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Conserved domains on  [gi|1242551340|gb|ATA72148|]
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carboxyl-terminal-processing protease [Capnocytophaga sp. H4358]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
 234-451 9.34e-83

C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs of the S41 family related to C-terminal processing peptidase (CPP). CPP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. CPP is synthesized with an extension on its carboxyl-terminus and specifically recognizes a C-terminal tripeptide, but cleaves at variable distance from the C-terminus. The CPP active site consists of a serine/lysine catalytic dyad. Conservation of these residues is seen in the CPP-like proteins of this group. CPP proteins contain a PDZ domain that promotes protein-protein interactions and is important for substrate recognition however, most of CPP-like proteins only have an internal fragment or lack the PDZ domain.


:

Pssm-ID: 143477 [Multi-domain]  Cd Length: 256  Bit Score: 256.80  E-value: 9.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 234 VIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITGLSKQN-VFAKERWNDK 312
Cdd:cd07561    58 YIVDGGKKVGYLVYNSFTSGYDDELNQAFAEFKAQGVTELVLDLRYNGGGLVSSANLLASLLAPAVALGqVFATLEYNDK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 313 LQPAFKDSDITNYFadkiikegvSYPINSLSgLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKNQGSITLYD 392
Cdd:cd07561   138 RSANNEDLLFSSKT---------LAGGNSLN-LSKVYVLTSGSTASASELVINSLKPYMDVVLIGETTYGKNVGSLTFED 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1242551340 393 SpagynkkgvnPKHKWAMQPLVLKIVNKDGEGDYTSGITPNHAIEEDWANFGELGQETE 451
Cdd:cd07561   208 D----------RKHKWALQPVVFKVVNADGQGDYSNGLTPDIEVNEDSSNLLPLGDPNE 256
Pept_S41_N pfam18294
Peptidase S41 N-terminal domain; This domain is found in the N-terminal region of proteins ...
 42-112 3.26e-11

Peptidase S41 N-terminal domain; This domain is found in the N-terminal region of proteins carrying the peptidase S41 domain (Pfam: PF03572) in Bacteroidetes.


:

Pssm-ID: 436392 [Multi-domain]  Cd Length: 49  Bit Score: 58.02  E-value: 3.26e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242551340  42 QIKNFIWKGLNLYYLWQADVPNLADTRFapslmktdfnnkeyvdflkkGQAPDNFFYSLLnnYPKIDRFSF 112
Cdd:pfam18294   1 EINDFIYDGMNDWYLWNDEVPDLVDPDY--------------------YSSPEDFFDALL--YKQDDRFSY 49
cpPDZ_Deg_HtrA-like super family cl49614
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 132-211 6.18e-05

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.


The actual alignment was detected with superfamily member cd23084:

Pssm-ID: 483954 [Multi-domain]  Cd Length: 83  Bit Score: 41.46  E-value: 6.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 132 GMDFA-LSRYGTQGGVLgiVRYVLPDTDAAQKGIKRGDVFTQVDGQAltINNyrqllfndktsmVIDINRIKIvnDKPTI 210
Cdd:cd23084     5 GATVSnVTDEDGGKGVV--VTEVDPGSPAAQSGLKKGDVIIGVNRQP--VKS------------IAELRKVLK--SKPSA 66


                  .
gi 1242551340 211 V 211
Cdd:cd23084    67 V 67
 
Name Accession Description Interval E-value
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
 234-451 9.34e-83

C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs of the S41 family related to C-terminal processing peptidase (CPP). CPP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. CPP is synthesized with an extension on its carboxyl-terminus and specifically recognizes a C-terminal tripeptide, but cleaves at variable distance from the C-terminus. The CPP active site consists of a serine/lysine catalytic dyad. Conservation of these residues is seen in the CPP-like proteins of this group. CPP proteins contain a PDZ domain that promotes protein-protein interactions and is important for substrate recognition however, most of CPP-like proteins only have an internal fragment or lack the PDZ domain.


Pssm-ID: 143477 [Multi-domain]  Cd Length: 256  Bit Score: 256.80  E-value: 9.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 234 VIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITGLSKQN-VFAKERWNDK 312
Cdd:cd07561    58 YIVDGGKKVGYLVYNSFTSGYDDELNQAFAEFKAQGVTELVLDLRYNGGGLVSSANLLASLLAPAVALGqVFATLEYNDK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 313 LQPAFKDSDITNYFadkiikegvSYPINSLSgLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKNQGSITLYD 392
Cdd:cd07561   138 RSANNEDLLFSSKT---------LAGGNSLN-LSKVYVLTSGSTASASELVINSLKPYMDVVLIGETTYGKNVGSLTFED 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1242551340 393 SpagynkkgvnPKHKWAMQPLVLKIVNKDGEGDYTSGITPNHAIEEDWANFGELGQETE 451
Cdd:cd07561   208 D----------RKHKWALQPVVFKVVNADGQGDYSNGLTPDIEVNEDSSNLLPLGDPNE 256
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 80-460 5.87e-43

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: 155.41  E-value: 5.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340  80 NKEYVDFLKKGQAPDNFFYSLLNNYPkiDRFSFI--TDDYEELERTFAGQVYSSGMDFALsrygTQGGVlgIVRYVLPDT 157
Cdd:COG0793    11 RDNYVDEYDDRDLAEGALNGMLGELG--DPHSYYldPEEYEDFQESTSGEFGGLGAELGE----EDGKV--VVVSVIPGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 158 DAAQKGIKRGDVFTQVDGQAL---TINNYRQLLFNDKTSMVidinRIKIVNDKptiVSENRTVTMAKKSIKENPVHiSKV 234
Cdd:COG0793    83 PAEKAGIKPGDIILAIDGKSVaglTLDDAVKLLRGKAGTKV----TLTIKRPG---EGEPITVTLTRAEIKLPSVE-AKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 235 IEKgshKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITglsKQNVFAKERWNDKLQ 314
Cdd:COG0793   155 LEG---KIGYIRIPSFGENTAEEFKRALKELKKQGAKGLILDLRNNPGGLLDEAVELADLFL---PKGPIVYTRGRNGKV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 315 PAFKDSDITNYFAdkiikegvsypinslsglKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKN--QGSITLYD 392
Cdd:COG0793   229 ETYKATPGGALYD------------------GPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGsvQTVFPLPD 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242551340 393 SPagynkkgvnpkhkwAMQPLVLKIVNKDGEGDYTSGITPNHAIEEDwanFGELGQETEPFLAKALEL 460
Cdd:COG0793   291 GG--------------ALKLTTARYYTPSGRSIQGKGVEPDIEVPLT---PEDLLKGRDPQLEKALEL 341
Peptidase_S41 pfam03572
Peptidase family S41;
241-404 6.24e-17

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 78.03  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 241 KVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITGlskqnvfakerwnDKLQPAFKDS 320
Cdd:pfam03572   1 KIGYIRIPSFSEKTAKELAEALKELKKQGVKGLILDLRGNPGGLLSAAVEIASLFLP-------------DGTIVSTRGR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 321 DITNYfadkiiKEGVSYPINSLSGLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKN--QGSITLYD------ 392
Cdd:pfam03572  68 DGSKE------VYFAAGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGtvQTVYPLPDgsalkl 141

                         170       180
                  ....*....|....*....|
gi 1242551340 393 ------SPAGY--NKKGVNP 404
Cdd:pfam03572 142 tiakyyTPDGRsiEGKGIEP 161
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
 145-404 1.22e-14

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 75.09  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 145 GVLGIVRyVLPDTDAAQKGIKRGDVFTQVDGQ---ALTINNYRQLLFNDK-TSMVIDINRIKivndKPTIVSENRTvtma 220
Cdd:TIGR00225  62 GKIVIVS-PFEGSPAEKAGIKPGDKIIKINGKsvaGMSLDDAVALIRGKKgTKVSLEILRAG----KSKPLSFTLK---- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 221 KKSIKENPVHiSKVIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMItgLSK 300
Cdd:TIGR00225 133 RDRIELETVK-ASVKKVGGHSVGYIRISSFSEHTAEDVAKALDKLEKKNAKGYILDLRGNPGGLLQSAVDISRLF--ITK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 301 QNVfakerwndkLQPAFKDSDITNYFADKiiKEGVSYPINslsglkriyILTTERTASASELVINGLKPYIEVIQIGGTT 380
Cdd:TIGR00225 210 GPI---------VQTKDRNGSKRHYKANG--RQKYNLPLV---------VLVNRGSASASEILAGALQDNGRATIVGEKT 269

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1242551340 381 TGK---------NQGS---ITL--YDSPAGY--NKKGVNP 404
Cdd:TIGR00225 270 FGKgtvqqvrplNDGSgikVTIakYYTPNGGsiHKKGIEP 309
TSPc smart00245
tail specific protease; tail specific protease
 212-404 8.85e-14

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 69.98  E-value: 8.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340  212 SENRTVTMAKKSIKENPVhISKVIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYL 291
Cdd:smart00245   1 SKERTIALIRDKIKIETL-EGNVGYLRFGFIGYIRIPEFSEHTSNLVEKAWKKLEKTNVEGLILDLRNNPGGLLSAAIDV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340  292 ASMitglskqnvfakerwndklqpaFKDSDITNYFADKIIKEGVSYPINSLSGLKR-IYILTTERTASASELVINGLKPY 370
Cdd:smart00245  80 SSL----------------------FLDKGVIVYTVYRRTGELWTYPANLGRKYSKpLVVLVNKGTASASEIFAGALKDL 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1242551340  371 IEVIQIGGTTTGK--NQGSITLYD------------SPAG--YNKKGVNP 404
Cdd:smart00245 138 GRATIVGERTFGKglVQQTVPLGDgsglkltvakyyTPSGksIEKKGVEP 187
Pept_S41_N pfam18294
Peptidase S41 N-terminal domain; This domain is found in the N-terminal region of proteins ...
 42-112 3.26e-11

Peptidase S41 N-terminal domain; This domain is found in the N-terminal region of proteins carrying the peptidase S41 domain (Pfam: PF03572) in Bacteroidetes.


Pssm-ID: 436392 [Multi-domain]  Cd Length: 49  Bit Score: 58.02  E-value: 3.26e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242551340  42 QIKNFIWKGLNLYYLWQADVPNLADTRFapslmktdfnnkeyvdflkkGQAPDNFFYSLLnnYPKIDRFSF 112
Cdd:pfam18294   1 EINDFIYDGMNDWYLWNDEVPDLVDPDY--------------------YSSPEDFFDALL--YKQDDRFSY 49
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
 117-424 4.73e-10

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 61.29  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 117 YEELERTFAGQVYSSGMDFAlsrYGTQGGVLGIVRYVL---PDTDAAQKGIKRGDVFTQVDG---QALTINNYRQLLFND 190
Cdd:PLN00049   73 FKSLRSGTKGAVTGVGLEVG---YPTGSDGPPAGLVVVapaPGGPAARAGIRPGDVILAIDGtstEGLSLYEAADRLQGP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 191 KTSMVidinrikivndKPTIVS--ENRTVTMAKKSIKENPVH----ISKVIEKGSHKVGYLMYNSFVADFDLQLNEAFGM 264
Cdd:PLN00049  150 EGSSV-----------ELTLRRgpETRLVTLTREKVSLNPVKsrlcEVPGPGAGSPKIGYIKLTTFNQNASSAVKEAIET 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 265 FKSQVINDLVLDLRYNGGGRISSAVYLASMitglskqnvfakerWNDKLQPAF-KDS----DItnYFADKIIKEGVSYPI 339
Cdd:PLN00049  219 LRANGVDAFVLDLRDNSGGLFPAGIEIAKL--------------WLDKGVIVYiADSrgvrDI--YDADGSSAIATSEPL 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 340 NslsglkriyILTTERTASASELVINGLKPYIEVIQIGGTTTGK---------NQGS---ITL--YDSPAG--YNKKGVN 403
Cdd:PLN00049  283 A---------VLVNKGTASASEILAGALKDNKRAVVLGEPTFGKgliqsvfelSDGSglaVTVarYQTPAGtdIDKVGIT 353

                         330       340
                  ....*....|....*....|.
gi 1242551340 404 PKHkwamqPLVlKIVNKDGEG 424
Cdd:PLN00049  354 PDH-----PLP-ESLPKDEEA 368
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 132-211 6.18e-05

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: 41.46  E-value: 6.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 132 GMDFA-LSRYGTQGGVLgiVRYVLPDTDAAQKGIKRGDVFTQVDGQAltINNyrqllfndktsmVIDINRIKIvnDKPTI 210
Cdd:cd23084     5 GATVSnVTDEDGGKGVV--VTEVDPGSPAAQSGLKKGDVIIGVNRQP--VKS------------IAELRKVLK--SKPSA 66


                  .
gi 1242551340 211 V 211
Cdd:cd23084    67 V 67
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 149-200 6.98e-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: 40.59  E-value: 6.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242551340 149 IVRYVLPDTDAAQKGIKRGDVFTQVDGQAL-TINNYRQLLFND-KTSMVIDINR 200
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVrSLEDVARLLQGSaGESVTLTVRR 54
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 141-187 1.70e-04

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: 43.21  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1242551340 141 GTQGGVLgiVRYVLPDTDAAQKGIKRGDVFTQVDGQalTINNYRQLL 187
Cdd:COG0265   198 PEPEGVL--VARVEPGSPAAKAGLRPGDVILAVDGK--PVTSARDLQ 240
 
Name Accession Description Interval E-value
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
 234-451 9.34e-83

C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs of the S41 family related to C-terminal processing peptidase (CPP). CPP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. CPP is synthesized with an extension on its carboxyl-terminus and specifically recognizes a C-terminal tripeptide, but cleaves at variable distance from the C-terminus. The CPP active site consists of a serine/lysine catalytic dyad. Conservation of these residues is seen in the CPP-like proteins of this group. CPP proteins contain a PDZ domain that promotes protein-protein interactions and is important for substrate recognition however, most of CPP-like proteins only have an internal fragment or lack the PDZ domain.


Pssm-ID: 143477 [Multi-domain]  Cd Length: 256  Bit Score: 256.80  E-value: 9.34e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 234 VIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITGLSKQN-VFAKERWNDK 312
Cdd:cd07561    58 YIVDGGKKVGYLVYNSFTSGYDDELNQAFAEFKAQGVTELVLDLRYNGGGLVSSANLLASLLAPAVALGqVFATLEYNDK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 313 LQPAFKDSDITNYFadkiikegvSYPINSLSgLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKNQGSITLYD 392
Cdd:cd07561   138 RSANNEDLLFSSKT---------LAGGNSLN-LSKVYVLTSGSTASASELVINSLKPYMDVVLIGETTYGKNVGSLTFED 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1242551340 393 SpagynkkgvnPKHKWAMQPLVLKIVNKDGEGDYTSGITPNHAIEEDWANFGELGQETE 451
Cdd:cd07561   208 D----------RKHKWALQPVVFKVVNADGQGDYSNGLTPDIEVNEDSSNLLPLGDPNE 256
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 80-460 5.87e-43

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: 155.41  E-value: 5.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340  80 NKEYVDFLKKGQAPDNFFYSLLNNYPkiDRFSFI--TDDYEELERTFAGQVYSSGMDFALsrygTQGGVlgIVRYVLPDT 157
Cdd:COG0793    11 RDNYVDEYDDRDLAEGALNGMLGELG--DPHSYYldPEEYEDFQESTSGEFGGLGAELGE----EDGKV--VVVSVIPGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 158 DAAQKGIKRGDVFTQVDGQAL---TINNYRQLLFNDKTSMVidinRIKIVNDKptiVSENRTVTMAKKSIKENPVHiSKV 234
Cdd:COG0793    83 PAEKAGIKPGDIILAIDGKSVaglTLDDAVKLLRGKAGTKV----TLTIKRPG---EGEPITVTLTRAEIKLPSVE-AKL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 235 IEKgshKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITglsKQNVFAKERWNDKLQ 314
Cdd:COG0793   155 LEG---KIGYIRIPSFGENTAEEFKRALKELKKQGAKGLILDLRNNPGGLLDEAVELADLFL---PKGPIVYTRGRNGKV 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 315 PAFKDSDITNYFAdkiikegvsypinslsglKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKN--QGSITLYD 392
Cdd:COG0793   229 ETYKATPGGALYD------------------GPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGsvQTVFPLPD 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242551340 393 SPagynkkgvnpkhkwAMQPLVLKIVNKDGEGDYTSGITPNHAIEEDwanFGELGQETEPFLAKALEL 460
Cdd:COG0793   291 GG--------------ALKLTTARYYTPSGRSIQGKGVEPDIEVPLT---PEDLLKGRDPQLEKALEL 341
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
 242-437 1.90e-28

C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing peptidase or CTPase family) contains very different subfamilies; it includes photosystem II D1 C-terminal processing protease (CTPase), interphotoreceptor retinoid-binding protein IRBP and tricorn protease (TRI). CTPase and TRI both contain the PDZ domain while IRBP, although being very similar to the tail-specific protease domain, lacks the PDZ insertion domain and hydrolytic activity. These serine proteases have distinctly different active sites: in CTPase, the active site consists of a serine/lysine catalytic dyad while in tricorn core protease, it is a tetrad (serine, histidine, serine, glutamate). CPases with different substrate specificities in different species include processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein; and others such as tricorn protease (TRI) act as a carboxypeptidase, involved in the degradation of proteasomal products. CTPase homolog IRBP, secreted by photoreceptors into the interphotoreceptor matrix, having arisen in the early evolution of the vertebrate eye, promotes the release of all-trans retinol from photoreceptors and facilitates its delivery to the retinal pigment epithelium.


Pssm-ID: 143475 [Multi-domain]  Cd Length: 224  Bit Score: 112.39  E-value: 1.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 242 VGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITGlSKQNVFAKERWNDKLQPAFKDSD 321
Cdd:cd06567    61 IGYIRIPSFSAESTAEELREALAELKKGVKGLILDLRNNPGGLLSAAVELASLFLP-KGKIVVTTRRRGGNETEYVAPGG 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 322 ITNYfadkiikegvsypinslsgLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKNqGSITLYDSPAGynkkg 401
Cdd:cd06567   140 GSLY-------------------DGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKG-SVQTVFPLLDG----- 194

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1242551340 402 vnpkhkWAMQPLVLKIVNKDGEGDYTSGITPNHAIE 437
Cdd:cd06567   195 ------SALKLTTAKYYTPSGRSIEGKGVEPDIEVP 224
Peptidase_S41 pfam03572
Peptidase family S41;
241-404 6.24e-17

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 78.03  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 241 KVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMITGlskqnvfakerwnDKLQPAFKDS 320
Cdd:pfam03572   1 KIGYIRIPSFSEKTAKELAEALKELKKQGVKGLILDLRGNPGGLLSAAVEIASLFLP-------------DGTIVSTRGR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 321 DITNYfadkiiKEGVSYPINSLSGLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTGKN--QGSITLYD------ 392
Cdd:pfam03572  68 DGSKE------VYFAAGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGtvQTVYPLPDgsalkl 141

                         170       180
                  ....*....|....*....|
gi 1242551340 393 ------SPAGY--NKKGVNP 404
Cdd:pfam03572 142 tiakyyTPDGRsiEGKGIEP 161
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
 145-404 1.22e-14

C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different species including processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein in E.coli E.coli and H influenza have the most distal branch of the tree and their proteins have an N-terminal 200 amino acids that show no homology to other proteins in the database. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Protein fate, Protein modification and repair]


Pssm-ID: 272970 [Multi-domain]  Cd Length: 334  Bit Score: 75.09  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 145 GVLGIVRyVLPDTDAAQKGIKRGDVFTQVDGQ---ALTINNYRQLLFNDK-TSMVIDINRIKivndKPTIVSENRTvtma 220
Cdd:TIGR00225  62 GKIVIVS-PFEGSPAEKAGIKPGDKIIKINGKsvaGMSLDDAVALIRGKKgTKVSLEILRAG----KSKPLSFTLK---- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 221 KKSIKENPVHiSKVIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMItgLSK 300
Cdd:TIGR00225 133 RDRIELETVK-ASVKKVGGHSVGYIRISSFSEHTAEDVAKALDKLEKKNAKGYILDLRGNPGGLLQSAVDISRLF--ITK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 301 QNVfakerwndkLQPAFKDSDITNYFADKiiKEGVSYPINslsglkriyILTTERTASASELVINGLKPYIEVIQIGGTT 380
Cdd:TIGR00225 210 GPI---------VQTKDRNGSKRHYKANG--RQKYNLPLV---------VLVNRGSASASEILAGALQDNGRATIVGEKT 269

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1242551340 381 TGK---------NQGS---ITL--YDSPAGY--NKKGVNP 404
Cdd:TIGR00225 270 FGKgtvqqvrplNDGSgikVTIakYYTPNGGsiHKKGIEP 309
TSPc smart00245
tail specific protease; tail specific protease
 212-404 8.85e-14

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 69.98  E-value: 8.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340  212 SENRTVTMAKKSIKENPVhISKVIEKGSHKVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYL 291
Cdd:smart00245   1 SKERTIALIRDKIKIETL-EGNVGYLRFGFIGYIRIPEFSEHTSNLVEKAWKKLEKTNVEGLILDLRNNPGGLLSAAIDV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340  292 ASMitglskqnvfakerwndklqpaFKDSDITNYFADKIIKEGVSYPINSLSGLKR-IYILTTERTASASELVINGLKPY 370
Cdd:smart00245  80 SSL----------------------FLDKGVIVYTVYRRTGELWTYPANLGRKYSKpLVVLVNKGTASASEIFAGALKDL 137

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1242551340  371 IEVIQIGGTTTGK--NQGSITLYD------------SPAG--YNKKGVNP 404
Cdd:smart00245 138 GRATIVGERTFGKglVQQTVPLGDgsglkltvakyyTPSGksIEKKGVEP 187
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 242-382 3.91e-12

Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor retinoid-binding protein (IRBP) is a homolog of the S41 protease, C-terminal processing peptidase (CTPase) family. It is thought to facilitate the compartmentalization of the visual cycle that requires poorly soluble and potentially toxic retinoids to cross the aqueous subretinal space between the photoreceptors and the retinal pigment epithelium (RPE). IRBP is secreted by photoreceptors into the interphotoreceptor matrix (IPM) where it is rapidly turned over by a combination of RPE and photoreceptor endocytosis. It is the most abundant soluble protein component of the IPM, consisting of homologous modules, each repeat structure arising through the duplication (as in teleost IRBP) or quadruplication (in tetrapods) of an ancient gene, arisen in the early evolution of the vertebrate eye. IRBP has been shown to promote the release of all-trans retinol from photoreceptors and facilitates its delivery to the RPE. Conversely, IRBP can promote the release of 11-cis-retinal from the RPE, prevent its isomerization in the subretinal space, and transfer it to photoreceptors. In vivo evidence implicates IRBP as a retinoid transporter in the visual cycle, suggesting a critical role for IRBP in cone function essential for human vision. IRBP is a dominant autoimmune antigen in the eye; IRBP proteolysis analysis has proven a useful biomarker for autoimmune uveitis (AU) disorders, a major cause of blindness. This family also includes a chlamydia-secreted protein, designated chlamydia protease-like activity factor (CPAF), known to degrade host proteins, enabling Chlamydia to evade host defenses and replicate.


Pssm-ID: 143479 [Multi-domain]  Cd Length: 250  Bit Score: 66.16  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 242 VGYLMYNSFVADFDLQLNEAFGMFKSQVIND--LVLDLRYNGGGRISSAVYLASMITGlSKQNVFAKERWNdklQPAFKD 319
Cdd:cd07563    65 IGYLRIDSFGGFEIAAAEALLDEALDKLADTdaLIIDLRYNGGGSDSLVAYLASYFTD-EDKPVHLYTIYK---RPGNTT 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1242551340 320 SDITNYFadKIIKEGVSYpinslsgLKRIYILTTERTASASELVINGLKPYIEVIQIGGTTTG 382
Cdd:cd07563   141 TELWTLP--VVPGGRYGY-------TKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAG 194
Pept_S41_N pfam18294
Peptidase S41 N-terminal domain; This domain is found in the N-terminal region of proteins ...
 42-112 3.26e-11

Peptidase S41 N-terminal domain; This domain is found in the N-terminal region of proteins carrying the peptidase S41 domain (Pfam: PF03572) in Bacteroidetes.


Pssm-ID: 436392 [Multi-domain]  Cd Length: 49  Bit Score: 58.02  E-value: 3.26e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242551340  42 QIKNFIWKGLNLYYLWQADVPNLADTRFapslmktdfnnkeyvdflkkGQAPDNFFYSLLnnYPKIDRFSF 112
Cdd:pfam18294   1 EINDFIYDGMNDWYLWNDEVPDLVDPDY--------------------YSSPEDFFDALL--YKQDDRFSY 49
PLN00049 PLN00049
carboxyl-terminal processing protease; Provisional
 117-424 4.73e-10

carboxyl-terminal processing protease; Provisional


Pssm-ID: 177681 [Multi-domain]  Cd Length: 389  Bit Score: 61.29  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 117 YEELERTFAGQVYSSGMDFAlsrYGTQGGVLGIVRYVL---PDTDAAQKGIKRGDVFTQVDG---QALTINNYRQLLFND 190
Cdd:PLN00049   73 FKSLRSGTKGAVTGVGLEVG---YPTGSDGPPAGLVVVapaPGGPAARAGIRPGDVILAIDGtstEGLSLYEAADRLQGP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 191 KTSMVidinrikivndKPTIVS--ENRTVTMAKKSIKENPVH----ISKVIEKGSHKVGYLMYNSFVADFDLQLNEAFGM 264
Cdd:PLN00049  150 EGSSV-----------ELTLRRgpETRLVTLTREKVSLNPVKsrlcEVPGPGAGSPKIGYIKLTTFNQNASSAVKEAIET 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 265 FKSQVINDLVLDLRYNGGGRISSAVYLASMitglskqnvfakerWNDKLQPAF-KDS----DItnYFADKIIKEGVSYPI 339
Cdd:PLN00049  219 LRANGVDAFVLDLRDNSGGLFPAGIEIAKL--------------WLDKGVIVYiADSrgvrDI--YDADGSSAIATSEPL 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 340 NslsglkriyILTTERTASASELVINGLKPYIEVIQIGGTTTGK---------NQGS---ITL--YDSPAG--YNKKGVN 403
Cdd:PLN00049  283 A---------VLVNKGTASASEILAGALKDNKRAVVLGEPTFGKgliqsvfelSDGSglaVTVarYQTPAGtdIDKVGIT 353

                         330       340
                  ....*....|....*....|.
gi 1242551340 404 PKHkwamqPLVlKIVNKDGEG 424
Cdd:PLN00049  354 PDH-----PLP-ESLPKDEEA 368
Peptidase_S41_CPP cd07560
C-terminal processing peptidase; serine protease family S41; The C-terminal processing ...
 241-404 8.06e-09

C-terminal processing peptidase; serine protease family S41; The C-terminal processing peptidase (CPP, EC 3.4.21.102) also known as tail-specific protease (tsp), the photosystem II D1 C-terminal processing protease (D1P), and other related S41 protease family members are present in this CD. CPP is synthesized as a precursor form with a carboxyl-terminal extension. It specifically recognizes a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. The C-terminal carboxylate group is essential, and proteins where this group is amidated are not substrates. This family of proteases contains the PDZ domain that promotes protein-protein interactions and is important for substrate recognition. The active site consists of a serine/lysine catalytic dyad. The bacterial CCP-1 is believed to be important for the degradation of incorrectly synthesized proteins as well as protection from thermal and osmotic stresses. In E. coli, it is involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II, allowing the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.


Pssm-ID: 143476 [Multi-domain]  Cd Length: 211  Bit Score: 55.88  E-value: 8.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 241 KVGYLMYNSFVADFDLQLNEAFGMFKSQVINDLVLDLRYNGGGRISSAVYLASMItgLSKQNVFA-KERWNDKLQPAFKD 319
Cdd:cd07560    49 PIGYIRITSFSENTAEELKKALKELKKQGMKGLILDLRNNPGGLLDEAVEIADLF--LPGGPIVStKGRNGKREAYASDD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 320 SDITNyfadkiikegvsYPinslsglkrIYILTTERTASASELVINGLKPYIEVIQIGGTTTGK----------NQGSIT 389
Cdd:cd07560   127 GGLYD------------GP---------LVVLVNGGSASASEIVAGALQDNGRAVLVGERTFGKgsvqtvfplsDGSALK 185

                         170       180
                  ....*....|....*....|.
gi 1242551340 390 L----YDSPAGY--NKKGVNP 404
Cdd:cd07560   186 LttakYYTPSGRsiQKKGIEP 206
cpPDZ2_DegP-like cd23084
circularly permuted second PDZ domain (PDZ2) of Escherichia coli periplasmic serine ...
 132-211 6.18e-05

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: 41.46  E-value: 6.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 132 GMDFA-LSRYGTQGGVLgiVRYVLPDTDAAQKGIKRGDVFTQVDGQAltINNyrqllfndktsmVIDINRIKIvnDKPTI 210
Cdd:cd23084     5 GATVSnVTDEDGGKGVV--VTEVDPGSPAAQSGLKKGDVIIGVNRQP--VKS------------IAELRKVLK--SKPSA 66


                  .
gi 1242551340 211 V 211
Cdd:cd23084    67 V 67
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
 149-200 6.98e-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: 40.59  E-value: 6.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242551340 149 IVRYVLPDTDAAQKGIKRGDVFTQVDGQAL-TINNYRQLLFND-KTSMVIDINR 200
Cdd:pfam17820   1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVrSLEDVARLLQGSaGESVTLTVRR 54
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
 233-362 1.09e-04

Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 peptidase family and named for its tricorn-like shape, exists only in some archaea and eubacteria. It has been shown to act as a carboxypeptidase, involved in the degradation of proteasomal products to preferentially yield di- and tripeptides, with subsequent and final degradations to free amino acid residues by tricorn interacting factors, F1, F2 and F3. Tricorn is a hexameric D3-symmetric protease of 720kD, and can self-associate further into a giant icosahedral capsid structure containing twenty copies of the complex. Each tricorn peptidase monomer consists of five structural domains: a six-bladed beta-propeller and a seven-bladed beta-propeller that limit access to the active site, the two domains (C1 and C2) that carry the active site residues, and a PDZ-like domain (proposed to be important for substrate recognition) between the C1 and C2 domains. The active site tetrad residues are distributed between the C1 and C2 domains, with serine and histidine on C1 and serine and glutamate on C2.


Pssm-ID: 143478 [Multi-domain]  Cd Length: 266  Bit Score: 44.11  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 233 KVIEKGSH-KVGYLMYNSFVADfdlQLNEAFGMFKSQVIND-LVLDLRYNGGGRISSavYLASMITGlskqnvfakerwn 310
Cdd:cd07562    79 EYVEELSDgRIGYVHIPDMGDD---GFAEFLRDLLAEVDKDgLIIDVRFNGGGNVAD--LLLDFLSR------------- 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242551340 311 dklqpafkdsDITNYFADKIIKEGVSYPINSLSGlkRIYILTTERTASASEL 362
Cdd:cd07562   141 ----------RRYGYDIPRGGGKPVTYPSGRWRG--PVVVLVNEGSASDAEI 180
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 141-187 1.70e-04

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: 43.21  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1242551340 141 GTQGGVLgiVRYVLPDTDAAQKGIKRGDVFTQVDGQalTINNYRQLL 187
Cdd:COG0265   198 PEPEGVL--VARVEPGSPAAKAGLRPGDVILAVDGK--PVTSARDLQ 240
PRK11186 PRK11186
carboxy terminal-processing peptidase;
201-298 3.35e-04

carboxy terminal-processing peptidase;


Pssm-ID: 236873 [Multi-domain]  Cd Length: 667  Bit Score: 43.34  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242551340 201 IKIVNDKptIVSENRTVTMakksikenpvhisKVIEKGSHKVGYL----MYNSFVADFDLQLNEafgmFKSQVINDLVLD 276
Cdd:PRK11186  329 VTLTRDK--IRLEDRAVKM-------------SVKTVGGEKVGVLdipgFYVGLTDDVKKQLQK----LEKQNVSGIIID 389

                          90       100
                  ....*....|....*....|..
gi 1242551340 277 LRYNGGGRISSAVYLasmiTGL 298
Cdd:PRK11186  390 LRGNGGGALTEAVSL----SGL 407
cpPDZ_HhoA-like cd10838
circularly permuted PDZ domain of Synechocystis sp. PCC 6803 putative serine proteases HhoA, ...
 145-179 6.76e-04

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: 39.22  E-value: 6.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1242551340 145 GVLgIVRyVLPDTDAAQKGIKRGDVFTQVDGQALT 179
Cdd:cd10838    34 GVL-IMQ-VLPNSPAARAGLRRGDVIQAVDGQPVT 66
cpPDZ_Deg_HtrA-like cd06779
permuted PDZ domain of Deg/high-temperature requirement factor A (HtrA) family of housekeeping ...
 142-179 1.58e-03

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: 37.66  E-value: 1.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1242551340 142 TQGGVLgiVRYVLPDTDAAQKGIKRGDVFTQVDGQALT 179
Cdd:cd06779    23 VNRGVL--VAEVIPGSPAAKAGLKEGDVILSVNGKPVT 58
 
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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