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Conserved domains on  [gi|50540432|ref|NP_001002682|]
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calsequestrin-2 precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Calsequestrin super family cl37643
Calsequestrin;
23-372 0e+00

Calsequestrin;


The actual alignment was detected with superfamily member pfam01216:

Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 576.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    23 GLEFPRYDGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPPAAKELQKQLHLTELVLELAAQVLEEKDIGFGMVDSQKDAK 102
Cdd:pfam01216   1 GLDFPEYDGKDRVINLNAKNFKNVFKKYDVLALLYHEPPEDDKAAQKQFELEEIILELAAQVLEDKDIGFGLVDAEKDAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   103 VAKKLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLEDPVEIIDNALELRAFDRMEEDIKLIGFFKSQESEHYLA 182
Cdd:pfam01216  81 LAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   183 FQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPVTIPDKPHSEEELVAFISEHRRPTLRKLKAEDMFETW 262
Cdd:pfam01216 161 FEDAAEEFHPYIKFFATFDKGVAKKLSLKLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTLRKLKPEDMFETW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   263 EDDLNGIHIVAFAEEEDPDGFEFLEILKEVARDNTHNPDLSIVWIDPDNFPLLIPYWEMTFKVDLFRPQIGVVNVTDADS 342
Cdd:pfam01216 241 EDDLDGIHIVAFAEEADPDGFEFLEILKAVAQDNTDNPDLSIIWIDPDDFPLLVAYWEKTFDIDLFAPQIGVVNVTDADS 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 50540432   343 VWLEIPNDDELPSAEELENWIEDVLSGTVN 372
Cdd:pfam01216 321 VWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
 
Name Accession Description Interval E-value
Calsequestrin pfam01216
Calsequestrin;
23-372 0e+00

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 576.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    23 GLEFPRYDGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPPAAKELQKQLHLTELVLELAAQVLEEKDIGFGMVDSQKDAK 102
Cdd:pfam01216   1 GLDFPEYDGKDRVINLNAKNFKNVFKKYDVLALLYHEPPEDDKAAQKQFELEEIILELAAQVLEDKDIGFGLVDAEKDAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   103 VAKKLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLEDPVEIIDNALELRAFDRMEEDIKLIGFFKSQESEHYLA 182
Cdd:pfam01216  81 LAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   183 FQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPVTIPDKPHSEEELVAFISEHRRPTLRKLKAEDMFETW 262
Cdd:pfam01216 161 FEDAAEEFHPYIKFFATFDKGVAKKLSLKLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTLRKLKPEDMFETW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   263 EDDLNGIHIVAFAEEEDPDGFEFLEILKEVARDNTHNPDLSIVWIDPDNFPLLIPYWEMTFKVDLFRPQIGVVNVTDADS 342
Cdd:pfam01216 241 EDDLDGIHIVAFAEEADPDGFEFLEILKAVAQDNTDNPDLSIIWIDPDDFPLLVAYWEKTFDIDLFAPQIGVVNVTDADS 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 50540432   343 VWLEIPNDDELPSAEELENWIEDVLSGTVN 372
Cdd:pfam01216 321 VWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
PDI_b'_Calsequestrin_C cd03074
Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold ...
248-367 4.29e-70

Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The C-terminal TRX-fold domain (or domain III) mediates back-to-back dimer interaction and also contriubutes to the front-to-front dimer interface, both of which are important features in the formation of calsequestrin polymers.


Pssm-ID: 239372  Cd Length: 120  Bit Score: 216.58  E-value: 4.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432 248 PTLRKLKAEDMFETWEDDLNGIHIVAFAEEEDPDGFEFLEILKEVARDNTHNPDLSIVWIDPDNFPLLIPYWEMTFKVDL 327
Cdd:cd03074   1 PTLRKLKPENMFETWEDDLDGIHIVAFAEEEDPDGYEFLEILKEVARDNTDNPDLSIIWIDPDDFPLLVPYWEKTFGIDL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50540432 328 FRPQIGVVNVTDADSVWLEIPNDDELPSAEELENWIEDVL 367
Cdd:cd03074  81 FRPQIGVVNVTDADSVWMEMDDDEDLPTAEELEDWIEDVL 120
PTZ00102 PTZ00102
disulphide isomerase; Provisional
3-312 5.99e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.08  E-value: 5.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    3 TIWILLLASMAFFTLASAKKGLefprydGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPPAakelqkqlHLTELVLEL-- 80
Cdd:PTZ00102   8 SSLFLLLILLAFAVFGSAEEHF------ISEHVTVLTDSTFDKFITENEIVLVKFYAPWCG--------HCKRLAPEYkk 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   81 AAQVLEEK--DIGFGMVDSQKDAKVAKKLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLEDPVEIIDNALElra 158
Cdd:PTZ00102  74 AAKMLKEKksEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASE--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432  159 fDRMEEDIKLIGF---FKSQESEHYLAFQEAAEQFQPFIKFFATFEKSVAKELTLKMNevdfyepfmEEPVTIPdKPHSE 235
Cdd:PTZ00102 151 -IKLIAKKIFVAFygeYTSKDSELYKKFEEVADKHREHAKFFVKKHEGKNKIYVLHKD---------EEGVELF-MGKTK 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50540432  236 EELVAFISEHRRPTLRKLKAEDMFETWEddlNGIHIVAF-AEEEDPDgfEFLEILKEVARDNTHNpdLSIVWIDPDNF 312
Cdd:PTZ00102 220 EELEEFVSTESFPLFAEINAENYRRYIS---SGKDLVWFcGTTEDYD--KYKSVVRKVARKLREK--YAFVWLDTEQF 290
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
79-371 7.17e-12

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 66.62  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    79 ELAAQVLEEKD--IGFGMVDSQKDAKVAKKLGLHEEGSVYIFKDDR--VIEFDGLPSADTLVEFLLDLLEDPVEIIDNAL 154
Cdd:TIGR01130  41 EKAADELKKKGppIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGEdsVSDYNGPRDADGIVKYMKKQSGPAVKEIETVA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   155 ELRAFDRmEEDIKLIGFFKSQESEHYLAFQEAAEQ-FQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPVTIP---D 230
Cdd:TIGR01130 121 DLEAFLA-DDDVVVIGFFKDLDSELNDTFLSVAEKlRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKvdgE 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   231 KPHSEEELVAFISEHRRPTLRKLKAEDMFETWEDDlNGIHIVAFAEEEDPDGFEFLEILKEVARDNThNPDLSIVWIDPD 310
Cdd:TIGR01130 200 MDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESG-PLVVLYYNVDESLDPFEELRNRFLEAAKKFR-GKFVNFAVADEE 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50540432   311 NFPLLIPYWEMtfKVDLFrPQIGVVNVTDAdsvwLEIPNDDELPSAEELENWIEDVLSGTV 371
Cdd:TIGR01130 278 DFGRELEYFGL--KAEKF-PAVAIQDLEGN----KKYPMDQEEFSSENLEAFVKDFLDGKL 331
 
Name Accession Description Interval E-value
Calsequestrin pfam01216
Calsequestrin;
23-372 0e+00

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 576.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    23 GLEFPRYDGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPPAAKELQKQLHLTELVLELAAQVLEEKDIGFGMVDSQKDAK 102
Cdd:pfam01216   1 GLDFPEYDGKDRVINLNAKNFKNVFKKYDVLALLYHEPPEDDKAAQKQFELEEIILELAAQVLEDKDIGFGLVDAEKDAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   103 VAKKLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLEDPVEIIDNALELRAFDRMEEDIKLIGFFKSQESEHYLA 182
Cdd:pfam01216  81 LAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   183 FQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPVTIPDKPHSEEELVAFISEHRRPTLRKLKAEDMFETW 262
Cdd:pfam01216 161 FEDAAEEFHPYIKFFATFDKGVAKKLSLKLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTLRKLKPEDMFETW 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   263 EDDLNGIHIVAFAEEEDPDGFEFLEILKEVARDNTHNPDLSIVWIDPDNFPLLIPYWEMTFKVDLFRPQIGVVNVTDADS 342
Cdd:pfam01216 241 EDDLDGIHIVAFAEEADPDGFEFLEILKAVAQDNTDNPDLSIIWIDPDDFPLLVAYWEKTFDIDLFAPQIGVVNVTDADS 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 50540432   343 VWLEIPNDDELPSAEELENWIEDVLSGTVN 372
Cdd:pfam01216 321 VWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
PDI_b'_Calsequestrin_C cd03074
Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold ...
248-367 4.29e-70

Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The C-terminal TRX-fold domain (or domain III) mediates back-to-back dimer interaction and also contriubutes to the front-to-front dimer interface, both of which are important features in the formation of calsequestrin polymers.


Pssm-ID: 239372  Cd Length: 120  Bit Score: 216.58  E-value: 4.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432 248 PTLRKLKAEDMFETWEDDLNGIHIVAFAEEEDPDGFEFLEILKEVARDNTHNPDLSIVWIDPDNFPLLIPYWEMTFKVDL 327
Cdd:cd03074   1 PTLRKLKPENMFETWEDDLDGIHIVAFAEEEDPDGYEFLEILKEVARDNTDNPDLSIIWIDPDDFPLLVPYWEKTFGIDL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50540432 328 FRPQIGVVNVTDADSVWLEIPNDDELPSAEELENWIEDVL 367
Cdd:cd03074  81 FRPQIGVVNVTDADSVWMEMDDDEDLPTAEELEDWIEDVL 120
PDI_b_Calsequestrin_N cd03065
PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major ...
25-144 2.35e-63

PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The N-terminal TRX-fold domain (or domain I) mediates front-to-front dimer interaction, an important feature in the formation of calsequestrin polymers.


Pssm-ID: 239363  Cd Length: 120  Bit Score: 199.20  E-value: 2.35e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432  25 EFPRYDGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPPAAKELQKQLHLTELVLELAAQVLEEKDIGFGMVDSQKDAKVA 104
Cdd:cd03065   1 DFPEYDGKDRVIDLNEKNYKQVLKKYDVLCLLYHEPVESDKEAQKQFQMEELVLELAAQVLEDKGIGFGLVDSKKDAKVA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50540432 105 KKLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLE 144
Cdd:cd03065  81 KKLGLDEEDSIYVFKDDEVIEYDGEFAADTLVEFLLDLIE 120
PDI_b_Calsequestrin_middle cd03066
PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major ...
146-247 1.15e-55

PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store.


Pssm-ID: 239364 [Multi-domain]  Cd Length: 102  Bit Score: 178.77  E-value: 1.15e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432 146 PVEIIDNALELRAFDRMEEDIKLIGFFKSQESEHYLAFQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEP 225
Cdd:cd03066   1 PVEIINSERELQAFENIEDDIKLIGYFKSEDSEHYKAFEEAAEEFHPYIKFFATFDSKVAKKLGLKMNEVDFYEPFMEEP 80
                        90       100
                ....*....|....*....|..
gi 50540432 226 VTIPDKPHSEEELVAFISEHRR 247
Cdd:cd03066  81 VTIPDKPYSEEELVDFVEEHKR 102
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
147-245 4.93e-18

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 78.53  E-value: 4.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432 147 VEIIDNALELRAFDRmEEDIKLIGFFKSQESEHYLAFQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPV 226
Cdd:cd02981   1 VKELTSKEELEKFLD-KDDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFGHTSDKEVAKKLKVKPGSVVLFKPFEEEPV 79
                        90
                ....*....|....*....
gi 50540432 227 TIPDKPHsEEELVAFISEH 245
Cdd:cd02981  80 EYDGEFT-EESLVEFIKDN 97
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
172-365 3.63e-16

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 76.25  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   172 FKSQESEHYLAFQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPVTIPDKPHSEEELVAFISEHRRPTLR 251
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLPLVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   252 KLKAEDMFETWEDDLNgIHIVAFAEEEDPDGFEFLEILKEVARDntHNPDLSIVWIDPDNFPLLIPYWEMTfKVDLfrPQ 331
Cdd:pfam13848  81 EFTPENAEELFEEGIP-PLLLLFLKKDDESTEEFKKALEKVAKK--FRGKINFALVDAKSFGRPLEYFGLS-ESDL--PV 154
                         170       180       190
                  ....*....|....*....|....*....|....
gi 50540432   332 IGVVNVTdaDSVWLEIPNDDelPSAEELENWIED 365
Cdd:pfam13848 155 IVIVDSF--SHMYKYFPSDE--FSPESLKEFIND 184
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
258-367 1.97e-14

Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5 and PDIR. PDI, ERp57, ERp72, P5 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive domains are implicated in substrate recognition with the b' domain serving as the primary substrate binding site. Only the b' domain is necessary for the binding of small peptide substrates. In addition to the b' domain, other domains are required for the binding of larger polypeptide substrates. The b' domain is also implicated in chaperone activity.


Pssm-ID: 239280 [Multi-domain]  Cd Length: 103  Bit Score: 68.84  E-value: 1.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432 258 MFETWED--DLNGIHIVAFAEEEDPDGFEFLEILKEVARDNTHNpdLSIVWIDPDNFPlliPYWEMTFKVDLFRPQIGVV 335
Cdd:cd02982   1 NAETFFNyeESGKPLLVLFYNKDDSESEELRERFKEVAKKFKGK--LLFVVVDADDFG---RHLEYFGLKEEDLPVIAII 75
                        90       100       110
                ....*....|....*....|....*....|..
gi 50540432 336 NVTDADSVWLeipnDDELPSAEELENWIEDVL 367
Cdd:cd02982  76 NLSDGKKYLM----PEEELTAESLEEFVEDFL 103
PTZ00102 PTZ00102
disulphide isomerase; Provisional
3-312 5.99e-12

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 67.08  E-value: 5.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    3 TIWILLLASMAFFTLASAKKGLefprydGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPPAakelqkqlHLTELVLEL-- 80
Cdd:PTZ00102   8 SSLFLLLILLAFAVFGSAEEHF------ISEHVTVLTDSTFDKFITENEIVLVKFYAPWCG--------HCKRLAPEYkk 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   81 AAQVLEEK--DIGFGMVDSQKDAKVAKKLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLEDPVEIIDNALElra 158
Cdd:PTZ00102  74 AAKMLKEKksEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASE--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432  159 fDRMEEDIKLIGF---FKSQESEHYLAFQEAAEQFQPFIKFFATFEKSVAKELTLKMNevdfyepfmEEPVTIPdKPHSE 235
Cdd:PTZ00102 151 -IKLIAKKIFVAFygeYTSKDSELYKKFEEVADKHREHAKFFVKKHEGKNKIYVLHKD---------EEGVELF-MGKTK 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50540432  236 EELVAFISEHRRPTLRKLKAEDMFETWEddlNGIHIVAF-AEEEDPDgfEFLEILKEVARDNTHNpdLSIVWIDPDNF 312
Cdd:PTZ00102 220 EELEEFVSTESFPLFAEINAENYRRYIS---SGKDLVWFcGTTEDYD--KYKSVVRKVARKLREK--YAFVWLDTEQF 290
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
79-371 7.17e-12

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 66.62  E-value: 7.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432    79 ELAAQVLEEKD--IGFGMVDSQKDAKVAKKLGLHEEGSVYIFKDDR--VIEFDGLPSADTLVEFLLDLLEDPVEIIDNAL 154
Cdd:TIGR01130  41 EKAADELKKKGppIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGEdsVSDYNGPRDADGIVKYMKKQSGPAVKEIETVA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   155 ELRAFDRmEEDIKLIGFFKSQESEHYLAFQEAAEQ-FQPFIKFFATFEKSVAKELTLKMNEVDFYEPFMEEPVTIP---D 230
Cdd:TIGR01130 121 DLEAFLA-DDDVVVIGFFKDLDSELNDTFLSVAEKlRDVYFFFAHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKvdgE 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432   231 KPHSEEELVAFISEHRRPTLRKLKAEDMFETWEDDlNGIHIVAFAEEEDPDGFEFLEILKEVARDNThNPDLSIVWIDPD 310
Cdd:TIGR01130 200 MDTDVSDLEKFIRAESLPLVGEFTQETAAKYFESG-PLVVLYYNVDESLDPFEELRNRFLEAAKKFR-GKFVNFAVADEE 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50540432   311 NFPLLIPYWEMtfKVDLFrPQIGVVNVTDAdsvwLEIPNDDELPSAEELENWIEDVLSGTV 371
Cdd:TIGR01130 278 DFGRELEYFGL--KAEKF-PAVAIQDLEGN----KKYPMDQEEFSSENLEAFVKDFLDGKL 331
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
35-141 1.91e-06

Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI, calsequestrin and other PDI-related proteins like ERp72, ERp57, ERp44 and PDIR. PDI, ERp57 (or ERp60), ERp72 and PDIR are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and one or more redox inactive TRX-like (b) domains. The molecular structure of PDI is abb'a'. Also included in this family is the PDI-related protein ERp27, which contains only redox-inactive TRX-like (b and b') domains. The redox inactive b domains are implicated in substrate recognition.


Pssm-ID: 239279  Cd Length: 97  Bit Score: 45.79  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432  35 VLDIDDKNYRKA-LKKYDMLCLFYHapppaaKELQKQLHLTelvLELAAQVLEEkDIGFGMVDsqkDAKVAKKLGLhEEG 113
Cdd:cd02981   1 VKELTSKEELEKfLDKDDVVVVGFF------KDEESEEYKT---FEKVAESLRD-DYGFGHTS---DKEVAKKLKV-KPG 66
                        90       100       110
                ....*....|....*....|....*....|
gi 50540432 114 SVYIFK--DDRVIEFDGLPSADTLVEFLLD 141
Cdd:cd02981  67 SVVLFKpfEEEPVEYDGEFTEESLVEFIKD 96
PDI_b_ERp72 cd03068
PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both ...
155-245 6.88e-06

PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both disulfide oxidase and reductase functions like PDI, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER and acting as isomerases to correct any non-native disulfide bonds. It also displays chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp72 contains three redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. Its molecular structure is a"abb'a', compared to the abb'a' structure of PDI. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. Similar to PDI, the b domain of ERp72 is likely involved in binding to substrates.


Pssm-ID: 239366  Cd Length: 107  Bit Score: 44.78  E-value: 6.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540432 155 ELRAFDRMEEDIKLIGFFKSQESEHYLAFQEAAEQFQPFIKFFATFEKSVAKELTLKMNEVDFYEP--FME--EP----V 226
Cdd:cd03068  10 QVQEFLRDGDDVIIIGVFSGEEDPAYQLYQDAANSLREDYKFHHTFDSEIFKSLKVSPGQLVVFQPekFQSkyEPkshvL 89
                        90
                ....*....|....*....
gi 50540432 227 TIPDKPhSEEELVAFISEH 245
Cdd:cd03068  90 NKKDST-SEDELKDFFKEH 107
 
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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