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Conserved domains on  [gi|1002281098|ref|XP_015644844|]
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peptidyl-prolyl cis-trans isomerase FKBP19, chloroplastic [Oryza sativa Japonica Group]

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

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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 ...
99-233 1.46e-22

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


:

Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 88.32  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  99 LQYKDLRVGDGPSPKKGETVVVDWDGYTIGyyGRIFEArnktkggSFEGGDKdfFKFKIGSGQVIPAFEEAISDMAPGGV 178
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLD--GTVFDS-------SYDRGEP--ATFPLGVGQVIPGWDEGLQGMKVGGK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002281098 179 RRIIVPPDLGYPDNDYNKLGPKpttfsgqraldfvlrnqgliDKTLLFDIELLKI 233
Cdd:COG0545    70 RRLVIPPELAYGERGAGGVIPP--------------------NSTLVFEVELLDV 104
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
99-233 1.46e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 88.32  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  99 LQYKDLRVGDGPSPKKGETVVVDWDGYTIGyyGRIFEArnktkggSFEGGDKdfFKFKIGSGQVIPAFEEAISDMAPGGV 178
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLD--GTVFDS-------SYDRGEP--ATFPLGVGQVIPGWDEGLQGMKVGGK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002281098 179 RRIIVPPDLGYPDNDYNKLGPKpttfsgqraldfvlrnqgliDKTLLFDIELLKI 233
Cdd:COG0545    70 RRLVIPPELAYGERGAGGVIPP--------------------NSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
112-231 1.76e-18

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 77.24  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098 112 PKKGETVVVDWDGYTIGyyGRIFEarnktkgGSFEGGDKdfFKFKIGSGQVIPAFEEAISDMAPGGVRRIIVPPDLGYPD 191
Cdd:pfam00254   5 AKKGDRVTVHYTGTLED--GTVFD-------SSYDRGKP--FEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002281098 192 NDYNKLGPKPttfsgqraldfvlrnqgliDKTLLFDIELL 231
Cdd:pfam00254  74 EGLAGPVIPP-------------------NATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
55-235 6.72e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 63.24  E-value: 6.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  55 ISISIGSFD---KGAAKAEF---ADMPALRGKDYGKTKMKYPDYTETESGLQYKDLRVGDGPSPKKGETVVVDWDGYTIG 128
Cdd:PRK10902   98 IEQTLQAFEarvKSAAQAKMekdAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLID 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098 129 yyGRIFEarnktkgGSFEGGDKDFFKFKigsgQVIPAFEEAISDMAPGGVRRIIVPPDLGYpdndynklgpkpttfsGQR 208
Cdd:PRK10902  178 --GKEFD-------NSYTRGEPLSFRLD----GVIPGWTEGLKNIKKGGKIKLVIPPELAY----------------GKA 228
                         170       180
                  ....*....|....*....|....*..
gi 1002281098 209 ALDFVLRNQglidkTLLFDIELLKIIP 235
Cdd:PRK10902  229 GVPGIPANS-----TLVFDVELLDVKP 250
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
68-205 3.66e-08

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 52.94  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  68 KAEFADMPALRGKDYGKTKMKYPDYTETESGL---------QYKDLRVGDGPSPKKGETVVVDWDGYTigyygrifearn 138
Cdd:TIGR00115  96 TAEFEVYPEVELGDYKGIEVEKPEVEVTDEDVdeelerlreQNATLVPVERGAAEKGDRVTIDFEGFI------------ 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002281098 139 ktKGGSFEGGDKDFFKFKIGSGQVIPAFEEAISDMAPGGVRRIivppDLGYPDNDYNK-LGPKPTTFS 205
Cdd:TIGR00115 164 --DGEAFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEI----KVTFPEDYHAEeLAGKEATFK 225
 
Name Accession Description Interval E-value
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
99-233 1.46e-22

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 88.32  E-value: 1.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  99 LQYKDLRVGDGPSPKKGETVVVDWDGYTIGyyGRIFEArnktkggSFEGGDKdfFKFKIGSGQVIPAFEEAISDMAPGGV 178
Cdd:COG0545     1 LQYKVLKEGTGAKPKAGDTVTVHYTGTLLD--GTVFDS-------SYDRGEP--ATFPLGVGQVIPGWDEGLQGMKVGGK 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002281098 179 RRIIVPPDLGYPDNDYNKLGPKpttfsgqraldfvlrnqgliDKTLLFDIELLKI 233
Cdd:COG0545    70 RRLVIPPELAYGERGAGGVIPP--------------------NSTLVFEVELLDV 104
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
112-231 1.76e-18

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 77.24  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098 112 PKKGETVVVDWDGYTIGyyGRIFEarnktkgGSFEGGDKdfFKFKIGSGQVIPAFEEAISDMAPGGVRRIIVPPDLGYPD 191
Cdd:pfam00254   5 AKKGDRVTVHYTGTLED--GTVFD-------SSYDRGKP--FEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGE 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002281098 192 NDYNKLGPKPttfsgqraldfvlrnqgliDKTLLFDIELL 231
Cdd:pfam00254  74 EGLAGPVIPP-------------------NATLVFEVELL 94
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
55-235 6.72e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 63.24  E-value: 6.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  55 ISISIGSFD---KGAAKAEF---ADMPALRGKDYGKTKMKYPDYTETESGLQYKDLRVGDGPSPKKGETVVVDWDGYTIG 128
Cdd:PRK10902   98 IEQTLQAFEarvKSAAQAKMekdAADNEAKGKKYREKFAKEKGVKTTSTGLLYKVEKEGTGEAPKDSDTVVVNYKGTLID 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098 129 yyGRIFEarnktkgGSFEGGDKDFFKFKigsgQVIPAFEEAISDMAPGGVRRIIVPPDLGYpdndynklgpkpttfsGQR 208
Cdd:PRK10902  178 --GKEFD-------NSYTRGEPLSFRLD----GVIPGWTEGLKNIKKGGKIKLVIPPELAY----------------GKA 228
                         170       180
                  ....*....|....*....|....*..
gi 1002281098 209 ALDFVLRNQglidkTLLFDIELLKIIP 235
Cdd:PRK10902  229 GVPGIPANS-----TLVFDVELLDVKP 250
tig TIGR00115
trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first ...
68-205 3.66e-08

trigger factor; Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization]


Pssm-ID: 272913 [Multi-domain]  Cd Length: 410  Bit Score: 52.94  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  68 KAEFADMPALRGKDYGKTKMKYPDYTETESGL---------QYKDLRVGDGPSPKKGETVVVDWDGYTigyygrifearn 138
Cdd:TIGR00115  96 TAEFEVYPEVELGDYKGIEVEKPEVEVTDEDVdeelerlreQNATLVPVERGAAEKGDRVTIDFEGFI------------ 163
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002281098 139 ktKGGSFEGGDKDFFKFKIGSGQVIPAFEEAISDMAPGGVRRIivppDLGYPDNDYNK-LGPKPTTFS 205
Cdd:TIGR00115 164 --DGEAFEGGKAENFSLELGSGQFIPGFEEQLVGMKAGEEKEI----KVTFPEDYHAEeLAGKEATFK 225
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
76-234 6.43e-07

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 48.26  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  76 ALRGKDYGKTKMKYPDYTETESGLQYKDLRVGDGPSPKKGETVVVDWDGYTIGyyGRIFEArnktkggSFEGGDKDFFKF 155
Cdd:PRK11570   81 AAEGVKFLEENAKKEGVNSTESGLQFRVLTQGEGAIPARTDRVRVHYTGKLID--GTVFDS-------SVARGEPAEFPV 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002281098 156 kigSGqVIPAFEEAISDMAPGGVRRIIVPPDLGYPDNDynkLGPKPTTFSgqraldfvlrnqglidkTLLFDIELLKII 234
Cdd:PRK11570  152 ---NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERG---AGASIPPFS-----------------TLVFEVELLEIL 206
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
113-189 3.37e-06

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 45.09  E-value: 3.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002281098 113 KKGETVVVDWDGYTIGyyGRIFEArnktkggSFEGGDkdfFKFKIGSGQVIPAFEEAISDMAPGGVRRIIVPPDLGY 189
Cdd:COG1047     2 EKGDVVTLHYTLKLED--GEVFDS-------TFEGEP---LEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAY 66
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
56-191 1.01e-05

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 45.89  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098  56 SISIGSFDKGAA---KAEFADMPALRGKDYGKTKMKYPDYTETESGL---------QYKDLRVGDGPSpKKGETVVVDwd 123
Cdd:COG0544    91 EIDVVELEEGKDlefTAEVEVRPEVELGDYKGLEVEKPVVEVTDEDVdeelerlreQFATLVPVERAA-EEGDRVTID-- 167
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002281098 124 gytigyygriFEArnKTKGGSFEGGDKDFFKFKIGSGQVIPAFEEAISDMAPGGVRRIIV--PPDLGYPD 191
Cdd:COG0544   168 ----------FEG--TIDGEEFEGGKAEDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEVtfPEDYHAEE 225
 
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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