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Conserved domains on  [gi|224003773|ref|XP_002291558|]
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predicted protein [Thalassiosira pseudonana CCMP1335]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 11425492)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755
SCOP:  4001062

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-97 1.21e-50

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 154.95  E-value: 1.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   2 IEGTGASPTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKFGLG--QVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGSG 79
Cdd:COG0545    7 KEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAG 86
                         90
                 ....*....|....*...
gi 224003773  80 GAVPPGATLKFEVELFKV 97
Cdd:COG0545   87 GVIPPNSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-97 1.21e-50

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 154.95  E-value: 1.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   2 IEGTGASPTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKFGLG--QVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGSG 79
Cdd:COG0545    7 KEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAG 86
                         90
                 ....*....|....*...
gi 224003773  80 GAVPPGATLKFEVELFKV 97
Cdd:COG0545   87 GVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
3-99 6.41e-37

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 125.26  E-value: 6.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   3 EGTGASPTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKFGLGQVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGSGGaV 82
Cdd:PRK10902 155 EGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-I 233
                         90
                 ....*....|....*..
gi 224003773  83 PPGATLKFEVELFKVNP 99
Cdd:PRK10902 234 PANSTLVFDVELLDVKP 250
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
9-94 8.48e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 116.91  E-value: 8.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   9 PTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKF--GLGQVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGS-GGAVPPG 85
Cdd:pfam00254  5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFtlGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIPPN 84

                 ....*....
gi 224003773  86 ATLKFEVEL 94
Cdd:pfam00254 85 ATLVFEVEL 93
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
2-97 1.21e-50

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 154.95  E-value: 1.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   2 IEGTGASPTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKFGLG--QVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGSG 79
Cdd:COG0545    7 KEGTGAKPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGvgQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAG 86
                         90
                 ....*....|....*...
gi 224003773  80 GAVPPGATLKFEVELFKV 97
Cdd:COG0545   87 GVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
3-99 6.41e-37

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 125.26  E-value: 6.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   3 EGTGASPTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKFGLGQVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGSGGaV 82
Cdd:PRK10902 155 EGTGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-I 233
                         90
                 ....*....|....*..
gi 224003773  83 PPGATLKFEVELFKVNP 99
Cdd:PRK10902 234 PANSTLVFDVELLDVKP 250
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
9-94 8.48e-36

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 116.91  E-value: 8.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   9 PTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKF--GLGQVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGS-GGAVPPG 85
Cdd:pfam00254  5 AKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFtlGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLaGPVIPPN 84

                 ....*....
gi 224003773  86 ATLKFEVEL 94
Cdd:pfam00254 85 ATLVFEVEL 93
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
1-97 1.45e-32

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 112.20  E-value: 1.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224003773   1 MIEGTGASPTVSDTVEVHYHGTLTDGTVFDSSVDRGATIKFGLGQVIKGWQEGLAMMKEGGKATLVIPSELAYGDNGSGG 80
Cdd:PRK11570 109 LTQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGA 188
                         90
                 ....*....|....*..
gi 224003773  81 AVPPGATLKFEVELFKV 97
Cdd:PRK11570 189 SIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
13-75 1.02e-13

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 62.04  E-value: 1.02e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224003773  13 DTVEVHYHGTLTDGTVFDSSVDRG-ATIKFGLGQVIKGWQEGLAMMKEGGKATLVIPSELAYGD 75
Cdd:COG1047    5 DVVTLHYTLKLEDGEVFDSTFEGEpLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
15-74 9.00e-03

FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 33.53  E-value: 9.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224003773  15 VEVHYHGTLTDGTVFDSSVDRG--ATIKFGLGQVIKGWQEGLAMMKEGGKATLVIPSELAYG 74
Cdd:PRK15095  11 VLVHFTLKLDDGSTAESTRNNGkpALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFG 72
 
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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