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Conserved domains on  [gi|547235570|ref|NP_001271270|]
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peptidyl-prolyl cis-trans isomerase FKBP9 isoform 2 precursor [Homo sapiens]

Protein Classification

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;
324-415 2.85e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  324 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 401
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 547235570  402 IPGSAVLVFDIHVI 415
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
212-304 4.32e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 127.70  E-value: 4.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  212 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 290
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 547235570  291 IPGQASLVFDVALL 304
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
435-527 5.53e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 5.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  435 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 513
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 547235570  514 VPGSAVLVFDIELL 527
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-191 1.52e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 109.21  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570   47 CPRTVRSGDFVRYHYVGTFPDGQKFDSrywdtaedkadkspcpqvrvgvntspscrlkqkgvgiywkdlqflvrvqnhgl 126
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDS----------------------------------------------------- 27

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547235570  127 SYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSG-VIPPNSVLHFDVLL 191
Cdd:pfam00254  28 SYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpVIPPNATLVFEVEL 93
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
524-612 8.50e-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: 48.63  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 524 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 603
Cdd:COG5126   22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                 ....*....
gi 547235570 604 GKVTAEEFK 612
Cdd:COG5126   84 GKISADEFR 92
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
324-415 2.85e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  324 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 401
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 547235570  402 IPGSAVLVFDIHVI 415
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
212-304 4.32e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 127.70  E-value: 4.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  212 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 290
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 547235570  291 IPGQASLVFDVALL 304
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
435-527 5.53e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 5.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  435 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 513
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 547235570  514 VPGSAVLVFDIELL 527
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 329-417 1.71e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.89  E-value: 1.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 329 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 407
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                         90
                 ....*....|
gi 547235570 408 LVFDIHVIDF 417
Cdd:COG0545   95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 215-305 3.14e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 111.43  E-value: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 215 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQ 294
Cdd:COG0545   13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                         90
                 ....*....|.
gi 547235570 295 ASLVFDVALLD 305
Cdd:COG0545   93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 440-528 1.32e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.89  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 440 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 519
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                 ....*....
gi 547235570 520 LVFDIELLE 528
Cdd:COG0545   95 LVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-191 1.52e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 109.21  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570   47 CPRTVRSGDFVRYHYVGTFPDGQKFDSrywdtaedkadkspcpqvrvgvntspscrlkqkgvgiywkdlqflvrvqnhgl 126
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDS----------------------------------------------------- 27

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547235570  127 SYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSG-VIPPNSVLHFDVLL 191
Cdd:pfam00254  28 SYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 50-194 7.37e-23

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 93.32  E-value: 7.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  50 TVRSGDFVRYHYVGTFPDGQKFDSrywdtaedkadkspcpqvrvgvntspscrlkqkgvgiywkdlqflvrvqnhglSYD 129
Cdd:COG0545   13 KPKAGDTVTVHYTGTLLDGTVFDS-----------------------------------------------------SYD 39

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547235570 130 RDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDI 194
Cdd:COG0545   40 RGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 338-416 5.06e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 5.06e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547235570 338 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 416
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 219-306 1.30e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 75.99  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 219 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLV 298
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 547235570 299 FDVALLDL 306
Cdd:PRK11570 198 FEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 440-529 1.93e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 440 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 519
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 547235570 520 LVFDIELLEL 529
Cdd:PRK10902 239 LVFDVELLDV 248
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 55-194 4.81e-07

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 51.69  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  55 DFVRYHYVGTFPDGQKFDSRYwdtaedkADKSPCpqvrvgvntspSCRLKqkGVGIYWKDlqflvrvqnhGLSYdrdstf 134
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSY-------TRGEPL-----------SFRLD--GVIPGWTE----------GLKN------ 208

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 135 nvfVGKGQLITgmdqaLVgmcvnerrfvkIPPKLAYGNEGVSGvIPPNSVLHFDVLLMDI 194
Cdd:PRK10902 209 ---IKKGGKIK-----LV-----------IPPELAYGKAGVPG-IPANSTLVFDVELLDV 248
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
524-612 8.50e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.63  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 524 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 603
Cdd:COG5126   22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                 ....*....
gi 547235570 604 GKVTAEEFK 612
Cdd:COG5126   84 GKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 550-611 2.93e-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: 44.85  E-value: 2.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547235570 550 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 611
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
549-612 5.70e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 5.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547235570  549 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 612
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 591-612 9.47e-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: 33.89  E-value: 9.47e-03
                           10        20
                   ....*....|....*....|..
gi 547235570   591 VKNMFTNQDRNGDGKVTAEEFK 612
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFK 23
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
324-415 2.85e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.85e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  324 CERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGR--GN 401
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 547235570  402 IPGSAVLVFDIHVI 415
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
212-304 4.32e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 127.70  E-value: 4.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  212 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDG-DGKD 290
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 547235570  291 IPGQASLVFDVALL 304
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
435-527 5.53e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 124.62  E-value: 5.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  435 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 513
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 547235570  514 VPGSAVLVFDIELL 527
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 329-417 1.71e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 114.89  E-value: 1.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 329 QSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGN-IPGSAV 407
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGvIPPNST 94

                         90
                 ....*....|
gi 547235570 408 LVFDIHVIDF 417
Cdd:COG0545   95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 215-305 3.14e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 111.43  E-value: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 215 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQ 294
Cdd:COG0545   13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                         90
                 ....*....|.
gi 547235570 295 ASLVFDVALLD 305
Cdd:COG0545   93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 440-528 1.32e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.89  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 440 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 519
Cdd:COG0545   15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                 ....*....
gi 547235570 520 LVFDIELLE 528
Cdd:COG0545   95 LVFEVELLD 103
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-191 1.52e-28

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 109.21  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570   47 CPRTVRSGDFVRYHYVGTFPDGQKFDSrywdtaedkadkspcpqvrvgvntspscrlkqkgvgiywkdlqflvrvqnhgl 126
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDS----------------------------------------------------- 27

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547235570  127 SYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSG-VIPPNSVLHFDVLL 191
Cdd:pfam00254  28 SYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 50-194 7.37e-23

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 93.32  E-value: 7.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  50 TVRSGDFVRYHYVGTFPDGQKFDSrywdtaedkadkspcpqvrvgvntspscrlkqkgvgiywkdlqflvrvqnhglSYD 129
Cdd:COG0545   13 KPKAGDTVTVHYTGTLLDGTVFDS-----------------------------------------------------SYD 39

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547235570 130 RDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDI 194
Cdd:COG0545   40 RGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNSTLVFEVELLDV 104
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 338-416 5.06e-16

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 78.65  E-value: 5.06e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547235570 338 YNGTLLDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVID 416
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 219-306 1.30e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 75.99  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 219 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLV 298
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 547235570 299 FDVALLDL 306
Cdd:PRK11570 198 FEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 216-284 3.35e-13

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 67.05  E-value: 3.35e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 216 IQVSDFVRYHYNGTFLDGTLFDSSHNRMKTydTY-VGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGE 284
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPL--EFlHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 332-416 1.01e-12

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 67.52  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 332 DFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQgyVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRG-NIPGSAVLVF 410
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVF 198


                 ....*.
gi 547235570 411 DIHVID 416
Cdd:PRK11570 199 EVELLE 204
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 219-306 4.30e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 66.71  E-value: 4.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 219 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDtyVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKdIPGQASLV 298
Cdd:PRK10902 164 SDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLV 240


                 ....*...
gi 547235570 299 FDVALLDL 306
Cdd:PRK10902 241 FDVELLDV 248
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 440-529 1.93e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 440 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 519
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 547235570 520 LVFDIELLEL 529
Cdd:PRK10902 239 LVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 329-396 3.06e-11

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 61.27  E-value: 3.06e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547235570 329 QSGDFLRYHYNGTLLDGTLFDSSYSRN-RTFdtYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGE 396
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 440-507 1.83e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 58.96  E-value: 1.83e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547235570 440 KKGDYLKYHYNASLLDGTLLDSTWNlGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGE 507
Cdd:COG1047    2 EKGDVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 443-530 1.94e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 60.97  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 443 DYLKYHYNASLLDGTLLDSTWNLGKTYNIVLgSGqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVF 522
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*...
gi 547235570 523 DIELLELV 530
Cdd:PRK11570 199 EVELLEIL 206
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 55-194 4.81e-07

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 51.69  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  55 DFVRYHYVGTFPDGQKFDSRYwdtaedkADKSPCpqvrvgvntspSCRLKqkGVGIYWKDlqflvrvqnhGLSYdrdstf 134
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSY-------TRGEPL-----------SFRLD--GVIPGWTE----------GLKN------ 208

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 135 nvfVGKGQLITgmdqaLVgmcvnerrfvkIPPKLAYGNEGVSGvIPPNSVLHFDVLLMDI 194
Cdd:PRK10902 209 ---IKKGGKIK-----LV-----------IPPELAYGKAGVPG-IPANSTLVFDVELLDV 248
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
524-612 8.50e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.63  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 524 IELLELVAGlpegYMFIWNGevspnLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLApgfdaelivKNMFTNQDRNGD 603
Cdd:COG5126   22 LERDDFEAL----FRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEATVEPFA---------RAAFDLLDTDGD 83


                 ....*....
gi 547235570 604 GKVTAEEFK 612
Cdd:COG5126   84 GKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 550-611 2.93e-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: 44.85  E-value: 2.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547235570 550 FEEIDKDGNGEVLLEEFSEYIHAqvasgkgkLAPGFDAELIvKNMFTNQDRNGDGKVTAEEF 611
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKS--------LGEGLSEEEI-DEMIREVDKDGDGKIDFEEF 58
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 104-194 4.15e-06

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 47.87  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 104 KQKGVGIYWKDLQFLVRVQNHG---LSYDR----------DST-FNVFVGKGQ--------LITGMDQALVGMCVNERRF 161
Cdd:PRK11570  93 KKEGVNSTESGLQFRVLTQGEGaipARTDRvrvhytgkliDGTvFDSSVARGEpaefpvngVIPGWIEALTLMPVGSKWE 172

                         90       100       110
                 ....*....|....*....|....*....|...
gi 547235570 162 VKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDI 194
Cdd:PRK11570 173 LTIPHELAYGERGAGASIPPFSTLVFEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 51-171 5.40e-06

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 46.25  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570  51 VRSGDFVRYHYVGTFPDGQKFDSrywdTAEDKAdkspcpqvrvgvntspscrlkqkgvgiywkdLQFLVrvqnhglsydr 130
Cdd:COG1047    1 IEKGDVVTLHYTLKLEDGEVFDS----TFEGEP-------------------------------LEFLH----------- 34

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 547235570 131 dstfnvfvGKGQLITGMDQALVGMCVNERRFVKIPPKLAYG 171
Cdd:COG1047   35 --------GAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
549-612 8.79e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 8.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547235570 549 LFEEIDKDGNGEVLLEEFSEYIHAQvasgkgklapGFDAELIvKNMFTNQDRNGDGKVTAEEFK 612
Cdd:COG5126   74 AFDLLDTDGDGKISADEFRRLLTAL----------GVSEEEA-DELFARLDTDGDGKISFEEFV 126
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 215-284 1.64e-04

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 42.39  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 215 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGE 284
Cdd:PRK15095   4 SVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGV 73
EF-hand_7 pfam13499
EF-hand domain pair;
549-612 5.70e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 5.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547235570  549 LFEEIDKDGNGEVLLEEFSEYIHaqvASGKGKLAPGFDAELIVKNMftnqDRNGDGKVTAEEFK 612
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR---KLEEGEPLSDEEVEELFKEF----DLDKDGRISFEEFL 63
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 322-397 7.56e-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: 7.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547235570 322 ENCERISQSGDFLRYHYNGTLlDGTLFDSSYSRNRTFDtyIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEE 397
Cdd:COG0544  152 VPVERAAEEGDRVTIDFEGTI-DGEEFEGGKAEDYSLE--LGSGSFIPGFEEQLVGMKAGEEKTFEVTFPEDYHAE 224
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 214-322 1.93e-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: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547235570 214 RTIQVSDFVRYHYNGtFLDGTLFDSSHNrmKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIppflAYGEDGDGKDIPG 293
Cdd:COG0544  156 RAAEEGDRVTIDFEG-TIDGEEFEGGKA--EDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEV----TFPEDYHAEELAG 228

                         90       100
                 ....*....|....*....|....*....
gi 547235570 294 QASlVFDVALldlhnpkdsISIENKVVPE 322
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 ...
 590-612 7.37e-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: 34.30  E-value: 7.37e-03
                          10        20
                  ....*....|....*....|...
gi 547235570  590 IVKNMFTNQDRNGDGKVTAEEFK 612
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFK 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 591-612 9.47e-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: 33.89  E-value: 9.47e-03
                           10        20
                   ....*....|....*....|..
gi 547235570   591 VKNMFTNQDRNGDGKVTAEEFK 612
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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