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Conserved domains on  [gi|17507841|ref|NP_492792|]
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peptidylprolyl isomerase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
86-179 3.14e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 88.79  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507841    86 CPQQAKRLDFVTFHYKVFTEDNKKVYQTYGTG-PVTIQLGTGMIMPGLDKGLKGMCAEELRKVRVPYRMSRKSKSKVWKN 164
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGPV 80

                          90
                  ....*....|....*
gi 17507841   165 IPNDEnWLIFNIEMV 179
Cdd:pfam00254  81 IPPNA-TLVFEVELL 94
EFh_SPARC_EC super family cl25349
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 189-254 4.82e-04

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


The actual alignment was detected with superfamily member cd16234:

Pssm-ID: 330171  Cd Length: 104  Bit Score: 38.80  E-value: 4.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507841 189 QFKFLDLNEDEQLTNKEVQDFQKKMKKEFG--KTWKNedidnvtaagyYIKYFDVNGDGIVTEVEWLK 254
Cdd:cd16234  44 KFSQLDKNKNGVLERKEWKPFKRLLKKAVKpkKCARK-----------FPKYCDVNKDKKISLTEWLN 100
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
86-179 3.14e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 88.79  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507841    86 CPQQAKRLDFVTFHYKVFTEDNKKVYQTYGTG-PVTIQLGTGMIMPGLDKGLKGMCAEELRKVRVPYRMSRKSKSKVWKN 164
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGPV 80

                          90
                  ....*....|....*
gi 17507841   165 IPNDEnWLIFNIEMV 179
Cdd:pfam00254  81 IPPNA-TLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 94-181 2.54e-09

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 54.03  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507841  94 DFVTFHYKVFTEDNKKVYQTYGTG-PVTIQLGTGMIMPGLDKGLKGMCAEELRKVRVPYRM---SRKSKSKvwknIPNDE 169
Cdd:COG0545  18 DTVTVHYTGTLLDGTVFDSSYDRGePATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELaygERGAGGV----IPPNS 93

                        90
                ....*....|..
gi 17507841 170 NwLIFNIEMVEI 181
Cdd:COG0545  94 T-LVFEVELLDV 104
EFh_SPARC_SMOC cd16234
EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding ...
 189-254 4.82e-04

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins; SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.


Pssm-ID: 320013  Cd Length: 104  Bit Score: 38.80  E-value: 4.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507841 189 QFKFLDLNEDEQLTNKEVQDFQKKMKKEFG--KTWKNedidnvtaagyYIKYFDVNGDGIVTEVEWLK 254
Cdd:cd16234  44 KFSQLDKNKNGVLERKEWKPFKRLLKKAVKpkKCARK-----------FPKYCDVNKDKKISLTEWLN 100
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
86-179 3.14e-22

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 88.79  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507841    86 CPQQAKRLDFVTFHYKVFTEDNKKVYQTYGTG-PVTIQLGTGMIMPGLDKGLKGMCAEELRKVRVPYRMSRKSKSKVWKN 164
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGkPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGPV 80

                          90
                  ....*....|....*
gi 17507841   165 IPNDEnWLIFNIEMV 179
Cdd:pfam00254  81 IPPNA-TLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 94-181 2.54e-09

FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 54.03  E-value: 2.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17507841  94 DFVTFHYKVFTEDNKKVYQTYGTG-PVTIQLGTGMIMPGLDKGLKGMCAEELRKVRVPYRM---SRKSKSKvwknIPNDE 169
Cdd:COG0545  18 DTVTVHYTGTLLDGTVFDSSYDRGePATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELaygERGAGGV----IPPNS 93

                        90
                ....*....|..
gi 17507841 170 NwLIFNIEMVEI 181
Cdd:COG0545  94 T-LVFEVELLDV 104
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 94-150 4.17e-09

Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 54.34  E-value: 4.17e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17507841  94 DFVTFHYKVFTEDNKKVYQTYGTGPVTIQLGTGMIMPGLDKGLKGMCAEELRKVRVP 150
Cdd:COG1047   5 DVVTLHYTLKLEDGEVFDSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLP 61
EFh_SPARC_SMOC cd16234
EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding ...
 189-254 4.82e-04

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins; SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.


Pssm-ID: 320013  Cd Length: 104  Bit Score: 38.80  E-value: 4.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17507841 189 QFKFLDLNEDEQLTNKEVQDFQKKMKKEFG--KTWKNedidnvtaagyYIKYFDVNGDGIVTEVEWLK 254
Cdd:cd16234  44 KFSQLDKNKNGVLERKEWKPFKRLLKKAVKpkKCARK-----------FPKYCDVNKDKKISLTEWLN 100
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 190-256 1.91e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.99  E-value: 1.91e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17507841 190 FKFLDLNEDEQLTNKEVqdfqKKMKKEFGKTWKNEDIDNVtaagyyIKYFDVNGDGIVTEVEWLKIM 256
Cdd:cd00051   6 FRLFDKDGDGTISADEL----KAALKSLGEGLSEEEIDEM------IREVDKDGDGKIDFEEFLELM 62
 
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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