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Conserved domains on  [gi|320578932|gb|ADW54294|]
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interphotoreceptor retinoid binding protein, partial [Abrothrix illuteus]

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 ...
 3-274 2.75e-68

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: 215.62  E-value: 2.75e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   3 GMQAAIEQAMKSREILGISDPQMLAHVLTAGVQSsLNDPRLFISYepstletpqqapmltnltreelmaqlqknihhevl 82
Cdd:cd07563   21 IDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY----------------------------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  83 egnVGYLRVDDLPGQEVlsELGEFLVDHVWRQLMSTSSLVLDLRHCAGGHISGIPYVISYLYPGNTVMHVDTIYDRPSNT 162
Cdd:cd07563   65 ---IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNT 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 163 TTEIWTLPKVIGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGALDLQKLRIGQsNFFLTVPVSRSL 242
Cdd:cd07563  140 TTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSV 218

                        250       260       270
                 ....*....|....*....|....*....|..
gi 320578932 243 GPLggGGQTWEGSGVLPCVGIPA*QALEKALA 274
Cdd:cd07563  219 DPI--TGTNWEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
 265-385 2.23e-51

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: 167.88  E-value: 2.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  265 A*QALEKALAILTLRRALPGVVLRLQEALQDYYTLVDRVPGLLHHLASM----DYSAVVSEDDLVTKLNAGLQAVSEDPR 340
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 320578932  341 LLVRATGPKESSSRPETGPNdPPEAAPEVPKEEAARRALVDSVFQ 385
Cdd:pfam11918  81 LKVRYIRPEPASDEPEAADN-IPGLVPMQPPSPEMLEALIKSSFK 124
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 3-274 2.75e-68

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: 215.62  E-value: 2.75e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   3 GMQAAIEQAMKSREILGISDPQMLAHVLTAGVQSsLNDPRLFISYepstletpqqapmltnltreelmaqlqknihhevl 82
Cdd:cd07563   21 IDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY----------------------------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  83 egnVGYLRVDDLPGQEVlsELGEFLVDHVWRQLMSTSSLVLDLRHCAGGHISGIPYVISYLYPGNTVMHVDTIYDRPSNT 162
Cdd:cd07563   65 ---IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNT 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 163 TTEIWTLPKVIGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGALDLQKLRIGQsNFFLTVPVSRSL 242
Cdd:cd07563  140 TTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSV 218

                        250       260       270
                 ....*....|....*....|....*....|..
gi 320578932 243 GPLggGGQTWEGSGVLPCVGIPA*QALEKALA 274
Cdd:cd07563  219 DPI--TGTNWEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
 265-385 2.23e-51

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: 167.88  E-value: 2.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  265 A*QALEKALAILTLRRALPGVVLRLQEALQDYYTLVDRVPGLLHHLASM----DYSAVVSEDDLVTKLNAGLQAVSEDPR 340
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 320578932  341 LLVRATGPKESSSRPETGPNdPPEAAPEVPKEEAARRALVDSVFQ 385
Cdd:pfam11918  81 LKVRYIRPEPASDEPEAADN-IPGLVPMQPPSPEMLEALIKSSFK 124
TSPc smart00245
tail specific protease; tail specific protease
 65-264 2.46e-51

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 170.13  E-value: 2.46e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932    65 TREELMAQLQKNIHHEVLEGNVGYLRVDDLpGQEVLSELGE---FLVDHVWRQLMST--SSLVLDLRHCAGGHISGIPYV 139
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   140 ISYLYPGNTvmHVDTIYDRpsntTTEIWTLPKVIGERYSadKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGA 219
Cdd:smart00245  80 SSLFLDKGV--IVYTVYRR----TGELWTYPANLGRKYS--KPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 320578932   220 LDLQKLRIGqSNFFLTVPVSRSLGPlggGGQTWEGSGVLPCVGIP 264
Cdd:smart00245 152 LVQQTVPLG-DGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 59-259 4.86e-16

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: 4.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  59 PMLTNLTREELmaqLQKNIHHEVLEGNVGYLRVDDL---PGQEVLSELGEFLVDHVwrqlmstSSLVLDLRHCAGGHISG 135
Cdd:COG0793  135 PITVTLTRAEI---KLPSVEAKLLEGKIGYIRIPSFgenTAEEFKRALKELKKQGA-------KGLILDLRNNPGGLLDE 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 136 IPYVISYLYPGNTVMhvdtiYDRPSNTTTEIWtlpKVIGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERT 215
Cdd:COG0793  205 AVELADLFLPKGPIV-----YTRGRNGKVETY---KATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRT 276

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 320578932 216 EGGAldlqklrIGQSNF------FLTVPVSRSLGPlggGGQTWEGSGVLP 259
Cdd:COG0793  277 FGKG-------SVQTVFplpdggALKLTTARYYTP---SGRSIQGKGVEP 316
Peptidase_S41 pfam03572
Peptidase family S41;
85-259 9.41e-13

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 65.70  E-value: 9.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   85 NVGYLRV---DDLPGQEVLSELGEFLVDHVwrqlmstSSLVLDLRHCAGGHISGIPYVISYLYPGNTVMHVDtiyDRPSN 161
Cdd:pfam03572   1 KIGYIRIpsfSEKTAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTR---GRDGS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  162 TTTEIWTLPkviGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTeGGALDLQKLRIGQSNFFLTVPVSRS 241
Cdd:pfam03572  71 KEVYFAAGK---ADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERT-FGKGTVQTVYPLPDGSALKLTIAKY 146

                         170
                  ....*....|....*...
gi 320578932  242 LGPlggGGQTWEGSGVLP 259
Cdd:pfam03572 147 YTP---DGRSIEGKGIEP 161
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 285-347 1.78e-04

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: 42.66  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320578932 285 VVLRLQEALQDYY----TLVDRVPGLLHHLASMDYSAVVSEDDLVTKLNAGLQAVsEDPRLLVRATG 347
Cdd:cd07563    1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYIG 66
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 3-274 2.75e-68

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: 215.62  E-value: 2.75e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   3 GMQAAIEQAMKSREILGISDPQMLAHVLTAGVQSsLNDPRLFISYepstletpqqapmltnltreelmaqlqknihhevl 82
Cdd:cd07563   21 IDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY----------------------------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  83 egnVGYLRVDDLPGQEVlsELGEFLVDHVWRQLMSTSSLVLDLRHCAGGHISGIPYVISYLYPGNTVMHVDTIYDRPSNT 162
Cdd:cd07563   65 ---IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNT 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 163 TTEIWTLPKVIGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGALDLQKLRIGQsNFFLTVPVSRSL 242
Cdd:cd07563  140 TTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSV 218

                        250       260       270
                 ....*....|....*....|....*....|..
gi 320578932 243 GPLggGGQTWEGSGVLPCVGIPA*QALEKALA 274
Cdd:cd07563  219 DPI--TGTNWEGVGVPPDIEVPATPGYDDALE 248
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
 265-385 2.23e-51

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: 167.88  E-value: 2.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  265 A*QALEKALAILTLRRALPGVVLRLQEALQDYYTLVDRVPGLLHHLASM----DYSAVVSEDDLVTKLNAGLQAVSEDPR 340
Cdd:pfam11918   1 AEEALEKALEILALRRAIPALVQTLGKLLADNYAFPERVPAVAAHLASLlasgDYSSVVSEEDLASKLNADLQALSGDPR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 320578932  341 LLVRATGPKESSSRPETGPNdPPEAAPEVPKEEAARRALVDSVFQ 385
Cdd:pfam11918  81 LKVRYIRPEPASDEPEAADN-IPGLVPMQPPSPEMLEALIKSSFK 124
TSPc smart00245
tail specific protease; tail specific protease
 65-264 2.46e-51

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 170.13  E-value: 2.46e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932    65 TREELMAQLQKNIHHEVLEGNVGYLRVDDLpGQEVLSELGE---FLVDHVWRQLMST--SSLVLDLRHCAGGHISGIPYV 139
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   140 ISYLYPGNTvmHVDTIYDRpsntTTEIWTLPKVIGERYSadKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGA 219
Cdd:smart00245  80 SSLFLDKGV--IVYTVYRR----TGELWTYPANLGRKYS--KPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 320578932   220 LDLQKLRIGqSNFFLTVPVSRSLGPlggGGQTWEGSGVLPCVGIP 264
Cdd:smart00245 152 LVQQTVPLG-DGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
 15-264 8.48e-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: 111.62  E-value: 8.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  15 REILGISDPQMLAHVLTAGVQSsLNDPRLFISYepstletpqqapmltnltreelmaqlqknihhevlegnVGYLRVDDL 94
Cdd:cd06567   29 DLLDAVDDRELLAGALNGMLGE-LGDPHSRYLT--------------------------------------IGYIRIPSF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  95 PGQEVLSELGEFLVDhvwrQLMSTSSLVLDLRHCAGGHISGIPYVISYLYPGNTVMHVDTIYDRPsnttteiWTLPKVIG 174
Cdd:cd06567   70 SAESTAEELREALAE----LKKGVKGLILDLRNNPGGLLSAAVELASLFLPKGKIVVTTRRRGGN-------ETEYVAPG 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 175 ERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGALDlQKLRIGQSNFFLTVPVSRSLGPlggGGQTWEG 254
Cdd:cd06567  139 GGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSV-QTVFPLLDGSALKLTTAKYYTP---SGRSIEG 214

                        250
                 ....*....|
gi 320578932 255 SGVLPCVGIP 264
Cdd:cd06567  215 KGVEPDIEVP 224
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 59-259 4.86e-16

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: 4.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  59 PMLTNLTREELmaqLQKNIHHEVLEGNVGYLRVDDL---PGQEVLSELGEFLVDHVwrqlmstSSLVLDLRHCAGGHISG 135
Cdd:COG0793  135 PITVTLTRAEI---KLPSVEAKLLEGKIGYIRIPSFgenTAEEFKRALKELKKQGA-------KGLILDLRNNPGGLLDE 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 136 IPYVISYLYPGNTVMhvdtiYDRPSNTTTEIWtlpKVIGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERT 215
Cdd:COG0793  205 AVELADLFLPKGPIV-----YTRGRNGKVETY---KATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRT 276

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 320578932 216 EGGAldlqklrIGQSNF------FLTVPVSRSLGPlggGGQTWEGSGVLP 259
Cdd:COG0793  277 FGKG-------SVQTVFplpdggALKLTTARYYTP---SGRSIQGKGVEP 316
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
 79-276 6.19e-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: 71.08  E-value: 6.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  79 HEVLEGNVGYLRVDDLpGQEVLSELgeflvdhvWRQLMSTSS---LVLDLRHCAGGHISGipYVISYLypgntvMHVDTI 155
Cdd:cd07562   82 EELSDGRIGYVHIPDM-GDDGFAEF--------LRDLLAEVDkdgLIIDVRFNGGGNVAD--LLLDFL------SRRRYG 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932 156 YDRPSNTTTEIWTlpkvigERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTEGGALDLQKLR-IGQSnfFL 234
Cdd:cd07562  145 YDIPRGGGKPVTY------PSGRWRGPVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRlPDGG--SL 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 320578932 235 TVPVSRSLGPLGGGGqtwEGSGVLPCVGIPA*---------QALEKALAIL 276
Cdd:cd07562  217 TVPEFGVYLPDGGPL---ENRGVAPDIEVENTpedvaagrdPQLEAAIEEL 264
Peptidase_S41 pfam03572
Peptidase family S41;
85-259 9.41e-13

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 65.70  E-value: 9.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932   85 NVGYLRV---DDLPGQEVLSELGEFLVDHVwrqlmstSSLVLDLRHCAGGHISGIPYVISYLYPGNTVMHVDtiyDRPSN 161
Cdd:pfam03572   1 KIGYIRIpsfSEKTAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTR---GRDGS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320578932  162 TTTEIWTLPkviGERYSADKDVVVLTSGHTGGVAEDITYILKQMRRAIVVGERTeGGALDLQKLRIGQSNFFLTVPVSRS 241
Cdd:pfam03572  71 KEVYFAAGK---ADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERT-FGKGTVQTVYPLPDGSALKLTIAKY 146

                         170
                  ....*....|....*...
gi 320578932  242 LGPlggGGQTWEGSGVLP 259
Cdd:pfam03572 147 YTP---DGRSIEGKGIEP 161
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 285-347 1.78e-04

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: 42.66  E-value: 1.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320578932 285 VVLRLQEALQDYY----TLVDRVPGLLHHLASMDYSAVVSEDDLVTKLNAGLQAVsEDPRLLVRATG 347
Cdd:cd07563    1 VFEALAKLLEENYafpeAKGIDWDALAARLRAQVYLDITSPEELAAVLTADLQEL-GDGHLNVSYIG 66
 
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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