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Conserved domains on  [gi|2217365497|ref|XP_047275805|]
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peptidyl-prolyl cis-trans isomerase FKBP9 isoform X1 [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;
178-269 1.13e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 132.71  E-value: 1.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 178 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 255
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 2217365497 256 IPGSAVLVFDIHVI 269
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
66-158 1.90e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  66 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 144
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 2217365497 145 IPGQASLVFDVALL 158
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
289-381 2.74e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 2.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 289 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 367
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 2217365497 368 VPGSAVLVFDIELL 381
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-45 4.44e-15

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 70.69  E-value: 4.44e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217365497   1 MDQALVGMCVNERRFVKIPPKLAYGNEGVSG-VIPPNSVLHFDVLL 45
Cdd:pfam00254  48 WDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpVIPPNATLVFEVEL 93
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
378-466 4.99e-07

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: 49.02  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 378 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 457
Cdd:COG5126    22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                  ....*....
gi 2217365497 458 GKVTAEEFK 466
Cdd:COG5126    84 GKISADEFR 92
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
178-269 1.13e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 132.71  E-value: 1.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 178 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 255
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 2217365497 256 IPGSAVLVFDIHVI 269
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
66-158 1.90e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  66 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 144
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 2217365497 145 IPGQASLVFDVALL 158
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
289-381 2.74e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 2.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 289 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 367
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 2217365497 368 VPGSAVLVFDIELL 381
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 183-271 9.47e-31

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: 9.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 183 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 261
Cdd:COG0545    15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                          90
                  ....*....|
gi 2217365497 262 LVFDIHVIDF 271
Cdd:COG0545    95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 69-159 1.87e-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: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  69 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQ 148
Cdd:COG0545    13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                          90
                  ....*....|.
gi 2217365497 149 ASLVFDVALLD 159
Cdd:COG0545    93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 294-382 8.13e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.12  E-value: 8.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 294 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 373
Cdd:COG0545    15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                  ....*....
gi 2217365497 374 LVFDIELLE 382
Cdd:COG0545    95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 192-270 3.30e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 3.30e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365497 192 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 270
Cdd:PRK10902  171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 73-160 8.92e-16

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 75.99  E-value: 8.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  73 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLV 152
Cdd:PRK11570  120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                  ....*...
gi 2217365497 153 FDVALLDL 160
Cdd:PRK11570  198 FEVELLEI 205
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-45 4.44e-15

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 70.69  E-value: 4.44e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217365497   1 MDQALVGMCVNERRFVKIPPKLAYGNEGVSG-VIPPNSVLHFDVLL 45
Cdd:pfam00254  48 WDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 1-48 1.59e-12

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 63.66  E-value: 1.59e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217365497   1 MDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDI 48
Cdd:COG0545    57 WDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 294-383 1.30e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 294 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 373
Cdd:PRK10902  162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                          90
                  ....*....|
gi 2217365497 374 LVFDIELLEL 383
Cdd:PRK10902  239 LVFDVELLDV 248
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
378-466 4.99e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 378 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 457
Cdd:COG5126    22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                  ....*....
gi 2217365497 458 GKVTAEEFK 466
Cdd:COG5126    84 GKISADEFR 92
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 18-48 6.15e-07

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 50.92  E-value: 6.15e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217365497  18 IPPKLAYGNEGVSGvIPPNSVLHFDVLLMDI 48
Cdd:PRK10902  219 IPPELAYGKAGVPG-IPANSTLVFDVELLDV 248
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 404-465 3.85e-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: 44.08  E-value: 3.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217365497 404 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 465
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
403-466 6.34e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 6.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217365497 403 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 466
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
PLN02964 PLN02964
phosphatidylserine decarboxylase
 407-476 9.36e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 9.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365497 407 IDKDGNGEVLLEEFSEYIHA---QVASGKgklapgfdaeliVKNMFTNQDRNGDGKVTAEEfkLKDQEAKHDE 476
Cdd:PLN02964  188 VDYDEDGQLSFSEFSDLIKAfgnLVAANK------------KEELFKAADLNGDGVVTIDE--LAALLALQQE 246
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
178-269 1.13e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 132.71  E-value: 1.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 178 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 255
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 2217365497 256 IPGSAVLVFDIHVI 269
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
66-158 1.90e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 126.93  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  66 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 144
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 2217365497 145 IPGQASLVFDVALL 158
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
289-381 2.74e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.85  E-value: 2.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 289 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 367
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 2217365497 368 VPGSAVLVFDIELL 381
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 183-271 9.47e-31

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: 9.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 183 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 261
Cdd:COG0545    15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                          90
                  ....*....|
gi 2217365497 262 LVFDIHVIDF 271
Cdd:COG0545    95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 69-159 1.87e-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: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  69 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQ 148
Cdd:COG0545    13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                          90
                  ....*....|.
gi 2217365497 149 ASLVFDVALLD 159
Cdd:COG0545    93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 294-382 8.13e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.12  E-value: 8.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 294 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 373
Cdd:COG0545    15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                  ....*....
gi 2217365497 374 LVFDIELLE 382
Cdd:COG0545    95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 192-270 3.30e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 3.30e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365497 192 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 270
Cdd:PRK10902  171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 73-160 8.92e-16

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 75.99  E-value: 8.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  73 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLV 152
Cdd:PRK11570  120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                  ....*...
gi 2217365497 153 FDVALLDL 160
Cdd:PRK11570  198 FEVELLEI 205
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
1-45 4.44e-15

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 70.69  E-value: 4.44e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217365497   1 MDQALVGMCVNERRFVKIPPKLAYGNEGVSG-VIPPNSVLHFDVLL 45
Cdd:pfam00254  48 WDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpVIPPNATLVFEVEL 93
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 70-138 4.42e-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: 4.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  70 IQVSDFVRYHYNGTFLDGTLFDSSHNRMKTydTY-VGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGE 138
Cdd:COG1047     1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPL--EFlHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 186-270 7.08e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 67.52  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 186 DFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQgyVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRG-NIPGSAVLVF 264
Cdd:PRK11570  121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVF 198


                  ....*.
gi 2217365497 265 DIHVID 270
Cdd:PRK11570  199 EVELLE 204
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 1-48 1.59e-12

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 63.66  E-value: 1.59e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217365497   1 MDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDI 48
Cdd:COG0545    57 WDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 73-160 2.89e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 66.71  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  73 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDtyVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKdIPGQASLV 152
Cdd:PRK10902  164 SDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLV 240


                  ....*...
gi 2217365497 153 FDVALLDL 160
Cdd:PRK10902  241 FDVELLDV 248
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 294-383 1.30e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 294 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 373
Cdd:PRK10902  162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                          90
                  ....*....|
gi 2217365497 374 LVFDIELLEL 383
Cdd:PRK10902  239 LVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 183-250 3.85e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 60.50  E-value: 3.85e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217365497 183 QSGDFLRYHYNGTLLDGTLFDSSYSRN-RTFdtYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGE 250
Cdd:COG1047     2 EKGDVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 297-384 1.36e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 60.97  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 297 DYLKYHYNASLLDGTLLDSTWNLGKTYNIVLgSGqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVF 376
Cdd:PRK11570  121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                  ....*...
gi 2217365497 377 DIELLELV 384
Cdd:PRK11570  199 EVELLEIL 206
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 294-361 2.19e-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: 2.19e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217365497 294 KKGDYLKYHYNASLLDGTLLDSTWNlGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGE 361
Cdd:COG1047     2 EKGDVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
378-466 4.99e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497 378 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 457
Cdd:COG5126    22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                  ....*....
gi 2217365497 458 GKVTAEEFK 466
Cdd:COG5126    84 GKISADEFR 92
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 18-48 6.15e-07

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 50.92  E-value: 6.15e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217365497  18 IPPKLAYGNEGVSGvIPPNSVLHFDVLLMDI 48
Cdd:PRK10902  219 IPPELAYGKAGVPG-IPANSTLVFDVELLDV 248
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 404-465 3.85e-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: 44.08  E-value: 3.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217365497 404 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 465
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
403-466 5.48e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.94  E-value: 5.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217365497 403 LFEEIDKDGNGEVLLEEFSEYIHAQvasgkgklapGFDAELIvKNMFTNQDRNGDGKVTAEEFK 466
Cdd:COG5126    74 AFDLLDTDGDGKISADEFRRLLTAL----------GVSEEEA-DELFARLDTDGDGKISFEEFV 126
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 3-48 1.28e-04

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 43.25  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2217365497   3 QALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDI 48
Cdd:PRK11570  160 EALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 69-138 1.37e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 42.39  E-value: 1.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  69 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGE 138
Cdd:PRK15095    4 SVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 176-251 5.55e-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: 42.04  E-value: 5.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217365497 176 ENCERISQSGDFLRYHYNGTLlDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEE 251
Cdd:COG0544   152 VPVERAAEEGDRVTIDFEGTI-DGEEFEGGKAEDYSLE--LGSGSFIPGFEEQLVGMKAGEEKTFEVTFPEDYHAE 224
EF-hand_7 pfam13499
EF-hand domain pair;
403-466 6.34e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 6.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217365497 403 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 466
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 68-176 1.44e-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: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365497  68 RTIQVSDFVRYHYNGtFLDGTLFDSSHNrmKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIppflAYGEDGDGKDIPG 147
Cdd:COG0544   156 RAAEEGDRVTIDFEG-TIDGEEFEGGKA--EDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEV----TFPEDYHAEELAG 228

                          90       100
                  ....*....|....*....|....*....
gi 2217365497 148 QASlVFDVALldlhnpkdsISIENKVVPE 176
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 ...
 444-466 7.61e-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: 7.61e-03
                          10        20
                  ....*....|....*....|...
gi 2217365497 444 IVKNMFTNQDRNGDGKVTAEEFK 466
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFK 23
PLN02964 PLN02964
phosphatidylserine decarboxylase
 407-476 9.36e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 9.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365497 407 IDKDGNGEVLLEEFSEYIHA---QVASGKgklapgfdaeliVKNMFTNQDRNGDGKVTAEEfkLKDQEAKHDE 476
Cdd:PLN02964  188 VDYDEDGQLSFSEFSDLIKAfgnLVAANK------------KEELFKAADLNGDGVVTIDE--LAALLALQQE 246
 
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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