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Conserved domains on  [gi|405133449|gb|AFS17532|]
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interphotoreceptor retinoid binding protein, partial [Rhea pennata]

Protein Classification

interphotoreceptor retinoid-binding protein( domain architecture ID 10166016)

interphotoreceptor retinoid-binding protein (IRBP) is a large glycoprotein known to bind retinoids and found primarily in the interphotoreceptor matrix of the retina between the retinal pigment epithelium and the photoreceptor cells

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
1-277 1.30e-73

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: 237.19  E-value: 1.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   1 YPENLVGMQEAIEQAIKSGEILDISDPKRLASVLTAGVQgALNDPRLVISYepsphaapkqdaedsptreqllsliehvv 80
Cdd:cd07563   15 FPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQ-ELGDGHLNVSY----------------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  81 mydklegnVGYLRIDYIIGQEvvQKVGAFLVDKVWKTLIDTSALVIDLRHSTGGQISGLPFIISYLHEADKVLHIETVYN 160
Cdd:cd07563   65 --------IGYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 161 RPSNTTTEIWTLPKVLGERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGSLDIKKMRIgPSNFYLMVP 240
Cdd:cd07563  135 RPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPL-PNGLYLTVP 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 405133449 241 VSRSVSPLTggGQSWEVSGVMPCVATEADQALQKSLD 277
Cdd:cd07563  214 TSRSVDPIT--GTNWEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
288-584 1.87e-64

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: 212.92  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 288 TLSKLTAILKDNYSLVE----RVPVLLQHLTTFDFSSVQSAEDLATKLNTEMQTLsEDPRLLVRVmmpgeavsppaekpv 363
Cdd:cd07563    1 VFEALAKLLEENYAFPEakgiDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSY--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 364 aaaanlpdneqflhalvdtvfkvsvlagnVGYMRFDEFADASVlaKLGPYIVHKVWEPLQNTENLIMDLRYNPGGpSSSA 443
Cdd:cd07563   65 -----------------------------IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGG-SDSL 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 444 VPLLLSYFQDpAAGPVHLFTTYDRCTNHTQEHNSQAELLGQPYGAQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEI 523
Cdd:cd07563  113 VAYLASYFTD-EDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGET 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405133449 524 TAGSLSHTRTFPLlqpkqgiTHGLTITVPVITFIDNH-GESWMGGGVVPDAIVLA----EDALQKA 584
Cdd:cd07563  192 TAGGASPVLPFPL-------PNGLYLTVPTSRSVDPItGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
577-656 7.44e-29

N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at the N-terminus of the functional unit of interphotoreceptor retinoid binding proteins 3, IRBP, in eukaryotes. From the structure of PDB:1j7x, the domain forms the N-terminal end of the module which is characterized as a serine-peptidase, pfam03572. Peptidase_S41_N forms a three-helix bundle followed by a small beta strand and is termed domain A. Part of the peptidase domain folds back over domain A to create a largely hydrophobic cleft between the two domains. On binding of ligand domain A is structurally rearranged with respect to domain B.


:

Pssm-ID: 463396  Cd Length: 129  Bit Score: 111.65  E-value: 7.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  577 AEDALQKAEEVLTFHRNMGILVEATGQLLEAHYAIPEVAGKASVMLSTKQAHGGYRSAVDFETLASQLTSDLQEASGDHR 656
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPR 80
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
1-277 1.30e-73

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: 237.19  E-value: 1.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   1 YPENLVGMQEAIEQAIKSGEILDISDPKRLASVLTAGVQgALNDPRLVISYepsphaapkqdaedsptreqllsliehvv 80
Cdd:cd07563   15 FPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQ-ELGDGHLNVSY----------------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  81 mydklegnVGYLRIDYIIGQEvvQKVGAFLVDKVWKTLIDTSALVIDLRHSTGGQISGLPFIISYLHEADKVLHIETVYN 160
Cdd:cd07563   65 --------IGYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 161 RPSNTTTEIWTLPKVLGERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGSLDIKKMRIgPSNFYLMVP 240
Cdd:cd07563  135 RPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPL-PNGLYLTVP 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 405133449 241 VSRSVSPLTggGQSWEVSGVMPCVATEADQALQKSLD 277
Cdd:cd07563  214 TSRSVDPIT--GTNWEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
288-584 1.87e-64

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: 212.92  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 288 TLSKLTAILKDNYSLVE----RVPVLLQHLTTFDFSSVQSAEDLATKLNTEMQTLsEDPRLLVRVmmpgeavsppaekpv 363
Cdd:cd07563    1 VFEALAKLLEENYAFPEakgiDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSY--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 364 aaaanlpdneqflhalvdtvfkvsvlagnVGYMRFDEFADASVlaKLGPYIVHKVWEPLQNTENLIMDLRYNPGGpSSSA 443
Cdd:cd07563   65 -----------------------------IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGG-SDSL 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 444 VPLLLSYFQDpAAGPVHLFTTYDRCTNHTQEHNSQAELLGQPYGAQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEI 523
Cdd:cd07563  113 VAYLASYFTD-EDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGET 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405133449 524 TAGSLSHTRTFPLlqpkqgiTHGLTITVPVITFIDNH-GESWMGGGVVPDAIVLA----EDALQKA 584
Cdd:cd07563  192 TAGGASPVLPFPL-------PNGLYLTVPTSRSVDPItGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
268-389 2.99e-44

N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at the N-terminus of the functional unit of interphotoreceptor retinoid binding proteins 3, IRBP, in eukaryotes. From the structure of PDB:1j7x, the domain forms the N-terminal end of the module which is characterized as a serine-peptidase, pfam03572. Peptidase_S41_N forms a three-helix bundle followed by a small beta strand and is termed domain A. Part of the peptidase domain folds back over domain A to create a largely hydrophobic cleft between the two domains. On binding of ligand domain A is structurally rearranged with respect to domain B.


Pssm-ID: 463396  Cd Length: 129  Bit Score: 154.40  E-value: 2.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  268 ADQALQKSLDILAVRRAVPGTLSKLTAILKDNYSLVERVPVLLQHLTTF----DFSSVQSAEDLATKLNTEMQTLSEDPR 343
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 405133449  344 LLVRVMMPGEAVSPP--AEKPVAAAANLPDNEQFLHALVDTVFKVSVL 389
Cdd:pfam11918  81 LKVRYIRPEPASDEPeaADNIPGLVPMQPPSPEMLEALIKSSFKVDVL 128
TSPc smart00245
tail specific protease; tail specific protease
378-575 1.20e-43

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 155.11  E-value: 1.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   378 ALVDTVFKVSVLAGNVGYMRFDeFADASVLAKLGP---YIVHKVWEPLQNT--ENLIMDLRYNPGGPSSSAVpLLLSYFQ 452
Cdd:smart00245   7 ALIRDKIKIETLEGNVGYLRFG-FIGYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAI-DVSSLFL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   453 DPAagpVHLFTTYDRctnhTQEHNSQAELLGQPYgaQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTR 532
Cdd:smart00245  85 DKG---VIVYTVYRR----TGELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKGLVQQ 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 405133449   533 TFPLlqpkqGITHGLTITVPVitFIDNHGESWMGGGVVPDAIV 575
Cdd:smart00245 156 TVPL-----GDGSGLKLTVAK--YYTPSGKSIEKKGVEPDIQV 191
TSPc smart00245
tail specific protease; tail specific protease
68-267 2.86e-41

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 148.56  E-value: 2.86e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449    68 TREQLLSLIEHVVMYDKLEGNVGYLRIdYIIGQEVVQKVG---AFLVDKVWKTLIDT--SALVIDLRHSTGGQISGLPFI 142
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRF-GFIGYIRIPEFSehtSNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   143 ISYLHEADkvLHIETVYNRpsntTTEIWTLPKVLGERYSKDkdVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGS 222
Cdd:smart00245  80 SSLFLDKG--VIVYTVYRR----TGELWTYPANLGRKYSKP--LVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 405133449   223 LDIKKMRIGpSNFYLMVPVSRSVSPltgGGQSWEVSGVMPCVATE 267
Cdd:smart00245 152 LVQQTVPLG-DGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
577-656 7.44e-29

N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at the N-terminus of the functional unit of interphotoreceptor retinoid binding proteins 3, IRBP, in eukaryotes. From the structure of PDB:1j7x, the domain forms the N-terminal end of the module which is characterized as a serine-peptidase, pfam03572. Peptidase_S41_N forms a three-helix bundle followed by a small beta strand and is termed domain A. Part of the peptidase domain folds back over domain A to create a largely hydrophobic cleft between the two domains. On binding of ligand domain A is structurally rearranged with respect to domain B.


Pssm-ID: 463396  Cd Length: 129  Bit Score: 111.65  E-value: 7.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  577 AEDALQKAEEVLTFHRNMGILVEATGQLLEAHYAIPEVAGKASVMLSTKQAHGGYRSAVDFETLASQLTSDLQEASGDHR 656
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPR 80
Peptidase_S41 pfam03572
Peptidase family S41;
392-575 8.52e-27

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 106.92  E-value: 8.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  392 NVGYMRFDEFAdasvlaKLGPYIVHKVWEPL--QNTENLIMDLRYNPGGPSSSAVpLLLSYFQDPaaGPVhlFTTYDRCT 469
Cdd:pfam03572   1 KIGYIRIPSFS------EKTAKELAEALKELkkQGVKGLILDLRGNPGGLLSAAV-EIASLFLPD--GTI--VSTRGRDG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  470 NHTQEHnsqAELLGQPYGAQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTRTFPLlqpkqgiTHGLTI 549
Cdd:pfam03572  70 SKEVYF---AAGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPL-------PDGSAL 139
                         170       180
                  ....*....|....*....|....*.
gi 405133449  550 TVPVITFIDNHGESWMGGGVVPDAIV 575
Cdd:pfam03572 140 KLTIAKYYTPDGRSIEGKGIEPDIEV 165
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
385-587 6.32e-18

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: 85.69  E-value: 6.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 385 KVSVLAGNVGYMRFDEFADASV------LAKLGPyivhkvweplQNTENLIMDLRYNPGGPSSSAVPLLlSYFQDpaAGP 458
Cdd:COG0793  151 EAKLLEGKIGYIRIPSFGENTAeefkraLKELKK----------QGAKGLILDLRNNPGGLLDEAVELA-DLFLP--KGP 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 459 VhlFTTYDRctnhtqeHNSQAELLGQPYGAQRG--IYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTRTFPL 536
Cdd:COG0793  218 I--VYTRGR-------NGKVETYKATPGGALYDgpLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSVQTVFPL 288
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405133449 537 lqpkqgiTHGLTITVPVITFIDNHGESWMGGGVVPDaIVLAEDA----------LQKAEEV 587
Cdd:COG0793  289 -------PDGGALKLTTARYYTPSGRSIQGKGVEPD-IEVPLTPedllkgrdpqLEKALEL 341
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
80-277 2.34e-11

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: 65.66  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  80 VMYDKLEGNVGYLRI-----DYiiGQEVVQKVGAFLVDKVwktlidtSALVIDLRHSTGGQISGLPFIISYLHEADKVlh 154
Cdd:COG0793  150 VEAKLLEGKIGYIRIpsfgeNT--AEEFKRALKELKKQGA-------KGLILDLRNNPGGLLDEAVELADLFLPKGPI-- 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 155 ietVYNRPSNTTTEIWtlpKVLGERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGsLDIKKMRIGPSN 234
Cdd:COG0793  219 ---VYTRGRNGKVETY---KATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGK-GSVQTVFPLPDG 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 405133449 235 FYLMVPVSRSVSPltgGGQSWEVSGVMP-CVATEADQALQKSLD 277
Cdd:COG0793  292 GALKLTTARYYTP---SGRSIQGKGVEPdIEVPLTPEDLLKGRD 332
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
392-586 1.61e-07

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: 53.52  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  392 NVGYMRFDEF-ADASV-LAKLgpyiVHKVWEplQNTENLIMDLRYNPGGPSSSAVPLLLSYFQDpaaGPVhlFTTYDRct 469
Cdd:TIGR00225 152 SVGYIRISSFsEHTAEdVAKA----LDKLEK--KNAKGYILDLRGNPGGLLQSAVDISRLFITK---GPI--VQTKDR-- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  470 NHTQEH---NSQaellgQPYgaQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEIT--AGSLSHTRTFpllqpkqGIT 544
Cdd:TIGR00225 219 NGSKRHykaNGR-----QKY--NLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTfgKGTVQQVRPL-------NDG 284
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 405133449  545 HGLTITVPviTFIDNHGESWMGGGVVPDAIV-LAEDALQKAEE 586
Cdd:TIGR00225 285 SGIKVTIA--KYYTPNGGSIHKKGIEPDIVIeQPDYSKELEEK 325
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
597-655 1.41e-05

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: 46.90  E-value: 1.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 405133449 597 LVEATGQLLEAHYAIPEVAGKASVMLSTKQAHGGYRSAVDFETLASQLTSDLQEASGDH 655
Cdd:cd07563    1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQELGDGH 59
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
1-277 1.30e-73

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: 237.19  E-value: 1.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   1 YPENLVGMQEAIEQAIKSGEILDISDPKRLASVLTAGVQgALNDPRLVISYepsphaapkqdaedsptreqllsliehvv 80
Cdd:cd07563   15 FPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQ-ELGDGHLNVSY----------------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  81 mydklegnVGYLRIDYIIGQEvvQKVGAFLVDKVWKTLIDTSALVIDLRHSTGGQISGLPFIISYLHEADKVLHIETVYN 160
Cdd:cd07563   65 --------IGYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 161 RPSNTTTEIWTLPKVLGERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGSLDIKKMRIgPSNFYLMVP 240
Cdd:cd07563  135 RPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPL-PNGLYLTVP 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 405133449 241 VSRSVSPLTggGQSWEVSGVMPCVATEADQALQKSLD 277
Cdd:cd07563  214 TSRSVDPIT--GTNWEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
288-584 1.87e-64

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: 212.92  E-value: 1.87e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 288 TLSKLTAILKDNYSLVE----RVPVLLQHLTTFDFSSVQSAEDLATKLNTEMQTLsEDPRLLVRVmmpgeavsppaekpv 363
Cdd:cd07563    1 VFEALAKLLEENYAFPEakgiDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSY--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 364 aaaanlpdneqflhalvdtvfkvsvlagnVGYMRFDEFADASVlaKLGPYIVHKVWEPLQNTENLIMDLRYNPGGpSSSA 443
Cdd:cd07563   65 -----------------------------IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGG-SDSL 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 444 VPLLLSYFQDpAAGPVHLFTTYDRCTNHTQEHNSQAELLGQPYGAQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEI 523
Cdd:cd07563  113 VAYLASYFTD-EDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGET 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405133449 524 TAGSLSHTRTFPLlqpkqgiTHGLTITVPVITFIDNH-GESWMGGGVVPDAIVLA----EDALQKA 584
Cdd:cd07563  192 TAGGASPVLPFPL-------PNGLYLTVPTSRSVDPItGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
268-389 2.99e-44

N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at the N-terminus of the functional unit of interphotoreceptor retinoid binding proteins 3, IRBP, in eukaryotes. From the structure of PDB:1j7x, the domain forms the N-terminal end of the module which is characterized as a serine-peptidase, pfam03572. Peptidase_S41_N forms a three-helix bundle followed by a small beta strand and is termed domain A. Part of the peptidase domain folds back over domain A to create a largely hydrophobic cleft between the two domains. On binding of ligand domain A is structurally rearranged with respect to domain B.


Pssm-ID: 463396  Cd Length: 129  Bit Score: 154.40  E-value: 2.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  268 ADQALQKSLDILAVRRAVPGTLSKLTAILKDNYSLVERVPVLLQHLTTF----DFSSVQSAEDLATKLNTEMQTLSEDPR 343
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 405133449  344 LLVRVMMPGEAVSPP--AEKPVAAAANLPDNEQFLHALVDTVFKVSVL 389
Cdd:pfam11918  81 LKVRYIRPEPASDEPeaADNIPGLVPMQPPSPEMLEALIKSSFKVDVL 128
TSPc smart00245
tail specific protease; tail specific protease
378-575 1.20e-43

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 155.11  E-value: 1.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   378 ALVDTVFKVSVLAGNVGYMRFDeFADASVLAKLGP---YIVHKVWEPLQNT--ENLIMDLRYNPGGPSSSAVpLLLSYFQ 452
Cdd:smart00245   7 ALIRDKIKIETLEGNVGYLRFG-FIGYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAI-DVSSLFL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   453 DPAagpVHLFTTYDRctnhTQEHNSQAELLGQPYgaQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTR 532
Cdd:smart00245  85 DKG---VIVYTVYRR----TGELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKGLVQQ 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 405133449   533 TFPLlqpkqGITHGLTITVPVitFIDNHGESWMGGGVVPDAIV 575
Cdd:smart00245 156 TVPL-----GDGSGLKLTVAK--YYTPSGKSIEKKGVEPDIQV 191
TSPc smart00245
tail specific protease; tail specific protease
68-267 2.86e-41

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 148.56  E-value: 2.86e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449    68 TREQLLSLIEHVVMYDKLEGNVGYLRIdYIIGQEVVQKVG---AFLVDKVWKTLIDT--SALVIDLRHSTGGQISGLPFI 142
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRF-GFIGYIRIPEFSehtSNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   143 ISYLHEADkvLHIETVYNRpsntTTEIWTLPKVLGERYSKDkdVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGS 222
Cdd:smart00245  80 SSLFLDKG--VIVYTVYRR----TGELWTYPANLGRKYSKP--LVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 405133449   223 LDIKKMRIGpSNFYLMVPVSRSVSPltgGGQSWEVSGVMPCVATE 267
Cdd:smart00245 152 LVQQTVPLG-DGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
392-575 5.69e-32

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: 123.56  E-value: 5.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 392 NVGYMRFDEFADASVLAKLgpyiVHKVWEPLQNTENLIMDLRYNPGGPSSSAVpLLLSYFQDPaagPVHLFTTYDRCTNH 471
Cdd:cd06567   60 TIGYIRIPSFSAESTAEEL----REALAELKKGVKGLILDLRNNPGGLLSAAV-ELASLFLPK---GKIVVTTRRRGGNE 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 472 TQEhnsqaELLGQPYGAQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTRTFPLLqpkqgitHGLTITV 551
Cdd:cd06567  132 TEY-----VAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQTVFPLL-------DGSALKL 199
                        170       180
                 ....*....|....*....|....
gi 405133449 552 PVITFIDNHGESWMGGGVVPDAIV 575
Cdd:cd06567  200 TTAKYYTPSGRSIEGKGVEPDIEV 223
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
577-656 7.44e-29

N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at the N-terminus of the functional unit of interphotoreceptor retinoid binding proteins 3, IRBP, in eukaryotes. From the structure of PDB:1j7x, the domain forms the N-terminal end of the module which is characterized as a serine-peptidase, pfam03572. Peptidase_S41_N forms a three-helix bundle followed by a small beta strand and is termed domain A. Part of the peptidase domain folds back over domain A to create a largely hydrophobic cleft between the two domains. On binding of ligand domain A is structurally rearranged with respect to domain B.


Pssm-ID: 463396  Cd Length: 129  Bit Score: 111.65  E-value: 7.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  577 AEDALQKAEEVLTFHRNMGILVEATGQLLEAHYAIPEVAGKASVMLSTKQAHGGYRSAVDFETLASQLTSDLQEASGDHR 656
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPR 80
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
20-267 1.87e-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: 113.54  E-value: 1.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  20 EILDISDPKRLASVLTAGVqGALNDPRLVISYepsphaapkqdaedsptreqllsliehvvmydklegnVGYLRIDYIIG 99
Cdd:cd06567   30 LLDAVDDRELLAGALNGML-GELGDPHSRYLT-------------------------------------IGYIRIPSFSA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 100 QEVVQKVGAFLVDkvwkTLIDTSALVIDLRHSTGGQISGLPFIISYLHEADKVLHIETVYNRPsnttteiWTLPKVLGER 179
Cdd:cd06567   72 ESTAEELREALAE----LKKGVKGLILDLRNNPGGLLSAAVELASLFLPKGKIVVTTRRRGGN-------ETEYVAPGGG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 180 YSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGSLDIkKMRIGPSNFYLMVPVSRSVSPltgGGQSWEVSG 259
Cdd:cd06567  141 SLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQ-TVFPLLDGSALKLTTAKYYTP---SGRSIEGKG 216

                 ....*...
gi 405133449 260 VMPCVATE 267
Cdd:cd06567  217 VEPDIEVP 224
Peptidase_S41 pfam03572
Peptidase family S41;
392-575 8.52e-27

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 106.92  E-value: 8.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  392 NVGYMRFDEFAdasvlaKLGPYIVHKVWEPL--QNTENLIMDLRYNPGGPSSSAVpLLLSYFQDPaaGPVhlFTTYDRCT 469
Cdd:pfam03572   1 KIGYIRIPSFS------EKTAKELAEALKELkkQGVKGLILDLRGNPGGLLSAAV-EIASLFLPD--GTI--VSTRGRDG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  470 NHTQEHnsqAELLGQPYGAQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTRTFPLlqpkqgiTHGLTI 549
Cdd:pfam03572  70 SKEVYF---AAGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPL-------PDGSAL 139
                         170       180
                  ....*....|....*....|....*.
gi 405133449  550 TVPVITFIDNHGESWMGGGVVPDAIV 575
Cdd:pfam03572 140 KLTIAKYYTPDGRSIEGKGIEPDIEV 165
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
385-587 6.32e-18

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: 85.69  E-value: 6.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 385 KVSVLAGNVGYMRFDEFADASV------LAKLGPyivhkvweplQNTENLIMDLRYNPGGPSSSAVPLLlSYFQDpaAGP 458
Cdd:COG0793  151 EAKLLEGKIGYIRIPSFGENTAeefkraLKELKK----------QGAKGLILDLRNNPGGLLDEAVELA-DLFLP--KGP 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 459 VhlFTTYDRctnhtqeHNSQAELLGQPYGAQRG--IYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTRTFPL 536
Cdd:COG0793  218 I--VYTRGR-------NGKVETYKATPGGALYDgpLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSVQTVFPL 288
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405133449 537 lqpkqgiTHGLTITVPVITFIDNHGESWMGGGVVPDaIVLAEDA----------LQKAEEV 587
Cdd:COG0793  289 -------PDGGALKLTTARYYTPSGRSIQGKGVEPD-IEVPLTPedllkgrdpqLEKALEL 341
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
391-572 1.96e-14

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: 73.77  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 391 GNVGYMRFDEFADASvLAKLgpyivHKVWEPLQNTENLIMDLRYNPGGPSSSavpLLLSYFQDPAAGpvhlfTTYDRctn 470
Cdd:cd07562   87 GRIGYVHIPDMGDDG-FAEF-----LRDLLAEVDKDGLIIDVRFNGGGNVAD---LLLDFLSRRRYG-----YDIPR--- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 471 htqehnSQAELLGQPYGAQRG-IYLLTSRHTATAAEEFAYLMQSLGRATLIGEITAGSLSHTRTFPLLQpkqgithGLTI 549
Cdd:cd07562  150 ------GGGKPVTYPSGRWRGpVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRLPD-------GGSL 216
                        170       180
                 ....*....|....*....|...
gi 405133449 550 TVPVITFIDNHGESWMGGGVVPD 572
Cdd:cd07562  217 TVPEFGVYLPDGGPLENRGVAPD 239
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
80-277 2.34e-11

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: 65.66  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  80 VMYDKLEGNVGYLRI-----DYiiGQEVVQKVGAFLVDKVwktlidtSALVIDLRHSTGGQISGLPFIISYLHEADKVlh 154
Cdd:COG0793  150 VEAKLLEGKIGYIRIpsfgeNT--AEEFKRALKELKKQGA-------KGLILDLRNNPGGLLDEAVELADLFLPKGPI-- 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 155 ietVYNRPSNTTTEIWtlpKVLGERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGsLDIKKMRIGPSN 234
Cdd:COG0793  219 ---VYTRGRNGKVETY---KATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGK-GSVQTVFPLPDG 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 405133449 235 FYLMVPVSRSVSPltgGGQSWEVSGVMP-CVATEADQALQKSLD 277
Cdd:COG0793  292 GALKLTTARYYTP---SGRSIQGKGVEPdIEVPLTPEDLLKGRD 332
Peptidase_S41 pfam03572
Peptidase family S41;
88-262 1.86e-10

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 59.93  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449   88 NVGYLRI---DYIIGQEVvqkvgaflvDKVWKTLI--DTSALVIDLRHSTGGQISGLPFIISYLHEADKVLhieTVYNRP 162
Cdd:pfam03572   1 KIGYIRIpsfSEKTAKEL---------AEALKELKkqGVKGLILDLRGNPGGLLSAAVEIASLFLPDGTIV---STRGRD 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  163 SNTTTEIWTLPkvlGERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGGSLDIKKMRIgPSNFYLMVPVS 242
Cdd:pfam03572  69 GSKEVYFAAGK---ADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPL-PDGSALKLTIA 144
                         170       180
                  ....*....|....*....|
gi 405133449  243 RSVSPltgGGQSWEVSGVMP 262
Cdd:pfam03572 145 KYYTP---DGRSIEGKGIEP 161
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
81-221 4.03e-10

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: 61.06  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  81 MYDKL-EGNVGYLRIDYIIGQEVVQkvgaFLVDkvWKTLIDTSALVIDLRHSTGGQISGlpFIISYLHEAdkvLHIETVY 159
Cdd:cd07562   80 YVEELsDGRIGYVHIPDMGDDGFAE----FLRD--LLAEVDKDGLIIDVRFNGGGNVAD--LLLDFLSRR---RYGYDIP 148
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 405133449 160 NRPSNTTTEiwtlpkvlgERYSKDKDVIVLISRHTTGVAEDVAYILKHMHRAFTVGEKTAGG 221
Cdd:cd07562  149 RGGGKPVTY---------PSGRWRGPVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGG 201
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
370-580 1.02e-08

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: 56.49  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 370 PDNEQFLHALV---DTVFKVSVL---AGNVGYMRFDEF----ADA--SVLAKLgpyivhKVweplQNTENLIMDLRYNPG 437
Cdd:cd07561   37 DDPEDFLESLLsekDGKDRFSYIvdgGKKVGYLVYNSFtsgyDDElnQAFAEF------KA----QGVTELVLDLRYNGG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 438 GPSSSAVpLLLSYFQdPAAGPVHLFTTYDRCTNHTQEH-----NSQAELLGQPYGAQRgIYLLTSRHTATAAEE-----F 507
Cdd:cd07561  107 GLVSSAN-LLASLLA-PAVALGQVFATLEYNDKRSANNedllfSSKTLAGGNSLNLSK-VYVLTSGSTASASELvinslK 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 405133449 508 AYLmqslgRATLIGEITAGSLSHTRTFpllqpKQGITHGLTItVPVITFIDN-HGESWMGGGVVPDaIVLAEDA 580
Cdd:cd07561  184 PYM-----DVVLIGETTYGKNVGSLTF-----EDDRKHKWAL-QPVVFKVVNaDGQGDYSNGLTPD-IEVNEDS 245
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
392-586 1.61e-07

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: 53.52  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  392 NVGYMRFDEF-ADASV-LAKLgpyiVHKVWEplQNTENLIMDLRYNPGGPSSSAVPLLLSYFQDpaaGPVhlFTTYDRct 469
Cdd:TIGR00225 152 SVGYIRISSFsEHTAEdVAKA----LDKLEK--KNAKGYILDLRGNPGGLLQSAVDISRLFITK---GPI--VQTKDR-- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  470 NHTQEH---NSQaellgQPYgaQRGIYLLTSRHTATAAEEFAYLMQSLGRATLIGEIT--AGSLSHTRTFpllqpkqGIT 544
Cdd:TIGR00225 219 NGSKRHykaNGR-----QKY--NLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTfgKGTVQQVRPL-------NDG 284
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 405133449  545 HGLTITVPviTFIDNHGESWMGGGVVPDAIV-LAEDALQKAEE 586
Cdd:TIGR00225 285 SGIKVTIA--KYYTPNGGSIHKKGIEPDIVIeQPDYSKELEEK 325
Peptidase_S41_CPP cd07560
C-terminal processing peptidase; serine protease family S41; The C-terminal processing ...
393-534 1.89e-06

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: 48.95  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449 393 VGYMRFDEFAD------ASVLAKLgpyivHKvweplQNTENLIMDLRYNPGGPSSSAVpLLLSYFQDpaAGPVhlFTTYD 466
Cdd:cd07560   50 IGYIRITSFSEntaeelKKALKEL-----KK-----QGMKGLILDLRNNPGGLLDEAV-EIADLFLP--GGPI--VSTKG 114
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405133449 467 RCTNHTQEHNSQAELLGQPygaqrgIYLLTSRHTATAAEEFAYLMQSLGRATLIGEitagslshtRTF 534
Cdd:cd07560  115 RNGKREAYASDDGGLYDGP------LVVLVNGGSASASEIVAGALQDNGRAVLVGE---------RTF 167
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
2-79 5.94e-06

N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at the N-terminus of the functional unit of interphotoreceptor retinoid binding proteins 3, IRBP, in eukaryotes. From the structure of PDB:1j7x, the domain forms the N-terminal end of the module which is characterized as a serine-peptidase, pfam03572. Peptidase_S41_N forms a three-helix bundle followed by a small beta strand and is termed domain A. Part of the peptidase domain folds back over domain A to create a largely hydrophobic cleft between the two domains. On binding of ligand domain A is structurally rearranged with respect to domain B.


Pssm-ID: 463396  Cd Length: 129  Bit Score: 46.16  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449    2 PENLVGMQEAIEQAIKSGEILDISDPKRLASVLTAGVQGALNDPRLVISYEPSPHAAPKQDAED---------SPTREQL 72
Cdd:pfam11918  36 PERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPRLKVRYIRPEPASDEPEAADnipglvpmqPPSPEML 115

                  ....*..
gi 405133449   73 LSLIEHV 79
Cdd:pfam11918 116 EALIKSS 122
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
597-655 1.41e-05

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: 46.90  E-value: 1.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 405133449 597 LVEATGQLLEAHYAIPEVAGKASVMLSTKQAHGGYRSAVDFETLASQLTSDLQEASGDH 655
Cdd:cd07563    1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQELGDGH 59
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
88-220 2.45e-03

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: 40.32  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405133449  88 NVGYLRIDYII---GQEVVQKVGAFLVDKVwktlidtSALVIDLRHSTGGQISGLPFIISYLHEADKV--LHIETVYN-- 160
Cdd:cd07561   65 KVGYLVYNSFTsgyDDELNQAFAEFKAQGV-------TELVLDLRYNGGGLVSSANLLASLLAPAVALgqVFATLEYNdk 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405133449 161 RPSNTTTEIWTLPKVLGERYSKDKDVIVLISRHTTGVAEDVAYILK-HMhRAFTVGEKTAG 220
Cdd:cd07561  138 RSANNEDLLFSSKTLAGGNSLNLSKVYVLTSGSTASASELVINSLKpYM-DVVLIGETTYG 197
 
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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