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Conserved domains on  [gi|987857430|gb|AME16428|]
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interstitial retinol binding protein 3, partial [Tateomys rhinogradoides]

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 ...
3-274 8.78e-71

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: 218.32  E-value: 8.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   3 GMQAAIEQAMKSHEILGISDPQTLAHVLTAGVQSsLNDPRLFISYepstleapqqapaltnltreellaqiqrnihhevl 82
Cdd:cd07563   21 IDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY----------------------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  83 egnVGYLRVDDLPGQEVlsELGEFLVSHVWKQLMSTSSLVLDLRHCAGGHVSGIPYVISYLHPGNTVLHVDTIYDRPSNT 162
Cdd:cd07563   65 ---IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 163 TTEIWTLPKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDLQKLRIGQsNFFLTVPVSRSL 242
Cdd:cd07563  140 TTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSV 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 987857430 243 GPLggGGQTWEGSGVLPCVGIPAEQALEKALA 274
Cdd:cd07563  219 DPI--TGTNWEGVGVPPDIEVPATPGYDDALE 248
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
3-274 8.78e-71

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: 218.32  E-value: 8.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   3 GMQAAIEQAMKSHEILGISDPQTLAHVLTAGVQSsLNDPRLFISYepstleapqqapaltnltreellaqiqrnihhevl 82
Cdd:cd07563   21 IDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY----------------------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  83 egnVGYLRVDDLPGQEVlsELGEFLVSHVWKQLMSTSSLVLDLRHCAGGHVSGIPYVISYLHPGNTVLHVDTIYDRPSNT 162
Cdd:cd07563   65 ---IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 163 TTEIWTLPKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDLQKLRIGQsNFFLTVPVSRSL 242
Cdd:cd07563  140 TTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSV 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 987857430 243 GPLggGGQTWEGSGVLPCVGIPAEQALEKALA 274
Cdd:cd07563  219 DPI--TGTNWEGVGVPPDIEVPATPGYDDALE 248
TSPc smart00245
tail specific protease; tail specific protease
65-264 1.31e-55

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 177.45  E-value: 1.31e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430    65 TREELLAQIQRNIHHEVLEGNVGYLRVDDLpGQEVLSELGE---FLVSHVWKQLMST--SSLVLDLRHCAGGHVSGIPYV 139
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   140 ISYLHPGNTvlHVDTIYDRpsntTTEIWTLPKVLGERYSadKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGA 219
Cdd:smart00245  80 SSLFLDKGV--IVYTVYRR----TGELWTYPANLGRKYS--KPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 987857430   220 LDLQKLRIGqSNFFLTVPVSRSLGPlggGGQTWEGSGVLPCVGIP 264
Cdd:smart00245 152 LVQQTVPLG-DGSGLKLTVAKYYTP---SGKSIEKKGVEPDIQVP 192
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
63-259 1.98e-17

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: 80.68  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  63 NLTREEllaqIQRN-IHHEVLEGNVGYLRVDDL---PGQEVLSELGEFlvshvwkQLMSTSSLVLDLRHCAGGHVSGIPY 138
Cdd:COG0793  139 TLTRAE----IKLPsVEAKLLEGKIGYIRIPSFgenTAEEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVE 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 139 VISYLHPGNTVLhvdtiYDRPSNTTTEIWtlpKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGG 218
Cdd:COG0793  208 LADLFLPKGPIV-----YTRGRNGKVETY---KATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGK 279
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 987857430 219 AldlqklrIGQSNF------FLTVPVSRSLGPlggGGQTWEGSGVLP 259
Cdd:COG0793  280 G-------SVQTVFplpdggALKLTTARYYTP---SGRSIQGKGVEP 316
Peptidase_S41 pfam03572
Peptidase family S41;
85-259 4.26e-14

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 68.40  E-value: 4.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   85 NVGYLRV---DDLPGQEVLSELGEFLVSHVwkqlmstSSLVLDLRHCAGGHVSGIPYVISY-LHPGNTVLHVDTIYDRPS 160
Cdd:pfam03572   1 KIGYIRIpsfSEKTAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLfLPDGTIVSTRGRDGSKEV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  161 NTTTEIwtlpkvlGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTeGGALDLQKLRIGQSNFFLTVPVSR 240
Cdd:pfam03572  74 YFAAGK-------ADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERT-FGKGTVQTVYPLPDGSALKLTIAK 145
                         170
                  ....*....|....*....
gi 987857430  241 SLGPlggGGQTWEGSGVLP 259
Cdd:pfam03572 146 YYTP---DGRSIEGKGIEP 161
 
Name Accession Description Interval E-value
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
3-274 8.78e-71

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: 218.32  E-value: 8.78e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   3 GMQAAIEQAMKSHEILGISDPQTLAHVLTAGVQSsLNDPRLFISYepstleapqqapaltnltreellaqiqrnihhevl 82
Cdd:cd07563   21 IDWDALAARLRAQVYLDITSPEELAAVLTADLQE-LGDGHLNVSY----------------------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  83 egnVGYLRVDDLPGQEVlsELGEFLVSHVWKQLMSTSSLVLDLRHCAGGHVSGIPYVISYLHPGNTVLHVDTIYDRPSNT 162
Cdd:cd07563   65 ---IGYLRIDSFGGFEI--AAAEALLDEALDKLADTDALIIDLRYNGGGSDSLVAYLASYFTDEDKPVHLYTIYKRPGNT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 163 TTEIWTLPKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDLQKLRIGQsNFFLTVPVSRSL 242
Cdd:cd07563  140 TTELWTLPVVPGGRYGYTKPVYVLTSPVTFSAAEEFAYALKQLKRATVVGETTAGGASPVLPFPLPN-GLYLTVPTSRSV 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 987857430 243 GPLggGGQTWEGSGVLPCVGIPAEQALEKALA 274
Cdd:cd07563  219 DPI--TGTNWEGVGVPPDIEVPATPGYDDALE 248
TSPc smart00245
tail specific protease; tail specific protease
65-264 1.31e-55

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 177.45  E-value: 1.31e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430    65 TREELLAQIQRNIHHEVLEGNVGYLRVDDLpGQEVLSELGE---FLVSHVWKQLMST--SSLVLDLRHCAGGHVSGIPYV 139
Cdd:smart00245   1 SKERTIALIRDKIKIETLEGNVGYLRFGFI-GYIRIPEFSEhtsNLVEKAWKKLEKTnvEGLILDLRNNPGGLLSAAIDV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   140 ISYLHPGNTvlHVDTIYDRpsntTTEIWTLPKVLGERYSadKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGA 219
Cdd:smart00245  80 SSLFLDKGV--IVYTVYRR----TGELWTYPANLGRKYS--KPLVVLVNKGTASASEIFAGALKDLGRATIVGERTFGKG 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 987857430   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 ...
85-264 7.49e-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: 114.70  E-value: 7.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  85 NVGYLRVDDLPGQEVLSELGEFLVshvwKQLMSTSSLVLDLRHCAGGHVSGIPYVISYLHPGNTVLHVDTIYDRPsnttt 164
Cdd:cd06567   60 TIGYIRIPSFSAESTAEELREALA----ELKKGVKGLILDLRNNPGGLLSAAVELASLFLPKGKIVVTTRRRGGN----- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 165 eiWTLPKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDlQKLRIGQSNFFLTVPVSRSLGP 244
Cdd:cd06567  131 --ETEYVAPGGGSLYDGPLVVLVNEGSASASEIFAGALQDLGRATLVGERTFGKGSV-QTVFPLLDGSALKLTTAKYYTP 207
                        170       180
                 ....*....|....*....|
gi 987857430 245 lggGGQTWEGSGVLPCVGIP 264
Cdd:cd06567  208 ---SGRSIEGKGVEPDIEVP 224
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
63-259 1.98e-17

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: 80.68  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  63 NLTREEllaqIQRN-IHHEVLEGNVGYLRVDDL---PGQEVLSELGEFlvshvwkQLMSTSSLVLDLRHCAGGHVSGIPY 138
Cdd:COG0793  139 TLTRAE----IKLPsVEAKLLEGKIGYIRIPSFgenTAEEFKRALKEL-------KKQGAKGLILDLRNNPGGLLDEAVE 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 139 VISYLHPGNTVLhvdtiYDRPSNTTTEIWtlpKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGG 218
Cdd:COG0793  208 LADLFLPKGPIV-----YTRGRNGKVETY---KATPGGALYDGPLVVLVNEGSASASEIFAGALQDYGRGVIVGTRTFGK 279
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 987857430 219 AldlqklrIGQSNF------FLTVPVSRSLGPlggGGQTWEGSGVLP 259
Cdd:COG0793  280 G-------SVQTVFplpdggALKLTTARYYTP---SGRSIQGKGVEP 316
Peptidase_S41_TRI cd07562
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ...
79-276 5.77e-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: 72.62  E-value: 5.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  79 HEVLEGNVGYLRVDDLpGQEVLSELgeflvshvWKQLMSTSS---LVLDLRHCAGGHVSGipYVISYLHPGNTvlhvdtI 155
Cdd:cd07562   82 EELSDGRIGYVHIPDM-GDDGFAEF--------LRDLLAEVDkdgLIIDVRFNGGGNVAD--LLLDFLSRRRY------G 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 156 YDRPSNTTTEIWTlpkvlgERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEGGALDLQKLR-IGQSnfFL 234
Cdd:cd07562  145 YDIPRGGGKPVTY------PSGRWRGPVVVLVNEGSASDAEIFAYGFRALGLGPVVGTRTAGGVIISGRYRlPDGG--SL 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 987857430 235 TVPVSRSLGPLGGGGqtwEGSGVLPCVGIPAE---------QALEKALAIL 276
Cdd:cd07562  217 TVPEFGVYLPDGGPL---ENRGVAPDIEVENTpedvaagrdPQLEAAIEEL 264
Peptidase_S41 pfam03572
Peptidase family S41;
85-259 4.26e-14

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 68.40  E-value: 4.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430   85 NVGYLRV---DDLPGQEVLSELGEFLVSHVwkqlmstSSLVLDLRHCAGGHVSGIPYVISY-LHPGNTVLHVDTIYDRPS 160
Cdd:pfam03572   1 KIGYIRIpsfSEKTAKELAEALKELKKQGV-------KGLILDLRGNPGGLLSAAVEIASLfLPDGTIVSTRGRDGSKEV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  161 NTTTEIwtlpkvlGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTeGGALDLQKLRIGQSNFFLTVPVSR 240
Cdd:pfam03572  74 YFAAGK-------ADEVLWKGPLVVLVNEGSASASEIFAGALQDNGRATLVGERT-FGKGTVQTVYPLPDGSALKLTIAK 145
                         170
                  ....*....|....*....
gi 987857430  241 SLGPlggGGQTWEGSGVLP 259
Cdd:pfam03572 146 YYTP---DGRSIEGKGIEP 161
Peptidase_S41_N pfam11918
N-terminal domain of Peptidase_S41 in eukaryotic IRBP; Peptidase_S41_N is a family found at ...
3-83 3.31e-04

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: 39.61  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430    3 GMQAAIEQAMKSHEILGISDPQTLAHVLTAGVQSSLNDPRLFISY--------EPSTLEAPQQAPALTNLTREELLAQIQ 74
Cdd:pfam11918  41 AVAAHLASLLASGDYSSVVSEEDLASKLNADLQALSGDPRLKVRYirpepasdEPEAADNIPGLVPMQPPSPEMLEALIK 120

                  ....*....
gi 987857430   75 RNIHHEVLE 83
Cdd:pfam11918 121 SSFKVDVLP 129
Peptidase_S41_CPP_like cd07561
C-terminal processing peptidase-like; serine protease family S41; Bacterial protease homologs ...
85-217 2.18e-03

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


Pssm-ID: 143477 [Multi-domain]  Cd Length: 256  Bit Score: 38.77  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430  85 NVGYLRVDDLP---GQEVLSELGEFLVSHVwkqlmstSSLVLDLRHCAGGHVSGIPYVISYLHPGNTV--LHVDTIY--D 157
Cdd:cd07561   65 KVGYLVYNSFTsgyDDELNQAFAEFKAQGV-------TELVLDLRYNGGGLVSSANLLASLLAPAVALgqVFATLEYndK 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 987857430 158 RPSNTTTEIWTLPKVLGERYSADKDVVVLTSGHTGGVAEDIAYILKQMRRAIVVGERTEG 217
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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