NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|31317231|ref|NP_851939|]
View 

peptidyl-prolyl cis-trans isomerase FKBP7 isoform a precursor [Homo sapiens]

Protein Classification

CREC-EF hand family protein( domain architecture ID 707362)

CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family protein; the family consists of a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55, reticulocalbin-3 (RCN-3), cab45 Ca2+-binding protein, and calumenin (also known as crocalbin or CBP-50)

Gene Ontology:  GO:0005509
PubMed:  28707401

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
46-141 5.50e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 129.62  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231    46 CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYA 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 31317231   126 EGKIPPDATLIFEIEL 141
Cdd:pfam00254  78 GPVIPPNATLVFEVEL 93
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
127-213 3.76e-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: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231 127 GKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLqrefekdekpRDKSYQDAVLEDIFKKNDHDGD 206
Cdd:COG5126  48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGD 117


                ....*..
gi 31317231 207 GFISPKE 213
Cdd:COG5126 118 GKISFEE 124
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
46-141 5.50e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 129.62  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231    46 CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYA 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 31317231   126 EGKIPPDATLIFEIEL 141
Cdd:pfam00254  78 GPVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 51-144 1.94e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 108.35  E-value: 1.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231  51 KKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGyAEGKIP 130
Cdd:COG0545  15 KAGDTVTVHYTGTLL-DGTVFDSSY--DRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERG-AGGVIP 90

                        90
                ....*....|....
gi 31317231 131 PDATLIFEIELYAV 144
Cdd:COG0545  91 PNSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 54-141 6.33e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 56.73  E-value: 6.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231   54 DLLNAHYDGYLAkDGSKFYCSRTQneGHPKWFvlGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGyAEGKIPPDA 133
Cdd:PRK11570 121 DRVRVHYTGKLI-DGTVFDSSVAR--GEPAEF--PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERG-AGASIPPFS 194


                 ....*...
gi 31317231  134 TLIFEIEL 141
Cdd:PRK11570 195 TLVFEVEL 202
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
127-213 3.76e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231 127 GKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLqrefekdekpRDKSYQDAVLEDIFKKNDHDGD 206
Cdd:COG5126  48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGD 117


                ....*..
gi 31317231 207 GFISPKE 213
Cdd:COG5126 118 GKISFEE 124
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 149-220 5.87e-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: 5.87e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31317231 149 RSIETFKQIDMDNDRQLSKAEINLYLQREFekdekpRDKSYQDAvlEDIFKKNDHDGDGFISPKEYNVYQHD 220
Cdd:cd16224  37 RLKSIIKKIDTDSDGFLTEEELSSWIQQSF------RHYALEDA--KQQFPEYDKDGDGAVTWDEYNMQMYD 100
EF-hand_7 pfam13499
EF-hand domain pair;
152-214 1.92e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 1.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31317231   152 ETFKQIDMDNDRQLSKAEINLYLQReFEKDEKPRDKSyqdavLEDIFKKNDHDGDGFISPKEY 214
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRK-LEEGEPLSDEE-----VEELFKEFDLDKDGRISFEEF 62
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
46-141 5.50e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 129.62  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231    46 CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYA 125
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 31317231   126 EGKIPPDATLIFEIEL 141
Cdd:pfam00254  78 GPVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 51-144 1.94e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 108.35  E-value: 1.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231  51 KKGDLLNAHYDGYLAkDGSKFYCSRtqNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGyAEGKIP 130
Cdd:COG0545  15 KAGDTVTVHYTGTLL-DGTVFDSSY--DRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERG-AGGVIP 90

                        90
                ....*....|....
gi 31317231 131 PDATLIFEIELYAV 144
Cdd:COG0545  91 PNSTLVFEVELLDV 104
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 51-141 1.76e-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: 1.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231  51 KKGDLLNAHYDGYLAkDGSKFycsRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGkegyaegkiP 130
Cdd:COG1047   2 EKGDVVTLHYTLKLE-DGEVF---DSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG---------E 68

                        90
                ....*....|.
gi 31317231 131 PDATLIFEIEL 141
Cdd:COG1047  69 RDPELVQTVPR 79
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 54-141 6.33e-10

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 56.73  E-value: 6.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231   54 DLLNAHYDGYLAkDGSKFYCSRTQneGHPKWFvlGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGyAEGKIPPDA 133
Cdd:PRK11570 121 DRVRVHYTGKLI-DGTVFDSSVAR--GEPAEF--PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERG-AGASIPPFS 194


                 ....*...
gi 31317231  134 TLIFEIEL 141
Cdd:PRK11570 195 TLVFEVEL 202
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 28-150 4.84e-09

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 54.77  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231   28 KEESTEEVKIEVLHRPEN--CSKTSKKGDLLNAHYDGYLAkDGSKFYCSRTQNEghPKWFVLGvgQVIKGLDIAMTDMCP 105
Cdd:PRK10902 137 KEKGVKTTSTGLLYKVEKegTGEAPKDSDTVVVNYKGTLI-DGKEFDNSYTRGE--PLSFRLD--GVIPGWTEGLKNIKK 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 31317231  106 GEKRKVVIPPSFAYGKEGYAegKIPPDATLIFEIELYAVTKGPRS 150
Cdd:PRK10902 212 GGKIKLVIPPELAYGKAGVP--GIPANSTLVFDVELLDVKPAPKA 254
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
127-213 3.76e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 3.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231 127 GKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLqrefekdekpRDKSYQDAVLEDIFKKNDHDGD 206
Cdd:COG5126  48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGD 117


                ....*..
gi 31317231 207 GFISPKE 213
Cdd:COG5126 118 GKISFEE 124
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 149-220 5.87e-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: 5.87e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31317231 149 RSIETFKQIDMDNDRQLSKAEINLYLQREFekdekpRDKSYQDAvlEDIFKKNDHDGDGFISPKEYNVYQHD 220
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 ...
 151-217 2.66e-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: 2.66e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31317231 151 IETFKQIDMDNDRQLSKAEINLYLQREFEkdekprdKSYQDAVLED--IFKKNDHDGDGFISPKEYNVY 217
Cdd:cd16225  37 KEIFKKVDVNTDGFLSAEELEDWIMEKTQ-------EHFQEAVEENeqIFKAVDTDKDGNVSWEEYRVH 98
EF-hand_7 pfam13499
EF-hand domain pair;
152-214 1.92e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 1.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31317231   152 ETFKQIDMDNDRQLSKAEINLYLQReFEKDEKPRDKSyqdavLEDIFKKNDHDGDGFISPKEY 214
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRK-LEEGEPLSDEE-----VEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
145-214 4.17e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.00  E-value: 4.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31317231 145 TKGPRSIETFKQIDMDNDRQLSKAEINLYLQR--------------------EFEKDEKPRDKSYQDAVLEDIFKKNDHD 204
Cdd:COG5126   2 LQRRKLDRRFDLLDADGDGVLERDDFEALFRRlwatlfseadtdgdgrisreEFVAGMESLFEATVEPFARAAFDLLDTD 81

                        90
                ....*....|
gi 31317231 205 GDGFISPKEY 214
Cdd:COG5126  82 GDGKISADEF 91
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 152-213 8.39e-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: 36.76  E-value: 8.39e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31317231 152 ETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRdksyqdavLEDIFKKNDHDGDGFISPKE 213
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH