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Conserved domains on  [gi|2528269286|ref|WP_289106721|]
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S41 family peptidase [uncultured Pseudoalteromonas sp.]

Protein Classification

S41 family peptidase( domain architecture ID 1219)

S41 family peptidase similar to Aspergillus flavus peptidase S41 family protein ustP and Lactococcus lactis nisin-resistance protein

CATH:  3.90.226.10|3.30.750.44
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
CtpA super family cl34043
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 215-319 6.13e-05

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0793:

Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 44.86  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286 215 PIDLTWPEKNIAWIAMPSFSSTekqtaAYNKVFEKIQQQRSKllTAKAVVLDLRHNQGGSSYWSSQIAKELWGK-KIVEQ 293
Cdd:COG0793   149 SVEAKLLEGKIGYIRIPSFGEN-----TAEEFKRALKELKKQ--GAKGLILDLRNNPGGLLDEAVELADLFLPKgPIVYT 221

                          90       100
                  ....*....|....*....|....*.
gi 2528269286 294 KVNNTSQNTQVWWRASKDNTDHVVSL 319
Cdd:COG0793   222 RGRNGKVETYKATPGGALYDGPLVVL 247
 
Name Accession Description Interval E-value
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 215-319 6.13e-05

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: 44.86  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286 215 PIDLTWPEKNIAWIAMPSFSSTekqtaAYNKVFEKIQQQRSKllTAKAVVLDLRHNQGGSSYWSSQIAKELWGK-KIVEQ 293
Cdd:COG0793   149 SVEAKLLEGKIGYIRIPSFGEN-----TAEEFKRALKELKKQ--GAKGLILDLRNNPGGLLDEAVELADLFLPKgPIVYT 221

                          90       100
                  ....*....|....*....|....*.
gi 2528269286 294 KVNNTSQNTQVWWRASKDNTDHVVSL 319
Cdd:COG0793   222 RGRNGKVETYKATPGGALYDGPLVVL 247
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 225-282 1.38e-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: 43.43  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286 225 IAWIAMPSFSSTEKQTAAY--NKVFEKIQQqrsklltAKAVVLDLRHNQGGSSYWSSQIA 282
Cdd:cd07563    65 IGYLRIDSFGGFEIAAAEAllDEALDKLAD-------TDALIIDLRYNGGGSDSLVAYLA 117
TSPc smart00245
tail specific protease; tail specific protease
 221-299 8.10e-04

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 40.32  E-value: 8.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286  221 PEKNIAWIAMPSFSstEKQTAAYNKVFEKIQQQRsklltAKAVVLDLRHNQGGSSYWSSQIAKeLWGKK--IVEQKVNNT 298
Cdd:smart00245  26 RFGFIGYIRIPEFS--EHTSNLVEKAWKKLEKTN-----VEGLILDLRNNPGGLLSAAIDVSS-LFLDKgvIVYTVYRRT 97


                   .
gi 2528269286  299 S 299
Cdd:smart00245  98 G 98
Peptidase_S41 pfam03572
Peptidase family S41;
224-296 1.27e-03

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 39.51  E-value: 1.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528269286 224 NIAWIAMPSFSSTEKQTAAynKVFEKIQQQRsklltAKAVVLDLRHNQGGSSYWSSQIAKELWGKKIVEQKVN 296
Cdd:pfam03572   1 KIGYIRIPSFSEKTAKELA--EALKELKKQG-----VKGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTRG 66
 
Name Accession Description Interval E-value
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
 215-319 6.13e-05

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: 44.86  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286 215 PIDLTWPEKNIAWIAMPSFSSTekqtaAYNKVFEKIQQQRSKllTAKAVVLDLRHNQGGSSYWSSQIAKELWGK-KIVEQ 293
Cdd:COG0793   149 SVEAKLLEGKIGYIRIPSFGEN-----TAEEFKRALKELKKQ--GAKGLILDLRNNPGGLLDEAVELADLFLPKgPIVYT 221

                          90       100
                  ....*....|....*....|....*.
gi 2528269286 294 KVNNTSQNTQVWWRASKDNTDHVVSL 319
Cdd:COG0793   222 RGRNGKVETYKATPGGALYDGPLVVL 247
Peptidase_S41_IRBP cd07563
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ...
 225-282 1.38e-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: 43.43  E-value: 1.38e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286 225 IAWIAMPSFSSTEKQTAAY--NKVFEKIQQqrsklltAKAVVLDLRHNQGGSSYWSSQIA 282
Cdd:cd07563    65 IGYLRIDSFGGFEIAAAEAllDEALDKLAD-------TDALIIDLRYNGGGSDSLVAYLA 117
Peptidase_S41 cd06567
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ...
 224-312 5.63e-04

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: 41.13  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286 224 NIAWIAMPSFSSTekqtAAYNKVFEKIQQQRSKlltAKAVVLDLRHNQGGSSYWSSQIAKELWGKKIVEQKVNNTSQNTQ 303
Cdd:cd06567    60 TIGYIRIPSFSAE----STAEELREALAELKKG---VKGLILDLRNNPGGLLSAAVELASLFLPKGKIVVTTRRRGGNET 132


                  ....*....
gi 2528269286 304 VWWRASKDN 312
Cdd:cd06567   133 EYVAPGGGS 141
TSPc smart00245
tail specific protease; tail specific protease
 221-299 8.10e-04

tail specific protease; tail specific protease


Pssm-ID: 214582  Cd Length: 192  Bit Score: 40.32  E-value: 8.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2528269286  221 PEKNIAWIAMPSFSstEKQTAAYNKVFEKIQQQRsklltAKAVVLDLRHNQGGSSYWSSQIAKeLWGKK--IVEQKVNNT 298
Cdd:smart00245  26 RFGFIGYIRIPEFS--EHTSNLVEKAWKKLEKTN-----VEGLILDLRNNPGGLLSAAIDVSS-LFLDKgvIVYTVYRRT 97


                   .
gi 2528269286  299 S 299
Cdd:smart00245  98 G 98
Peptidase_S41 pfam03572
Peptidase family S41;
224-296 1.27e-03

Peptidase family S41;


Pssm-ID: 460977  Cd Length: 165  Bit Score: 39.51  E-value: 1.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2528269286 224 NIAWIAMPSFSSTEKQTAAynKVFEKIQQQRsklltAKAVVLDLRHNQGGSSYWSSQIAKELWGKKIVEQKVN 296
Cdd:pfam03572   1 KIGYIRIPSFSEKTAKELA--EALKELKKQG-----VKGLILDLRGNPGGLLSAAVEIASLFLPDGTIVSTRG 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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