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Conserved domains on  [gi|1411179691|ref|XP_025252766|]
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retinol-binding protein 3 [Theropithecus gelada]

Protein Classification

S41 family peptidase( domain architecture ID 10165999)

S41 family peptidase similar to vertebrate retinol-binding protein 3 (Rbp3), the major soluble component of the interphotoreceptor matrix and is critical to the function, integrity, and development of the retina

EC:  3.4.-.-
Gene Ontology:  GO:0006508|GO:0008236
MEROPS:  S41

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 ...
940-1226 1.38e-80

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: 264.54  E-value: 1.38e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  940 VLQTAGKLVADNYAFAELGAKTAIKLSGL--QSRYSRVTSEVALAEILGADLQMLsGDPHLKAAHIpenakdripgivpm 1017
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARlrAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1018 qipspevfeelikfsfhtnvfedniGYLRFDMFGDGEllTQVSKLLVEHVWKKIMHTDAMIIDMRFNIGGPTSSIPILCS 1097
Cdd:cd07563     66 -------------------------GYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLAS 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1098 YFFDEGPPILLDKIYSRPDDSISELWTHAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGCQP 1177
Cdd:cd07563    119 YFTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASP 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1411179691 1178 PQTYHVDDtNLYLTIPTARSVGASDGSSWEGVGVTPHMVVPA----EEALTRA 1226
Cdd:cd07563    199 VLPFPLPN-GLYLTVPTSRSVDPITGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
639-931 3.06e-80

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: 263.77  E-value: 3.06e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  639 LVEGTGHLLEAHYARPEVVGQTSALLRAKLAQGAYRTAVDLESLASQLTADLQEVsGDHRLLVFHspgelvveeappppp 718
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSY--------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  719 avpspeeltyliealfktevlpgqLGYLRFDAMAELEtvKAVGPQLVRLVWQQLVDTAALVIDLRYNPGSYSTAIPLLCS 798
Cdd:cd07563     65 ------------------------IGYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLAS 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  799 YFFEAEPRQHLYSVFDRATSKVMEVWTLPQVAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALS 878
Cdd:cd07563    119 YFTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASP 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1411179691  879 VGIYQVGSSpLYASMPTQMALSATTGKAWDLAGVEPDITVPMIEALSTAQDIV 931
Cdd:cd07563    199 VLPFPLPNG-LYLTVPTSRSVDPITGTNWEGVGVPPDIEVPATPGYDDALERA 250
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
27-318 2.03e-76

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: 252.98  E-value: 2.03e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   27 LVLDMAKVLLDNYCFPENLLGMQEAIQQAIKSHEILSISDPQTLASVLTAGVQSsLNDPRLVISYepstpepppqvpalt 106
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY--------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  107 slseeellawlqrglrhevlegnVGYLRVDSVPGQEVlsMMGEFLVAHVWGKLMGTSALVLDLRHCTGGQISGIPYIISY 186
Cdd:cd07563     65 -----------------------IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASY 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  187 LHPGNTILHVDTIYNRPSNTTTEIWTLPQVLGERYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGALDL 266
Cdd:cd07563    120 FTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPV 199
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1411179691  267 RKLRIGEsDFFFTVPVSRSLGPLGGGSqtWEGSGVLPCVGTPAEQALEKALD 318
Cdd:cd07563    200 LPFPLPN-GLYLTVPTSRSVDPITGTN--WEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
329-626 5.82e-65

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: 220.63  E-value: 5.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  329 VVHCLQEALKDYY----TLVDRVPTLLQHLASMDFSTVVSEDDLVTKLNAGLQAAsEDPRLLVRAIrpretpsgpvpdaa 404
Cdd:cd07563      1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  405 aedppgaapelpeddairqalvesvfqvsvlpgnvGYLRFDSFADASvlGVLAPYVLRQVWEPLQDTEHLIMDLRHNPGG 484
Cdd:cd07563     66 -----------------------------------GYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGG 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  485 PSSAVPLLLSYFQGPEaGPVHLFTTYDRRTNITQEHFSHMELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATL 564
Cdd:cd07563    109 SDSLVAYLASYFTDED-KPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATV 187
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411179691  565 VGEITAGNLLHTRTVPLldtPEGsLALTVPVLTFIDNH-GEAWLGGGVVPDAIVLA----EEALDKA 626
Cdd:cd07563    188 VGETTAGGASPVLPFPL---PNG-LYLTVPTSRSVDPItGTNWEGVGVPPDIEVPAtpgyDDALERA 250
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
940-1226 1.38e-80

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: 264.54  E-value: 1.38e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  940 VLQTAGKLVADNYAFAELGAKTAIKLSGL--QSRYSRVTSEVALAEILGADLQMLsGDPHLKAAHIpenakdripgivpm 1017
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARlrAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1018 qipspevfeelikfsfhtnvfedniGYLRFDMFGDGEllTQVSKLLVEHVWKKIMHTDAMIIDMRFNIGGPTSSIPILCS 1097
Cdd:cd07563     66 -------------------------GYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLAS 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1098 YFFDEGPPILLDKIYSRPDDSISELWTHAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGCQP 1177
Cdd:cd07563    119 YFTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASP 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1411179691 1178 PQTYHVDDtNLYLTIPTARSVGASDGSSWEGVGVTPHMVVPA----EEALTRA 1226
Cdd:cd07563    199 VLPFPLPN-GLYLTVPTSRSVDPITGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
639-931 3.06e-80

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: 263.77  E-value: 3.06e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  639 LVEGTGHLLEAHYARPEVVGQTSALLRAKLAQGAYRTAVDLESLASQLTADLQEVsGDHRLLVFHspgelvveeappppp 718
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSY--------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  719 avpspeeltyliealfktevlpgqLGYLRFDAMAELEtvKAVGPQLVRLVWQQLVDTAALVIDLRYNPGSYSTAIPLLCS 798
Cdd:cd07563     65 ------------------------IGYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLAS 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  799 YFFEAEPRQHLYSVFDRATSKVMEVWTLPQVAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALS 878
Cdd:cd07563    119 YFTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASP 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1411179691  879 VGIYQVGSSpLYASMPTQMALSATTGKAWDLAGVEPDITVPMIEALSTAQDIV 931
Cdd:cd07563    199 VLPFPLPNG-LYLTVPTSRSVDPITGTNWEGVGVPPDIEVPATPGYDDALERA 250
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
27-318 2.03e-76

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: 252.98  E-value: 2.03e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   27 LVLDMAKVLLDNYCFPENLLGMQEAIQQAIKSHEILSISDPQTLASVLTAGVQSsLNDPRLVISYepstpepppqvpalt 106
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY--------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  107 slseeellawlqrglrhevlegnVGYLRVDSVPGQEVlsMMGEFLVAHVWGKLMGTSALVLDLRHCTGGQISGIPYIISY 186
Cdd:cd07563     65 -----------------------IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASY 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  187 LHPGNTILHVDTIYNRPSNTTTEIWTLPQVLGERYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGALDL 266
Cdd:cd07563    120 FTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPV 199
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1411179691  267 RKLRIGEsDFFFTVPVSRSLGPLGGGSqtWEGSGVLPCVGTPAEQALEKALD 318
Cdd:cd07563    200 LPFPLPN-GLYLTVPTSRSVDPITGTN--WEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
329-626 5.82e-65

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: 220.63  E-value: 5.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  329 VVHCLQEALKDYY----TLVDRVPTLLQHLASMDFSTVVSEDDLVTKLNAGLQAAsEDPRLLVRAIrpretpsgpvpdaa 404
Cdd:cd07563      1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  405 aedppgaapelpeddairqalvesvfqvsvlpgnvGYLRFDSFADASvlGVLAPYVLRQVWEPLQDTEHLIMDLRHNPGG 484
Cdd:cd07563     66 -----------------------------------GYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGG 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  485 PSSAVPLLLSYFQGPEaGPVHLFTTYDRRTNITQEHFSHMELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATL 564
Cdd:cd07563    109 SDSLVAYLASYFTDED-KPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATV 187
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411179691  565 VGEITAGNLLHTRTVPLldtPEGsLALTVPVLTFIDNH-GEAWLGGGVVPDAIVLA----EEALDKA 626
Cdd:cd07563    188 VGETTAGGASPVLPFPL---PNG-LYLTVPTSRSVDPItGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
309-436 6.35e-54

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: 184.06  E-value: 6.35e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  309 AEQALEKALDILTLRSALPGVVHCLQEALKDYYTLVDRVPTLLQHLASM----DFSTVVSEDDLVTKLNAGLQAASEDPR 384
Cdd:pfam11918    1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1411179691  385 LLVRAIRPRETPSGPvpdAAAEDPPGAAPELPEDDAIRQALVESVFQVSVLP 436
Cdd:pfam11918   81 LKVRYIRPEPASDEP---EAADNIPGLVPMQPPSPEMLEALIKSSFKVDVLP 129
TSPc smart00245
tail specific protease; tail specific protease
728-919 1.97e-49

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 173.60  E-value: 1.97e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   728 YLIEALFKTEVLPGQLGYLRFdAMAELETVKAVGPQ---LVRLVWQQLVDT--AALVIDLRYNPGSYSTAIPLLCSYFFE 802
Cdd:smart00245    7 ALIRDKIKIETLEGNVGYLRF-GFIGYIRIPEFSEHtsnLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDVSSLFLD 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   803 AEPrqHLYSVFDRATskvmEVWTLPQVAGQRYgsHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIY 882
Cdd:smart00245   86 KGV--IVYTVYRRTG----ELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKGLVQQTV 157
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1411179691   883 QVGSSpLYASMPTQMALSAtTGKAWDLAGVEPDITVP 919
Cdd:smart00245  158 PLGDG-SGLKLTVAKYYTP-SGKSIEKKGVEPDIQVP 192
TSPc smart00245
tail specific protease; tail specific protease
1021-1218 3.49e-49

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 173.21  E-value: 3.49e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  1021 SPEVFEELIKFSFHTNVFEDNIGYLRFdMFGDGELLTQVSKL---LVEHVWKKIMHT--DAMIIDMRFNIGGPTSSIPIL 1095
Cdd:smart00245    1 SKERTIALIRDKIKIETLEGNVGYLRF-GFIGYIRIPEFSEHtsnLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  1096 CSYFFDEGppILLDKIYSRPddsiSELWTHAQVVGERYgsKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGC 1175
Cdd:smart00245   80 SSLFLDKG--VIVYTVYRRT----GELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....
gi 1411179691  1176 QPPQTYHV-DDTNLYLTIPTARSVgasDGSSWEGVGVTPHMVVP 1218
Cdd:smart00245  152 LVQQTVPLgDGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
TSPc smart00245
tail specific protease; tail specific protease
109-308 9.40e-47

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 165.89  E-value: 9.40e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   109 SEEELLAWLQRGLRHEVLEGNVGYLRVDSVpGQEVLSMMGE---FLVAHVWGKLMGT--SALVLDLRHCTGGQISGIPYI 183
Cdd:smart00245    1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   184 ISYLHPGNTIlhVDTIYNRpsntTTEIWTLPQVLGERYgaDKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGA 263
Cdd:smart00245   80 SSLFLDKGVI--VYTVYRR----TGELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1411179691   264 LDLRKLRIGEsDFFFTVPVSRSLGPLGggsQTWEGSGVLPCVGTP 308
Cdd:smart00245  152 LVQQTVPLGD-GSGLKLTVAKYYTPSG---KSIEKKGVEPDIQVP 192
TSPc smart00245
tail specific protease; tail specific protease
424-617 9.68e-47

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 165.89  E-value: 9.68e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   424 ALVESVFQVSVLPGNVGYLRFDS--FADASVLGVLAPYVLRQVWEPLQDT--EHLIMDLRHNPGGPSSAVPLLLSYFQGP 499
Cdd:smart00245    7 ALIRDKIKIETLEGNVGYLRFGFigYIRIPEFSEHTSNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDVSSLFLDK 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   500 EagpVHLFTTYDRrtniTQEHFSHMELPGPRYStqRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTV 579
Cdd:smart00245   87 G---VIVYTVYRR----TGELWTYPANLGRKYS--KPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKGLVQQTV 157
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1411179691   580 PLLDtpEGSLALTVPVltFIDNHGEAWLGGGVVPDAIV 617
Cdd:smart00245  158 PLGD--GSGLKLTVAK--YYTPSGKSIEKKGVEPDIQV 191
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
619-740 9.36e-39

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: 140.54  E-value: 9.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  619 AEEALDKAQEVLEFHQSLGALVEGTGHLLEAHYARPEVVGQTSALLRAKLAQGAYRTAVDLESLASQLTADLQEVSGDHR 698
Cdd:pfam11918    1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1411179691  699 LLVFHSPGELVVEEAPPPPPAVPSPE-------ELTYLIEALFKTEVLP 740
Cdd:pfam11918   81 LKVRYIRPEPASDEPEAADNIPGLVPmqppspeMLEALIKSSFKVDVLP 129
Peptidase_S41 pfam03572
Peptidase family S41;
438-617 2.30e-29

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 115.01  E-value: 2.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  438 NVGYLRFDSFadasvlGVLAPYVLRQVWEPL--QDTEHLIMDLRHNPGGPSSAVPLLLSYFQGPEAgpvhLFTTYDRRTN 515
Cdd:pfam03572    1 KIGYIRIPSF------SEKTAKELAEALKELkkQGVKGLILDLRGNPGGLLSAAVEIASLFLPDGT----IVSTRGRDGS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  516 ITQEHFshmELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLldtPEGSlALTVPV 595
Cdd:pfam03572   71 KEVYFA---AGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPL---PDGS-ALKLTI 143
                          170       180
                   ....*....|....*....|..
gi 1411179691  596 LTFIDNHGEAWLGGGVVPDAIV 617
Cdd:pfam03572  144 AKYYTPDGRSIEGKGIEPDIEV 165
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
735-929 3.59e-20

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: 93.40  E-value: 3.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  735 KTEVLPGQLGYLRFDAMAElETVKAVGPQLVRLVWQqlvDTAALVIDLRYNPGSYSTAIPLLCSYFFEAEPrqhLYSVFD 814
Cdd:COG0793    151 EAKLLEGKIGYIRIPSFGE-NTAEEFKRALKELKKQ---GAKGLILDLRNNPGGLLDEAVELADLFLPKGP---IVYTRG 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  815 RAtSKVMEVWTLPQvaGQRYGshKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIYqvgssplyaSMP 894
Cdd:COG0793    224 RN-GKVETYKATPG--GALYD--GPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSVQTVF---------PLP 289
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1411179691  895 TQMALSATTGKAWD-------LAGVEPDITVP-MIEALSTAQD 929
Cdd:COG0793    290 DGGALKLTTARYYTpsgrsiqGKGVEPDIEVPlTPEDLLKGRD 332
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1019-1218 1.30e-15

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: 79.91  E-value: 1.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1019 IPSPEVFEELIkfsfhtnvfEDNIGYLRFDMFGDG---ELLTQVSKLlvehvwkKIMHTDAMIIDMRFNIGGPTSSIPIL 1095
Cdd:COG0793    145 IKLPSVEAKLL---------EGKIGYIRIPSFGENtaeEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVEL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1096 CSYFFDEGPpILldkiYSRPDDSISELWThAQVVGERYGSKksMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGC 1175
Cdd:COG0793    209 ADLFLPKGP-IV----YTRGRNGKVETYK-ATPGGALYDGP--LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKG 280
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1411179691 1176 QPPQTYHVDDtNLYLTIPTARSVGASdGSSWEGVGVTPHMVVP 1218
Cdd:COG0793    281 SVQTVFPLPD-GGALKLTTARYYTPS-GRSIQGKGVEPDIEVP 321
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
426-624 4.19e-15

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: 78.37  E-value: 4.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  426 VESVFqVSVLPGNVGYLRFDSFADASvlgvlAPYVLRQVWE-PLQDTEHLIMDLRHNPGGPSSAVPLLLSYFQgpEAGPV 504
Cdd:COG0793    147 LPSVE-AKLLEGKIGYIRIPSFGENT-----AEEFKRALKElKKQGAKGLILDLRNNPGGLLDEAVELADLFL--PKGPI 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  505 hlFTTYDRRTNITQEHFShmelPGPRYSTQRgVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLldt 584
Cdd:COG0793    219 --VYTRGRNGKVETYKAT----PGGALYDGP-LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSVQTVFPL--- 288
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1411179691  585 PEGSlALTVPVLTFIDNHGEAWLGGGVVPDaIVLAEEALD 624
Cdd:COG0793    289 PDGG-ALKLTTARYYTPSGRSIQGKGVEPD-IEVPLTPED 326
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
21-127 2.17e-14

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: 71.20  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   21 HLFQPSLVLDMAKVLLDNYCFPENLLGMQEAIQQAIKSHEILSISDPQTLASVLTAGVQSSLNDPRLVISY---EPSTPE 97
Cdd:pfam11918   15 RRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPRLKVRYirpEPASDE 94
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1411179691   98 P-----PPQVPALTSLSEEELLAWLQRGLRHEVLE 127
Cdd:pfam11918   95 PeaadnIPGLVPMQPPSPEMLEALIKSSFKVDVLP 129
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
122-319 6.19e-13

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: 71.44  E-value: 6.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  122 RHEVLEGNVGYLRVDSV---PGQEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPGNTIL---- 194
Cdd:COG0793    151 EAKLLEGKIGYIRIPSFgenTAEEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVELADLFLPKGPIVytrg 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  195 ---HVDTIYNRPSNTtteIWTLPqvlgerygadkdVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGAL--DLRKL 269
Cdd:COG0793    224 rngKVETYKATPGGA---LYDGP------------LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSvqTVFPL 288
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411179691  270 rigESDFFFTVPVSRSLGPLGGGsqtWEGSGVLP--CVGTPAEQ-------ALEKALDI 319
Cdd:COG0793    289 ---PDGGALKLTTARYYTPSGRS---IQGKGVEPdiEVPLTPEDllkgrdpQLEKALEL 341
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
744-919 6.00e-08

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: 56.21  E-value: 6.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  744 GYLRFDAMAElETVKAVGPQLVRLVWQQLVdtaALVIDLRYNPGSYSTAIPLLCSYFFEAEPrqhLYSVFDRATSKvmEV 823
Cdd:TIGR00225  154 GYIRISSFSE-HTAEDVAKALDKLEKKNAK---GYILDLRGNPGGLLQSAVDISRLFITKGP---IVQTKDRNGSK--RH 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  824 WTlpqvAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALsvgIYQVgsSPLYASMPTQMALS--- 900
Cdd:TIGR00225  225 YK----ANGRQKYNLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTFGKGT---VQQV--RPLNDGSGIKVTIAkyy 295
                          170
                   ....*....|....*....
gi 1411179691  901 ATTGKAWDLAGVEPDITVP 919
Cdd:TIGR00225  296 TPNGGSIHKKGIEPDIVIE 314
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
438-593 1.63e-05

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: 48.51  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  438 NVGYLRFDSFAdasvlgvlaPYVLRQVWEPLQDTEH-----LIMDLRHNPGGPSSAVPLLLSYFQgpEAGPVhlFTTYDR 512
Cdd:TIGR00225  152 SVGYIRISSFS---------EHTAEDVAKALDKLEKknakgYILDLRGNPGGLLQSAVDISRLFI--TKGPI--VQTKDR 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  513 rtNITQEHFShmelPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLLDTpeGSLALT 592
Cdd:TIGR00225  219 --NGSKRHYK----ANGRQKYNLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTFGKGTVQQVRPLNDG--SGIKVT 290

                   .
gi 1411179691  593 V 593
Cdd:TIGR00225  291 I 291
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
940-1226 1.38e-80

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: 264.54  E-value: 1.38e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  940 VLQTAGKLVADNYAFAELGAKTAIKLSGL--QSRYSRVTSEVALAEILGADLQMLsGDPHLKAAHIpenakdripgivpm 1017
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARlrAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1018 qipspevfeelikfsfhtnvfedniGYLRFDMFGDGEllTQVSKLLVEHVWKKIMHTDAMIIDMRFNIGGPTSSIPILCS 1097
Cdd:cd07563     66 -------------------------GYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLAS 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1098 YFFDEGPPILLDKIYSRPDDSISELWTHAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGCQP 1177
Cdd:cd07563    119 YFTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASP 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1411179691 1178 PQTYHVDDtNLYLTIPTARSVGASDGSSWEGVGVTPHMVVPA----EEALTRA 1226
Cdd:cd07563    199 VLPFPLPN-GLYLTVPTSRSVDPITGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
639-931 3.06e-80

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: 263.77  E-value: 3.06e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  639 LVEGTGHLLEAHYARPEVVGQTSALLRAKLAQGAYRTAVDLESLASQLTADLQEVsGDHRLLVFHspgelvveeappppp 718
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSY--------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  719 avpspeeltyliealfktevlpgqLGYLRFDAMAELEtvKAVGPQLVRLVWQQLVDTAALVIDLRYNPGSYSTAIPLLCS 798
Cdd:cd07563     65 ------------------------IGYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLAS 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  799 YFFEAEPRQHLYSVFDRATSKVMEVWTLPQVAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALS 878
Cdd:cd07563    119 YFTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASP 198
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1411179691  879 VGIYQVGSSpLYASMPTQMALSATTGKAWDLAGVEPDITVPMIEALSTAQDIV 931
Cdd:cd07563    199 VLPFPLPNG-LYLTVPTSRSVDPITGTNWEGVGVPPDIEVPATPGYDDALERA 250
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
27-318 2.03e-76

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: 252.98  E-value: 2.03e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   27 LVLDMAKVLLDNYCFPENLLGMQEAIQQAIKSHEILSISDPQTLASVLTAGVQSsLNDPRLVISYepstpepppqvpalt 106
Cdd:cd07563      1 VFEALAKLLEENYAFPEAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY--------------- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  107 slseeellawlqrglrhevlegnVGYLRVDSVPGQEVlsMMGEFLVAHVWGKLMGTSALVLDLRHCTGGQISGIPYIISY 186
Cdd:cd07563     65 -----------------------IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASY 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  187 LHPGNTILHVDTIYNRPSNTTTEIWTLPQVLGERYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGALDL 266
Cdd:cd07563    120 FTDEDKPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPV 199
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1411179691  267 RKLRIGEsDFFFTVPVSRSLGPLGGGSqtWEGSGVLPCVGTPAEQALEKALD 318
Cdd:cd07563    200 LPFPLPN-GLYLTVPTSRSVDPITGTN--WEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
329-626 5.82e-65

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: 220.63  E-value: 5.82e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  329 VVHCLQEALKDYY----TLVDRVPTLLQHLASMDFSTVVSEDDLVTKLNAGLQAAsEDPRLLVRAIrpretpsgpvpdaa 404
Cdd:cd07563      1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  405 aedppgaapelpeddairqalvesvfqvsvlpgnvGYLRFDSFADASvlGVLAPYVLRQVWEPLQDTEHLIMDLRHNPGG 484
Cdd:cd07563     66 -----------------------------------GYLRIDSFGGFE--IAAAEALLDEALDKLADTDALIIDLRYNGGG 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  485 PSSAVPLLLSYFQGPEaGPVHLFTTYDRRTNITQEHFSHMELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATL 564
Cdd:cd07563    109 SDSLVAYLASYFTDED-KPVHLYTIYKRPGNTTTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATV 187
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411179691  565 VGEITAGNLLHTRTVPLldtPEGsLALTVPVLTFIDNH-GEAWLGGGVVPDAIVLA----EEALDKA 626
Cdd:cd07563    188 VGETTAGGASPVLPFPL---PNG-LYLTVPTSRSVDPItGTNWEGVGVPPDIEVPAtpgyDDALERA 250
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
309-436 6.35e-54

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: 184.06  E-value: 6.35e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  309 AEQALEKALDILTLRSALPGVVHCLQEALKDYYTLVDRVPTLLQHLASM----DFSTVVSEDDLVTKLNAGLQAASEDPR 384
Cdd:pfam11918    1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1411179691  385 LLVRAIRPRETPSGPvpdAAAEDPPGAAPELPEDDAIRQALVESVFQVSVLP 436
Cdd:pfam11918   81 LKVRYIRPEPASDEP---EAADNIPGLVPMQPPSPEMLEALIKSSFKVDVLP 129
TSPc smart00245
tail specific protease; tail specific protease
728-919 1.97e-49

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 173.60  E-value: 1.97e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   728 YLIEALFKTEVLPGQLGYLRFdAMAELETVKAVGPQ---LVRLVWQQLVDT--AALVIDLRYNPGSYSTAIPLLCSYFFE 802
Cdd:smart00245    7 ALIRDKIKIETLEGNVGYLRF-GFIGYIRIPEFSEHtsnLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDVSSLFLD 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   803 AEPrqHLYSVFDRATskvmEVWTLPQVAGQRYgsHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIY 882
Cdd:smart00245   86 KGV--IVYTVYRRTG----ELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKGLVQQTV 157
                           170       180       190
                    ....*....|....*....|....*....|....*..
gi 1411179691   883 QVGSSpLYASMPTQMALSAtTGKAWDLAGVEPDITVP 919
Cdd:smart00245  158 PLGDG-SGLKLTVAKYYTP-SGKSIEKKGVEPDIQVP 192
TSPc smart00245
tail specific protease; tail specific protease
1021-1218 3.49e-49

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 173.21  E-value: 3.49e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  1021 SPEVFEELIKFSFHTNVFEDNIGYLRFdMFGDGELLTQVSKL---LVEHVWKKIMHT--DAMIIDMRFNIGGPTSSIPIL 1095
Cdd:smart00245    1 SKERTIALIRDKIKIETLEGNVGYLRF-GFIGYIRIPEFSEHtsnLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  1096 CSYFFDEGppILLDKIYSRPddsiSELWTHAQVVGERYgsKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGC 1175
Cdd:smart00245   80 SSLFLDKG--VIVYTVYRRT----GELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....
gi 1411179691  1176 QPPQTYHV-DDTNLYLTIPTARSVgasDGSSWEGVGVTPHMVVP 1218
Cdd:smart00245  152 LVQQTVPLgDGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
TSPc smart00245
tail specific protease; tail specific protease
109-308 9.40e-47

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 165.89  E-value: 9.40e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   109 SEEELLAWLQRGLRHEVLEGNVGYLRVDSVpGQEVLSMMGE---FLVAHVWGKLMGT--SALVLDLRHCTGGQISGIPYI 183
Cdd:smart00245    1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   184 ISYLHPGNTIlhVDTIYNRpsntTTEIWTLPQVLGERYgaDKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGA 263
Cdd:smart00245   80 SSLFLDKGVI--VYTVYRR----TGELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 1411179691   264 LDLRKLRIGEsDFFFTVPVSRSLGPLGggsQTWEGSGVLPCVGTP 308
Cdd:smart00245  152 LVQQTVPLGD-GSGLKLTVAKYYTPSG---KSIEKKGVEPDIQVP 192
TSPc smart00245
tail specific protease; tail specific protease
424-617 9.68e-47

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 165.89  E-value: 9.68e-47
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   424 ALVESVFQVSVLPGNVGYLRFDS--FADASVLGVLAPYVLRQVWEPLQDT--EHLIMDLRHNPGGPSSAVPLLLSYFQGP 499
Cdd:smart00245    7 ALIRDKIKIETLEGNVGYLRFGFigYIRIPEFSEHTSNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDVSSLFLDK 86
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   500 EagpVHLFTTYDRrtniTQEHFSHMELPGPRYStqRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTV 579
Cdd:smart00245   87 G---VIVYTVYRR----TGELWTYPANLGRKYS--KPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKGLVQQTV 157
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1411179691   580 PLLDtpEGSLALTVPVltFIDNHGEAWLGGGVVPDAIV 617
Cdd:smart00245  158 PLGD--GSGLKLTVAK--YYTPSGKSIEKKGVEPDIQV 191
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
922-1039 3.61e-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: 156.33  E-value: 3.61e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  922 EALSTAQDIVALRAKVPTVLQTAGKLVADNYAFAELGAKTAIKLSGLQS--RYSRVTSEVALAEILGADLQMLSGDPHLK 999
Cdd:pfam11918    3 EALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLAsgDYSSVVSEEDLASKLNADLQALSGDPRLK 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1411179691 1000 AAHI--------PENAkDRIPGIVPMQIPSPEVFEELIKFSFHTNVFE 1039
Cdd:pfam11918   83 VRYIrpepasdePEAA-DNIPGLVPMQPPSPEMLEALIKSSFKVDVLP 129
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
619-740 9.36e-39

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: 140.54  E-value: 9.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  619 AEEALDKAQEVLEFHQSLGALVEGTGHLLEAHYARPEVVGQTSALLRAKLAQGAYRTAVDLESLASQLTADLQEVSGDHR 698
Cdd:pfam11918    1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1411179691  699 LLVFHSPGELVVEEAPPPPPAVPSPE-------ELTYLIEALFKTEVLP 740
Cdd:pfam11918   81 LKVRYIRPEPASDEPEAADNIPGLVPmqppspeMLEALIKSSFKVDVLP 129
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
944-1218 4.04e-37

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: 139.74  E-value: 4.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  944 AGKLVADNYAFAELGAKTAIKLSgLQSRYSRVTSEVALAEILGADLQMLsGDPHlkaahipenakdripgivpmqipspe 1023
Cdd:cd06567      4 AWRLLRENYYDPHGVDWDALRDR-YVDLLDAVDDRELLAGALNGMLGEL-GDPH-------------------------- 55
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1024 vfeelikfsfhTNVFedNIGYLRFDMFGDGELLTQVSKLLVEHVWKKimhtDAMIIDMRFNIGGPTSSIPILCSYFFDEG 1103
Cdd:cd06567     56 -----------SRYL--TIGYIRIPSFSAESTAEELREALAELKKGV----KGLILDLRNNPGGLLSAAVELASLFLPKG 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1104 PPILLDKIYSRPddsiselWTHAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGCQPPQTYHV 1183
Cdd:cd06567    119 KIVVTTRRRGGN-------ETEYVAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQTVFPL 191
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1411179691 1184 DDtNLYLTIPTARSVGAsDGSSWEGVGVTPHMVVP 1218
Cdd:cd06567    192 LD-GSALKLTTAKYYTP-SGRSIEGKGVEPDIEVP 224
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
743-919 5.46e-34

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: 130.49  E-value: 5.46e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  743 LGYLRFDAMAeletvkavGPQLVRLVWQQLVDTA----ALVIDLRYNPGSYSTAIPLLCSYFFeaePRQHLYSVFDRATS 818
Cdd:cd06567     61 IGYIRIPSFS--------AESTAEELREALAELKkgvkGLILDLRNNPGGLLSAAVELASLFL---PKGKIVVTTRRRGG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  819 KvmevWTLPQVAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIYQVGSSpLYASMPTQMA 898
Cdd:cd06567    130 N----ETEYVAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQTVFPLLDG-SALKLTTAKY 204
                          170       180
                   ....*....|....*....|.
gi 1411179691  899 LSAtTGKAWDLAGVEPDITVP 919
Cdd:cd06567    205 YTP-SGRSIEGKGVEPDIEVP 224
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
438-617 2.65e-31

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: 122.79  E-value: 2.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  438 NVGYLRFDSFADASVlgvlAPYVLRQVWEPLQDTEHLIMDLRHNPGGPSSAVPLLLSYFQGPeagPVHLFTTYDRRTNIT 517
Cdd:cd06567     60 TIGYIRIPSFSAEST----AEELREALAELKKGVKGLILDLRNNPGGLLSAAVELASLFLPK---GKIVVTTRRRGGNET 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  518 QEhfshmELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLLDtpeGSlALTVPVLT 597
Cdd:cd06567    133 EY-----VAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQTVFPLLD---GS-ALKLTTAK 203
                          170       180
                   ....*....|....*....|
gi 1411179691  598 FIDNHGEAWLGGGVVPDAIV 617
Cdd:cd06567    204 YYTPSGRSIEGKGVEPDIEV 223
Peptidase_S41 pfam03572
Peptidase family S41;
438-617 2.30e-29

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 115.01  E-value: 2.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  438 NVGYLRFDSFadasvlGVLAPYVLRQVWEPL--QDTEHLIMDLRHNPGGPSSAVPLLLSYFQGPEAgpvhLFTTYDRRTN 515
Cdd:pfam03572    1 KIGYIRIPSF------SEKTAKELAEALKELkkQGVKGLILDLRGNPGGLLSAAVEIASLFLPDGT----IVSTRGRDGS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  516 ITQEHFshmELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLldtPEGSlALTVPV 595
Cdd:pfam03572   71 KEVYFA---AGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPL---PDGS-ALKLTI 143
                          170       180
                   ....*....|....*....|..
gi 1411179691  596 LTFIDNHGEAWLGGGVVPDAIV 617
Cdd:pfam03572  144 AKYYTPDGRSIEGKGIEPDIEV 165
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
30-305 3.46e-29

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: 116.63  E-value: 3.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   30 DMAKVLLDNYCFPenllGMQEAIQQAIKSHEIL-SISDPQTLASVLTAGVQSsLNDPRLVISYepstpepppqvpaltsl 108
Cdd:cd06567      3 EAWRLLRENYYDP----HGVDWDALRDRYVDLLdAVDDRELLAGALNGMLGE-LGDPHSRYLT----------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  109 seeellawlqrglrhevlegnVGYLRVDSvpgqevlsMMGEFLVAHVWGKLM----GTSALVLDLRHCTGGQISGIPYII 184
Cdd:cd06567     61 ---------------------IGYIRIPS--------FSAESTAEELREALAelkkGVKGLILDLRNNPGGLLSAAVELA 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  185 SYLHPGNTILHVDTIYNRPsnttteiWTLPQVLGERYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGAL 264
Cdd:cd06567    112 SLFLPKGKIVVTTRRRGGN-------ETEYVAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGS 184
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1411179691  265 DLRKLRIGeSDFFFTVPVSRSLGPLGGgsqTWEGSGVLPCV 305
Cdd:cd06567    185 VQTVFPLL-DGSALKLTTAKYYTPSGR---SIEGKGVEPDI 221
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
735-929 3.59e-20

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: 93.40  E-value: 3.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  735 KTEVLPGQLGYLRFDAMAElETVKAVGPQLVRLVWQqlvDTAALVIDLRYNPGSYSTAIPLLCSYFFEAEPrqhLYSVFD 814
Cdd:COG0793    151 EAKLLEGKIGYIRIPSFGE-NTAEEFKRALKELKKQ---GAKGLILDLRNNPGGLLDEAVELADLFLPKGP---IVYTRG 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  815 RAtSKVMEVWTLPQvaGQRYGshKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIYqvgssplyaSMP 894
Cdd:COG0793    224 RN-GKVETYKATPG--GALYD--GPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSVQTVF---------PLP 289
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1411179691  895 TQMALSATTGKAWD-------LAGVEPDITVP-MIEALSTAQD 929
Cdd:COG0793    290 DGGALKLTTARYYTpsgrsiqGKGVEPDIEVPlTPEDLLKGRD 332
Peptidase_S41 pfam03572
Peptidase family S41;
743-918 5.01e-18

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 82.65  E-value: 5.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  743 LGYLRFDAMAELetvkavGPQLVRLVWQQL--VDTAALVIDLRYNPGSYSTAIPLLCSYFFEAEPrqhLYSVFDRATSKV 820
Cdd:pfam03572    2 IGYIRIPSFSEK------TAKELAEALKELkkQGVKGLILDLRGNPGGLLSAAVEIASLFLPDGT---IVSTRGRDGSKE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  821 MEVWTLPQvagQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIYQVGSSPlyasmptqmALS 900
Cdd:pfam03572   73 VYFAAGKA---DEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPLPDGS---------ALK 140
                          170       180
                   ....*....|....*....|....*
gi 1411179691  901 ATTGKAWDLA-------GVEPDITV 918
Cdd:pfam03572  141 LTIAKYYTPDgrsiegkGIEPDIEV 165
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
741-920 1.41e-16

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: 81.09  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  741 GQLGYLRFDAMaeletvkavGPQLVRLVWQQL---VDTAALVIDLRYNPGSYstaiplLCSYFFEAE-PRQHLYSV---F 813
Cdd:cd07562     87 GRIGYVHIPDM---------GDDGFAEFLRDLlaeVDKDGLIIDVRFNGGGN------VADLLLDFLsRRRYGYDIprgG 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  814 DRATSKVMEVWTLPQVAgqrygshkdlyiLMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALSVGIYQV--GSsplYA 891
Cdd:cd07562    152 GKPVTYPSGRWRGPVVV------------LVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRLpdGG---SL 216
                          170       180
                   ....*....|....*....|....*....
gi 1411179691  892 SMPtQMALSATTGKAWDLAGVEPDITVPM 920
Cdd:cd07562    217 TVP-EFGVYLPDGGPLENRGVAPDIEVEN 244
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1019-1218 1.30e-15

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: 79.91  E-value: 1.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1019 IPSPEVFEELIkfsfhtnvfEDNIGYLRFDMFGDG---ELLTQVSKLlvehvwkKIMHTDAMIIDMRFNIGGPTSSIPIL 1095
Cdd:COG0793    145 IKLPSVEAKLL---------EGKIGYIRIPSFGENtaeEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVEL 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1096 CSYFFDEGPpILldkiYSRPDDSISELWThAQVVGERYGSKksMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGC 1175
Cdd:COG0793    209 ADLFLPKGP-IV----YTRGRNGKVETYK-ATPGGALYDGP--LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKG 280
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1411179691 1176 QPPQTYHVDDtNLYLTIPTARSVGASdGSSWEGVGVTPHMVVP 1218
Cdd:COG0793    281 SVQTVFPLPD-GGALKLTTARYYTPS-GRSIQGKGVEPDIEVP 321
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
437-631 2.40e-15

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: 77.63  E-value: 2.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  437 GNVGYLRFDSFADASvlgvlapyvLRQVWE---PLQDTEHLIMDLRHNPGGpsSAVPLLLSYFQGPEAGpvhlfTTYDRR 513
Cdd:cd07562     87 GRIGYVHIPDMGDDG---------FAEFLRdllAEVDKDGLIIDVRFNGGG--NVADLLLDFLSRRRYG-----YDIPRG 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  514 TNitqehfshMELPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLLDtpeGSLaLTV 593
Cdd:cd07562    151 GG--------KPVTYPSGRWRGPVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRLPD---GGS-LTV 218
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1411179691  594 PVLTFIDNHGEAWLGGGVVPDAIVLAE---------EALDKAQEVLE 631
Cdd:cd07562    219 PEFGVYLPDGGPLENRGVAPDIEVENTpedvaagrdPQLEAAIEELL 265
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
426-624 4.19e-15

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: 78.37  E-value: 4.19e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  426 VESVFqVSVLPGNVGYLRFDSFADASvlgvlAPYVLRQVWE-PLQDTEHLIMDLRHNPGGPSSAVPLLLSYFQgpEAGPV 504
Cdd:COG0793    147 LPSVE-AKLLEGKIGYIRIPSFGENT-----AEEFKRALKElKKQGAKGLILDLRNNPGGLLDEAVELADLFL--PKGPI 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  505 hlFTTYDRRTNITQEHFShmelPGPRYSTQRgVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLldt 584
Cdd:COG0793    219 --VYTRGRNGKVETYKAT----PGGALYDGP-LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSVQTVFPL--- 288
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1411179691  585 PEGSlALTVPVLTFIDNHGEAWLGGGVVPDaIVLAEEALD 624
Cdd:COG0793    289 PDGG-ALKLTTARYYTPSGRSIQGKGVEPD-IEVPLTPED 326
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
1039-1231 4.37e-15

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: 76.85  E-value: 4.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1039 EDNIGYLRF-DMFGDG------ELLTQVSKllvehvwkkimhtDAMIIDMRFNIGGPTSSipilcsyffdegppILLDKI 1111
Cdd:cd07562     86 DGRIGYVHIpDMGDDGfaeflrDLLAEVDK-------------DGLIIDVRFNGGGNVAD--------------LLLDFL 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1112 YSRPDDSISELWTHAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSGGCQPPQTYHVDDtNLYLT 1191
Cdd:cd07562    139 SRRRYGYDIPRGGGKPVTYPSGRWRGPVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRLPD-GGSLT 217
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1411179691 1192 IPTARSVGAsDGSSWEGVGVTPHMVVPAE---------EALTRAKEMLQ 1231
Cdd:cd07562    218 VPEFGVYLP-DGGPLENRGVAPDIEVENTpedvaagrdPQLEAAIEELL 265
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
21-127 2.17e-14

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: 71.20  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691   21 HLFQPSLVLDMAKVLLDNYCFPENLLGMQEAIQQAIKSHEILSISDPQTLASVLTAGVQSSLNDPRLVISY---EPSTPE 97
Cdd:pfam11918   15 RRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPRLKVRYirpEPASDE 94
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1411179691   98 P-----PPQVPALTSLSEEELLAWLQRGLRHEVLE 127
Cdd:pfam11918   95 PeaadnIPGLVPMQPPSPEMLEALIKSSFKVDVLP 129
Peptidase_S41 pfam03572
Peptidase family S41;
1041-1217 2.34e-14

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 72.25  E-value: 2.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1041 NIGYLRFDMFG---DGELLTQVSKLLVEHVwkkimhtDAMIIDMRFNIGGPTSSIPILCSYFFDEGPpILL--DKIYSRP 1115
Cdd:pfam03572    1 KIGYIRIPSFSektAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLFLPDGT-IVStrGRDGSKE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1116 DDSiselwthAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVT--SGGCQPPQTYhVDDTNLYLTIP 1193
Cdd:pfam03572   73 VYF-------AAGKADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTfgKGTVQTVYPL-PDGSALKLTIA 144
                          170       180
                   ....*....|....*....|....
gi 1411179691 1194 TARSvgaSDGSSWEGVGVTPHMVV 1217
Cdd:pfam03572  145 KYYT---PDGRSIEGKGIEPDIEV 165
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
123-320 4.44e-13

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: 70.69  E-value: 4.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  123 HEVLEGNVGYLRVDSvpgqevlsMMGEFLvAHVWGKLMGTS---ALVLDLRHCTGGQISGipYIISYLHPGNTILHVDTI 199
Cdd:cd07562     82 EELSDGRIGYVHIPD--------MGDDGF-AEFLRDLLAEVdkdGLIIDVRFNGGGNVAD--LLLDFLSRRRYGYDIPRG 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  200 YNRPSNTTTEIWTLPqvlgerygadkdVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRKLR-IGESdfFF 278
Cdd:cd07562    151 GGKPVTYPSGRWRGP------------VVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRlPDGG--SL 216
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1411179691  279 TVPVSRSLGPLGGGSqtwEGSGVLPCV---GTPAEQA------LEKALDIL 320
Cdd:cd07562    217 TVPEFGVYLPDGGPL---ENRGVAPDIeveNTPEDVAagrdpqLEAAIEEL 264
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
122-319 6.19e-13

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: 71.44  E-value: 6.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  122 RHEVLEGNVGYLRVDSV---PGQEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPGNTIL---- 194
Cdd:COG0793    151 EAKLLEGKIGYIRIPSFgenTAEEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVELADLFLPKGPIVytrg 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  195 ---HVDTIYNRPSNTtteIWTLPqvlgerygadkdVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGAL--DLRKL 269
Cdd:COG0793    224 rngKVETYKATPGGA---LYDGP------------LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGSvqTVFPL 288
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1411179691  270 rigESDFFFTVPVSRSLGPLGGGsqtWEGSGVLP--CVGTPAEQ-------ALEKALDI 319
Cdd:COG0793    289 ---PDGGALKLTTARYYTPSGRS---IQGKGVEPdiEVPLTPEDllkgrdpQLEKALEL 341
Peptidase_S41 pfam03572
Peptidase family S41;
129-303 3.84e-10

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 59.93  E-value: 3.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  129 NVGYLRVDS---VPGQEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPGNTILHVDtiyNRPSN 205
Cdd:pfam03572    1 KIGYIRIPSfseKTAKELAEALKEL-------KKQGVKGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTR---GRDGS 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  206 TTTEIWTLPQVlgeRYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRKLRIGeSDFFFTVPVSRS 285
Cdd:pfam03572   71 KEVYFAAGKAD---EVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPLP-DGSALKLTIAKY 146
                          170
                   ....*....|....*...
gi 1411179691  286 LGPlGGGSQtwEGSGVLP 303
Cdd:pfam03572  147 YTP-DGRSI--EGKGIEP 161
Peptidase_S41_CPP cd07560
C-terminal processing peptidase; serine protease family S41; The C-terminal processing ...
777-919 8.49e-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: 57.04  E-value: 8.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  777 ALVIDLRYNPG-SYSTAIpLLCSYFFEAEPrqhLYSVFDRA------TSKVMEVWTLPqvagqrygshkdLYILMSHTSG 849
Cdd:cd07560     80 GLILDLRNNPGgLLDEAV-EIADLFLPGGP---IVSTKGRNgkreayASDDGGLYDGP------------LVVLVNGGSA 143
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411179691  850 SAAEAFAHTMQDLQRATVIGEPTAGGalsvGIYQVgsspLYaSMPTQMALSATTGKaW--------DLAGVEPDITVP 919
Cdd:cd07560    144 SASEIVAGALQDNGRAVLVGERTFGK----GSVQT----VF-PLSDGSALKLTTAK-YytpsgrsiQKKGIEPDIEVP 211
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
744-919 6.00e-08

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: 56.21  E-value: 6.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  744 GYLRFDAMAElETVKAVGPQLVRLVWQQLVdtaALVIDLRYNPGSYSTAIPLLCSYFFEAEPrqhLYSVFDRATSKvmEV 823
Cdd:TIGR00225  154 GYIRISSFSE-HTAEDVAKALDKLEKKNAK---GYILDLRGNPGGLLQSAVDISRLFITKGP---IVQTKDRNGSK--RH 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  824 WTlpqvAGQRYGSHKDLYILMSHTSGSAAEAFAHTMQDLQRATVIGEPTAGGALsvgIYQVgsSPLYASMPTQMALS--- 900
Cdd:TIGR00225  225 YK----ANGRQKYNLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTFGKGT---VQQV--RPLNDGSGIKVTIAkyy 295
                          170
                   ....*....|....*....
gi 1411179691  901 ATTGKAWDLAGVEPDITVP 919
Cdd:TIGR00225  296 TPNGGSIHKKGIEPDIVIE 314
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
438-550 1.16e-05

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: 48.40  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  438 NVGYLRFDSFAdasvlgvlAPYV--LRQVWEPLQDTE--HLIMDLRHNPGGPSSAVPLLLSYFqgpeAGPVH---LFTTY 510
Cdd:cd07561     65 KVGYLVYNSFT--------SGYDdeLNQAFAEFKAQGvtELVLDLRYNGGGLVSSANLLASLL----APAVAlgqVFATL 132
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1411179691  511 DRRTNITQEhfsHMELPGPRYSTQRG-------VYLLTSHRTATAAE 550
Cdd:cd07561    133 EYNDKRSAN---NEDLLFSSKTLAGGnslnlskVYVLTSGSTASASE 176
prc TIGR00225
C-terminal peptidase (prc); A C-terminal peptidase with different substrates in different ...
438-593 1.63e-05

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: 48.51  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  438 NVGYLRFDSFAdasvlgvlaPYVLRQVWEPLQDTEH-----LIMDLRHNPGGPSSAVPLLLSYFQgpEAGPVhlFTTYDR 512
Cdd:TIGR00225  152 SVGYIRISSFS---------EHTAEDVAKALDKLEKknakgYILDLRGNPGGLLQSAVDISRLFI--TKGPI--VQTKDR 218
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  513 rtNITQEHFShmelPGPRYSTQRGVYLLTSHRTATAAEEFAFLMQSLGWATLVGEITAGNLLHTRTVPLLDTpeGSLALT 592
Cdd:TIGR00225  219 --NGSKRHYK----ANGRQKYNLPLVVLVNRGSASASEILAGALQDNGRATIVGEKTFGKGTVQQVRPLNDG--SGIKVT 290

                   .
gi 1411179691  593 V 593
Cdd:TIGR00225  291 I 291
Peptidase_S41_CPP cd07560
C-terminal processing peptidase; serine protease family S41; The C-terminal processing ...
1034-1218 3.07e-05

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: 46.64  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1034 HTNvFEDNIGYLRFDMFGDG---ELLTQVSKLLVEHVwkkimhtDAMIIDMRFNIGGP-TSSIPIlCSYFFDEGPpIlld 1109
Cdd:cd07560     43 YSR-YLTPIGYIRITSFSENtaeELKKALKELKKQGM-------KGLILDLRNNPGGLlDEAVEI-ADLFLPGGP-I--- 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691 1110 kIYSRPDDSISElwthAQVVGERYGSKKSMVILTSSVTAGTAEEFTYIMKRLGRALVIGEVTSG-GCQppQTYHV--DDT 1186
Cdd:cd07560    110 -VSTKGRNGKRE----AYASDDGGLYDGPLVVLVNGGSASASEIVAGALQDNGRAVLVGERTFGkGSV--QTVFPlsDGS 182
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1411179691 1187 NLYLTI-----PTARSVgasdgsswEGVGVTPHMVVP 1218
Cdd:cd07560    183 ALKLTTakyytPSGRSI--------QKKGIEPDIEVP 211
Peptidase_S41_CPP cd07560
C-terminal processing peptidase; serine protease family S41; The C-terminal processing ...
439-617 5.20e-05

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: 45.87  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  439 VGYLRFDSFADASvlgvlAPYVLRQVWEpLQDT--EHLIMDLRHNPGGP-SSAVpLLLSYFqgPEAGPVhlFTTYDRRTN 515
Cdd:cd07560     50 IGYIRITSFSENT-----AEELKKALKE-LKKQgmKGLILDLRNNPGGLlDEAV-EIADLF--LPGGPI--VSTKGRNGK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  516 I-TQEHFSHMELPGPrystqrgVYLLTSHRTATAAEEFAFLMQSLGWATLVGEitagnllhtRT---------VPLLDtp 585
Cdd:cd07560    119 ReAYASDDGGLYDGP-------LVVLVNGGSASASEIVAGALQDNGRAVLVGE---------RTfgkgsvqtvFPLSD-- 180
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1411179691  586 EGSLALTV-----PVLTFIDnhgeawlGGGVVPDAIV 617
Cdd:cd07560    181 GSALKLTTakyytPSGRSIQ-------KKGIEPDIEV 210
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
129-261 5.43e-04

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: 43.40  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  129 NVGYLRVDS-VPG--QEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPGNTI--LHVDTIYN-- 201
Cdd:cd07561     65 KVGYLVYNSfTSGydDELNQAFAEF-------KAQGVTELVLDLRYNGGGLVSSANLLASLLAPAVALgqVFATLEYNdk 137
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  202 RPSNTTTEIWTLPQVLGERYGADKDVVVLTSSQTRGVAEDIAHILKQMRRAIVVGERTGG 261
Cdd:cd07561    138 RSANNEDLLFSSKTLAGGNSLNLSKVYVLTSGSTASASELVINSLKPYMDVVLIGETTYG 197
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
778-918 7.18e-04

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: 43.01  E-value: 7.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411179691  778 LVIDLRYNPGSY-STAIpLLCSYFFEAEPRQHLYSVF----DRATSKVMEVWTLPQVAGQRYGSHKDLYILMSHTSGSAA 852
Cdd:cd07561     97 LVLDLRYNGGGLvSSAN-LLASLLAPAVALGQVFATLeyndKRSANNEDLLFSSKTLAGGNSLNLSKVYVLTSGSTASAS 175
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411179691  853 EAFAHTMQDLQRATVIGEPTAGGAlsvgiyqVGSSPLYASMPTQMALSATTGKAWDLA-------GVEPDITV 918
Cdd:cd07561    176 ELVINSLKPYMDVVLIGETTYGKN-------VGSLTFEDDRKHKWALQPVVFKVVNADgqgdysnGLTPDIEV 241
 
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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