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Conserved domains on  [gi|3860029|gb|AAC72964|]
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FK506 binding protein [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 502)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-139 2.90e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 2.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029     47 CPRTVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSG-V 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 3860029    126 IPPNSVLHFDVLLV 139
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
271-362 2.04e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    271 CERRSQSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGR--GS 348
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 3860029    349 IPGSAVLVFDIHVI 362
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
159-251 1.15e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 128.85  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    159 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEG-DGKD 237
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 3860029    238 IPGQASLVFDVALL 251
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
382-474 2.90e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    382 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 460
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 3860029    461 VPGSAVLVFDIELL 474
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
480-559 6.33e-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: 6.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  480 LPEGYMFIWNGevspnLFEEIDRDGNGEVLLEEFSEYIHAQVATGkgklapgfnAEMIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:COG5126  27 FEALFRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEAT---------VEPFARAAFDLLDTDGDGKISADEFR 92
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-139 2.90e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 2.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029     47 CPRTVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSG-V 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 3860029    126 IPPNSVLHFDVLLV 139
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
271-362 2.04e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    271 CERRSQSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGR--GS 348
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 3860029    349 IPGSAVLVFDIHVI 362
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
159-251 1.15e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 128.85  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    159 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEG-DGKD 237
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 3860029    238 IPGQASLVFDVALL 251
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
382-474 2.90e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    382 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 460
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 3860029    461 VPGSAVLVFDIELL 474
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 50-141 3.48e-34

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 124.91  E-value: 3.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   50 TVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGVIPPN 129
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|..
gi 3860029  130 SVLHFDVLLVDI 141
Cdd:COG0545  93 STLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 276-364 3.30e-30

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: 3.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  276 QSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGRG-SIPGSAV 354
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGgVIPPNST 94

                        90
                ....*....|
gi 3860029  355 LVFDIHVIDF 364
Cdd:COG0545  95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 162-252 6.88e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 110.27  E-value: 6.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  162 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKDIPGQ 241
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|.
gi 3860029  242 ASLVFDVALLD 252
Cdd:COG0545  93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 387-475 1.19e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.50  E-value: 1.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 466
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                ....*....
gi 3860029  467 LVFDIELLE 475
Cdd:COG0545  95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 285-363 1.22e-15

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 77.11  E-value: 1.22e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3860029   285 YNGTLLDGTLFDSSYSRNHTFDtyIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGRGSIPGSAVLVFDIHVID 363
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 166-253 2.70e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 74.83  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   166 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKDIPGQASLV 245
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 3860029   246 FDVALLDL 253
Cdd:PRK11570 198 FEVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 55-141 6.13e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 70.98  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    55 DFVRYHYVGTFLDGQKFDSSYDRD--STFNVfvgkGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGVIPPNSVL 132
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGepAEFPV----NGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTL 196


                 ....*....
gi 3860029   133 HFDVLLVDI 141
Cdd:PRK11570 197 VFEVELLEI 205
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 387-476 1.70e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 466
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 3860029   467 LVFDIELLEL 476
Cdd:PRK10902 239 LVFDVELLDV 248
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
480-559 6.33e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 6.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  480 LPEGYMFIWNGevspnLFEEIDRDGNGEVLLEEFSEYIHAQVATGkgklapgfnAEMIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:COG5126  27 FEALFRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEAT---------VEPFARAAFDLLDTDGDGKISADEFR 92
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 497-558 1.08e-05

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: 43.31  E-value: 1.08e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3860029  497 FEEIDRDGNGEVLLEEFSEYIHAqvaTGKGKLapgfnaEMIVKNMFTNQDRNGDGKVTAEEF 558
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKS---LGEGLS------EEEIDEMIREVDKDGDGKIDFEEF 58
EF-hand_7 pfam13499
EF-hand domain pair;
496-559 1.73e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3860029    496 LFEEIDRDGNGEVLLEEFSEYIHaqvatgkgKLAPGFN-AEMIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR--------KLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFL 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 538-559 6.99e-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: 34.28  E-value: 6.99e-03
                           10        20
                   ....*....|....*....|..
gi 3860029     538 VKNMFTNQDRNGDGKVTAEEFK 559
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFK 23
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
47-139 2.90e-40

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 141.18  E-value: 2.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029     47 CPRTVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSG-V 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 3860029    126 IPPNSVLHFDVLLV 139
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
271-362 2.04e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 133.48  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    271 CERRSQSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGR--GS 348
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLagPV 80

                          90
                  ....*....|....
gi 3860029    349 IPGSAVLVFDIHVI 362
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
159-251 1.15e-35

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 128.85  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    159 CPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEG-DGKD 237
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGlAGPV 80

                          90
                  ....*....|....
gi 3860029    238 IPGQASLVFDVALL 251
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
382-474 2.90e-34

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    382 CSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDG-E 460
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLEDGTVFDSSYDRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLAGpV 80

                          90
                  ....*....|....
gi 3860029    461 VPGSAVLVFDIELL 474
Cdd:pfam00254  81 IPPNATLVFEVELL 94
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 50-141 3.48e-34

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 124.91  E-value: 3.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   50 TVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGVIPPN 129
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|..
gi 3860029  130 SVLHFDVLLVDI 141
Cdd:COG0545  93 STLVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 276-364 3.30e-30

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: 3.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  276 QSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGRG-SIPGSAV 354
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGgVIPPNST 94

                        90
                ....*....|
gi 3860029  355 LVFDIHVIDF 364
Cdd:COG0545  95 LVFEVELLDV 104
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 162-252 6.88e-29

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 110.27  E-value: 6.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  162 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKDIPGQ 241
Cdd:COG0545  13 KPKAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPN 92

                        90
                ....*....|.
gi 3860029  242 ASLVFDVALLD 252
Cdd:COG0545  93 STLVFEVELLD 103
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 387-475 1.19e-28

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 109.50  E-value: 1.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAV 466
Cdd:COG0545  15 KAGDTVTVHYTGTLLDGTVFDSSYDRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPPNST 94


                ....*....
gi 3860029  467 LVFDIELLE 475
Cdd:COG0545  95 LVFEVELLD 103
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 285-363 1.22e-15

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 77.11  E-value: 1.22e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3860029   285 YNGTLLDGTLFDSSYSRNHTFDtyIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGRGSIPGSAVLVFDIHVID 363
Cdd:PRK10902 171 YKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPANSTLVFDVELLD 247
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 166-253 2.70e-15

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 74.83  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   166 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGigWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKDIPGQASLV 245
Cdd:PRK11570 120 TDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVN--GVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLV 197


                 ....*...
gi 3860029   246 FDVALLDL 253
Cdd:PRK11570 198 FEVELLEI 205
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 51-118 4.41e-15

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 72.06  E-value: 4.41e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3860029   51 VHSGDFVRYHYVGTFLDGQKFDSSYDRDsTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYG 118
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGE-PLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 55-141 6.13e-14

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 70.98  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    55 DFVRYHYVGTFLDGQKFDSSYDRD--STFNVfvgkGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGVIPPNSVL 132
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGepAEFPV----NGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTL 196


                 ....*....
gi 3860029   133 HFDVLLVDI 141
Cdd:PRK11570 197 VFEVELLEI 205
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 279-363 2.67e-13

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 69.06  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   279 DFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQgyVIPGMDEGLLGVCIGERRRIVVPPHLGYGEKGRG-SIPGSAVLVF 357
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNG--VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGaSIPPFSTLVF 198


                 ....*.
gi 3860029   358 DIHVID 363
Cdd:PRK11570 199 EVELLE 204
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 163-231 5.30e-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: 5.30e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  163 IQVSDFVRYHYNGTFLDGTLFDSSHNRMKTydTY-VGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGE 231
Cdd:COG1047   1 IEKGDVVTLHYTLKLEDGEVFDSTFEGEPL--EFlHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 55-141 5.59e-12

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 66.33  E-value: 5.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029    55 DFVRYHYVGTFLDGQKFDSSYDRDSTFNvFVGKGqLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGvIPPNSVLHF 134
Cdd:PRK10902 165 DTVVVNYKGTLIDGKEFDNSYTRGEPLS-FRLDG-VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLVF 241


                 ....*..
gi 3860029   135 DVLLVDI 141
Cdd:PRK10902 242 DVELLDV 248
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 166-253 1.68e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   166 SDFVRYHYNGTFLDGTLFDSSHNRMKTYDtyVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKdIPGQASLV 245
Cdd:PRK10902 164 SDTVVVNYKGTLIDGKEFDNSYTRGEPLS--FRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANSTLV 240


                 ....*...
gi 3860029   246 FDVALLDL 253
Cdd:PRK10902 241 FDVELLDV 248
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 387-476 1.70e-11

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 64.78  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   387 KKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSgqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGeVPGSAV 466
Cdd:PRK10902 162 KDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDG--VIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPG-IPANST 238

                         90
                 ....*....|
gi 3860029   467 LVFDIELLEL 476
Cdd:PRK10902 239 LVFDVELLDV 248
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 276-343 7.06e-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: 7.06e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3860029  276 QSGDFLRYHYNGTLLDGTLFDSSYSRN-HTFdtYIGQGYVIPGMDEGLLGVCIGERRRIVVPPHLGYGE 343
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFEGEpLEF--LHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 387-454 1.80e-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: 1.80e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3860029  387 KKGDYLKYHYNASLLDGTLLDSTWNlGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGE 454
Cdd:COG1047   2 EKGDVVTLHYTLKLEDGEVFDSTFE-GEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYGE 68
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 390-477 2.13e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 60.58  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029   390 DYLKYHYNASLLDGTLLDSTWNLGKTYNIVLgSGqVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVF 469
Cdd:PRK11570 121 DRVRVHYTGKLIDGTVFDSSVARGEPAEFPV-NG-VIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFSTLVF 198


                 ....*...
gi 3860029   470 DIELLELV 477
Cdd:PRK11570 199 EVELLEIL 206
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
480-559 6.33e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 6.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  480 LPEGYMFIWNGevspnLFEEIDRDGNGEVLLEEFSEYIHAQVATGkgklapgfnAEMIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:COG5126  27 FEALFRRLWAT-----LFSEADTDGDGRISREEFVAGMESLFEAT---------VEPFARAAFDLLDTDGDGKISADEFR 92
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
496-559 2.98e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 2.98e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3860029  496 LFEEIDRDGNGEVLLEEFSEYIHAQVATgkgklapgfnaEMIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:COG5126  74 AFDLLDTDGDGKISADEFRRLLTALGVS-----------EEEADELFARLDTDGDGKISFEEFV 126
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 497-558 1.08e-05

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: 43.31  E-value: 1.08e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3860029  497 FEEIDRDGNGEVLLEEFSEYIHAqvaTGKGKLapgfnaEMIVKNMFTNQDRNGDGKVTAEEF 558
Cdd:cd00051   6 FRLFDKDGDGTISADELKAALKS---LGEGLS------EEEIDEMIREVDKDGDGKIDFEEF 58
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 162-232 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 3860029   162 TIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEE 232
Cdd:PRK15095   4 SVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 269-335 6.20e-04

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


Pssm-ID: 440310 [Multi-domain]  Cd Length: 424  Bit Score: 42.42  E-value: 6.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3860029  269 ENCERRSQSGDFLRYHYNGTLlDGTLFDSSYSRNHTFDtyIGQGYVIPGMDEGLLGVCIGERRRIVV 335
Cdd:COG0544 152 VPVERAAEEGDRVTIDFEGTI-DGEEFEGGKAEDYSLE--LGSGSFIPGFEEQLVGMKAGEEKTFEV 215
Tig COG0544
FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor) [Posttranslational modification, ...
 161-269 1.28e-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: 41.27  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860029  161 RTIQVSDFVRYHYNGtFLDGTLFDSSHNrmKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVppflAYGEEGDGKDIPG 240
Cdd:COG0544 156 RAAEEGDRVTIDFEG-TIDGEEFEGGKA--EDYSLELGSGSFIPGFEEQLVGMKAGEEKTFEV----TFPEDYHAEELAG 228

                        90       100       110
                ....*....|....*....|....*....|
gi 3860029  241 QASlVFDValldlhnpkdTI-SIENKVVPE 269
Cdd:COG0544 229 KTA-TFKV----------TVkEVKEKELPE 247
EF-hand_7 pfam13499
EF-hand domain pair;
496-559 1.73e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3860029    496 LFEEIDRDGNGEVLLEEFSEYIHaqvatgkgKLAPGFN-AEMIVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLR--------KLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFL 63
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 537-559 5.44e-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: 34.68  E-value: 5.44e-03
                          10        20
                  ....*....|....*....|...
gi 3860029    537 IVKNMFTNQDRNGDGKVTAEEFK 559
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFK 23
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 538-559 6.99e-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: 34.28  E-value: 6.99e-03
                           10        20
                   ....*....|....*....|..
gi 3860029     538 VKNMFTNQDRNGDGKVTAEEFK 559
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFK 23
PRK15095 PRK15095
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 50-120 7.23e-03

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


Pssm-ID: 237908 [Multi-domain]  Cd Length: 156  Bit Score: 37.38  E-value: 7.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3860029    50 TVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSE 120
Cdd:PRK15095   4 SVQSNSAVLVHFTLKLDDGSTAESTRNNGKPALFRLGDGSLSEGLEQQLLGLKVGDKKTFSLEPEAAFGVP 74
 
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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