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Conserved domains on  [gi|547235580|ref|NP_001271272|]
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peptidyl-prolyl cis-trans isomerase FKBP9 isoform 3 [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;
39-130 1.57e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 132.32  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580   39 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 547235580  117 IPGSAVLVFDIHVI 130
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
150-242 4.58e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.08  E-value: 4.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580  150 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 228
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 547235580  229 VPGSAVLVFDIELL 242
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
239-327 6.64e-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: 47.86  E-value: 6.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 239 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 318
Cdd:COG5126   22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                 ....*....
gi 547235580 319 GKVTAEEFK 327
Cdd:COG5126   84 GKISADEFR 92
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
39-130 1.57e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 132.32  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580   39 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 547235580  117 IPGSAVLVFDIHVI 130
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
150-242 4.58e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.08  E-value: 4.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580  150 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 228
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 547235580  229 VPGSAVLVFDIELL 242
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 44-132 1.41e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.12  E-value: 1.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580  44 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 122
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                         90
                 ....*....|
gi 547235580 123 LVFDIHVIDF 132
Cdd:COG0545   95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 155-243 1.39e-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: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 155 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 234
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                 ....*....
gi 547235580 235 LVFDIELLE 243
Cdd:COG0545   95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 53-131 1.25e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 1.25e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547235580  53 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 131
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 155-244 6.56e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 155 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 234
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 547235580 235 LVFDIELLEL 244
Cdd:PRK10902 239 LVFDVELLDV 248
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
239-327 6.64e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 6.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 239 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 318
Cdd:COG5126   22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                 ....*....
gi 547235580 319 GKVTAEEFK 327
Cdd:COG5126   84 GKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 265-326 4.69e-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: 43.69  E-value: 4.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547235580 265 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 326
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
264-327 6.86e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 6.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547235580  264 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 327
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
PLN02964 PLN02964
phosphatidylserine decarboxylase
 268-337 6.25e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 6.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547235580 268 IDKDGNGEVLLEEFSEYIHA---QVASGKgklapgfdaeliVKNMFTNQDRNGDGKVTAEEfkLKDQEAKHDE 337
Cdd:PLN02964 188 VDYDEDGQLSFSEFSDLIKAfgnLVAANK------------KEELFKAADLNGDGVVTIDE--LAALLALQQE 246
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 306-327 9.11e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.51  E-value: 9.11e-03
                           10        20
                   ....*....|....*....|..
gi 547235580   306 VKNMFTNQDRNGDGKVTAEEFK 327
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFK 23
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
39-130 1.57e-38

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 132.32  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580   39 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 116
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 547235580  117 IPGSAVLVFDIHVI 130
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
150-242 4.58e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 123.08  E-value: 4.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580  150 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 228
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 547235580  229 VPGSAVLVFDIELL 242
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 44-132 1.41e-31

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.12  E-value: 1.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580  44 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 122
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                         90
                 ....*....|
gi 547235580 123 LVFDIHVIDF 132
Cdd:COG0545   95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 155-243 1.39e-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: 1.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 155 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 234
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                 ....*....
gi 547235580 235 LVFDIELLE 243
Cdd:COG0545   95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 53-131 1.25e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 1.25e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547235580  53 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 131
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 47-131 4.96e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 67.13  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580  47 DFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQgyVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRG-NIPGSAVLVF 125
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVF 198


                 ....*.
gi 547235580 126 DIHVID 131
Cdd:PRK11570 199 EVELLE 204
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 155-244 6.56e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 155 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 234
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 547235580 235 LVFDIELLEL 244
Cdd:PRK10902 239 LVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 44-111 3.92e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 60.11  E-value: 3.92e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547235580  44 QSGDFLRYHYNGTLLDGTLFDSSYSRN-RTFdtYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGE 111
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 158-245 1.02e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 60.58  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 158 DYLKYHYNASLLDGTLLDSTWNLGKTYNIVLgSGqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVF 237
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*...
gi 547235580 238 DIELLELV 245
Cdd:PRK11570 199 EVELLEIL 206
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 155-222 2.17e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 57.80  E-value: 2.17e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547235580 155 KKGDYLKYHYNASLLDGTLLDSTWNlGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGE 222
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
239-327 6.64e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 6.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235580 239 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 318
Cdd:COG5126   22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                 ....*....
gi 547235580 319 GKVTAEEFK 327
Cdd:COG5126   84 GKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 265-326 4.69e-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: 43.69  E-value: 4.69e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547235580 265 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 326
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
264-327 6.14e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 6.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547235580 264 LFEEIDKDGNGEVLLEEFSEYIHAQvasgkgklapGFDAELIvKNMFTNQDRNGDGKVTAEEFK 327
Cdd:COG5126   74 AFDLLDTDGDGKISADEFRRLLTAL----------GVSEEEA-DELFARLDTDGDGKISFEEFV 126
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 37-112 6.63e-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: 41.27  E-value: 6.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547235580  37 ENCERISQSGDFLRYHYNGTLlDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEE 112
Cdd:COG0544  152 VPVERAAEEGDRVTIDFEGTI-DGEEFEGGKAEDYSLE--LGSGSFIPGFEEQLVGMKAGEEKTFEVTFPEDYHAE 224
EF-hand_7 pfam13499
EF-hand domain pair;
264-327 6.86e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 6.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547235580  264 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 327
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
PLN02964 PLN02964
phosphatidylserine decarboxylase
 268-337 6.25e-03

phosphatidylserine decarboxylase


Pssm-ID: 215520 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 6.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547235580 268 IDKDGNGEVLLEEFSEYIHA---QVASGKgklapgfdaeliVKNMFTNQDRNGDGKVTAEEfkLKDQEAKHDE 337
Cdd:PLN02964 188 VDYDEDGQLSFSEFSDLIKAfgnLVAANK------------KEELFKAADLNGDGVVTIDE--LAALLALQQE 246
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 305-327 6.61e-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: 6.61e-03
                          10        20
                  ....*....|....*....|...
gi 547235580  305 IVKNMFTNQDRNGDGKVTAEEFK 327
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFK 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 306-327 9.11e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.51  E-value: 9.11e-03
                           10        20
                   ....*....|....*....|..
gi 547235580   306 VKNMFTNQDRNGDGKVTAEEFK 327
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFK 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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