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Conserved domains on  [gi|42521616|gb|AAS18302|]
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interphotoreceptor retinoid binding protein, partial [Colobus guereza]

Protein Classification

interphotoreceptor retinoid-binding protein( domain architecture ID 10166016)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 27-215 1.02e-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: 206.76  E-value: 1.02e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  27 VGYLRVDSVPGQEVlsMMGEFLVAHVWGKLMGTSALVLDLRHCTGGQISGIPYIISYLHPG*TILHVDTIYNRPSNTTTE 106
Cdd:cd07563  65 IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNTTTE 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616 107 IWTLPQVLGERYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*RIGEsDFFFTVPVSRSLGPL 186
Cdd:cd07563 143 LWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSVDPI 221

                       170       180
                ....*....|....*....|....*....
gi 42521616 187 GGGSqtWEGSGVLPCVGTPAEQALEKALD 215
Cdd:cd07563 222 TGTN--WEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
 206-314 1.62e-47

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: 155.94  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616   206 AEQALEKALDILTLRSALPGVVHCLQEALKDYYTLVDRVPTLLQHLASM----DFSTVVSEDDLVTKLNAGLQAASEDPR 281
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 42521616   282 LLVRAIRPRETPSGPvpdAAAEDPPGAAPELPE 314
Cdd:pfam11918  81 LKVRYIRPEPASDEP---EAADNIPGLVPMQPP 110
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 27-215 1.02e-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: 206.76  E-value: 1.02e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  27 VGYLRVDSVPGQEVlsMMGEFLVAHVWGKLMGTSALVLDLRHCTGGQISGIPYIISYLHPG*TILHVDTIYNRPSNTTTE 106
Cdd:cd07563  65 IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNTTTE 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616 107 IWTLPQVLGERYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*RIGEsDFFFTVPVSRSLGPL 186
Cdd:cd07563 143 LWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSVDPI 221

                       170       180
                ....*....|....*....|....*....
gi 42521616 187 GGGSqtWEGSGVLPCVGTPAEQALEKALD 215
Cdd:cd07563 222 TGTN--WEGVGVPPDIEVPATPGYDDALE 248
TSPc smart00245
tail specific protease; tail specific protease
 6-205 1.90e-49

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 162.81  E-value: 1.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616      6 SEEELLAWLQRGLRHEVLEGNVGYLRVDSVpGQEVLSMMGE---FLVAHVWGKLMGT--SALVLDLRHCTGGQISGIPYI 80
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616     81 ISYLHPG*TIlhVDTIYNRpsntTTEIWTLPQVLGERYgaDKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGA 160
Cdd:smart00245  80 SSLFLDKGVI--VYTVYRR----TGELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 42521616    161 LDLRK*RIGEsDFFFTVPVSRSLGPLGggsQTWEGSGVLPCVGTP 205
Cdd:smart00245 152 LVQQTVPLGD-GSGLKLTVAKYYTPSG---KSIEKKGVEPDIQVP 192
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
 206-314 1.62e-47

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: 155.94  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616   206 AEQALEKALDILTLRSALPGVVHCLQEALKDYYTLVDRVPTLLQHLASM----DFSTVVSEDDLVTKLNAGLQAASEDPR 281
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 42521616   282 LLVRAIRPRETPSGPvpdAAAEDPPGAAPELPE 314
Cdd:pfam11918  81 LKVRYIRPEPASDEP---EAADNIPGLVPMQPP 110
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 19-161 8.58e-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: 67.97  E-value: 8.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  19 RHEVLEGNVGYLRVDSV---PGQEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPG*TIL---- 91
Cdd:COG0793 151 EAKLLEGKIGYIRIPSFgenTAEEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVELADLFLPKGPIVytrg 223

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42521616  92 ---HVDTIYNRPSNTtteIWTLPqvlgerygadkdVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGAL 161
Cdd:COG0793 224 rngKVETYKATPGGA---LYDGP------------LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGS 281
Peptidase_S41 pfam03572
Peptidase family S41;
26-200 8.76e-11

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 59.54  E-value: 8.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616    26 NVGYLRVDS---VPGQEVLSMMGEFLVAHVwgklmgtSALVLDLRHCTGGQISGIPYIISYLHPG*TILHVDtiyNRPSN 102
Cdd:pfam03572   1 KIGYIRIPSfseKTAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTR---GRDGS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616   103 TTTEIWTLPQVlgeRYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*RIGeSDFFFTVPVSRS 182
Cdd:pfam03572  71 KEVYFAAGKAD---EVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPLP-DGSALKLTIAKY 146

                         170
                  ....*....|....*...
gi 42521616   183 LGPlGGGSQtwEGSGVLP 200
Cdd:pfam03572 147 YTP-DGRSI--EGKGIEP 161
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 226-287 4.01e-05

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


Pssm-ID: 143479 [Multi-domain]  Cd Length: 250  Bit Score: 44.20  E-value: 4.01e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42521616 226 VVHCLQEALKDYY----TLVDRVPTLLQHLASMDFSTVVSEDDLVTKLNAGLQAAsEDPRLLVRAI 287
Cdd:cd07563   1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI 65
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 27-215 1.02e-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: 206.76  E-value: 1.02e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  27 VGYLRVDSVPGQEVlsMMGEFLVAHVWGKLMGTSALVLDLRHCTGGQISGIPYIISYLHPG*TILHVDTIYNRPSNTTTE 106
Cdd:cd07563  65 IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNTTTE 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616 107 IWTLPQVLGERYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*RIGEsDFFFTVPVSRSLGPL 186
Cdd:cd07563 143 LWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSVDPI 221

                       170       180
                ....*....|....*....|....*....
gi 42521616 187 GGGSqtWEGSGVLPCVGTPAEQALEKALD 215
Cdd:cd07563 222 TGTN--WEGVGVPPDIEVPATPGYDDALE 248
TSPc smart00245
tail specific protease; tail specific protease
 6-205 1.90e-49

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 162.81  E-value: 1.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616      6 SEEELLAWLQRGLRHEVLEGNVGYLRVDSVpGQEVLSMMGE---FLVAHVWGKLMGT--SALVLDLRHCTGGQISGIPYI 80
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616     81 ISYLHPG*TIlhVDTIYNRpsntTTEIWTLPQVLGERYgaDKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGA 160
Cdd:smart00245  80 SSLFLDKGVI--VYTVYRR----TGELWTYPANLGRKY--SKPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 42521616    161 LDLRK*RIGEsDFFFTVPVSRSLGPLGggsQTWEGSGVLPCVGTP 205
Cdd:smart00245 152 LVQQTVPLGD-GSGLKLTVAKYYTPSG---KSIEKKGVEPDIQVP 192
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
 206-314 1.62e-47

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: 155.94  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616   206 AEQALEKALDILTLRSALPGVVHCLQEALKDYYTLVDRVPTLLQHLASM----DFSTVVSEDDLVTKLNAGLQAASEDPR 281
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 42521616   282 LLVRAIRPRETPSGPvpdAAAEDPPGAAPELPE 314
Cdd:pfam11918  81 LKVRYIRPEPASDEP---EAADNIPGLVPMQPP 110
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
 26-202 1.18e-28

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


Pssm-ID: 143475 [Multi-domain]  Cd Length: 224  Bit Score: 109.69  E-value: 1.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  26 NVGYLRVDSvpgqevlsMMGEFLVAHVWGKLM----GTSALVLDLRHCTGGQISGIPYIISYLHPG*TILHVDTIYNRPs 101
Cdd:cd06567  60 TIGYIRIPS--------FSAESTAEELREALAelkkGVKGLILDLRNNPGGLLSAAVELASLFLPKGKIVVTTRRRGGN- 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616 102 nttteiWTLPQVLGERYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*RIGeSDFFFTVPVSR 181
Cdd:cd06567 131 ------ETEYVAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSVQTVFPLL-DGSALKLTTAK 203

                       170       180
                ....*....|....*....|.
gi 42521616 182 SLGPLGGgsqTWEGSGVLPCV 202
Cdd:cd06567 204 YYTPSGR---SIEGKGVEPDI 221
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
 20-217 5.70e-14

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


Pssm-ID: 143478 [Multi-domain]  Cd Length: 266  Bit Score: 70.69  E-value: 5.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  20 HEVLEGNVGYLRVDSvpgqevlsMMGEFLvAHVWGKLMGTS---ALVLDLRHCTGGQISGipYIISYLHPG*TILHVDTI 96
Cdd:cd07562  82 EELSDGRIGYVHIPD--------MGDDGF-AEFLRDLLAEVdkdGLIIDVRFNGGGNVAD--LLLDFLSRRRYGYDIPRG 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  97 YNRPSNTTTEIWTLPqvlgerygadkdVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*R-IGESdfFF 175
Cdd:cd07562 151 GGKPVTYPSGRWRGP------------VVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRlPDGG--SL 216

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42521616 176 TVPVSRSLGPLGGGSqtwEGSGVLPCV---GTPAEQA------LEKALDIL 217
Cdd:cd07562 217 TVPEFGVYLPDGGPL---ENRGVAPDIeveNTPEDVAagrdpqLEAAIEEL 264
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 19-161 8.58e-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: 67.97  E-value: 8.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  19 RHEVLEGNVGYLRVDSV---PGQEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPG*TIL---- 91
Cdd:COG0793 151 EAKLLEGKIGYIRIPSFgenTAEEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVELADLFLPKGPIVytrg 223

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42521616  92 ---HVDTIYNRPSNTtteIWTLPqvlgerygadkdVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGAL 161
Cdd:COG0793 224 rngKVETYKATPGGA---LYDGP------------LVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGKGS 281
Peptidase_S41 pfam03572
Peptidase family S41;
26-200 8.76e-11

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 59.54  E-value: 8.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616    26 NVGYLRVDS---VPGQEVLSMMGEFLVAHVwgklmgtSALVLDLRHCTGGQISGIPYIISYLHPG*TILHVDtiyNRPSN 102
Cdd:pfam03572   1 KIGYIRIPSfseKTAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTR---GRDGS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616   103 TTTEIWTLPQVlgeRYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGGGALDLRK*RIGeSDFFFTVPVSRS 182
Cdd:pfam03572  71 KEVYFAAGKAD---EVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERTFGKGTVQTVYPLP-DGSALKLTIAKY 146

                         170
                  ....*....|....*...
gi 42521616   183 LGPlGGGSQtwEGSGVLP 200
Cdd:pfam03572 147 YTP-DGRSI--EGKGIEP 161
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 226-287 4.01e-05

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


Pssm-ID: 143479 [Multi-domain]  Cd Length: 250  Bit Score: 44.20  E-value: 4.01e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42521616 226 VVHCLQEALKDYY----TLVDRVPTLLQHLASMDFSTVVSEDDLVTKLNAGLQAAsEDPRLLVRAI 287
Cdd:cd07563   1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYI 65
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
 26-158 6.51e-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: 40.70  E-value: 6.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  26 NVGYLRVDS-VPG--QEVLSMMGEFlvahvwgKLMGTSALVLDLRHCTGGQISGIPYIISYLHPG*TI--LHVDTIYN-- 98
Cdd:cd07561  65 KVGYLVYNSfTSGydDELNQAFAEF-------KAQGVTELVLDLRYNGGGLVSSANLLASLLAPAVALgqVFATLEYNdk 137

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42521616  99 RPSNTTTEIWTLPQVLGERYGADKDVVVLTS*QTRGVAEDIAHILKQMRRAIVVGERTGG 158
Cdd:cd07561 138 RSANNEDLLFSSKTLAGGNSLNLSKVYVLTSGSTASASELVINSLKPYMDVVLIGETTYG 197
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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