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Conserved domains on  [gi|1002280142|ref|XP_015644377|]
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protease Do-like 9 [Oryza sativa Japonica Group]

Protein Classification

S1C family serine protease( domain architecture ID 14288683)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDZ_3 pfam17815
PDZ domain; This entry contains the second PDZ domain from plant peptidases such as Deg2. This ...
 480-625 2.23e-57

PDZ domain; This entry contains the second PDZ domain from plant peptidases such as Deg2. This domain is involved in cage assembly.


:

Pssm-ID: 436064  Cd Length: 145  Bit Score: 189.70  E-value: 2.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 480 IPAHIKGRPPSYYIVAGFVFMVVSVPYLRsEYGKDYEYDAPVKLLDKHLHAMAQSPDEQLVVVSQVLVADINIGYEEIVN 559
Cdd:pfam17815   1 VPVHQYDKRPSYFIYGGLVFVPLTQPYLE-EWGDDWSNKAPRKLLDLALSGVPTEEGEQVVVLSQVLADEVNVGYEDIRN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280142 560 IQVLSFNGKPVKNLKHLATMVEDCNEEYLKFDMDYDQLVVLEAKTAKAATQDILTTHCIPSAMSED 625
Cdd:pfam17815  80 LIVLKVNGEKVKNLRHLVRLVESCTEEFLRFDLEDGRVIVLDRKEAEAATPRILKRYRIPSDRSPD 145
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 196-474 1.16e-52

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: 181.89  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIG--GHrVLTNAHSVEHYTQVKLKKrgSD-TKYLATVLAIGTECDIAMLTVEDdefwKGVSPLEFGSLPALQ--DAV 270
Cdd:COG0265     5 GVIISpdGY-ILTNNHVVEGADEITVTL--ADgREYPAKVVGRDPLTDLAVLKIDA----KDLPAAPLGDSDKLRvgDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 271 TVVGYPIGGDTiSVTSGVVSRIE-ILSYVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGIAFQSL-KHEDVENIGYV 348
Cdd:COG0265    78 LAIGNPFGLGQ-TVTAGIVSALGrSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIIsRSGGSQGIGFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 349 IPTPVINHFIQDYEKSGEYTgFPILGIEWQKMeNPDLRKAMGMKSDQkGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDI 427
Cdd:COG0265   157 IPINLAKRVVEQLIETGRVR-RGWLGVTIQPV-TPELAEALGLPEPE-GVLVARVEPGSPaAKAGLRPGDVILAVDGKPV 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002280142 428 ANDGTvpfrhgerigFSYLISQKYTGEKAHVKILRNSKVLEFNIKLA 474
Cdd:COG0265   234 TSARD----------LQRLLASLKPGDTVTLTVLRGGKELTVTVTLG 270
 
Name Accession Description Interval E-value
PDZ_3 pfam17815
PDZ domain; This entry contains the second PDZ domain from plant peptidases such as Deg2. This ...
 480-625 2.23e-57

PDZ domain; This entry contains the second PDZ domain from plant peptidases such as Deg2. This domain is involved in cage assembly.


Pssm-ID: 436064  Cd Length: 145  Bit Score: 189.70  E-value: 2.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 480 IPAHIKGRPPSYYIVAGFVFMVVSVPYLRsEYGKDYEYDAPVKLLDKHLHAMAQSPDEQLVVVSQVLVADINIGYEEIVN 559
Cdd:pfam17815   1 VPVHQYDKRPSYFIYGGLVFVPLTQPYLE-EWGDDWSNKAPRKLLDLALSGVPTEEGEQVVVLSQVLADEVNVGYEDIRN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280142 560 IQVLSFNGKPVKNLKHLATMVEDCNEEYLKFDMDYDQLVVLEAKTAKAATQDILTTHCIPSAMSED 625
Cdd:pfam17815  80 LIVLKVNGEKVKNLRHLVRLVESCTEEFLRFDLEDGRVIVLDRKEAEAATPRILKRYRIPSDRSPD 145
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 196-474 1.16e-52

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: 181.89  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIG--GHrVLTNAHSVEHYTQVKLKKrgSD-TKYLATVLAIGTECDIAMLTVEDdefwKGVSPLEFGSLPALQ--DAV 270
Cdd:COG0265     5 GVIISpdGY-ILTNNHVVEGADEITVTL--ADgREYPAKVVGRDPLTDLAVLKIDA----KDLPAAPLGDSDKLRvgDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 271 TVVGYPIGGDTiSVTSGVVSRIE-ILSYVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGIAFQSL-KHEDVENIGYV 348
Cdd:COG0265    78 LAIGNPFGLGQ-TVTAGIVSALGrSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIIsRSGGSQGIGFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 349 IPTPVINHFIQDYEKSGEYTgFPILGIEWQKMeNPDLRKAMGMKSDQkGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDI 427
Cdd:COG0265   157 IPINLAKRVVEQLIETGRVR-RGWLGVTIQPV-TPELAEALGLPEPE-GVLVARVEPGSPaAKAGLRPGDVILAVDGKPV 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002280142 428 ANDGTvpfrhgerigFSYLISQKYTGEKAHVKILRNSKVLEFNIKLA 474
Cdd:COG0265   234 TSARD----------LQRLLASLKPGDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 158-475 1.18e-31

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: 127.72  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 158 VAKVMPsmdAVVKVFCVHTE---------------------PNFSLPwQRKRQYSSSSSGFII--GGHrVLTNAHSVEHY 214
Cdd:TIGR02037   7 VEKVAP---AVVNISVEGTVkrrnrppalppffrqffgddmPDFPRQ-QREQKVRGLGSGVIIsaDGY-VLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 215 T--QVKLkkrgSD-TKYLATVLAIGTECDIAMLTVEDDefwKGVSPLEFGSLPALQ--DAVTVVGYPIGGDTiSVTSGVV 289
Cdd:TIGR02037  82 DeiTVTL----SDgREFKAKLVGKDPRTDIAVLKIDAK---KNLPVIKLGDSDKLRvgDWVLAIGNPFGLGQ-TVTSGIV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 290 S---RieilSYVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGI--AFQSLKHEDVeNIGYVIPTPVINHFIQDYEKS 364
Cdd:TIGR02037 154 SalgR----SGLGIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGIntAILSPSGGNV-GIGFAIPSNMAKNVVDQLIEG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 365 GEYTgFPILGIEWQKMeNPDLRKAMGMKSdQKGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDIANDGTVPFRhgerigf 443
Cdd:TIGR02037 229 GKVK-RGWLGVTIQEV-TSDLAKSLGLEK-QRGALVAQVLPGSPaEKAGLKAGDVITSVNGKPISSFADLRRA------- 298

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1002280142 444 sylISQKYTGEKAHVKILRNSKVLEFNIKLAT 475
Cdd:TIGR02037 299 ---IGTLKPGKKVTLGILRKGKEKTITVTLGA 327
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 196-332 7.19e-22

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 92.10  E-value: 7.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIG-GHRVLTNAH---SVEHYTQVKLKKRGSD-TKYLATVLAIGTECDIAMLTVEDDEFWKGVSPLEFGSLPALQDAV 270
Cdd:pfam13365   3 GFVVSsDGLVLTNAHvvdDAEEAAVELVSVVLADgREYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGERV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002280142 271 TVVGYPIGGDTISVTSGVVSRIEILSYVHGSTELlgLQIDAAINSGNSGGPAFNDKGKCVGI 332
Cdd:pfam13365  83 YAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRV--IQTDAALSPGSSGGPVFDADGRVVGI 142
PRK10942 PRK10942
serine endoprotease DegP;
196-473 1.76e-15

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 79.42  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIGGHR--VLTNAHSVEHYTqvKLKKRGSD-TKYLATVLAIGTECDIAMLTVEDdefWKGVSPLEFGSLPALQ--DAV 270
Cdd:PRK10942  115 GVIIDADKgyVVTNNHVVDNAT--KIKVQLSDgRKFDAKVVGKDPRSDIALIQLQN---PKNLTAIKMADSDALRvgDYT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 271 TVVGYPIG-GDTisVTSGVVSRI-----EILSYVHGstellgLQIDAAINSGNSGGPAFNDKGKCVGIAFQSLKhEDVEN 344
Cdd:PRK10942  190 VAIGNPYGlGET--VTSGIVSALgrsglNVENYENF------IQTDAAINRGNSGGALVNLNGELIGINTAILA-PDGGN 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 345 --IGYVIPTPVINHFI-QDYE----KSGEytgFPILGIEWqkmeNPDLRKAMGMKSdQKGVRVRRVEP--TAPESGcLQP 415
Cdd:PRK10942  261 igIGFAIPSNMVKNLTsQMVEygqvKRGE---LGIMGTEL----NSELAKAMKVDA-QRGAFVSQVLPnsSAAKAG-IKA 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002280142 416 SDIILSFDGIDIANdgtvpfrhgerigFSYLISQKYT---GEKAHVKILRNSKVLEFNIKL 473
Cdd:PRK10942  332 GDVITSLNGKPISS-------------FAALRAQVGTmpvGSKLTLGLLRDGKPVNVNVEL 379
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 196-349 2.01e-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: 72.14  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIGGHRVLTNAHSVEHYTQVKLKKRGSDTkYLATVLAIGTECDIAMLTVEDDefwkGVSPLEFGSLPALQ-DAVTVVG 274
Cdd:NF033740  215 GFVVAPDRVMTNAHVVAGTDEVTVETVGGGT-LDARVVYYDPDRDIAVLAVPGL----GLPPLPFADEPAETgDDAIVLG 289

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280142 275 YPIGGDTISVTSGVVSRIEILS---YVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGIAFQslKHEDVENIGYVI 349
Cdd:NF033740  290 YPEGGPFTATPARVRERIALSGpdiYGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGVVFA--AAVDDSDTGYAL 365
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 373-471 3.44e-11

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


Pssm-ID: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 59.80  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 373 LGIEWQKMeNPDLRKAMGMKsDQKGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDIANDGTVPFRhgerigfsylISQKY 451
Cdd:cd10839     4 LGVQIQEL-TPDLAESFGLK-EPKGALVAQVLPDSPaAKAGLKAGDVILSLNGKPITSSADLRNR----------VATTK 71

                          90       100
                  ....*....|....*....|
gi 1002280142 452 TGEKAHVKILRNSKVLEFNI 471
Cdd:cd10839    72 PGTKVELKILRDGKEKTLTV 91
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 390-464 6.32e-03

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: 36.20  E-value: 6.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280142  390 GMKSDQKGVRVRRVEPTAPESGC-LQPSDIILSFDGIDIANdgtvpFRHGERIgfsylISQKYTGEKAHVKILRNS 464
Cdd:smart00228  20 GGKDEGGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEG-----LTHLEAV-----DLLKKAGGKVTLTVLRGG 85
 
Name Accession Description Interval E-value
PDZ_3 pfam17815
PDZ domain; This entry contains the second PDZ domain from plant peptidases such as Deg2. This ...
 480-625 2.23e-57

PDZ domain; This entry contains the second PDZ domain from plant peptidases such as Deg2. This domain is involved in cage assembly.


Pssm-ID: 436064  Cd Length: 145  Bit Score: 189.70  E-value: 2.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 480 IPAHIKGRPPSYYIVAGFVFMVVSVPYLRsEYGKDYEYDAPVKLLDKHLHAMAQSPDEQLVVVSQVLVADINIGYEEIVN 559
Cdd:pfam17815   1 VPVHQYDKRPSYFIYGGLVFVPLTQPYLE-EWGDDWSNKAPRKLLDLALSGVPTEEGEQVVVLSQVLADEVNVGYEDIRN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280142 560 IQVLSFNGKPVKNLKHLATMVEDCNEEYLKFDMDYDQLVVLEAKTAKAATQDILTTHCIPSAMSED 625
Cdd:pfam17815  80 LIVLKVNGEKVKNLRHLVRLVESCTEEFLRFDLEDGRVIVLDRKEAEAATPRILKRYRIPSDRSPD 145
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 196-474 1.16e-52

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: 181.89  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIG--GHrVLTNAHSVEHYTQVKLKKrgSD-TKYLATVLAIGTECDIAMLTVEDdefwKGVSPLEFGSLPALQ--DAV 270
Cdd:COG0265     5 GVIISpdGY-ILTNNHVVEGADEITVTL--ADgREYPAKVVGRDPLTDLAVLKIDA----KDLPAAPLGDSDKLRvgDWV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 271 TVVGYPIGGDTiSVTSGVVSRIE-ILSYVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGIAFQSL-KHEDVENIGYV 348
Cdd:COG0265    78 LAIGNPFGLGQ-TVTAGIVSALGrSIGSSGGGTYDDFIQTDAAINPGNSGGPLVNLNGEVIGINTAIIsRSGGSQGIGFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 349 IPTPVINHFIQDYEKSGEYTgFPILGIEWQKMeNPDLRKAMGMKSDQkGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDI 427
Cdd:COG0265   157 IPINLAKRVVEQLIETGRVR-RGWLGVTIQPV-TPELAEALGLPEPE-GVLVARVEPGSPaAKAGLRPGDVILAVDGKPV 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1002280142 428 ANDGTvpfrhgerigFSYLISQKYTGEKAHVKILRNSKVLEFNIKLA 474
Cdd:COG0265   234 TSARD----------LQRLLASLKPGDTVTLTVLRGGKELTVTVTLG 270
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 158-475 1.18e-31

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: 127.72  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 158 VAKVMPsmdAVVKVFCVHTE---------------------PNFSLPwQRKRQYSSSSSGFII--GGHrVLTNAHSVEHY 214
Cdd:TIGR02037   7 VEKVAP---AVVNISVEGTVkrrnrppalppffrqffgddmPDFPRQ-QREQKVRGLGSGVIIsaDGY-VLTNNHVVDGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 215 T--QVKLkkrgSD-TKYLATVLAIGTECDIAMLTVEDDefwKGVSPLEFGSLPALQ--DAVTVVGYPIGGDTiSVTSGVV 289
Cdd:TIGR02037  82 DeiTVTL----SDgREFKAKLVGKDPRTDIAVLKIDAK---KNLPVIKLGDSDKLRvgDWVLAIGNPFGLGQ-TVTSGIV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 290 S---RieilSYVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGI--AFQSLKHEDVeNIGYVIPTPVINHFIQDYEKS 364
Cdd:TIGR02037 154 SalgR----SGLGIGDYENFIQTDAAINPGNSGGPLVNLRGEVIGIntAILSPSGGNV-GIGFAIPSNMAKNVVDQLIEG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 365 GEYTgFPILGIEWQKMeNPDLRKAMGMKSdQKGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDIANDGTVPFRhgerigf 443
Cdd:TIGR02037 229 GKVK-RGWLGVTIQEV-TSDLAKSLGLEK-QRGALVAQVLPGSPaEKAGLKAGDVITSVNGKPISSFADLRRA------- 298

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1002280142 444 sylISQKYTGEKAHVKILRNSKVLEFNIKLAT 475
Cdd:TIGR02037 299 ---IGTLKPGKKVTLGILRKGKEKTITVTLGA 327
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 196-332 7.19e-22

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 92.10  E-value: 7.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIG-GHRVLTNAH---SVEHYTQVKLKKRGSD-TKYLATVLAIGTECDIAMLTVEDDEFWKGVSPLEFGSLPALQDAV 270
Cdd:pfam13365   3 GFVVSsDGLVLTNAHvvdDAEEAAVELVSVVLADgREYPATVVARDPDLDLALLRVSGDGRGLPPLPLGDSEPLVGGERV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002280142 271 TVVGYPIGGDTISVTSGVVSRIEILSYVHGSTELlgLQIDAAINSGNSGGPAFNDKGKCVGI 332
Cdd:pfam13365  83 YAVGYPLGGEKLSLSEGIVSGVDEGRDGGDDGRV--IQTDAALSPGSSGGPVFDADGRVVGI 142
PRK10942 PRK10942
serine endoprotease DegP;
196-473 1.76e-15

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 79.42  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIGGHR--VLTNAHSVEHYTqvKLKKRGSD-TKYLATVLAIGTECDIAMLTVEDdefWKGVSPLEFGSLPALQ--DAV 270
Cdd:PRK10942  115 GVIIDADKgyVVTNNHVVDNAT--KIKVQLSDgRKFDAKVVGKDPRSDIALIQLQN---PKNLTAIKMADSDALRvgDYT 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 271 TVVGYPIG-GDTisVTSGVVSRI-----EILSYVHGstellgLQIDAAINSGNSGGPAFNDKGKCVGIAFQSLKhEDVEN 344
Cdd:PRK10942  190 VAIGNPYGlGET--VTSGIVSALgrsglNVENYENF------IQTDAAINRGNSGGALVNLNGELIGINTAILA-PDGGN 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 345 --IGYVIPTPVINHFI-QDYE----KSGEytgFPILGIEWqkmeNPDLRKAMGMKSdQKGVRVRRVEP--TAPESGcLQP 415
Cdd:PRK10942  261 igIGFAIPSNMVKNLTsQMVEygqvKRGE---LGIMGTEL----NSELAKAMKVDA-QRGAFVSQVLPnsSAAKAG-IKA 331

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002280142 416 SDIILSFDGIDIANdgtvpfrhgerigFSYLISQKYT---GEKAHVKILRNSKVLEFNIKL 473
Cdd:PRK10942  332 GDVITSLNGKPISS-------------FAALRAQVGTmpvGSKLTLGLLRDGKPVNVNVEL 379
Trypsin pfam00089
Trypsin;
181-358 1.80e-15

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 75.94  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 181 SLPWQRKRQYSSSSS---GFIIGGHRVLTNAHSVEHYTQVKLK------KRGSDTKYLATVLAI---------GTECDIA 242
Cdd:pfam00089  11 SFPWQVSLQLSSGKHfcgGSLISENWVLTAAHCVSGASDVKVVlgahniVLREGGEQKFDVEKIivhpnynpdTLDNDIA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 243 MLTVE-DDEFWKGVSPLEF---GSLPALQDAVTVVGYPIGG-----DTI-SVTSGVVSRIEILSYVHGSTELLGLQIDA- 311
Cdd:pfam00089  91 LLKLEsPVTLGDTVRPICLpdaSSDLPVGTTCTVSGWGNTKtlgpsDTLqEVTVPVVSRETCRSAYGGTVTDTMICAGAg 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1002280142 312 --AINSGNSGGPAFNDKGKCVGIAFQSLKHEDVENIGYVIPTPVINHFI 358
Cdd:pfam00089 171 gkDACQGDSGGPLVCSDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
MarP_fam_protase NF033740
MarP family serine protease; The founding member of this family of membrane-spanning serine ...
 196-349 2.01e-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: 72.14  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIGGHRVLTNAHSVEHYTQVKLKKRGSDTkYLATVLAIGTECDIAMLTVEDDefwkGVSPLEFGSLPALQ-DAVTVVG 274
Cdd:NF033740  215 GFVVAPDRVMTNAHVVAGTDEVTVETVGGGT-LDARVVYYDPDRDIAVLAVPGL----GLPPLPFADEPAETgDDAIVLG 289

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002280142 275 YPIGGDTISVTSGVVSRIEILS---YVHGSTELLGLQIDAAINSGNSGGPAFNDKGKCVGIAFQslKHEDVENIGYVI 349
Cdd:NF033740  290 YPEGGPFTATPARVRERIALSGpdiYGSGTVTREVYTLRGTVRPGNSGGPLLDPDGRVLGVVFA--AAVDDSDTGYAL 365
PRK10139 PRK10139
serine endoprotease DegQ;
181-475 4.60e-12

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 68.43  E-value: 4.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 181 SLPWQRKRQYSSSSSGFIIGGHR--VLTNAHSVEHYTQVKLKkRGSDTKYLATVLAIGTECDIAMLTVEDDEFWKGVSPL 258
Cdd:PRK10139   79 DLPDQPAQPFEGLGSGVIIDAAKgyVLTNNHVINQAQKISIQ-LNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 259 EFGSLpALQDAVTVVGYPIG-GDTisVTSGVVSRIEilsyvHGSTELLGL----QIDAAINSGNSGGPAFNDKGKCVGIA 333
Cdd:PRK10139  158 DSDKL-RVGDFAVAVGNPFGlGQT--ATSGIISALG-----RSGLNLEGLenfiQTDASINRGNSGGALLNLNGELIGIN 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 334 FQSLKHEDVE-NIGYVIPTPVINHFIQDYEKSGEYTGfPILGIEWQKMeNPDLRKAMGMKSdQKGVRVRRVEPTAPESGC 412
Cdd:PRK10139  230 TAILAPGGGSvGIGFAIPSNMARTLAQQLIDFGEIKR-GLLGIKGTEM-SADIAKAFNLDV-QRGAFVSEVLPNSGSAKA 306

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002280142 413 -LQPSDIILSFDGIDIANDGTVPFRhgerigfsylISQKYTGEKAHVKILRNSKVLEFNIKLAT 475
Cdd:PRK10139  307 gVKAGDIITSLNGKPLNSFAELRSR----------IATTEPGTKVKLGLLRNGKPLEVEVTLDT 360
cpPDZ1_DegP-like cd10839
circularly permuted first PDZ domain (PDZ1) of Escherichia coli periplasmic serine ...
 373-471 3.44e-11

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


Pssm-ID: 467630 [Multi-domain]  Cd Length: 91  Bit Score: 59.80  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 373 LGIEWQKMeNPDLRKAMGMKsDQKGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDIANDGTVPFRhgerigfsylISQKY 451
Cdd:cd10839     4 LGVQIQEL-TPDLAESFGLK-EPKGALVAQVLPDSPaAKAGLKAGDVILSLNGKPITSSADLRNR----------VATTK 71

                          90       100
                  ....*....|....*....|
gi 1002280142 452 TGEKAHVKILRNSKVLEFNI 471
Cdd:cd10839    72 PGTKVELKILRDGKEKTLTV 91
PRK10898 PRK10898
serine endoprotease DegS;
204-424 2.06e-10

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 62.71  E-value: 2.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 204 VLTNAHSVEHYTQ--VKLkkrgSDTK-YLATVLAIGTECDIAMLTVEDDEFwkGVSPLEFGSLPALQDAVTVVGYPIG-G 279
Cdd:PRK10898   91 ILTNKHVINDADQiiVAL----QDGRvFEALLVGSDSLTDLAVLKINATNL--PVIPINPKRVPHIGDVVLAIGNPYNlG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 280 DTIsvTSGVVS---RIEILSYVHGSTellgLQIDAAINSGNSGGPAFNDKGKCVGI---AF-QSLKHEDVENIGYVIP-- 350
Cdd:PRK10898  165 QTI--TQGIISatgRIGLSPTGRQNF----LQTDASINHGNSGGALVNSLGELMGIntlSFdKSNDGETPEGIGFAIPtq 238

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002280142 351 --TPVINHFIQDYEKSGEYTGfpILGIEWQKMENPDlrkaMGMKSDQkGVRVRRVEPTAP-ESGCLQPSDIILSFDG 424
Cdd:PRK10898  239 laTKIMDKLIRDGRVIRGYIG--IGGREIAPLHAQG----GGIDQLQ-GIVVNEVSPDGPaAKAGIQVNDLIISVNN 308
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 196-355 1.69e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.76  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 196 GFIIGGHRVLTNAHSVEHYTQVKLKK---------RGSDTKYLATVLAI--------GTECDIAMLTVEDD-EFWKGVSP 257
Cdd:COG3591    16 GTLIGPNLVLTAGHCVYDGAGGGWATnivfvpgynGGPYGTATATRFRVppgwvasgDAGYDYALLRLDEPlGDTTGWLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 258 LEFGSLPALQDAVTVVGYPiGGDTISVTSGVVSRIeilsyVHGSTELLGLQIDAAinSGNSGGPAFND---KGKCVGIaf 334
Cdd:COG3591    96 LAFNDAPLAGEPVTIIGYP-GDRPKDLSLDCSGRV-----TGVQGNRLSYDCDTT--GGSSGSPVLDDsdgGGRVVGV-- 165

                         170       180
                  ....*....|....*....|.
gi 1002280142 335 QSLKHEDVENIGYVIPTPVIN 355
Cdd:COG3591   166 HSAGGADRANTGVRLTSAIVA 186
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 370-471 2.09e-07

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: 49.21  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 370 FPILGIeWQKMENPDLRKAMGMKsDQKGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDIANdgtvpfrhGERIgfSYLIS 448
Cdd:cd06779     1 RPYLGI-EMENISPLLAKELGLP-VNRGVLVAEVIPGSPaAKAGLKEGDVILSVNGKPVTS--------FNDL--RAALD 68

                          90       100
                  ....*....|....*....|...
gi 1002280142 449 QKYTGEKAHVKILRNSKVLEFNI 471
Cdd:cd06779    69 TKKPGDSLNLTILRDGKTLTVTV 91
PDZ_2 pfam13180
PDZ domain;
391-473 8.09e-06

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 44.18  E-value: 8.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 391 MKSDQKGVRVRRVEPTAP--ESGcLQPSDIILSFDGIDIANDGtvpfrhgeriGFSYLISQKYTGEKAHVKILRNSKVLE 468
Cdd:pfam13180   1 FVDLEGGVVVVSVKSSGPaaKAG-LKAGDVILSIDGRKINDLT----------DLESALYGHKPGDTVTLQVYRDGKLLT 69


                  ....*
gi 1002280142 469 FNIKL 473
Cdd:pfam13180  70 VEVKL 74
cpPDZ_BsHtra-like cd06781
circularly permuted PDZ domain of Bacillus subtilis HtrA-type serine proteases HtrA, HtrB, and ...
 370-473 3.13e-05

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: 43.01  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002280142 370 FPILGIEwqkMENPD------LRKAMGMKSDQKGVRVRRVEPTAP-ESGCLQPSDIILSFDGIDIANDGTvpFRhgeRIG 442
Cdd:cd06781     1 RPSLGIS---MVDLSdvpeyeQQSLKLPSNVNKGVYVAQVQSNSPaEKAGLKKGDVITKLDGKKVESSSD--LR---QIL 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002280142 443 FSYLIsqkytGEKAHVKILRNSKVLEFNIKL 473
Cdd:cd06781    73 YSHKV-----GDTVKVTIYRDGKEKTLNIKL 98
PDZ_densin_erbin-like cd06749
PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95) ...
 392-429 1.04e-03

PDZ domain of densin, erbin, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of densin, erbin, and related domains. Densin (also known as leucine-rich repeat-containing protein 7, LRRC7, densin-180, protein LAP1) and erbin (also known as densin-180-like protein, Erbb2-interacting protein, protein LAP2) belong to the LAP (leucine-rich repeat and PDZ domain) family of scaffolding proteins that play roles in the maintenance of cell shape and apical-basal polarity. Densin and erbin are components of the excitatory postsynaptic compartment and are regulators of dendritic morphology and postsynaptic structure. The densin PDZ domain binds CaV1.3 alpha1 subunit, delta-catenin, and MAGUIN-1. Binding partners of the erbin PDZ domain include ErbB receptor tyrosine kinase ErbB2, HTLV-1 Tax1, Cav1.3 Ca2+channels, and constituents of the cadherin:catenin cell adhesion complex, in particular delta-catenin, p0071 and ARVCF. The erbin PDZ domain binds Smad3, a transductor of the TGFbeta pathway, possibly by a novel interface of binding. Erbin and two other LAP proteins (scribble and lano) redundantly regulate epithelial polarity and apical adhesion complex. 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 densin and erbin-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: 467231 [Multi-domain]  Cd Length: 87  Bit Score: 38.46  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1002280142 392 KSDQKGVRVRRVEPTAPESGCLQPSDIILSFDGIDIAN 429
Cdd:cd06749    27 RPDDDGIFVTKVQPDGPASKLLQPGDKILEVNGYDFVN 64
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
 390-464 6.32e-03

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: 36.20  E-value: 6.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002280142  390 GMKSDQKGVRVRRVEPTAPESGC-LQPSDIILSFDGIDIANdgtvpFRHGERIgfsylISQKYTGEKAHVKILRNS 464
Cdd:smart00228  20 GGKDEGGGVVVSSVVPGSPAAKAgLRVGDVILEVNGTSVEG-----LTHLEAV-----DLLKKAGGKVTLTVLRGG 85
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
 390-429 7.27e-03

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: 35.98  E-value: 7.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002280142 390 GMKSDQKGVRVRRVEP--TAPESGCLQPSDIILSFDGIDIAN 429
Cdd:cd00136    18 GGKDGGGGIFVSRVEPggPAARDGRLRVGDRILEVNGVSLEG 59
 
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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