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Conserved domains on  [gi|206725547|ref|NP_001128684|]
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peptidyl-prolyl cis-trans isomerase FKBP7 isoform b precursor [Homo sapiens]

Protein Classification

FKBP-type peptidyl-prolyl cis-trans isomerase( domain architecture ID 10446594)

FKBP-type peptidyl-prolyl cis-trans isomerase acts as a PPIase that accelerates the folding of proteins

CATH:  3.10.50.40
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0000413|GO:0061077
PubMed:  27664121
SCOP:  4001062

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;
46-140 4.32e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 4.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547   46 CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYE 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 206725547  126 G-KIPPDATLIFEIEL 140
Cdd:pfam00254  78 GpVIPPNATLVFEVEL 93
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
126-212 3.51e-06

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547 126 GKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLqrefekdekpRDKSYQDAVLEDIFKKNDHDGD 205
Cdd:COG5126   48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGD 117


                 ....*..
gi 206725547 206 GFISPKE 212
Cdd:COG5126  118 GKISFEE 124
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
46-140 4.32e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 4.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547   46 CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYE 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 206725547  126 G-KIPPDATLIFEIEL 140
Cdd:pfam00254  78 GpVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 51-143 7.81e-32

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 111.81  E-value: 7.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547  51 KKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYEGKIPP 130
Cdd:COG0545   15 KAGDTVTVHYTGTLL-DGTVFDSSY--DRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPP 91

                         90
                 ....*....|...
gi 206725547 131 DATLIFEIELYAV 143
Cdd:COG0545   92 NSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 54-140 1.74e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 58.27  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547  54 DLLNAHYDGYLAkDGSKFYCSRTQneGHPKWFvlGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYEGKIPPDAT 133
Cdd:PRK11570 121 DRVRVHYTGKLI-DGTVFDSSVAR--GEPAEF--PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFST 195


                 ....*..
gi 206725547 134 LIFEIEL 140
Cdd:PRK11570 196 LVFEVEL 202
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
126-212 3.51e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547 126 GKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLqrefekdekpRDKSYQDAVLEDIFKKNDHDGD 205
Cdd:COG5126   48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGD 117


                 ....*..
gi 206725547 206 GFISPKE 212
Cdd:COG5126  118 GKISFEE 124
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 148-219 6.19e-06

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 45.89  E-value: 6.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206725547 148 RSIETFKQIDMDNDRQLSKAEINLYLQREFekdekpRDKSYQDAvlEDIFKKNDHDGDGFISPKEYNVYQHD 219
Cdd:cd16224   37 RLKSIIKKIDTDSDGFLTEEELSSWIQQSF------RHYALEDA--KQQFPEYDKDGDGAVTWDEYNMQMYD 100
EF-hand_7 pfam13499
EF-hand domain pair;
151-213 2.09e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 2.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 206725547  151 ETFKQIDMDNDRQLSKAEINLYLQReFEKDEKPRDKSyqdavLEDIFKKNDHDGDGFISPKEY 213
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRK-LEEGEPLSDEE-----VEELFKEFDLDKDGRISFEEF 62
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
46-140 4.32e-37

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 125.00  E-value: 4.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547   46 CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYE 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 206725547  126 G-KIPPDATLIFEIEL 140
Cdd:pfam00254  78 GpVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 51-143 7.81e-32

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 111.81  E-value: 7.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547  51 KKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYEGKIPP 130
Cdd:COG0545   15 KAGDTVTVHYTGTLL-DGTVFDSSY--DRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERGAGGVIPP 91

                         90
                 ....*....|...
gi 206725547 131 DATLIFEIELYAV 143
Cdd:COG0545   92 NSTLVFEVELLDV 104
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 51-140 1.32e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 57.03  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547  51 KKGDLLNAHYDGYLAkDGSKFycsRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGkegyegkiPP 130
Cdd:COG1047    2 EKGDVVTLHYTLKLE-DGEVF---DSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG--------ER 69

                         90
                 ....*....|
gi 206725547 131 DATLIFEIEL 140
Cdd:COG1047   70 DPELVQTVPR 79
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 54-140 1.74e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 58.27  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547  54 DLLNAHYDGYLAkDGSKFYCSRTQneGHPKWFvlGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYEGKIPPDAT 133
Cdd:PRK11570 121 DRVRVHYTGKLI-DGTVFDSSVAR--GEPAEF--PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERGAGASIPPFST 195


                 ....*..
gi 206725547 134 LIFEIEL 140
Cdd:PRK11570 196 LVFEVEL 202
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 28-149 4.65e-10

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 57.85  E-value: 4.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547  28 KEESTEEVKIEVLHRPEN--CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRTQNEghPKWFVLGvgQVIKGLDIAMTDMCP 105
Cdd:PRK10902 137 KEKGVKTTSTGLLYKVEKegTGEAPKDSDTVVVNYKGTLI-DGKEFDNSYTRGE--PLSFRLD--GVIPGWTEGLKNIKK 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 206725547 106 GEKRKVVIPPSFAYGKEGYEGkIPPDATLIFEIELYAVTKGPRS 149
Cdd:PRK10902 212 GGKIKLVIPPELAYGKAGVPG-IPANSTLVFDVELLDVKPAPKA 254
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
126-212 3.51e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547 126 GKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLqrefekdekpRDKSYQDAVLEDIFKKNDHDGD 205
Cdd:COG5126   48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGD 117


                 ....*..
gi 206725547 206 GFISPKE 212
Cdd:COG5126  118 GKISFEE 124
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 148-219 6.19e-06

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 45.89  E-value: 6.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206725547 148 RSIETFKQIDMDNDRQLSKAEINLYLQREFekdekpRDKSYQDAvlEDIFKKNDHDGDGFISPKEYNVYQHD 219
Cdd:cd16224   37 RLKSIIKKIDTDSDGFLTEEELSSWIQQSF------RHYALEDA--KQQFPEYDKDGDGAVTWDEYNMQMYD 100
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 150-216 2.89e-05

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 43.83  E-value: 2.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 206725547 150 IETFKQIDMDNDRQLSKAEINLYLQREFEkdekprdKSYQDAVLED--IFKKNDHDGDGFISPKEYNVY 216
Cdd:cd16225   37 KEIFKKVDVNTDGFLSAEELEDWIMEKTQ-------EHFQEAVEENeqIFKAVDTDKDGNVSWEEYRVH 98
EF-hand_7 pfam13499
EF-hand domain pair;
151-213 2.09e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 2.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 206725547  151 ETFKQIDMDNDRQLSKAEINLYLQReFEKDEKPRDKSyqdavLEDIFKKNDHDGDGFISPKEY 213
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRK-LEEGEPLSDEE-----VEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
144-213 3.91e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206725547 144 TKGPRSIETFKQIDMDNDRQLSKAEINLYLQR--------------------EFEKDEKPRDKSYQDAVLEDIFKKNDHD 203
Cdd:COG5126    2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRlwatlfseadtdgdgrisreEFVAGMESLFEATVEPFARAAFDLLDTD 81

                         90
                 ....*....|
gi 206725547 204 GDGFISPKEY 213
Cdd:COG5126   82 GDGKISADEF 91
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 151-212 9.59e-04

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: 36.37  E-value: 9.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206725547 151 ETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRdksyqdavLEDIFKKNDHDGDGFISPKE 212
Cdd:cd00051    4 EAFRLFDKDGDGTISADELKAALKSLGEGLSEEE--------IDEMIREVDKDGDGKIDFEE 57
 
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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