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Conserved domains on  [gi|33469985|ref|NP_009201|]
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peptidyl-prolyl cis-trans isomerase FKBP9 isoform 1 precursor [Homo sapiens]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446598)

FKBP-type peptidyl-prolyl cis-trans isomerase, with EF-hand calcium binding motifs, acts as a PPIase that accelerates the folding of proteins; similar to Mus musculus peptidyl-prolyl cis-trans isomerase FKBP14

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;
47-138 2.30e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985    47 CPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSG-V 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|...
gi 33469985   126 IPPNSVLHFDVLL 138
Cdd:pfam00254  81 IPPNATLVFEVEL 93
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
271-362 2.97e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.09  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   271 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 348
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 33469985   349 IPGSAVLVFDIHVI 362
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
159-251 4.63e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 4.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   159 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 237
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 33469985   238 IPGQASLVFDVALL 251
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
382-474 6.17e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 6.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   382 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 460
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 33469985   461 VPGSAVLVFDIELL 474
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
471-559 1.14e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 471 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 550
Cdd:COG5126  22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                ....*....
gi 33469985 551 GKVTAEEFK 559
Cdd:COG5126  84 GKISADEFR 92
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-138 2.30e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985    47 CPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSG-V 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|...
gi 33469985   126 IPPNSVLHFDVLL 138
Cdd:pfam00254  81 IPPNATLVFEVEL 93
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
271-362 2.97e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.09  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   271 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 348
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 33469985   349 IPGSAVLVFDIHVI 362
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
159-251 4.63e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 4.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   159 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 237
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 33469985   238 IPGQASLVFDVALL 251
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
382-474 6.17e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 6.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   382 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 460
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 33469985   461 VPGSAVLVFDIELL 474
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 50-141 1.67e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 117.59  E-value: 1.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  50 TVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPN 129
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|..
gi 33469985 130 SVLHFDVLLMDI 141
Cdd:COG0545  93 STLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 276-364 1.93e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.51  E-value: 1.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 276 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 354
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                        90
                ....*....|
gi 33469985 355 LVFDIHVIDF 364
Cdd:COG0545  95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 162-252 3.54e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 111.04  E-value: 3.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 162 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQ 241
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|.
gi 33469985 242 ASLVFDVALLD 252
Cdd:COG0545  93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 387-475 1.51e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.50  E-value: 1.51e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 466
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                ....*....
gi 33469985 467 LVFDIELLE 475
Cdd:COG0545  95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 285-363 4.45e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 4.45e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33469985  285 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 363
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 166-253 1.17e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 75.99  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  166 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLV 245
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 33469985  246 FDVALLDL 253
Cdd:PRK11570 198 FEVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 55-141 9.84e-12

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 64.43  E-value: 9.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   55 DFVRYHYVGTFPDGQKFDSSYDRD--STFNVfvgkGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVL 132
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGepAEFPV----NGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTL 196


                 ....*....
gi 33469985  133 HFDVLLMDI 141
Cdd:PRK11570 197 VFEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 387-476 1.70e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 466
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 33469985  467 LVFDIELLEL 476
Cdd:PRK10902 239 LVFDVELLDV 248
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
471-559 1.14e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 471 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 550
Cdd:COG5126  22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                ....*....
gi 33469985 551 GKVTAEEFK 559
Cdd:COG5126  84 GKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 497-558 4.15e-06

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: 44.46  E-value: 4.15e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33469985 497 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 558
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
496-559 7.05e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33469985   496 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 559
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-138 2.30e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985    47 CPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSG-V 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|...
gi 33469985   126 IPPNSVLHFDVLL 138
Cdd:pfam00254  81 IPPNATLVFEVEL 93
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
271-362 2.97e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.09  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   271 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 348
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 33469985   349 IPGSAVLVFDIHVI 362
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
159-251 4.63e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 4.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   159 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 237
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 33469985   238 IPGQASLVFDVALL 251
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
382-474 6.17e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 6.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   382 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 460
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 33469985   461 VPGSAVLVFDIELL 474
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 50-141 1.67e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 117.59  E-value: 1.67e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  50 TVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPN 129
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|..
gi 33469985 130 SVLHFDVLLMDI 141
Cdd:COG0545  93 STLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 276-364 1.93e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.51  E-value: 1.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 276 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 354
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                        90
                ....*....|
gi 33469985 355 LVFDIHVIDF 364
Cdd:COG0545  95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 162-252 3.54e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 111.04  E-value: 3.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 162 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQ 241
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|.
gi 33469985 242 ASLVFDVALLD 252
Cdd:COG0545  93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 387-475 1.51e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.50  E-value: 1.51e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 466
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                ....*....
gi 33469985 467 LVFDIELLE 475
Cdd:COG0545  95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 285-363 4.45e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 4.45e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33469985  285 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 363
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 166-253 1.17e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 75.99  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  166 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLV 245
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 33469985  246 FDVALLDL 253
Cdd:PRK11570 198 FEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 51-118 1.09e-13

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 68.20  E-value: 1.09e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33469985  51 VRSGDFVRYHYVGTFPDGQKFDSSYDRDsTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYG 118
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGE-PLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 163-231 4.72e-13

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 66.28  E-value: 4.72e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 163 IQVSDFVRYHYNGTFLDGTLFDSSHNRMKTydTY-VGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGE 231
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPL--EFlHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 279-363 9.37e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 67.52  E-value: 9.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  279 DFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQgyVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRG-NIPGSAVLVF 357
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVF 198


                 ....*.
gi 33469985  358 DIHVID 363
Cdd:PRK11570 199 EVELLE 204
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 166-253 3.79e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 66.71  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  166 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDtyVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKdIPGQASLV 245
Cdd:PRK10902 164 SDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLV 240


                 ....*...
gi 33469985  246 FDVALLDL 253
Cdd:PRK10902 241 FDVELLDV 248
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 55-141 9.84e-12

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 64.43  E-value: 9.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   55 DFVRYHYVGTFPDGQKFDSSYDRD--STFNVfvgkGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVL 132
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGepAEFPV----NGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTL 196


                 ....*....
gi 33469985  133 HFDVLLMDI 141
Cdd:PRK11570 197 VFEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 387-476 1.70e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 466
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 33469985  467 LVFDIELLEL 476
Cdd:PRK10902 239 LVFDVELLDV 248
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 55-141 2.58e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.40  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985   55 DFVRYHYVGTFPDGQKFDSSYDRDSTFNvFVGKGqLITGMDQALvgmcvnerRFVK--------IPPKLAYGNEGVSGvI 126
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRGEPLS-FRLDG-VIPGWTEGL--------KNIKkggkiklvIPPELAYGKAGVPG-I 233

                         90
                 ....*....|....*
gi 33469985  127 PPNSVLHFDVLLMDI 141
Cdd:PRK10902 234 PANSTLVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 276-343 4.15e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 60.89  E-value: 4.15e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33469985 276 QSGDFLRYHYNGTLLDGTLFDSSYSRN-RTFdtYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGE 343
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 390-477 1.76e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 60.58  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  390 DYLKYHYNASLLDGTLLDSTWNLGKTYNIVLgSGqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVF 469
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*...
gi 33469985  470 DIELLELV 477
Cdd:PRK11570 199 EVELLEIL 206
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 387-454 2.45e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.57  E-value: 2.45e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33469985 387 KKGDYLKYHYNASLLDGTLLDSTWNlGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGE 454
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
471-559 1.14e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 1.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 471 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 550
Cdd:COG5126  22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                ....*....
gi 33469985 551 GKVTAEEFK 559
Cdd:COG5126  84 GKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 497-558 4.15e-06

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: 44.46  E-value: 4.15e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33469985 497 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 558
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
496-559 1.08e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.08e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33469985 496 LFEEIDKDGNGEVLLEEFSEYIHAQvasgkgklapGFDAElIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:COG5126  74 AFDLLDTDGDGKISADEFRRLLTAL----------GVSEE-EADELFARLDTDGDGKISFEEFV 126
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 162-231 1.58e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 42.39  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985  162 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGE 231
Cdd:PRK15095   4 SVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 269-344 6.71e-04

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 42.42  E-value: 6.71e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33469985 269 ENCERISQSGDFLRYHYNGTLlDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEE 344
Cdd:COG0544 152 VPVERAAEEGDRVTIDFEGTI-DGEEFEGGKAEDYSLE--LGSGSFIPGFEEQLVGMKAGEEKTFEVTFPEDYHAE 224
EF-hand_7 pfam13499
EF-hand domain pair;
496-559 7.05e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 7.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33469985   496 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 559
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 161-269 1.72e-03

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 40.88  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33469985 161 RTIQVSDFVRYHYNGtFLDGTLFDSSHNrmKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIppflAYGEDGDGKDIPG 240
Cdd:COG0544 156 RAAEEGDRVTIDFEG-TIDGEEFEGGKA--EDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEV----TFPEDYHAEELAG 228

                        90       100
                ....*....|....*....|....*....
gi 33469985 241 QASlVFDVALldlhnpkdsISIENKVVPE 269
Cdd:COG0544 229 KTA-TFKVTV---------KEVKEKELPE 247
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 537-559 8.55e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 8.55e-03
                          10        20
                  ....*....|....*....|...
gi 33469985   537 IVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFK 23
 
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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