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Conserved domains on  [gi|119395727|ref|NP_001223|]
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calsequestrin-2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Calsequestrin super family cl37643
Calsequestrin;
22-371 0e+00

Calsequestrin;


The actual alignment was detected with superfamily member pfam01216:

Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 648.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727   22 GLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAK 101
Cdd:pfam01216   1 GLDFPEYDGKDRVINLNAKNFKNVFKKYDVLALLYHEPPEDDKAAQKQFELEEIILELAAQVLEDKDIGFGLVDAEKDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  102 LAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKA 181
Cdd:pfam01216  81 LAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  182 FEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETW 261
Cdd:pfam01216 161 FEDAAEEFHPYIKFFATFDKGVAKKLSLKLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTLRKLKPEDMFETW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  262 EDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADS 341
Cdd:pfam01216 241 EDDLDGIHIVAFAEEADPDGFEFLEILKAVAQDNTDNPDLSIIWIDPDDFPLLVAYWEKTFDIDLFAPQIGVVNVTDADS 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 119395727  342 VWMEIPDDDDLPTAEELEDWIEDVLSGKIN 371
Cdd:pfam01216 321 VWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
 
Name Accession Description Interval E-value
Calsequestrin pfam01216
Calsequestrin;
22-371 0e+00

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 648.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727   22 GLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAK 101
Cdd:pfam01216   1 GLDFPEYDGKDRVINLNAKNFKNVFKKYDVLALLYHEPPEDDKAAQKQFELEEIILELAAQVLEDKDIGFGLVDAEKDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  102 LAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKA 181
Cdd:pfam01216  81 LAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  182 FEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETW 261
Cdd:pfam01216 161 FEDAAEEFHPYIKFFATFDKGVAKKLSLKLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTLRKLKPEDMFETW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  262 EDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADS 341
Cdd:pfam01216 241 EDDLDGIHIVAFAEEADPDGFEFLEILKAVAQDNTDNPDLSIIWIDPDDFPLLVAYWEKTFDIDLFAPQIGVVNVTDADS 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 119395727  342 VWMEIPDDDDLPTAEELEDWIEDVLSGKIN 371
Cdd:pfam01216 321 VWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
PDI_b'_Calsequestrin_C cd03074
Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold ...
 247-366 2.26e-72

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: 221.97  E-value: 2.26e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 247 PTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDL 326
Cdd:cd03074    1 PTLRKLKPENMFETWEDDLDGIHIVAFAEEEDPDGYEFLEILKEVARDNTDNPDLSIIWIDPDDFPLLVPYWEKTFGIDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 119395727 327 FRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVL 366
Cdd:cd03074   81 FRPQIGVVNVTDADSVWMEMDDDEDLPTAEELEDWIEDVL 120
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 120-370 2.41e-10

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: 62.00  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  120 DRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDyIKLIGFFKSEDSEYYKAFEEAAE-HFQPYIKFFAT 198
Cdd:TIGR01130  87 DSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDD-VVVIGFFKDLDSELNDTFLSVAEkLRDVYFFFAHS 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  199 FDKGVAKKLSLKMNEVDFYEPF-MDEPIAIPNKPYT--EEELVEFVKEHQRPTLRRLRPEEMFETWEDDlNGIHIVAFAE 275
Cdd:TIGR01130 166 SDVAAFAKLGAFPDSVVLFKPKdEDEKFSKVDGEMDtdVSDLEKFIRAESLPLVGEFTQETAAKYFESG-PLVVLYYNVD 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  276 KSDPDGYEFLEILKQVARDNTDNpDLSILWIDPDDFPLLVAYWEktFKIDLFrPQIGVVNVTDAdsvwMEIPDDDDLPTA 355
Cdd:TIGR01130 245 ESLDPFEELRNRFLEAAKKFRGK-FVNFAVADEEDFGRELEYFG--LKAEKF-PAVAIQDLEGN----KKYPMDQEEFSS 316

                         250
                  ....*....|....*
gi 119395727  356 EELEDWIEDVLSGKI 370
Cdd:TIGR01130 317 ENLEAFVKDFLDGKL 331
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 113-241 1.23e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.05  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 113 SLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERiEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPY 192
Cdd:PTZ00102 109 TIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIKLIAK-KIFVAFYGEYTSKDSELYKKFEEVADKHREH 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119395727 193 IKFFATFDKGVAKKLSLKMNEvDFYEPFMdepiaipnkPYTEEELVEFV 241
Cdd:PTZ00102 188 AKFFVKKHEGKNKIYVLHKDE-EGVELFM---------GKTKEELEEFV 226
 
Name Accession Description Interval E-value
Calsequestrin pfam01216
Calsequestrin;
22-371 0e+00

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 648.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727   22 GLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAK 101
Cdd:pfam01216   1 GLDFPEYDGKDRVINLNAKNFKNVFKKYDVLALLYHEPPEDDKAAQKQFELEEIILELAAQVLEDKDIGFGLVDAEKDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  102 LAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKA 181
Cdd:pfam01216  81 LAKKLGFDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  182 FEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETW 261
Cdd:pfam01216 161 FEDAAEEFHPYIKFFATFDKGVAKKLSLKLNEIDFYEAFMDEPIAIPDKPNSEEEIVEFVEEHQRPTLRKLKPEDMFETW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  262 EDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADS 341
Cdd:pfam01216 241 EDDLDGIHIVAFAEEADPDGFEFLEILKAVAQDNTDNPDLSIIWIDPDDFPLLVAYWEKTFDIDLFAPQIGVVNVTDADS 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 119395727  342 VWMEIPDDDDLPTAEELEDWIEDVLSGKIN 371
Cdd:pfam01216 321 VWMEIDDDDDLPSAEELEDWIEDVLEGEIN 350
PDI_b'_Calsequestrin_C cd03074
Protein Disulfide Isomerase (PDIb') family, Calsequestrin subfamily, C-terminal TRX-fold ...
 247-366 2.26e-72

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: 221.97  E-value: 2.26e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 247 PTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDL 326
Cdd:cd03074    1 PTLRKLKPENMFETWEDDLDGIHIVAFAEEEDPDGYEFLEILKEVARDNTDNPDLSIIWIDPDDFPLLVPYWEKTFGIDL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 119395727 327 FRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVL 366
Cdd:cd03074   81 FRPQIGVVNVTDADSVWMEMDDDEDLPTAEELEDWIEDVL 120
PDI_b_Calsequestrin_middle cd03066
PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major ...
 145-246 1.70e-56

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: 180.70  E-value: 1.70e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 145 PVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEP 224
Cdd:cd03066    1 PVEIINSERELQAFENIEDDIKLIGYFKSEDSEHYKAFEEAAEEFHPYIKFFATFDSKVAKKLGLKMNEVDFYEPFMEEP 80

                         90       100
                 ....*....|....*....|..
gi 119395727 225 IAIPNKPYTEEELVEFVKEHQR 246
Cdd:cd03066   81 VTIPDKPYSEEELVDFVEEHKR 102
PDI_b_Calsequestrin_N cd03065
PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major ...
 24-143 5.83e-53

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: 172.23  E-value: 5.83e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  24 NFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLA 103
Cdd:cd03065    1 DFPEYDGKDRVIDLNEKNYKQVLKKYDVLCLLYHEPVESDKEAQKQFQMEELVLELAAQVLEDKGIGFGLVDSKKDAKVA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 119395727 104 KKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIE 143
Cdd:cd03065   81 KKLGLDEEDSIYVFKDDEVIEYDGEFAADTLVEFLLDLIE 120
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 146-244 8.83e-21

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: 86.24  E-value: 8.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 146 VEIISSKLEVQAFERiEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPI 225
Cdd:cd02981    1 VKELTSKEELEKFLD-KDDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFGHTSDKEVAKKLKVKPGSVVLFKPFEEEPV 79

                         90
                 ....*....|....*....
gi 119395727 226 AIPNKpYTEEELVEFVKEH 244
Cdd:cd02981   80 EYDGE-FTEESLVEFIKDN 97
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
171-364 6.05e-17

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 78.17  E-value: 6.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  171 FKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLR 250
Cdd:pfam13848   1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKEPAILLFRKFDEETVHYPGDSINFEDLKKFIQKNCLPLVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  251 RLRPEEMFETWEDDLNgIHIVAFAEKSDPDGYEFLEILKQVARDNTDNpdLSILWIDPDDFPLLVAYWEKTFKIdlfRPQ 330
Cdd:pfam13848  81 EFTPENAEELFEEGIP-PLLLLFLKKDDESTEEFKKALEKVAKKFRGK--INFALVDAKSFGRPLEYFGLSESD---LPV 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 119395727  331 IGVVNVTdaDSVWMEIPDDDdlPTAEELEDWIED 364
Cdd:pfam13848 155 IVIVDSF--SHMYKYFPSDE--FSPESLKEFIND 184
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 257-366 4.23e-15

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: 70.76  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 257 MFETWED--DLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNpdLSILWIDPDDFPllvAYWEKTFKIDLFRPQIGVV 334
Cdd:cd02982    1 NAETFFNyeESGKPLLVLFYNKDDSESEELRERFKEVAKKFKGK--LLFVVVDADDFG---RHLEYFGLKEEDLPVIAII 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119395727 335 NVTDADSVWMeipdDDDLPTAEELEDWIEDVL 366
Cdd:cd02982   76 NLSDGKKYLM----PEEELTAESLEEFVEDFL 103
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 120-370 2.41e-10

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: 62.00  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  120 DRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDyIKLIGFFKSEDSEYYKAFEEAAE-HFQPYIKFFAT 198
Cdd:TIGR01130  87 DSVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFLADDD-VVVIGFFKDLDSELNDTFLSVAEkLRDVYFFFAHS 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  199 FDKGVAKKLSLKMNEVDFYEPF-MDEPIAIPNKPYT--EEELVEFVKEHQRPTLRRLRPEEMFETWEDDlNGIHIVAFAE 275
Cdd:TIGR01130 166 SDVAAFAKLGAFPDSVVLFKPKdEDEKFSKVDGEMDtdVSDLEKFIRAESLPLVGEFTQETAAKYFESG-PLVVLYYNVD 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  276 KSDPDGYEFLEILKQVARDNTDNpDLSILWIDPDDFPLLVAYWEktFKIDLFrPQIGVVNVTDAdsvwMEIPDDDDLPTA 355
Cdd:TIGR01130 245 ESLDPFEELRNRFLEAAKKFRGK-FVNFAVADEEDFGRELEYFG--LKAEKF-PAVAIQDLEGN----KKYPMDQEEFSS 316

                         250
                  ....*....|....*
gi 119395727  356 EELEDWIEDVLSGKI 370
Cdd:TIGR01130 317 ENLEAFVKDFLDGKL 331
PDI_b_ERp72 cd03068
PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both ...
 145-244 5.92e-08

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: 50.56  E-value: 5.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 145 PVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEP--FMD 222
Cdd:cd03068    1 PSKQLQTLKQVQEFLRDGDDVIIIGVFSGEEDPAYQLYQDAANSLREDYKFHHTFDSEIFKSLKVSPGQLVVFQPekFQS 80

                         90       100
                 ....*....|....*....|....*..
gi 119395727 223 --EPIA-IPNKPY--TEEELVEFVKEH 244
Cdd:cd03068   81 kyEPKShVLNKKDstSEDELKDFFKEH 107
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 113-241 1.23e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 47.05  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727 113 SLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERiEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPY 192
Cdd:PTZ00102 109 TIKFFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIKLIAK-KIFVAFYGEYTSKDSELYKKFEEVADKHREH 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119395727 193 IKFFATFDKGVAKKLSLKMNEvDFYEPFMdepiaipnkPYTEEELVEFV 241
Cdd:PTZ00102 188 AKFFVKKHEGKNKIYVLHKDE-EGVELFM---------GKTKEELEEFV 226
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 38-140 8.40e-04

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: 38.47  E-value: 8.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395727  38 SEKNFKQVLKKYDLLCLYYHEPVSSDKVTqkqfqlkeiVLELVAQVLEHKaIGFVMVDAKKEAKLakklGFDEEGSLYIL 117
Cdd:cd02981    6 SKEELEKFLDKDDVVVVGFFKDEESEEYK---------TFEKVAESLRDD-YGFGHTSDKEVAKK----LKVKPGSVVLF 71

                         90       100
                 ....*....|....*....|....*
gi 119395727 118 K--GDRTIEFDGEFAADVLVEFLLD 140
Cdd:cd02981   72 KpfEEEPVEYDGEFTEESLVEFIKD 96
 
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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