQAE-LPVLMLGRS 274
Cdd:COG0265    2 LGSGVIISPDGYILTNNHVVEGADEITVTLADGreypAKVVGRdPLTDLAVL-------------KIDAKdLPAAPLGDS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 275 SDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGkELGMKDSDMDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVT-- 352
Cdd:COG0265   69 DKLRVGDWVLAIGNPFGLGQTVTAGIVSALGRSI-GSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrs 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 353 ---DGISFAIPSDRVRQFLAEYHEHqmkGKAfsNKKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQS 429
Cdd:COG0265  148 ggsQGIGFAIPINLAKRVVEQLIET---GRV--RRGWLGVTIQPVTPELAEALGL------PEPEGVLVARVEPGSPAAK 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119583694 430 SGLRDHDVIVNINGKPITTTTDVVKALDS----DSLSMAVLRGKDNLLLTVIPE 479
Cdd:COG0265  217 AGLRPGDVILAVDGKPVTSARDLQRLLASlkpgDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 170-477 1.91e-57

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: 195.90  E-value: 1.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  170 IAAVVEKVAPSVVHV--------------------QLWGRLL------HGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQ 223
Cdd:TIGR02037   3 FAPLVEKVAPAVVNIsvegtvkrrnrppalppffrQFFGDDMpdfprqQREQKVRGL-GSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  224 QWIEVVLQNGaqavHTLWSILI---------VIcslpflsspslfgHVQA--ELPVLMLGRSSDLRAGEFVVALGSPFSL 292
Cdd:TIGR02037  82 DEITVTLSDG----REFKAKLVgkdprtdiaVL-------------KIDAkkNLPVIKLGDSDKLRVGDWVLAIGNPFGL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  293 QNTATAGIVSTKQRGGkeLGMKDSDmDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVTD-----GISFAIPSDRVRQF 367
Cdd:TIGR02037 145 GQTVTSGIVSALGRSG--LGIGDYE-NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPsggnvGIGFAIPSNMAKNV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  368 LAeyhehQMKGKAFSNKKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPIT 447
Cdd:TIGR02037 222 VD-----QLIEGGKVKRGWLGVTIQEVTSDLAKSLGL------EKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPIS 290

                         330       340       350
                  ....*....|....*....|....*....|....
gi 119583694  448 TTTDVVKAL----DSDSLSMAVLRGKDNLLLTVI 477
Cdd:TIGR02037 291 SFADLRRAIgtlkPGKKVTLGILRKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 384-479 1.88e-48

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: 161.51  E-value: 1.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 384 KKYLGLQMLSLTVPLSEELKMHYPDFPDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKAL-DSDSLS 462
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVkSGSSLL 80

                         90
                 ....*....|....*..
gi 119583694 463 MAVLRGKDNLLLTVIPE 479
Cdd:cd06785   81 VVVRRGNEDLLLTVTPE 97
PRK10139 PRK10139
serine endoprotease DegQ;
170-448 1.14e-33

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 132.38  E-value: 1.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 170 IAAVVEKVAPSVVHVQLWGRLLHGSRLVPVYS------------------GSGFIV-SEDGLIITNAHVVRNQQWIEVVL 230
Cdd:PRK10139  42 LAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKkffgddlpdqpaqpfeglGSGVIIdAAKGYVLTNNHVINQAQKISIQL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 231 QNGAQ-AVHTLWSILIVICSLPFLSSPSlfghvqaELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGK 309
Cdd:PRK10139 122 NDGREfDAKLIGSDDQSDIALLQIQNPS-------KLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRSGL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 310 EL-GMKdsdmDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVTD-----GISFAIPSDrvrqfLAEYHEHQMKGKAFSN 383
Cdd:PRK10139 195 NLeGLE----NFIQTDASINRGNSGGALLNLNGELIGINTAILAPgggsvGIGFAIPSN-----MARTLAQQLIDFGEIK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119583694 384 KKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITT 448
Cdd:PRK10139 266 RGLLGIKGTEMSADIAKAFNL------DVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNS 324
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 202-346 2.73e-22

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 92.48  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  202 GSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGAQAVHTLWSILIV-------ICSLPFLSSPslfghvqAELPVLMLGRS 274
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVardpdldLALLRVSGDG-------RGLPPLPLGDS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583694  275 SDLRAGEFVVALGSPFSLQ-NTATAGIVSTKQRGGKElgmkDSDMDYVQIDATINYGNSGGPLVNLDGDVIGV 346
Cdd:pfam13365  74 EPLVGGERVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
IGFBP pfam00219
Insulin-like growth factor binding protein;
40-94 1.43e-14

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 67.74  E-value: 1.43e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119583694   40 CPAVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCGGAQGqPCAPGLQC 94
Cdd:pfam00219   1 CPPPCDPERCPPPPpGCPAGVVL--DGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 171-370 4.33e-13

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: 70.60  E-value: 4.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 171 AAVVEKVAPSVVHVQlwGRLLHGSRLVpvySGSGFIVSeDGLIITNAHVVR--NQQWIEVVLQNGAQA--VHTLWSILIV 246
Cdd:NF033740 187 SPAVRRARPSVVKVR--GTAPSCGRAL---EGSGFVVA-PDRVMTNAHVVAgtDEVTVETVGGGTLDArvVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 247 IcslpfLSSPSLfghvqaELPVLMLGrSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQ--RGGKELGMKDSDMDYVQID 324
Cdd:NF033740 261 V-----LAVPGL------GLPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIalSGPDIYGSGTVTREVYTLR 328

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119583694 325 ATINYGNSGGPLVNLDGDVIGVNSLRVTDG--ISFAIPSDRVRQFLAE 370
Cdd:NF033740 329 GTVRPGNSGGPLLDPDGRVLGVVFAAAVDDsdTGYALTADEVRPDLAA 376
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 40-116 1.76e-09

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 54.01  E-value: 1.76e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119583694    40 CPaVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCgGAQGQPCAPGLQCLQPlrPGFPSTCGCPTLGGAVC 116
Cdd:smart00121   3 CP-PCDPARCPPCPpGCAELVRL--DGCGCCPVCARQEGEPC-GVYTPRCAPGLRCQPP--PGEERPLRALLHGQGVC 74
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 410-469 2.10e-08

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: 51.23  E-value: 2.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119583694   410 PDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTD--VVKALDS--DSLSMAVLRGK 469
Cdd:smart00228  22 KDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKagGKVTLTVLRGG 85
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 104-152 3.13e-08

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.80  E-value: 3.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 119583694  104 STCGCPTLGGA-VCGSDRRTYPSMCALRAENRAARRLGKVPAVpVQWGNC 152
Cdd:pfam07648   2 CNCQCPKTEYEpVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 108-152 1.92e-04

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 38.79  E-value: 1.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119583694 108 CPTLGGAVCGSDRRTYPSMCALRAENRAARRLGKVpavpVQWGNC 152
Cdd:cd00104    1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITV----AHNGPC 41
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 108-134 8.81e-04

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 37.27  E-value: 8.81e-04
                           10        20
                   ....*....|....*....|....*..
gi 119583694   108 CPTLGGAVCGSDRRTYPSMCALRAENR 134
Cdd:smart00280   6 CPREYDPVCGSDGVTYSNECHLCKAAC 32
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 201-479 1.92e-72

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: 230.42  E-value: 1.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 201 SGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNG----AQAVHT-LWSILIVIcslpflsspslfgHVQAE-LPVLMLGRS 274
Cdd:COG0265    2 LGSGVIISPDGYILTNNHVVEGADEITVTLADGreypAKVVGRdPLTDLAVL-------------KIDAKdLPAAPLGDS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 275 SDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGkELGMKDSDMDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVT-- 352
Cdd:COG0265   69 DKLRVGDWVLAIGNPFGLGQTVTAGIVSALGRSI-GSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIISrs 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 353 ---DGISFAIPSDRVRQFLAEYHEHqmkGKAfsNKKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQS 429
Cdd:COG0265  148 ggsQGIGFAIPINLAKRVVEQLIET---GRV--RRGWLGVTIQPVTPELAEALGL------PEPEGVLVARVEPGSPAAK 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119583694 430 SGLRDHDVIVNINGKPITTTTDVVKALDS----DSLSMAVLRGKDNLLLTVIPE 479
Cdd:COG0265  217 AGLRPGDVILAVDGKPVTSARDLQRLLASlkpgDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 170-477 1.91e-57

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: 195.90  E-value: 1.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  170 IAAVVEKVAPSVVHV--------------------QLWGRLL------HGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQ 223
Cdd:TIGR02037   3 FAPLVEKVAPAVVNIsvegtvkrrnrppalppffrQFFGDDMpdfprqQREQKVRGL-GSGVIISADGYVLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  224 QWIEVVLQNGaqavHTLWSILI---------VIcslpflsspslfgHVQA--ELPVLMLGRSSDLRAGEFVVALGSPFSL 292
Cdd:TIGR02037  82 DEITVTLSDG----REFKAKLVgkdprtdiaVL-------------KIDAkkNLPVIKLGDSDKLRVGDWVLAIGNPFGL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  293 QNTATAGIVSTKQRGGkeLGMKDSDmDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVTD-----GISFAIPSDRVRQF 367
Cdd:TIGR02037 145 GQTVTSGIVSALGRSG--LGIGDYE-NFIQTDAAINPGNSGGPLVNLRGEVIGINTAILSPsggnvGIGFAIPSNMAKNV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  368 LAeyhehQMKGKAFSNKKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPIT 447
Cdd:TIGR02037 222 VD-----QLIEGGKVKRGWLGVTIQEVTSDLAKSLGL------EKQRGALVAQVLPGSPAEKAGLKAGDVITSVNGKPIS 290

                         330       340       350
                  ....*....|....*....|....*....|....
gi 119583694  448 TTTDVVKAL----DSDSLSMAVLRGKDNLLLTVI 477
Cdd:TIGR02037 291 SFADLRRAIgtlkPGKKVTLGILRKGKEKTITVT 324
cpPDZ_HtrA-like cd06785
circularly permuted PDZ domain of high-temperature requirement factor A (HtrA) family serine ...
 384-479 1.88e-48

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: 161.51  E-value: 1.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 384 KKYLGLQMLSLTVPLSEELKMHYPDFPDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKAL-DSDSLS 462
Cdd:cd06785    1 KRYIGIRMLTLTPSLLEELKQRNPDFPDVSSGVYVHKVIPGSPAQRAGLKDGDVIISINGKPVKSSSDVYEAVkSGSSLL 80

                         90
                 ....*....|....*..
gi 119583694 463 MAVLRGKDNLLLTVIPE 479
Cdd:cd06785   81 VVVRRGNEDLLLTVTPE 97
PRK10139 PRK10139
serine endoprotease DegQ;
170-448 1.14e-33

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 132.38  E-value: 1.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 170 IAAVVEKVAPSVVHVQLWGRLLHGSRLVPVYS------------------GSGFIV-SEDGLIITNAHVVRNQQWIEVVL 230
Cdd:PRK10139  42 LAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKkffgddlpdqpaqpfeglGSGVIIdAAKGYVLTNNHVINQAQKISIQL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 231 QNGAQ-AVHTLWSILIVICSLPFLSSPSlfghvqaELPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRGGK 309
Cdd:PRK10139 122 NDGREfDAKLIGSDDQSDIALLQIQNPS-------KLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIISALGRSGL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 310 EL-GMKdsdmDYVQIDATINYGNSGGPLVNLDGDVIGVNSLRVTD-----GISFAIPSDrvrqfLAEYHEHQMKGKAFSN 383
Cdd:PRK10139 195 NLeGLE----NFIQTDASINRGNSGGALLNLNGELIGINTAILAPgggsvGIGFAIPSN-----MARTLAQQLIDFGEIK 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119583694 384 KKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITT 448
Cdd:PRK10139 266 RGLLGIKGTEMSADIAKAFNL------DVQRGAFVSEVLPNSGSAKAGVKAGDIITSLNGKPLNS 324
PRK10942 PRK10942
serine endoprotease DegP;
202-448 3.01e-33

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 131.43  E-value: 3.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 202 GSGFIV-SEDGLIITNAHVVRNQQWIEVVLQNGAQAVHTlwsiliVICSLPfLSSPSLFGHVQAE-LPVLMLGRSSDLRA 279
Cdd:PRK10942 113 GSGVIIdADKGYVVTNNHVVDNATKIKVQLSDGRKFDAK------VVGKDP-RSDIALIQLQNPKnLTAIKMADSDALRV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 280 GEFVVALGSPFSLQNTATAGIVSTKQRGGkeLGMKDSDmDYVQIDATINYGNSGGPLVNLDGDVIGVNS-LRVTD----G 354
Cdd:PRK10942 186 GDYTVAIGNPYGLGETVTSGIVSALGRSG--LNVENYE-NFIQTDAAINRGNSGGALVNLNGELIGINTaILAPDggniG 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 355 ISFAIPSDRVRQFLAEYHEH-QMKgkafsnKKYLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQSSGLR 433
Cdd:PRK10942 263 IGFAIPSNMVKNLTSQMVEYgQVK------RGELGIMGTELNSELAKAMKV------DAQRGAFVSQVLPNSSAAKAGIK 330

                        250
                 ....*....|....*
gi 119583694 434 DHDVIVNINGKPITT 448
Cdd:PRK10942 331 AGDVITSLNGKPISS 345
PRK10898 PRK10898
serine endoprotease DegS;
174-453 7.10e-26

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 108.17  E-value: 7.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 174 VEKVAPSVVHV--QLWGRLLHGSRLVPVYsGSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGaqavhTLWSILIVicslp 251
Cdd:PRK10898  51 VRRAAPAVVNVynRSLNSTSHNQLEIRTL-GSGVIMDQRGYILTNKHVINDADQIIVALQDG-----RVFEALLV----- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 252 flSSPSLFG----HVQAE-LPVLMLGRSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQRggkeLGMKDSD-MDYVQIDA 325
Cdd:PRK10898 120 --GSDSLTDlavlKINATnLPVIPINPKRVPHIGDVVLAIGNPYNLGQTITQGIISATGR----IGLSPTGrQNFLQTDA 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 326 TINYGNSGGPLVNLDGDVIGVNSL--------RVTDGISFAIPSDrvrqfLAEYHEHQM--KGKAFsnKKYLGLQmlslt 395
Cdd:PRK10898 194 SINHGNSGGALVNSLGELMGINTLsfdksndgETPEGIGFAIPTQ-----LATKIMDKLirDGRVI--RGYIGIG----- 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583694 396 vplSEEL-KMHYPDFP-DVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKP---ITTTTDVV 453
Cdd:PRK10898 262 ---GREIaPLHAQGGGiDQLQGIVVNEVSPDGPAAKAGIQVNDLIISVNNKPaisALETMDQV 321
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 202-346 2.73e-22

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 92.48  E-value: 2.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  202 GSGFIVSEDGLIITNAHVVRNQQWIEVVLQNGAQAVHTLWSILIV-------ICSLPFLSSPslfghvqAELPVLMLGRS 274
Cdd:pfam13365   1 GTGFVVSSDGLVLTNAHVVDDAEEAAVELVSVVLADGREYPATVVardpdldLALLRVSGDG-------RGLPPLPLGDS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583694  275 SDLRAGEFVVALGSPFSLQ-NTATAGIVSTKQRGGKElgmkDSDMDYVQIDATINYGNSGGPLVNLDGDVIGV 346
Cdd:pfam13365  74 EPLVGGERVYAVGYPLGGEkLSLSEGIVSGVDEGRDG----GDDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
cpPDZ_AtDEGP14-like cd23085
circularly permuted PDZ domain of Arabidopsis thaliana putative protease Do-like 14 (DEGP14) ...
 386-479 1.73e-20

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: 85.98  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 386 YLGLQMLSLTVPLSEELKMHYPDFPDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDSD---SLS 462
Cdd:cd23085    3 WLGMKMLELNEHIIAQLKERDPMFPDVKAGVLVPQVIPGSPAERAGLRPGDVIVEFDGKPVDSTKQIIDALGDKvgkPFK 82

                         90
                 ....*....|....*...
gi 119583694 463 MAVLRGKDNLL-LTVIPE 479
Cdd:cd23085   83 VVVKRANKVQVtLTVTPE 100
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 386-476 9.44e-15

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: 69.63  E-value: 9.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 386 YLGLQMLSLTVPLSEELkmhypdFPDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDS----DSL 461
Cdd:cd06779    3 YLGIEMENISPLLAKEL------GLPVNRGVLVAEVIPGSPAAKAGLKEGDVILSVNGKPVTSFNDLRAALDTkkpgDSL 76

                         90
                 ....*....|....*
gi 119583694 462 SMAVLRGKDNLLLTV 476
Cdd:cd06779   77 NLTILRDGKTLTVTV 91
IGFBP pfam00219
Insulin-like growth factor binding protein;
40-94 1.43e-14

Insulin-like growth factor binding protein;


Pssm-ID: 459717  Cd Length: 53  Bit Score: 67.74  E-value: 1.43e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119583694   40 CPAVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCGGAQGqPCAPGLQC 94
Cdd:pfam00219   1 CPPPCDPERCPPPPpGCPAGVVL--DGCGCCKVCARQEGEPCGVYTP-PCGKGLRC 53
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 386-479 2.15e-14

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: 68.89  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 386 YLGLQMLSLTVPLSEELKMHyPDFPDV---SSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDS---- 458
Cdd:cd10838    3 YLGIQMTTLTPELAQQNNRN-PNSPVRipeVDGVLIMQVLPNSPAARAGLRRGDVIQAVDGQPVTTADDVQRIVEQagvg 81

                         90       100
                 ....*....|....*....|.
gi 119583694 459 DSLSMAVLRGKDNLLLTVIPE 479
Cdd:cd10838   82 EELELTVLRGDRRQTLAVKPG 102
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 171-370 4.33e-13

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: 70.60  E-value: 4.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 171 AAVVEKVAPSVVHVQlwGRLLHGSRLVpvySGSGFIVSeDGLIITNAHVVR--NQQWIEVVLQNGAQA--VHTLWSILIV 246
Cdd:NF033740 187 SPAVRRARPSVVKVR--GTAPSCGRAL---EGSGFVVA-PDRVMTNAHVVAgtDEVTVETVGGGTLDArvVYYDPDRDIA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 247 IcslpfLSSPSLfghvqaELPVLMLGrSSDLRAGEFVVALGSPFSLQNTATAGIVSTKQ--RGGKELGMKDSDMDYVQID 324
Cdd:NF033740 261 V-----LAVPGL------GLPPLPFA-DEPAETGDDAIVLGYPEGGPFTATPARVRERIalSGPDIYGSGTVTREVYTLR 328

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119583694 325 ATINYGNSGGPLVNLDGDVIGVNSLRVTDG--ISFAIPSDRVRQFLAE 370
Cdd:NF033740 329 GTVRPGNSGGPLLDPDGRVLGVVFAAAVDDsdTGYALTADEVRPDLAA 376
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 386-471 5.87e-12

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: 61.88  E-value: 5.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 386 YLGLQMLSL-TVPLSEELKMHYPDfpDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKAL----DSDS 460
Cdd:cd06781    3 SLGISMVDLsDVPEYEQQSLKLPS--NVNKGVYVAQVQSNSPAEKAGLKKGDVITKLDGKKVESSSDLRQILyshkVGDT 80

                         90
                 ....*....|..
gi 119583694 461 LSMAVLR-GKDN 471
Cdd:cd06781   81 VKVTIYRdGKEK 92
IB smart00121
Insulin growth factor-binding protein homologues; High affinity binding partners of ...
 40-116 1.76e-09

Insulin growth factor-binding protein homologues; High affinity binding partners of insulin-like growth factors.


Pssm-ID: 197525  Cd Length: 75  Bit Score: 54.01  E-value: 1.76e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119583694    40 CPaVCQPTRCPALP-TCALGTTPvfDLCRCCRVCPAAEREVCgGAQGQPCAPGLQCLQPlrPGFPSTCGCPTLGGAVC 116
Cdd:smart00121   3 CP-PCDPARCPPCPpGCAELVRL--DGCGCCPVCARQEGEPC-GVYTPRCAPGLRCQPP--PGEERPLRALLHGQGVC 74
Trypsin pfam00089
Trypsin;
204-368 2.78e-09

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 57.07  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  204 GFIVSEDGlIITNAHVVRNQQWIEVVL-------QNGAQAVHTlwsILIVIC-------------SLPFLSSPSLFGHVQ 263
Cdd:pfam00089  29 GSLISENW-VLTAAHCVSGASDVKVVLgahnivlREGGEQKFD---VEKIIVhpnynpdtldndiALLKLESPVTLGDTV 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694  264 AELPVLMLGRSSDLRAGEFVVA------LGSPFSLQnTATAGIVSTKQRGGKELGMKDSDMdyVQIDAT---INYGNSGG 334
Cdd:pfam00089 105 RPICLPDASSDLPVGTTCTVSGwgntktLGPSDTLQ-EVTVPVVSRETCRSAYGGTVTDTM--ICAGAGgkdACQGDSGG 181

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 119583694  335 PLVNLDGDVIGVNSL----RVTDGISFAIPSDRVRQFL 368
Cdd:pfam00089 182 PLVCSDGELIGIVSWgygcASGNYPGVYTPVSSYLDWI 219
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 414-476 3.20e-09

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: 53.40  E-value: 3.20e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119583694 414 SGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDS--DSLSMAVLRGKDNLLLTV 476
Cdd:cd23084   18 KGVVVTEVDPGSPAAQSGLKKGDVIIGVNRQPVKSIAELRKVLKSkpSAVLLQIKRGDSSRYLAL 82
PDZ_2 pfam13180
PDZ domain;
409-476 5.99e-09

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 52.66  E-value: 5.99e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119583694  409 FPDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDS----DSLSMAVLRGKDNLLLTV 476
Cdd:pfam13180   1 FVDLEGGVVVVSVKSSGPAAKAGLKAGDVILSIDGRKINDLTDLESALYGhkpgDTVTLQVYRDGKLLTVEV 72
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 420-479 1.23e-08

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 56.63  E-value: 1.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583694 420 KVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDS---DSLSMAVLRGKDNLLLTVIPE 479
Cdd:COG0750  134 EVVPGSPAAKAGLQPGDRIVAINGQPVTSWDDLVDIIRAspgKPLTLTVERDGEELTLTVTPR 196
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 410-469 2.10e-08

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: 51.23  E-value: 2.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119583694   410 PDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTD--VVKALDS--DSLSMAVLRGK 469
Cdd:smart00228  22 KDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHleAVDLLKKagGKVTLTVLRGG 85
cpPDZ_EcRseP-like cd23081
circularly permuted PDZ domains of Escherichia coli Regulator of sigma-E protease (RseP) and ...
 420-479 2.29e-08

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: 51.04  E-value: 2.29e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583694 420 KVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDSD---SLSMAVLRGKDNLLLTVIPE 479
Cdd:cd23081    5 EVVANSPAAEAGLKPGDRILKIDGQKVRTWEDIVRIVRENpgkPLTLKIERDGKILTVTVTPE 67
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 104-152 3.13e-08

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 49.80  E-value: 3.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 119583694  104 STCGCPTLGGA-VCGSDRRTYPSMCALRAENRAARRLGKVPAVpVQWGNC 152
Cdd:pfam07648   2 CNCQCPKTEYEpVCGSDGVTYPSPCALCAAGCKLGKEVKEEKV-KYDGSC 50
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 386-476 7.06e-08

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: 50.17  E-value: 7.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 386 YLGLQMLSLTVPLSEELKMhypdfpDVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTD----VVKALDSDSL 461
Cdd:cd10839    3 WLGVQIQELTPDLAESFGL------KEPKGALVAQVLPDSPAAKAGLKAGDVILSLNGKPITSSADlrnrVATTKPGTKV 76

                         90
                 ....*....|....*
gi 119583694 462 SMAVLRGKDNLLLTV 476
Cdd:cd10839   77 ELKILRDGKEKTLTV 91
cpPDZ2_EcRseP-like cd23083
circularly permuted PDZ domain 2 (PDZ-C) of Escherichia coli Regulator of sigma-E protease ...
 421-480 1.69e-07

circularly permuted PDZ domain 2 (PDZ-C) 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-sigmaE) 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 it 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: 467640 [Multi-domain]  Cd Length: 85  Bit Score: 48.66  E-value: 1.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583694 421 VVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDSD---SLSMAVLRGKDNLLLTVIPET 480
Cdd:cd23083    6 VQPNSAAEKAGLQAGDRIVKVDGQPLTQWQTFVMAVRDNpgkPLALEIERQGSPLSLTLIPDS 68
Peptidase_M50 pfam02163
Peptidase family M50;
412-479 5.20e-07

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 51.34  E-value: 5.20e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119583694  412 VSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDS---DSLSMAVLRGKDNLLLTVIPE 479
Cdd:pfam02163  91 PPAPPVIGGVAPGSPAAKAGLKPGDVILSINGKKITSWQDLVEALAKspgKPITLTVERGGQTLTVTITPK 161
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
 415-456 2.62e-06

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 45.35  E-value: 2.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 119583694  415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTT--DVVKAL 456
Cdd:pfam00595  26 GIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTheEAVLAL 69
cpPDZ_AtDEGP1-like cd00990
circularly permuted PDZ domain of Arabidopsis thaliana DEGP1, and related domains; PDZ (PSD-95 ...
 412-476 3.23e-06

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: 45.65  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 412 VSSGVYVCKVVEGTAAQSSGL----RDH-------DVIVNINGKPITTTTDVVKALDS----DSLSMAVLRGKDNLLLTV 476
Cdd:cd00990   21 VRSGVLVLDVPPGGPAAKAGLrgtkRDEfgrivlgDVIVAVDGKPVKNESDLYRALDEykvgDVVTLKVLRGGTKVDLKV 100
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 417-467 2.08e-05

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


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 41.74  E-value: 2.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119583694  417 YVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDSD---SLSMAVLR 467
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSLEDVARLLQGSageSVTLTVRR 54
PDZ_RapGEF2_RapGEF6-like cd06755
PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange ...
 415-476 3.44e-05

PDZ domain of Rap guanine nucleotide exchange factor 2 and Rap guanine nucleotide exchange factor 6, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Rap guanine nucleotide exchange factor 2 (RapGEF2, also named RA-GEF-1, PDZ-GEF1, CNrasGEF and nRapGEP) and Rap guanine nucleotide exchange factor 6 (RapGEF6, also named RA-GEF-2 and PDZ-GEF2). RapGEF2 and RapGEF6 constitute a subfamily of guanine nucleotide exchange factors (GEFs) for RAP small GTPases that is characterized by the possession of the PDZ and Ras/Rap-associating domains. They activate Rap small GTPases, by catalyzing the release of GDP from the inactive GDP-bound forms, thereby accelerating GTP loading to yield the active GTP-bound forms. The PDZ domain of RapGEF6 (also known as PDZ-GEF2) binds junctional adhesion molecule A (JAM-A). 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 RapGEF2 and RapGEF6 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: 467237 [Multi-domain]  Cd Length: 83  Bit Score: 42.25  E-value: 3.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119583694 415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTdVVKALDsdslsmaVLRGKDNLLLTV 476
Cdd:cd06755   27 GIFVSKVEKGSKAAEAGLKRGDQILEVNGQNFENIT-LKKALE-------ILRNNTHLSITV 80
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
 417-466 4.19e-05

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. 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 tamalin-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: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 42.23  E-value: 4.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119583694 417 YVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTT--DVVKALDS--DSLSMAVL 466
Cdd:cd06713   38 YVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGAShqEIVELIRSsgNTLRLETL 91
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
 415-454 5.53e-05

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. 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 NHERF-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: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 41.27  E-value: 5.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119583694 415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTT--DVVK 454
Cdd:cd06768   24 GHFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESheQVVE 65
PDZ_TAX1BP3-like cd10822
PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic ...
 406-450 9.24e-05

PDZ domain of tax1-binding protein 3 (TAX1BP3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of TAX1BP3, and related domains. TAX1BP3 (also known as glutaminase-interacting protein 3, tax interaction protein 1, TIP-1, tax-interacting protein 1) may regulate a number of protein-protein interactions by competing for PDZ domain binding sites. TAX1BP3 binds beta-catenin and may act as an inhibitor of the Wnt signaling pathway. It competes with LIN7A (also known as Lin-7A or LIN-7A) for inward rectifier potassium channel 4 (KCNJ4) binding, and thereby promotes KCNJ4 internalization. It may play a role in the Rho signaling pathway, and in the activation of CDC42 by the viral protein HPV16 E6. Binding partners of the TAX1BP3 PDZ domain include beta-catenin, KCNJ4, glutaminase liver isoform (GLS2), rho guanine nucleotide exchange factor 16 (ARHGEF16), rhotekin, and CDK5 regulatory subunit-associated protein 3 (also known as LAPZ). 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 TAX1BP3-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: 467265 [Multi-domain]  Cd Length: 94  Bit Score: 41.17  E-value: 9.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119583694 406 YPDfpdvsSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTT 450
Cdd:cd10822   34 YTD-----KGIYVTRVSEGGPAEKAGLQVGDKILQVNGWDMTMVT 73
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
 413-456 9.78e-05

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: 40.93  E-value: 9.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119583694 413 SSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPIT--TTTDVVKAL 456
Cdd:cd06782   13 DGYLVVVSPIPGGPAEKAGIKPGDVIVAVDGESVRgmSLDEVVKLL 58
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 108-152 1.92e-04

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 38.79  E-value: 1.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 119583694 108 CPTLGGAVCGSDRRTYPSMCALRAENRAARRLGKVpavpVQWGNC 152
Cdd:cd00104    1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITV----AHNGPC 41
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 411-456 2.53e-04

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains 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: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 39.45  E-value: 2.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119583694 411 DVSSGVYVCKVVEGTAAQSSG-LRDHDVIVNINGKPITTTT--DVVKAL 456
Cdd:cd00136   21 DGGGGIFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTheEAVELL 69
PDZ1-PDZRN4-like cd06715
PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related ...
 413-450 3.64e-04

PDZ domain 1 of PDZ domain-containing RING finger protein 4 (PDZRN4), PDZRN3-B, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PDZRN4, PDZRN3-B, and related domains. PDZRN4 (also known as ligand of numb protein X 4, and SEMACAP3-like protein) contains an N-terminal RING domain and two tandem repeat PDZ domains. It is involved in the progression of cancer, including human liver cancer and breast cancer, and may contribute to the tumorigenesis of rectal adenocarcinoma. Danio rerio PDZRN3-B may participate in neurogenesis: the first PDZ domain of Danio rerio Pdzrn3 interacts with Kidins220 (Kinase D-interacting substrate 220 kD, also named Ankyrin Repeat-Rich Membrane Spanning), a crucial mediator of signal transduction in neural tissues. 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 PDZRN4-like family PDZ1 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: 467199 [Multi-domain]  Cd Length: 92  Bit Score: 39.68  E-value: 3.64e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119583694 413 SSGVYVCKVVE-GTAAQSSGLRDHDVIVNINGKPITTTT 450
Cdd:cd06715   33 SEGIYVSKIVEnGPAADEGGLQVHDRIIEVNGKDLSKAT 71
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 428-476 3.67e-04

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


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 41.89  E-value: 3.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119583694 428 QSSGLRDHDVIVNINGKPITTTTDVVKAL----DSDSLSMAVLRGKDNLLLTV 476
Cdd:COG3031  165 SKLGLQPGDVITSINGQDLTDPAQALELLqqlrDASEVTLTVERNGQPVTLTY 217
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 413-465 4.32e-04

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. 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 rhophilin-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: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 38.72  E-value: 4.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119583694 413 SSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPI--TTTTDVVKALDS---DSLSMAV 465
Cdd:cd06712   20 DSPVQVASVDPGSCAAEAGLKEGDYIVSVGGVDCkwSKHSEVVKLLKSageEGLELQV 77
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 415-479 4.69e-04

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: 42.16  E-value: 4.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119583694 415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPIT--TTTDVVKAldsdslsmavLRGK--DNLLLTVIPE 479
Cdd:COG0793   72 KVVVVSVIPGSPAEKAGIKPGDIILAIDGKSVAglTLDDAVKL----------LRGKagTKVTLTIKRP 130
PDZ3_Scribble-like cd06702
PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ...
 415-466 7.71e-04

PDZ domain 3 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. 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 Scribble-like family PDZ3 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: 467186 [Multi-domain]  Cd Length: 89  Bit Score: 38.39  E-value: 7.71e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119583694 415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTT--DVVKALDSDSLSMAVL 466
Cdd:cd06702   33 GIFISKVIPDGAAAKSGLRIGDRILSVNGKDLRHAThqEAVSALLSPGQEIKLL 86
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 108-134 8.81e-04

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 37.27  E-value: 8.81e-04
                           10        20
                   ....*....|....*....|....*..
gi 119583694   108 CPTLGGAVCGSDRRTYPSMCALRAENR 134
Cdd:smart00280   6 CPREYDPVCGSDGVTYSNECHLCKAAC 32
PDZ_nNOS-like cd06708
PDZ domain of neuronal nitric oxide synthase (nNOS), and related domains; PDZ (PSD-95 ...
 416-468 1.52e-03

PDZ domain of neuronal nitric oxide synthase (nNOS), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of nNOS, and related domains. nNOS produces a key signaling molecule, nitric oxide (NO), which has diverse functions throughout the body and acts as a neurotransmitter and intracellular signaling molecule in the central and peripheral nervous system. nNOS is concentrated at synaptic junctions in the brain and motor endplates in skeletal muscle. The PDZ domain of neuronal nitric oxide synthase (nNOS) interacts with the PDZ domain of alpha1-syntrophin (in muscle cells) and with the second PDZ domain of Disks large homolog 4 (Dlg4, also known as PSD-95), and nitric oxide synthase 1 adaptor protein NOS1AP in neurons. Dlg4 binds NMDA receptors, and nNOS, forming a complex in neurons. NOS1AP competes with Dgl4 for the nNOS PDZ domain and prevents the coupling of nNos activation with NMDA receptor-mediated calcium influx. 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 nNOS-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: 467192 [Multi-domain]  Cd Length: 110  Bit Score: 38.13  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119583694 416 VYVCKVVEGTAAQSSGL-RDHDVIVNINGKPITTTT-----DVVKALDSDSLSMAVLRG 468
Cdd:cd06708   28 VIISDLIRGGAAEQSGLvQVGDIILAVNGRPLVDVSyesalEVLRSIPSETPVVLILRG 86
PDZ3_MUPP1-like cd06791
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ...
 413-456 1.76e-03

PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. 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 MUPP1-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: 467253 [Multi-domain]  Cd Length: 89  Bit Score: 37.60  E-value: 1.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119583694 413 SSGVYVCKVVEGTAAQSSG-LRDHDVIVNINGKPIT--TTTDVVKAL 456
Cdd:cd06791   30 LSGIFVKSIIPGSAADQDGrIQVNDQIIAVDGVNLQgfTNQEAVEVL 76
PDZ_SNX27-like cd23070
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ...
 417-478 2.67e-03

PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. 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 SNX27-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: 467283 [Multi-domain]  Cd Length: 93  Bit Score: 37.00  E-value: 2.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119583694 417 YVCKVVEGTAAQSSGLRDHDVIVNINGKPI--TTTTDVVKALDSdslsmavlrGKDNLLLTVIP 478
Cdd:cd23070   39 HVSAVLEGGAADKAGVRKGDRILEVNGVNVegATHKQVVDLIKS---------GGDELTLTVIS 93
PDZ2_DLG5-like cd06765
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ...
 414-467 4.52e-03

PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. 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 Dlg5-like family PSZ2 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: 467246 [Multi-domain]  Cd Length: 77  Bit Score: 36.17  E-value: 4.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119583694 414 SGVYVCKVVEGT-AAQSSGLRDHDVIVNINGKPI--TTTTDVVKALDS--DSLSMAVLR 467
Cdd:cd06765   16 NGVFISRIVPGSpAAKEGSLTVGDRIIAINGIALdnKSLSECEALLRScrDSLSLSLMK 74
PRK10779 PRK10779
sigma E protease regulator RseP;
418-480 5.09e-03

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 39.28  E-value: 5.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119583694 418 VCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKALDSD---SLSMAVLRGKDNLLLTVIPET 480
Cdd:PRK10779 225 LAEVQPNSAASKAGLQAGDRIVKVDGQPLTQWQTFVTLVRDNpgkPLALEIERQGSPLSLTLTPDS 290
PDZ1_PDZD7-like cd10833
PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related ...
 415-467 5.46e-03

PDZ domain 1 of the canonical isoform 1 of PDZ domain containing 7 (PDZD7), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of the long isoform 1 of PDZD7, and related domains. PDZD7 is critical for the organization of Usher syndrome type 2 (USH2) complex. Usher syndrome is the leading cause of hereditary sensory deaf-blindness in humans; USH2 is the most common sub-type. Formation of the USH2 complex is based upon heterodimerization between PDZD7 and whirlin (another PDZ domain-containing protein) and a subsequent dynamic interplay between USH2 proteins via their multiple PDZ domains. The PDZD7 PDZ2 domain binds GPR98 (also known as VLGR1) and usherin (USH2A). PDZD7 and whirlin form heterodimers through their multiple PDZ domains; whirlin and PDZD7 interact with usherin and GPR98 to form an interdependent ankle link complex. PDZD7 also interacts with myosin VIIa. PDZD7 also forms homodimers through its PDZ2 domain. Various isoforms of PDZD7 produced by alternative splicing have been identified; this subgroup includes the first PDZ domain of the canonical isoform of PDZD7- isoform 1. 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 PDZD7-like family PDZ1 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: 467269 [Multi-domain]  Cd Length: 84  Bit Score: 35.87  E-value: 5.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119583694 415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPI--TTTTDVVKALDSDS-LSMAVLR 467
Cdd:cd10833   27 GIFVSKVEEGSAAERAGLCVGDKITEVNGVSLenITMSSAVKVLTGSNrLRMVVRR 82
PDZ_PDLIM-like cd06753
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 411-467 6.89e-03

PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). 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 PDLIM-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: 467235 [Multi-domain]  Cd Length: 79  Bit Score: 35.58  E-value: 6.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119583694 411 DVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTT-----DVVKAlDSDSLSMAVLR 467
Cdd:cd06753   19 DFNQPLTISRVTPGGKAAQANLRPGDVILAINGESTEGMThleaqNKIKA-ATGSLSLTLER 79
cpPDZ1_MamE-like cd23087
circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease ...
 415-470 7.41e-03

circularly permuted PDZ domain 1 of Magnetospirillum magneticum magnetosome formation protease MamE and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Magnetospirillum magneticum MamE (also known as magnetochrome MamE and magnetosome serine protease MamE), and related domains. MamE is a serine protease required to produce magnetite crystals in the magnetotactic bacterium M. magneticum. It is involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome, and likely cleaves at least itself, MamO and MamP. MamE-PDZ1 may bind MamB. Its autoproteolysis is stimulated by exogenous substrates or peptides that bind to its PDZ domains. Peptide binding to either the first or the second PDZ domain of MamE can activate proteolysis; activation through PDZ2 is much weaker. 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 MamE-like 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: 467634 [Multi-domain]  Cd Length: 91  Bit Score: 36.01  E-value: 7.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 415 GVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITTTTDVVKAL----DSDSLSMAVLRGKD 470
Cdd:cd23087   26 GVFVSGVTPNTPAAAAGLRPGDVILKVDGRPVHQPEEVSAIMaempNGRSVRLGVLRDGD 85
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
 418-466 7.76e-03

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. 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 SYNPO2-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: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 35.36  E-value: 7.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119583694 418 VCKVVEGTAAQSSGLRDHDVIVNINGKPIT--TTTDVVKALDS--DSLSMAVL 466
Cdd:cd10820   26 VAKIRKKSKAALAGLCEGDELLSINGKPCAdlSHSEAMDLIDSsgDTLQLLIK 78
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 107-133 9.33e-03

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 34.18  E-value: 9.33e-03
                         10        20
                 ....*....|....*....|....*..
gi 119583694 107 GCPTLGGAVCGSDRRTYPSMCALRAEN 133
Cdd:cd01327    4 GCPKDYDPVCGTDGVTYSNECLLCAEN 30
PDZ1_syntenin-like cd06721
PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
 411-465 9.50e-03

PDZ domain 1 of syntenin-1, syntenin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of syntenin-1, syntenin-2, and related domains. Syntenins are implicated in various cellular processes such as trafficking, signaling, and cancer metastasis. They bind to signaling and adhesion molecules, such as syndecans, neurexins, ephrin B, and phospholipid PIP2. Through its tandem PDZ domains (PDZ1 and PDZ2), syntenin links syndecans to other cell surface receptors and kinases, such as E-cadherin and ephrin-B, establishing signaling crosstalk. During syndecan binding, syntenin PDZ2 serves as a high-affinity domain, and PDZ1, also necessary for binding, acts as a complementary, low-affinity domain; this is also the case for syntenin binding to proto-oncogene c-Src. The syntenin PDZ domain-PIP2 interaction controls Arf6-mediated syndecan recycling through endosomal compartments; both PDZ1 and PDZ2 interact with PIP2. Different binding partners and downstream regulators of syntenin1 PDZ domains, such as to proto-oncogene c-Src, mitogen-activated protein kinase (MAPK), and focal adhesion kinase (FAK), have been identified that promote the progression and invasion of a variety of cancers, such as melanoma, glioblastoma multiforme and breast cancer. 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 syntenin-like family domain is a canonical PDZ domain containing 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.


Pssm-ID: 467204 [Multi-domain]  Cd Length: 79  Bit Score: 35.29  E-value: 9.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583694 411 DVSSGVYVCKVVEGTAAQSSGLRDHDVIVNINGKPITT-TTD----VVKALDSDSLSMAV 465
Cdd:cd06721   19 SIDKGVFVQLVQANSPAALAGLRFGDQILQINGENVAGwSSDkahkVLKKASPERITLAV 78
 
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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