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Conserved domains on  [gi|17647355|ref|NP_523428|]
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dodo [Drosophila melanogaster]

Protein Classification

WW and PTZ00356 domain-containing protein( domain architecture ID 11269771)

WW and PTZ00356 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 55-166 1.59e-56

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


:

Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 172.90  E-value: 1.59e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   55 PDEVHCLHLLVKHKGSRRPSSWREA-NITRTKEEAQLLLEVYRNKIVQQEATFDELARSYSDCSSAKRGGDLGKFGRGQM 133
Cdd:PTZ00356   3 GDTVRAAHLLIKHTGSRNPVSRRTGkPVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQM 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17647355  134 QAAFEDAAFKLNVNQLSGIVDSDSGLHIILRKA 166
Cdd:PTZ00356  83 QKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 7-39 9.46e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


:

Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 9.46e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 17647355      7 LPDGWEKRTSRStGMSYYLNMYTKESQWDQPTE 39
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 55-166 1.59e-56

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 172.90  E-value: 1.59e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   55 PDEVHCLHLLVKHKGSRRPSSWREA-NITRTKEEAQLLLEVYRNKIVQQEATFDELARSYSDCSSAKRGGDLGKFGRGQM 133
Cdd:PTZ00356   3 GDTVRAAHLLIKHTGSRNPVSRRTGkPVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQM 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17647355  134 QAAFEDAAFKLNVNQLSGIVDSDSGLHIILRKA 166
Cdd:PTZ00356  83 QKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 62-166 4.52e-29

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 102.76  E-value: 4.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355    62 HLLVKHKGSrrpsswreanITRTKEEAQLLLEVYRNKIVQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQMQAAFEDA 140
Cdd:pfam00639   1 HILIKTPEA----------SERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 17647355   141 AFKLNVNQLSGIVDSDSGLHIILRKA 166
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 55-162 2.20e-27

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 99.65  E-value: 2.20e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355  55 PDEVHCLHLLVKHKGSrrpsswreANITRTKEEAQLLLEVyrnkiVQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQM 133
Cdd:COG0760   6 PEEVRASHILVKVPPS--------EDRAKAEAKAEELLAQ-----LKAGADFAELAKEYSqDPGSAANGGDLGWFSRGQL 72

                        90       100
                ....*....|....*....|....*....
gi 17647355 134 QAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:COG0760  73 VPEFEEAAFALKPGEISGPVKTQFGYHII 101
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 7-39 9.46e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 9.46e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 17647355      7 LPDGWEKRTSRStGMSYYLNMYTKESQWDQPTE 39
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 8-39 3.87e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 46.75  E-value: 3.87e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 17647355   8 PDGWEKRTSRStGMSYYLNMYTKESQWDQPTE 39
Cdd:cd00201   1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 7-37 2.03e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 44.80  E-value: 2.03e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17647355     7 LPDGWEKRTSrSTGMSYYLNMYTKESQWDQP 37
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
 
Name Accession Description Interval E-value
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 55-166 1.59e-56

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 172.90  E-value: 1.59e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   55 PDEVHCLHLLVKHKGSRRPSSWREA-NITRTKEEAQLLLEVYRNKIVQQEATFDELARSYSDCSSAKRGGDLGKFGRGQM 133
Cdd:PTZ00356   3 GDTVRAAHLLIKHTGSRNPVSRRTGkPVTRSKEEAIKELAKWREQIVSGEKTFEEIARQRSDCGSAAKGGDLGFFGRGQM 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 17647355  134 QAAFEDAAFKLNVNQLSGIVDSDSGLHIILRKA 166
Cdd:PTZ00356  83 QKPFEDAAFALKVGEISDIVHTDSGVHIILRLA 115
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 62-166 4.52e-29

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 102.76  E-value: 4.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355    62 HLLVKHKGSrrpsswreanITRTKEEAQLLLEVYRNKIVQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQMQAAFEDA 140
Cdd:pfam00639   1 HILIKTPEA----------SERDRAEAKAKAEEILEQLKSGEDSFAELARKYSdDCPSAANGGDLGWFTRGQLPPEFEKA 70

                          90       100
                  ....*....|....*....|....*.
gi 17647355   141 AFKLNVNQLSGIVDSDSGLHIILRKA 166
Cdd:pfam00639  71 AFALKPGEISGPVETRFGFHIIKLTD 96
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 55-162 2.20e-27

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 99.65  E-value: 2.20e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355  55 PDEVHCLHLLVKHKGSrrpsswreANITRTKEEAQLLLEVyrnkiVQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQM 133
Cdd:COG0760   6 PEEVRASHILVKVPPS--------EDRAKAEAKAEELLAQ-----LKAGADFAELAKEYSqDPGSAANGGDLGWFSRGQL 72

                        90       100
                ....*....|....*....|....*....
gi 17647355 134 QAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:COG0760  73 VPEFEEAAFALKPGEISGPVKTQFGYHII 101
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 55-162 1.45e-22

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 86.65  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355    55 PDEVHCLHLLVKHkgsrrpsswrEANITRTKEEAQLLLEVYRNKIvQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQM 133
Cdd:pfam13616  13 PDSVKASHILISY----------SQAVSRTEEEAKAKADSLLAAL-KNGADFAALAKTYSdDPASKNNGGDLGWFTKGQM 81

                          90       100
                  ....*....|....*....|....*....
gi 17647355   134 QAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:pfam13616  82 VKEFEDAVFSLKVGEISGVVKTQFGFHII 110
prsA PRK03095
peptidylprolyl isomerase PrsA;
56-162 5.12e-14

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 67.71  E-value: 5.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   56 DEVHCLHLLVKHkgsrrpsswrEANITRTKEEaqlllevyrnkiVQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQMQ 134
Cdd:PRK03095 131 PEIKASHILVKD----------EATAKKVKEE------------LGQGKSFEELAKQYSeDTGSKEKGGDLGFFGAGKMV 188

                         90       100
                 ....*....|....*....|....*...
gi 17647355  135 AAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:PRK03095 189 KEFEDAAYKLKKDEVSEPVKSQFGYHII 216
prsA PRK03002
peptidylprolyl isomerase PrsA;
104-162 8.91e-13

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 64.19  E-value: 8.91e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355  104 ATFDELARSYS-DCSSAKRGGDLGKFGRGQMQAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:PRK03002 161 ASFEELAKQESqDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHII 220
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 85-162 2.69e-11

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 56.96  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   85 KEE--AQLLLEVyrnkiVQQEATFDELARSYSDCSSAKRGGDLGKFGRGQMQAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:PRK15441  13 KEEklALDLLEQ-----IKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 106-162 1.21e-10

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 58.44  E-value: 1.21e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17647355  106 FDELARSYS-DCSSAKRGGDLGKFGRGQMQAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:PRK02998 161 FAALAKQYSeDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHII 218
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 57-162 3.56e-09

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 54.36  E-value: 3.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   57 EVHCLHLLVKhkgsrrPSswreanITRTKEEAQLLLEVYRNKIVQQEATFDELARSYS-DCSSAKRGGDLGKFGRGQMQA 135
Cdd:PRK10770 266 EVHARHILLK------PS------PIMTDEQARAKLEQIAADIKSGKTTFAAAAKEFSqDPGSANQGGDLGWATPDIFDP 333

                         90       100
                 ....*....|....*....|....*..
gi 17647355  136 AFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:PRK10770 334 AFRDALMRLNKGQISAPVHSSFGWHLI 360
prsA PRK00059
peptidylprolyl isomerase; Provisional
 55-162 7.22e-09

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 53.56  E-value: 7.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355   55 PDEVHCLHLLVKhkgsrrpsswreanitrTKEEAQlllEVYrnKIVQQEATFDELARSYS-DCSSAKRGGDLGK--FGRG 131
Cdd:PRK00059 194 PNTMHLAHILVK-----------------TEDEAK---KVK--KRLDKGEDFAKVAKEVSqDPGSKDKGGDLGDvpYSDS 251

                         90       100       110
                 ....*....|....*....|....*....|.
gi 17647355  132 QMQAAFEDAAFKLNVNQLSGIVDSDSGLHII 162
Cdd:PRK00059 252 GYDKEFMDGAKALKEGEISAPVKTQFGYHII 282
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 7-39 9.46e-09

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 48.37  E-value: 9.46e-09
                           10        20        30
                   ....*....|....*....|....*....|...
gi 17647355      7 LPDGWEKRTSRStGMSYYLNMYTKESQWDQPTE 39
Cdd:smart00456   2 LPPGWEERKDPD-GRPYYYNHETKETQWEKPRE 33
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 8-39 3.87e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 46.75  E-value: 3.87e-08
                        10        20        30
                ....*....|....*....|....*....|..
gi 17647355   8 PDGWEKRTSRStGMSYYLNMYTKESQWDQPTE 39
Cdd:cd00201   1 PPGWEERWDPD-GRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 7-37 2.03e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 44.80  E-value: 2.03e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 17647355     7 LPDGWEKRTSrSTGMSYYLNMYTKESQWDQP 37
Cdd:pfam00397   1 LPPGWEERWD-PDGRVYYYNHETGETQWEKP 30
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
81-162 1.20e-03

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 37.04  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17647355    81 ITRTKEEAQLLLEVYRNKIvqqEATFDELARSYSDCSSAKRGGDLgkfgRGQMQAAFEDAAFKLNVNQLSGIVDSDSGLH 160
Cdd:pfam13145  29 VFKDQVAADAALALLKAGA---LEDFAALAKGEGIKAATLDIVES----AELLPEELAKAAFALKPGEVSGPIKTGNGYY 101


                  ..
gi 17647355   161 II 162
Cdd:pfam13145 102 VV 103
 
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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