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Conserved domains on  [gi|23396583|sp|O54998|]
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RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP7; Short=PPIase FKBP7; AltName: Full=23 kDa FK506-binding protein; Short=23 kDa FKBP; Short=FKBP-23; AltName: Full=FK506-binding protein 7; Short=FKBP-7; AltName: Full=Rotamase; Flags: Precursor

Protein Classification

FKBP_C and EFh_CREC domain-containing protein( domain architecture ID 11991424)

FKBP_C and EFh_CREC domain-containing protein

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;
42-137 1.95e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


:

Pssm-ID: 459735  Cd Length: 94  Bit Score: 130.78  E-value: 1.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583    42 CSKTSRKGDLLNAHYDGYLAkDGSKFYCSRtqDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGYA 121
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 23396583   122 EGKIPPNATLMFEIEL 137
Cdd:pfam00254  78 GPVIPPNATLVFEVEL 93
EFh_CREC super family cl25354
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 147-213 7.64e-07

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


The actual alignment was detected with superfamily member cd16225:

Pssm-ID: 330175 [Multi-domain]  Cd Length: 278  Bit Score: 48.45  E-value: 7.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23396583 147 IETFKQIDTDNDRQLSKAEIELYLQKDFEkdanprdKSYQKAVLED--IFKKNDHNGDGFISPKEYNVH 213
Cdd:cd16225  37 KEIFKKVDVNTDGFLSAEELEDWIMEKTQ-------EHFQEAVEENeqIFKAVDTDKDGNVSWEEYRVH 98
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-137 1.95e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 130.78  E-value: 1.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583    42 CSKTSRKGDLLNAHYDGYLAkDGSKFYCSRtqDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGYA 121
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 23396583   122 EGKIPPNATLMFEIEL 137
Cdd:pfam00254  78 GPVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 48-140 4.34e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 107.19  E-value: 4.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583  48 KGDLLNAHYDGYLAkDGSKFYCSRtqDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGyAEGKIPP 127
Cdd:COG0545  16 AGDTVTVHYTGTLL-DGTVFDSSY--DRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERG-AGGVIPP 91

                        90
                ....*....|...
gi 23396583 128 NATLMFEIELYAV 140
Cdd:COG0545  92 NSTLVFEVELLDV 104
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 50-137 1.93e-08

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 52.49  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583   50 DLLNAHYDGYLAkDGSKFYCSrtQDEGHPKWFvlGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGyAEGKIPPNA 129
Cdd:PRK11570 121 DRVRVHYTGKLI-DGTVFDSS--VARGEPAEF--PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERG-AGASIPPFS 194


                 ....*...
gi 23396583  130 TLMFEIEL 137
Cdd:PRK11570 195 TLVFEVEL 202
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 147-213 7.64e-07

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: 48.45  E-value: 7.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23396583 147 IETFKQIDTDNDRQLSKAEIELYLQKDFEkdanprdKSYQKAVLED--IFKKNDHNGDGFISPKEYNVH 213
Cdd:cd16225  37 KEIFKKVDVNTDGFLSAEELEDWIMEKTQ-------EHFQEAVEENeqIFKAVDTDKDGNVSWEEYRVH 98
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
137-216 1.35e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.32  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583 137 LYAVTKGPRSIETFKQIDTDNDRQLSKAEIELYLqkdfekdanpRDKSYQKAVLEDIFKKNDHNGDGFISPKEYNVHQHD 216
Cdd:COG5126  62 LFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
148-210 1.74e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 1.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23396583   148 ETFKQIDTDNDRQLSKAEIELYLQKdFEKDANPRDKSyqkavLEDIFKKNDHNGDGFISPKEY 210
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRK-LEEGEPLSDEE-----VEELFKEFDLDKDGRISFEEF 62
 
Name Accession Description Interval E-value
FKBP_C pfam00254
FKBP-type peptidyl-prolyl cis-trans isomerase;
42-137 1.95e-39

FKBP-type peptidyl-prolyl cis-trans isomerase;


Pssm-ID: 459735  Cd Length: 94  Bit Score: 130.78  E-value: 1.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583    42 CSKTSRKGDLLNAHYDGYLAkDGSKFYCSRtqDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGYA 121
Cdd:pfam00254   1 GPEKAKKGDRVTVHYTGTLE-DGTVFDSSY--DRGKPFEFTLGSGQVIPGWDEGLVGMKVGEKRKLTIPPELAYGEEGLA 77

                          90
                  ....*....|....*.
gi 23396583   122 EGKIPPNATLMFEIEL 137
Cdd:pfam00254  78 GPVIPPNATLVFEVEL 93
FkpA COG0545
FKBP-type peptidyl-prolyl cis-trans isomerase [Posttranslational modification, protein ...
 48-140 4.34e-30

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


Pssm-ID: 440311 [Multi-domain]  Cd Length: 104  Bit Score: 107.19  E-value: 4.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583  48 KGDLLNAHYDGYLAkDGSKFYCSRtqDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGyAEGKIPP 127
Cdd:COG0545  16 AGDTVTVHYTGTLL-DGTVFDSSY--DRGEPATFPLGVGQVIPGWDEGLQGMKVGGKRRLVIPPELAYGERG-AGGVIPP 91

                        90
                ....*....|...
gi 23396583 128 NATLMFEIELYAV 140
Cdd:COG0545  92 NSTLVFEVELLDV 104
SlpA COG1047
Peptidyl-prolyl cis-trans isomerase, FKBP type [Posttranslational modification, protein ...
 48-116 5.40e-10

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


Pssm-ID: 440668 [Multi-domain]  Cd Length: 138  Bit Score: 55.49  E-value: 5.40e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23396583  48 KGDLLNAHYDGYLAkDGSKFycsRTQDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYG 116
Cdd:COG1047   3 KGDVVTLHYTLKLE-DGEVF---DSTFEGEPLEFLHGAGQLIPGLEEALEGMEVGDKKTVTLPPEEAYG 67
PRK11570 PRK11570
peptidyl-prolyl cis-trans isomerase; Provisional
 50-137 1.93e-08

peptidyl-prolyl cis-trans isomerase; Provisional


Pssm-ID: 183207 [Multi-domain]  Cd Length: 206  Bit Score: 52.49  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583   50 DLLNAHYDGYLAkDGSKFYCSrtQDEGHPKWFvlGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGyAEGKIPPNA 129
Cdd:PRK11570 121 DRVRVHYTGKLI-DGTVFDSS--VARGEPAEF--PVNGVIPGWIEALTLMPVGSKWELTIPHELAYGERG-AGASIPPFS 194


                 ....*...
gi 23396583  130 TLMFEIEL 137
Cdd:PRK11570 195 TLVFEVEL 202
PRK10902 PRK10902
FKBP-type peptidyl-prolyl cis-trans isomerase; Provisional
 24-146 4.95e-08

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


Pssm-ID: 236791 [Multi-domain]  Cd Length: 269  Bit Score: 52.07  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583   24 KEESTEEVKIEVLHRPEN--CSKTSRKGDLLNAHYDGYLAkDGSKFYCSRTQDEghPKWFVLGvgHVIKGLDIAMMDMCP 101
Cdd:PRK10902 137 KEKGVKTTSTGLLYKVEKegTGEAPKDSDTVVVNYKGTLI-DGKEFDNSYTRGE--PLSFRLD--GVIPGWTEGLKNIKK 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 23396583  102 GEKRKVIIPPSFAYGKEGYAegKIPPNATLMFEIELYAVTKGPRS 146
Cdd:PRK10902 212 GGKIKLVIPPELAYGKAGVP--GIPANSTLVFDVELLDVKPAPKA 254
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 147-213 7.64e-07

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: 48.45  E-value: 7.64e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23396583 147 IETFKQIDTDNDRQLSKAEIELYLQKDFEkdanprdKSYQKAVLED--IFKKNDHNGDGFISPKEYNVH 213
Cdd:cd16225  37 KEIFKKVDVNTDGFLSAEELEDWIMEKTQ-------EHFQEAVEENeqIFKAVDTDKDGNVSWEEYRVH 98
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
137-216 1.35e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.32  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23396583 137 LYAVTKGPRSIETFKQIDTDNDRQLSKAEIELYLqkdfekdanpRDKSYQKAVLEDIFKKNDHNGDGFISPKEYNVHQHD 216
Cdd:COG5126  62 LFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----------TALGVSEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 145-216 1.44e-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: 47.81  E-value: 1.44e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23396583 145 RSIETFKQIDTDNDRQLSKAEIELYLQKDFekdanprdKSYQKAVLEDIFKKNDHNGDGFISPKEYNVHQHD 216
Cdd:cd16224  37 RLKSIIKKIDTDSDGFLTEEELSSWIQQSF--------RHYALEDAKQQFPEYDKDGDGAVTWDEYNMQMYD 100
EF-hand_7 pfam13499
EF-hand domain pair;
148-210 1.74e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.17  E-value: 1.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23396583   148 ETFKQIDTDNDRQLSKAEIELYLQKdFEKDANPRDKSyqkavLEDIFKKNDHNGDGFISPKEY 210
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRK-LEEGEPLSDEE-----VEELFKEFDLDKDGRISFEEF 62
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
150-210 1.01e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 1.01e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23396583 150 FKQIDTDNDRQLSKAEIELYLQKDFEKDANPRdksyqkavLEDIFKKNDHNGDGFISPKEY 210
Cdd:COG5126  39 FSEADTDGDGRISREEFVAGMESLFEATVEPF--------ARAAFDLLDTDGDGKISADEF 91
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 148-209 5.08e-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: 37.14  E-value: 5.08e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23396583 148 ETFKQIDTDNDRQLSKAEIELYLQKDFEKdanprdksYQKAVLEDIFKKNDHNGDGFISPKE 209
Cdd:cd00051   4 EAFRLFDKDGDGTISADELKAALKSLGEG--------LSEEEIDEMIREVDKDGDGKIDFEE 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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