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Conserved domains on  [gi|1564305953|gb|RXN04105|]
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disulfide-isomerase A4-like protein [Labeo rohita]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2286-2752 0e+00

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: 641.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2286 EATLVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2366 IFRKGK--AFDYNGPREKFGIVDYMSDQAGPPSKQVQTLKQVQELIrDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDY 2443
Cdd:TIGR01130   81 IFRNGEdsVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFL-ADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2444 KFM-HTFNNEVAKFLKASPGQVVMLQPEKFRSKYEPASHSLTlkdsTPASEVQEFFKKHILPLVGHRKQSNDAKRYTARP 2522
Cdd:TIGR01130  160 FFFaHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMD----TDVSDLEKFIRAESLPLVGEFTQETAAKYFESGP 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2523 LVVVYYGVDFSFDYrvaTQFWRSKVLEVAKDFP--EYTFAIADEEDYSDELKSLGLSESGEEVNVGILGEGGKKYAMEPE 2600
Cdd:TIGR01130  236 LVVLYYNVDESLDP---FEELRNRFLEAAKKFRgkFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2601 EFDSDVLRSFVMAFKKGKLKPIVKSQPIPKSNKGPVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKK 2680
Cdd:TIGR01130  313 EFSSENLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEK 392

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564305953 2681 YKN-EKNLVIAKMDATANDIPhdSYKAEGFPTIYFAPSNKKQNPVKFEGGkRDVEELSKFVEKHATKLSQKKD 2752
Cdd:TIGR01130  393 YKDaESDVVIAKMDATANDVP--PFEVEGFPTIKFVPAGKKSEPVPYDGD-RTLEDFSKFIAKHATFPLEGKA 462
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 2176-2277 3.63e-49

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


:

Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 170.55  E-value: 3.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2176 LTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKEnDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKG 2255
Cdd:TIGR01126    1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2256 -EPVDYDGDRSEQAIVERVKEVA 2277
Cdd:TIGR01126   80 sKPVDYEGGRDLEAIVEFVNEKS 102
PLAT super family cl00011
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1482-1598 1.44e-44

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


The actual alignment was detected with superfamily member cd01752:

Pssm-ID: 412108  Cd Length: 120  Bit Score: 157.82  E-value: 1.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1482 FLYAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTCNSRNTFILSSPESLGRVWKVHLWHDNGGSSPSW 1561
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1564305953 1562 YLSHVVVKDLVQGSCWFFLGQCWLAVDEGDGRVERSL 1598
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 402-621 2.84e-20

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


The actual alignment was detected with superfamily member pfam02010:

Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 96.80  E-value: 2.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  402 QCNISRGLLYRWTIYDMSG----QQLLLPHIDTGRQYiNLPKYLLHYGTYKAIAKVQITGSV-VYSNYSVLIEVIRSHPV 476
Cdd:pfam02010    7 GCFSAYTIDYLWSVFTVSSnlnlQTISSPKDLVLPQL-TIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIITVTVQPSPLV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  477 SVISEATNIFINRQSStiVTLDGRKSHDPDYPNNT---ISYSWSCRPVNTEESSCFNRNIV------------TTSAVLT 541
Cdd:pfam02010   86 AVIDGGSSRVVGYNQD--LTLDGSESYDPDVDPGSssgLTYLWSCRRSSSGDNPLLNNDPVcfsdqnegtllqSTSSSLT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  542 FPALALKSDFDlLKFTLTVYSGHRSSAS-NMFITVTSKPVSNVHMYCEHCQGNSVNWNEQFSVSA-FCEDCGLNAKSVTY 619
Cdd:pfam02010  164 IPASTLQANVT-YTFKLTVSKGSRNSAStTQTILVVDGNPPIIILSCISNCNRKNNPVDRLVLLAsTCLNCSSDLSDVTY 242


                   ..
gi 1564305953  620 YW 621
Cdd:pfam02010  243 RW 244
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 1826-1997 7.08e-16

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


The actual alignment was detected with superfamily member pfam20519:

Pssm-ID: 466668  Cd Length: 199  Bit Score: 78.62  E-value: 7.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1826 SFHSIQKHEDWWNWTTTTFLERLYDNANCHDKrvkNETDFSSPLSLIGSPVIRKIKSTyNSSCQILNLLGKNNIKCSDNH 1905
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKTPSGL---PGSFIAYESLLLGVPRLRQLRVR-NSSCLVHDKFVREINECHAGY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1906 TVE---KRHSLC----------------------------GKLGCYEGESVSVNLGKTRSEAIKSIKTLLDAGWMTPFTQ 1954
Cdd:pfam20519   77 SPPsedRKLYSAlpykpvhygskywfiytppgllmgydhwGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1564305953 1955 IVMIQFILYNGPSNLFTAVTILVEQTSTGALMPSASIQSTRLY 1997
Cdd:pfam20519  157 AVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 861-1050 1.15e-12

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


The actual alignment was detected with superfamily member pfam02010:

Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 72.92  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  861 VFESYTLTGLTSSDVTFKPFMLKPKSLYLLEVSAISEKRL-QGKSQLFFHTQAVPEGMSCQVQPNTGYEIHTHFSIFCSS 939
Cdd:pfam02010  258 QLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLvSGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTCQG 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  940 GKED---LVFE---YSFSVGNNVRKLLYEG-RDFQHYFSLPSGDPNDDYKVTIYIEIKNRFGAATKpCPVKVTVLPsfqr 1012
Cdd:pfam02010  338 WTDDdlpLTYQfgdISFREASEEWFLLYEGsSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATS-VSLTITVTP---- 412

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1564305953 1013 ssssQLKPDQELYMY-GVGNLTSLSKIGSNQDIVNYISL 1050
Cdd:pfam02010  413 ----PSSSDELLYFLlGTTSDLSALLQSGDPQQAAQLIL 447
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
 305-359 1.23e-09

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


:

Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 56.63  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564305953  305 NFTCRISSGTDVSYIWNFGDGTERNGSSTE-HHVYDRTGEYIVQVIMSNLVSSASL 359
Cdd:pfam00801   15 TFTATLADGSNVTYTWDFGDSPGTSGSGPTvTHTYLSPGTYTVTLTASNAVGSANA 70
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 219-417 1.18e-07

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 57.78  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  219 DIKFVAVTEGPDPLYFYWQFGDGPEIKTTSRIYK--KRYRLPDKYSITVSVSNGLtSISSDVYLVRIQRAVqpnrLLYSS 296
Cdd:TIGR00864 1358 EAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEvtFIYNDPGCYLVTVAASNNI-SAANDSALIEVLEPV----GATSF 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  297 SVLLHSSVNFTCR-------ISSGTDVSYIWNFGDGTERNGSSTEhHVYDRTGEYIVQVIMSNLVSSASLTGHIFVVEEs 369
Cdd:TIGR00864 1433 KHNGSHGNNLELGqpylfsaFGRARNASYLWDFGDGGLLEGPEIL-HAFNSPGDFNIRLAAANEVGKNEATLNVAVKAR- 1510

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1564305953  370 cqpppVKNMGPNKIQVwqyqTVRL--AVTFEAHIQCNISrgLLYRWTIYD 417
Cdd:TIGR00864 1511 -----VRGLTINASLT----NVPLngSVHFEAHLDAGDD--VRFSWILCD 1549
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2286-2752 0e+00

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: 641.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2286 EATLVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2366 IFRKGK--AFDYNGPREKFGIVDYMSDQAGPPSKQVQTLKQVQELIrDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDY 2443
Cdd:TIGR01130   81 IFRNGEdsVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFL-ADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2444 KFM-HTFNNEVAKFLKASPGQVVMLQPEKFRSKYEPASHSLTlkdsTPASEVQEFFKKHILPLVGHRKQSNDAKRYTARP 2522
Cdd:TIGR01130  160 FFFaHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMD----TDVSDLEKFIRAESLPLVGEFTQETAAKYFESGP 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2523 LVVVYYGVDFSFDYrvaTQFWRSKVLEVAKDFP--EYTFAIADEEDYSDELKSLGLSESGEEVNVGILGEGGKKYAMEPE 2600
Cdd:TIGR01130  236 LVVLYYNVDESLDP---FEELRNRFLEAAKKFRgkFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2601 EFDSDVLRSFVMAFKKGKLKPIVKSQPIPKSNKGPVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKK 2680
Cdd:TIGR01130  313 EFSSENLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEK 392

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564305953 2681 YKN-EKNLVIAKMDATANDIPhdSYKAEGFPTIYFAPSNKKQNPVKFEGGkRDVEELSKFVEKHATKLSQKKD 2752
Cdd:TIGR01130  393 YKDaESDVVIAKMDATANDVP--PFEVEGFPTIKFVPAGKKSEPVPYDGD-RTLEDFSKFIAKHATFPLEGKA 462
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2286-2754 4.61e-105

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 346.35  E-value: 4.61e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2286 EATLVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:PTZ00102    32 EHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIK 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2366 IFRKGKAFDYNGPREKFGIVDYMSDQAGPPSKQVQTLKQVQeLIRDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKF 2445
Cdd:PTZ00102   112 FFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIK-LIAKKIFVAFYGEYTSKDSELYKKFEEVADKHREHAKF 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2446 MHTFNNEVAKFLkaspgqvVMLQPEKFRSKYEPAShsltlkdstpASEVQEFFKKHILPLVGHRKQSNdAKRYTARPLVV 2525
Cdd:PTZ00102   191 FVKKHEGKNKIY-------VLHKDEEGVELFMGKT----------KEELEEFVSTESFPLFAEINAEN-YRRYISSGKDL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2526 VYY-GVDFSFDYrvatqfWRSKVLEVAKDFPE-YTFAIADEEDYSDELK-SLGLSE---SGEEVNVGilgeggkKYAMEP 2599
Cdd:PTZ00102   253 VWFcGTTEDYDK------YKSVVRKVARKLREkYAFVWLDTEQFGSHAKeHLLIEEfpgLAYQSPAG-------RYLLPP 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2600 --EEFDS-DVLRSFVMAFKKGKLKPIVKSQPIPKSNKGPVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTA 2676
Cdd:PTZ00102   320 akESFDSvEALIEFFKDVEAGKVEKSIKSEPIPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2677 LGKKYKNEKNLVIAKMDATANDIPHDSYKAEGFPTIYFAPSNKKqNPVKFEgGKRDVEELSKFVEKHATKL--SQKKDEL 2754
Cdd:PTZ00102   400 LGEKYKDNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGER-TPIPYE-GERTVEGFKEFVNKHATNPfeDDTHEEL 477
PDI_b_ERp72 cd03068
PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both ...
 2395-2501 1.05e-57

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: 195.01  E-value: 1.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2395 PSKQVQTLKQVQELIRDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKFMHTFNNEVAKFLKASPGQVVMLQPEKFRS 2474
Cdd:cd03068      1 PSKQLQTLKQVQEFLRDGDDVIIIGVFSGEEDPAYQLYQDAANSLREDYKFHHTFDSEIFKSLKVSPGQLVVFQPEKFQS 80

                           90       100
                   ....*....|....*....|....*..
gi 1564305953 2475 KYEPASHSLTLKDSTPASEVQEFFKKH 2501
Cdd:cd03068     81 KYEPKSHVLNKKDSTSEDELKDFFKEH 107
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 2176-2277 3.63e-49

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 170.55  E-value: 3.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2176 LTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKEnDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKG 2255
Cdd:TIGR01126    1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2256 -EPVDYDGDRSEQAIVERVKEVA 2277
Cdd:TIGR01126   80 sKPVDYEGGRDLEAIVEFVNEKS 102
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1482-1598 1.44e-44

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 157.82  E-value: 1.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1482 FLYAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTCNSRNTFILSSPESLGRVWKVHLWHDNGGSSPSW 1561
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1564305953 1562 YLSHVVVKDLVQGSCWFFLGQCWLAVDEGDGRVERSL 1598
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 2174-2271 2.03e-39

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; 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 and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 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 usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 142.36  E-value: 2.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2174 LVLTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKeNDPPIPVAKVDATKASALGSRFEVSGYPTIKILK 2253
Cdd:cd02961      1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELK-GDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                           90       100
                   ....*....|....*....|
gi 1564305953 2254 KG--EPVDYDGDRSEQAIVE 2271
Cdd:cd02961     80 NGskEPVKYEGPRTLESLVE 99
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2288-2390 3.83e-38

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 138.90  E-value: 3.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2288 TLVLTKDNFDDVVNNAD-IILVEFYAPWCGHCKRLAPEYEKAAKELSNrtpPIPLAKVDATAESELATRFGVSGYPTLKI 2366
Cdd:pfam00085    2 VVVLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                           90       100
                   ....*....|....*....|....*
gi 1564305953 2367 FRKGK-AFDYNGPREKFGIVDYMSD 2390
Cdd:pfam00085   79 FKNGQpVDDYVGARPKDALAAFLKA 103
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2172-2275 2.36e-34

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 128.12  E-value: 2.36e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2172 GVLVLTDENFDTF-MEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVAKVDATKASALGSRFEVSGYPTIK 2250
Cdd:pfam00085    1 VVVVLTDANFDEVvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN---VVFAKVDVDENPDLASKYGVRGYPTLI 77

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2251 ILKKGEPVD-YDGDRSEQAIVERVKE 2275
Cdd:pfam00085   78 FFKNGQPVDdYVGARPKDALAAFLKA 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2173-2276 2.76e-26

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 105.29  E-value: 2.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDT-FMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKI 2251
Cdd:COG3118      2 VVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELA---AEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2252 LKKGEPVD-YDGDRSEQAIVERVKEV 2276
Cdd:COG3118     79 FKDGQPVDrFVGALPKEQLREFLDKV 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2287-2374 2.29e-25

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 102.59  E-value: 2.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2287 ATLVLTKDNFD-DVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:COG3118      1 AVVELTDENFEeEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK---VKFVKVDVDENPELAAQFGVRSIPTLL 77


                   ....*....
gi 1564305953 2366 IFRKGKAFD 2374
Cdd:COG3118     78 LFKDGQPVD 86
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 2166-2303 6.72e-25

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 105.48  E-value: 6.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2166 DSEEENGVLVLTDENFDTFMEGKD-----TVLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVAKVDATKASALGSR 2240
Cdd:PTZ00443    25 DAEDANALVLLNDKNFEKLTQASTgattgPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKR 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564305953 2241 FEVSGYPTIKILKKGEPVDYD-GDRSeqaiVERVKEVAQPDWK-------PPPEATLVLTKDNFDDVVNNA 2303
Cdd:PTZ00443   102 FAIKGYPTLLLFDKGKMYQYEgGDRS----TEKLAAFALGDFKkalgapvPAPLSFFALTIDFFVSGTNEA 168
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 402-621 2.84e-20

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 96.80  E-value: 2.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  402 QCNISRGLLYRWTIYDMSG----QQLLLPHIDTGRQYiNLPKYLLHYGTYKAIAKVQITGSV-VYSNYSVLIEVIRSHPV 476
Cdd:pfam02010    7 GCFSAYTIDYLWSVFTVSSnlnlQTISSPKDLVLPQL-TIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIITVTVQPSPLV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  477 SVISEATNIFINRQSStiVTLDGRKSHDPDYPNNT---ISYSWSCRPVNTEESSCFNRNIV------------TTSAVLT 541
Cdd:pfam02010   86 AVIDGGSSRVVGYNQD--LTLDGSESYDPDVDPGSssgLTYLWSCRRSSSGDNPLLNNDPVcfsdqnegtllqSTSSSLT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  542 FPALALKSDFDlLKFTLTVYSGHRSSAS-NMFITVTSKPVSNVHMYCEHCQGNSVNWNEQFSVSA-FCEDCGLNAKSVTY 619
Cdd:pfam02010  164 IPASTLQANVT-YTFKLTVSKGSRNSAStTQTILVVDGNPPIIILSCISNCNRKNNPVDRLVLLAsTCLNCSSDLSDVTY 242


                   ..
gi 1564305953  620 YW 621
Cdd:pfam02010  243 RW 244
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 316-610 1.29e-17

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 90.91  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  316 VSYIWNFGDGT--ERNGSSTEHHVYDRTGEYIVQVIMSNLVSSASLTGHIFVVEESCQPPPVKNMGPNKIQVWQYQTVRL 393
Cdd:TIGR00864 2073 MACHWDFGDGSagQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLL 2152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  394 avtfEAHIQCN--ISRGLLYRWTIYD--------------MSGQQLLLP------HIDTGRQYINLPKYLLHYGTYKAIA 451
Cdd:TIGR00864 2153 ----EAHVDLKdcLRYGAEYLWEILRaascdndghfargaLNGATRSFPviplpaEVDVQRLQLSLPKLALAAGHYCFVF 2228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  452 KVQITGSVVYSNYSVLIEVIRSHPVSVISEATNIFINRQSStiVTLDGRKSHDPDY-PNNT--ISYSWSCRPVNTEESSC 528
Cdd:TIGR00864 2229 SLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNLdDDDQslLHFHWACQASSKGEAGC 2306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  529 --FNRNIVTTSAVLTFPALALKSDFDlLKFTLTVY-SGHRSSASNMFITVTSKPVSNVHMYCEHCQGNS---VNWNEQFS 602
Cdd:TIGR00864 2307 caLNFGLGGKGPTLGIPGEELAAGIE-YTFKLSIGkAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQAlyeVSQNSYVY 2385


                   ....*...
gi 1564305953  603 VSAFCEDC 610
Cdd:TIGR00864 2386 LEGRCLNC 2393
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 1826-1997 7.08e-16

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 78.62  E-value: 7.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1826 SFHSIQKHEDWWNWTTTTFLERLYDNANCHDKrvkNETDFSSPLSLIGSPVIRKIKSTyNSSCQILNLLGKNNIKCSDNH 1905
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKTPSGL---PGSFIAYESLLLGVPRLRQLRVR-NSSCLVHDKFVREINECHAGY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1906 TVE---KRHSLC----------------------------GKLGCYEGESVSVNLGKTRSEAIKSIKTLLDAGWMTPFTQ 1954
Cdd:pfam20519   77 SPPsedRKLYSAlpykpvhygskywfiytppgllmgydhwGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1564305953 1955 IVMIQFILYNGPSNLFTAVTILVEQTSTGALMPSASIQSTRLY 1997
Cdd:pfam20519  157 AVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1484-1599 7.44e-13

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 67.07  E-value: 7.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1484 YAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTcNSRNTFILSSPESLGRVWKVHLWHDNGGSSPSWYL 1563
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFER-GAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1564305953 1564 SHVVV-KDLVQGSCWFFLGQCWLAVDEgDGRVERSLV 1599
Cdd:pfam01477   80 KSITVeVPGETGGKYTFPCNSWVYGSK-KYKETRVFF 115
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 861-1050 1.15e-12

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 72.92  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  861 VFESYTLTGLTSSDVTFKPFMLKPKSLYLLEVSAISEKRL-QGKSQLFFHTQAVPEGMSCQVQPNTGYEIHTHFSIFCSS 939
Cdd:pfam02010  258 QLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLvSGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTCQG 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  940 GKED---LVFE---YSFSVGNNVRKLLYEG-RDFQHYFSLPSGDPNDDYKVTIYIEIKNRFGAATKpCPVKVTVLPsfqr 1012
Cdd:pfam02010  338 WTDDdlpLTYQfgdISFREASEEWFLLYEGsSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATS-VSLTITVTP---- 412

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1564305953 1013 ssssQLKPDQELYMY-GVGNLTSLSKIGSNQDIVNYISL 1050
Cdd:pfam02010  413 ----PSSSDELLYFLlGTTSDLSALLQSGDPQQAAQLIL 447
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
 305-359 1.23e-09

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 56.63  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564305953  305 NFTCRISSGTDVSYIWNFGDGTERNGSSTE-HHVYDRTGEYIVQVIMSNLVSSASL 359
Cdd:pfam00801   15 TFTATLADGSNVTYTWDFGDSPGTSGSGPTvTHTYLSPGTYTVTLTASNAVGSANA 70
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
 312-366 2.05e-08

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 53.22  E-value: 2.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1564305953   312 SGTDVSYIWNFGDGTERNGSSTEhHVYDRTGEYIVQVIMSNLVSSASLTGHIFVV 366
Cdd:smart00089   26 DGSIVSYTWDFGDGTSSTGPTVT-HTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 219-417 1.18e-07

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 57.78  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  219 DIKFVAVTEGPDPLYFYWQFGDGPEIKTTSRIYK--KRYRLPDKYSITVSVSNGLtSISSDVYLVRIQRAVqpnrLLYSS 296
Cdd:TIGR00864 1358 EAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEvtFIYNDPGCYLVTVAASNNI-SAANDSALIEVLEPV----GATSF 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  297 SVLLHSSVNFTCR-------ISSGTDVSYIWNFGDGTERNGSSTEhHVYDRTGEYIVQVIMSNLVSSASLTGHIFVVEEs 369
Cdd:TIGR00864 1433 KHNGSHGNNLELGqpylfsaFGRARNASYLWDFGDGGLLEGPEIL-HAFNSPGDFNIRLAAANEVGKNEATLNVAVKAR- 1510

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1564305953  370 cqpppVKNMGPNKIQVwqyqTVRL--AVTFEAHIQCNISrgLLYRWTIYD 417
Cdd:TIGR00864 1511 -----VRGLTINASLT----NVPLngSVHFEAHLDAGDD--VRFSWILCD 1549
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
 215-276 4.78e-07

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 49.31  E-value: 4.78e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564305953  215 ATETDIKFVAVTEGPDPLYFYWQFGDGPEIKTTSRIYKKRYRLPDKYSITVSVSNGLTSISS 276
Cdd:pfam00801    9 AAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1484-1578 6.89e-07

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 49.95  E-value: 6.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  1484 YAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTCNSRNTFILSSPESLGRVWKVHLWHDNggSSPSWYL 1563
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEH--RHPEWFL 80

                            90
                    ....*....|....*.
gi 1564305953  1564 SHVVVKDLV-QGSCWF 1578
Cdd:smart00308   81 KSITVKDLPtGGKYHF 96
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 311-366 2.16e-05

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 44.79  E-value: 2.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953  311 SSGTDVSYIWNFGDGTER-NGSSTEHHVYDRTGEYIVQVIMSNLVSSASLTGHIFVV 366
Cdd:cd00146     25 SGGSIVSYKWDFGDGEVSsSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
311-583 4.65e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 48.13  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  311 SSGTDVSYIWNFGDGTerngSSTEH---HVYDRTGEYIVQVIMSNLV-SSASLTGHIFVVEESCQPPPVKNMG-PNKIQV 385
Cdd:COG3291     20 SSGNATSYEWDFGDGT----TSTEAnpsHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTtVTTLAN 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  386 WQYQTVRLAVTFEAHIQCNISRGLLYRWTIYDMSGQQlllpHIDTGRQYINLPKYLLHYGTYKAIAKVQITGSVVYSNYS 465
Cdd:COG3291     96 TANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGT----TTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTS 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  466 VLIEVIRSHPVSVISEATNIFINRQSSTIVTLDGRKSHDPDYPNNTISYSWSCRPVNTEESSCFNRNIVTTSAVLTFPAL 545
Cdd:COG3291    172 ASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTV 251

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1564305953  546 ALKSDFDLLKFTLTVYSGHRSSASNMFITVTSKPVSNV 583
Cdd:COG3291    252 TTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLG 289
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 208-283 4.45e-03

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 38.25  E-value: 4.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953  208 FSDTRAYATETDIKFVA-VTEGPDPLYFYWQFGDGPEIKTTSRIYKKRYRLPDKYSITVSVSNGLTSISSDVYLVRI 283
Cdd:cd00146      5 VSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
 
Name Accession Description Interval E-value
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2286-2752 0e+00

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: 641.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2286 EATLVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:TIGR01130    1 EDVLVLTKDNFDDFIKSHEFVLVEFYAPWCGHCKSLAPEYEKAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2366 IFRKGK--AFDYNGPREKFGIVDYMSDQAGPPSKQVQTLKQVQELIrDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDY 2443
Cdd:TIGR01130   81 IFRNGEdsVSDYNGPRDADGIVKYMKKQSGPAVKEIETVADLEAFL-ADDDVVVIGFFKDLDSELNDTFLSVAEKLRDVY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2444 KFM-HTFNNEVAKFLKASPGQVVMLQPEKFRSKYEPASHSLTlkdsTPASEVQEFFKKHILPLVGHRKQSNDAKRYTARP 2522
Cdd:TIGR01130  160 FFFaHSSDVAAFAKLGAFPDSVVLFKPKDEDEKFSKVDGEMD----TDVSDLEKFIRAESLPLVGEFTQETAAKYFESGP 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2523 LVVVYYGVDFSFDYrvaTQFWRSKVLEVAKDFP--EYTFAIADEEDYSDELKSLGLSESGEEVNVGILGEGGKKYAMEPE 2600
Cdd:TIGR01130  236 LVVLYYNVDESLDP---FEELRNRFLEAAKKFRgkFVNFAVADEEDFGRELEYFGLKAEKFPAVAIQDLEGNKKYPMDQE 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2601 EFDSDVLRSFVMAFKKGKLKPIVKSQPIPKSNKGPVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKK 2680
Cdd:TIGR01130  313 EFSSENLEAFVKDFLDGKLKPYLKSEPIPEDDEGPVKVLVGKNFDEIVLDETKDVLVEFYAPWCGHCKNLAPIYEELAEK 392

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564305953 2681 YKN-EKNLVIAKMDATANDIPhdSYKAEGFPTIYFAPSNKKQNPVKFEGGkRDVEELSKFVEKHATKLSQKKD 2752
Cdd:TIGR01130  393 YKDaESDVVIAKMDATANDVP--PFEVEGFPTIKFVPAGKKSEPVPYDGD-RTLEDFSKFIAKHATFPLEGKA 462
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2286-2754 4.61e-105

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 346.35  E-value: 4.61e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2286 EATLVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:PTZ00102    32 EHVTVLTDSTFDKFITENEIVLVKFYAPWCGHCKRLAPEYKKAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIK 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2366 IFRKGKAFDYNGPREKFGIVDYMSDQAGPPSKQVQTLKQVQeLIRDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKF 2445
Cdd:PTZ00102   112 FFNKGNPVNYSGGRTADGIVSWIKKLTGPAVTEVESASEIK-LIAKKIFVAFYGEYTSKDSELYKKFEEVADKHREHAKF 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2446 MHTFNNEVAKFLkaspgqvVMLQPEKFRSKYEPAShsltlkdstpASEVQEFFKKHILPLVGHRKQSNdAKRYTARPLVV 2525
Cdd:PTZ00102   191 FVKKHEGKNKIY-------VLHKDEEGVELFMGKT----------KEELEEFVSTESFPLFAEINAEN-YRRYISSGKDL 252

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2526 VYY-GVDFSFDYrvatqfWRSKVLEVAKDFPE-YTFAIADEEDYSDELK-SLGLSE---SGEEVNVGilgeggkKYAMEP 2599
Cdd:PTZ00102   253 VWFcGTTEDYDK------YKSVVRKVARKLREkYAFVWLDTEQFGSHAKeHLLIEEfpgLAYQSPAG-------RYLLPP 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2600 --EEFDS-DVLRSFVMAFKKGKLKPIVKSQPIPKSNKGPVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTA 2676
Cdd:PTZ00102   320 akESFDSvEALIEFFKDVEAGKVEKSIKSEPIPEEQDGPVKVVVGNTFEEIVFKSDKDVLLEIYAPWCGHCKNLEPVYNE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2677 LGKKYKNEKNLVIAKMDATANDIPHDSYKAEGFPTIYFAPSNKKqNPVKFEgGKRDVEELSKFVEKHATKL--SQKKDEL 2754
Cdd:PTZ00102   400 LGEKYKDNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGER-TPIPYE-GERTVEGFKEFVNKHATNPfeDDTHEEL 477
PDI_b_ERp72 cd03068
PDIb family, ERp72 subfamily, first redox inactive TRX-like domain b; ERp72 exhibits both ...
 2395-2501 1.05e-57

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: 195.01  E-value: 1.05e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2395 PSKQVQTLKQVQELIRDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKFMHTFNNEVAKFLKASPGQVVMLQPEKFRS 2474
Cdd:cd03068      1 PSKQLQTLKQVQEFLRDGDDVIIIGVFSGEEDPAYQLYQDAANSLREDYKFHHTFDSEIFKSLKVSPGQLVVFQPEKFQS 80

                           90       100
                   ....*....|....*....|....*..
gi 1564305953 2475 KYEPASHSLTLKDSTPASEVQEFFKKH 2501
Cdd:cd03068     81 KYEPKSHVLNKKDSTSEDELKDFFKEH 107
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 2635-2740 1.71e-54

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 185.84  E-value: 1.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2635 PVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDATANDIPhDSYKAEGFPTIYF 2714
Cdd:cd02995      1 PVKVVVGKNFDEVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVVIAKMDATANDVP-SEFVVDGFPTILF 79

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2715 APSNKKQNPVKFEGGkRDVEELSKFV 2740
Cdd:cd02995     80 FPAGDKSNPIKYEGD-RTLEDLIKFI 104
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 2291-2392 1.09e-49

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 172.09  E-value: 1.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNrTPPIPLAKVDATAESELATRFGVSGYPTLKIFRKG 2370
Cdd:TIGR01126    1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2371 KA-FDYNGPREKFGIVDYMSDQA 2392
Cdd:TIGR01126   80 SKpVDYEGGRDLEAIVEFVNEKS 102
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 2176-2277 3.63e-49

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 170.55  E-value: 3.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2176 LTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKEnDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKG 2255
Cdd:TIGR01126    1 LTASNFDEIVLSNKDVLVEFYAPWCGHCKNLAPEYEKLAKELKK-DPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2256 -EPVDYDGDRSEQAIVERVKEVA 2277
Cdd:TIGR01126   80 sKPVDYEGGRDLEAIVEFVNEKS 102
PDI_b'_ERp72_ERp57 cd03073
PDIb' family, ERp72 and ERp57 subfamily, second redox inactive TRX-like domain b'; ERp72 and ...
 2506-2615 1.40e-46

PDIb' family, ERp72 and ERp57 subfamily, second redox inactive TRX-like domain b'; ERp72 and ER57 are involved in oxidative protein folding in the ER, like PDI. They exhibit both disulfide oxidase and reductase functions, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides and acting as isomerases to correct any non-native disulfide bonds. They also display chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. ERp57 contains two redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. It shares the same domain arrangement of abb'a' as PDI, but lacks the C-terminal acid-rich region (c domain) that is present in PDI. ERp72 contains one additional redox-active TRX (a) domain at the N-terminus with a molecular structure of a"abb'a'. ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. The b' domain of ERp57 is the primary binding site and is adapted for ER lectin association. Similarly, the b' domain of ERp72 is likely involved in substrate recognition.


Pssm-ID: 239371  Cd Length: 111  Bit Score: 163.28  E-value: 1.40e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2506 VGHRKQSNDAKRyTARPLVVVYYGVDFSFDYrVATQFWRSKVLEVAKDFP--EYTFAIADEEDYSDELKSLGLSES-GEE 2582
Cdd:cd03073      1 VGHRTKDNRAQF-TKKPLVVAYYNVDYSKNP-KGTNYWRNRVLKVAKDFPdrKLNFAVADKEDFSHELEEFGLDFSgGEK 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564305953 2583 VNVGILGEGGKKYAMEPEEFDSDVLRSFVMAFK 2615
Cdd:cd03073     79 PVVAIRTAKGKKYVMEEEFSDVDALEEFLEDFF 111
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 1482-1598 1.44e-44

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 157.82  E-value: 1.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1482 FLYAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTCNSRNTFILSSPESLGRVWKVHLWHDNGGSSPSW 1561
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1564305953 1562 YLSHVVVKDLVQGSCWFFLGQCWLAVDEGDGRVERSL 1598
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
pdi_dom TIGR01126
protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein ...
 2639-2744 4.02e-42

protein disulfide-isomerase domain; This model describes a domain of eukaryotic protein disulfide isomerases, generally found in two copies. The high cutoff for total score reflects the expectation of finding both copies. The domain is similar to thioredoxin but the redox-active disulfide region motif is APWCGHCK. [Protein fate, Protein folding and stabilization]


Pssm-ID: 273454 [Multi-domain]  Cd Length: 102  Bit Score: 150.13  E-value: 4.02e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2639 VVGKTFDEIVMDtKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDATANDIPHDSYKAEGFPTIYFAPSN 2718
Cdd:TIGR01126    1 LTASNFDEIVLS-NKDVLVEFYAPWCGHCKNLAPEYEKLAKELKKDPKIVLAKVDATAEKDLASRFGVSGFPTIKFFPKG 79

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2719 KKqnPVKFEGGkRDVEELSKFVEKHA 2744
Cdd:TIGR01126   80 SK--PVDYEGG-RDLEAIVEFVNEKS 102
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 2289-2388 1.28e-41

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; 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 and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 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 usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 148.91  E-value: 1.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2289 LVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtPPIPLAKVDATAESELATRFGVSGYPTLKIFR 2368
Cdd:cd02961      1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGD-GKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                           90       100
                   ....*....|....*....|..
gi 1564305953 2369 KG--KAFDYNGPREKFGIVDYM 2388
Cdd:cd02961     80 NGskEPVKYEGPRTLESLVEFI 101
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 2174-2271 2.03e-39

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; 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 and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 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 usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 142.36  E-value: 2.03e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2174 LVLTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKeNDPPIPVAKVDATKASALGSRFEVSGYPTIKILK 2253
Cdd:cd02961      1 VELTDDNFDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELK-GDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFP 79

                           90       100
                   ....*....|....*....|
gi 1564305953 2254 KG--EPVDYDGDRSEQAIVE 2271
Cdd:cd02961     80 NGskEPVKYEGPRTLESLVE 99
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 2172-2271 5.15e-39

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 141.62  E-value: 5.15e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2172 GVLVLTDENFDT-FMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKeNDPPIPVAKVDATKA-SALGSRFEVSGYPTI 2249
Cdd:cd02998      1 NVVELTDSNFDKvVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFA-NEDDVVIAKVDADEAnKDLAKKYGVSGFPTL 79

                           90       100
                   ....*....|....*....|....
gi 1564305953 2250 KILKKG--EPVDYDGDRSEQAIVE 2271
Cdd:cd02998     80 KFFPKGstEPVKYEGGRDLEDLVK 103
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 2636-2740 2.25e-38

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 139.69  E-value: 2.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2636 VKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDATAndiPHDS----YKAEGFPT 2711
Cdd:cd02998      2 VVELTDSNFDKVVGDDKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANEDDVVIAKVDADE---ANKDlakkYGVSGFPT 78

                           90       100
                   ....*....|....*....|....*....
gi 1564305953 2712 IYFAPSNKKqNPVKFEGGkRDVEELSKFV 2740
Cdd:cd02998     79 LKFFPKGST-EPVKYEGG-RDLEDLVKFV 105
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2288-2390 3.83e-38

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 138.90  E-value: 3.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2288 TLVLTKDNFDDVVNNAD-IILVEFYAPWCGHCKRLAPEYEKAAKELSNrtpPIPLAKVDATAESELATRFGVSGYPTLKI 2366
Cdd:pfam00085    2 VVVLTDANFDEVVQKSSkPVLVDFYAPWCGPCKMLAPEYEELAQEYKG---NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                           90       100
                   ....*....|....*....|....*
gi 1564305953 2367 FRKGK-AFDYNGPREKFGIVDYMSD 2390
Cdd:pfam00085   79 FKNGQpVDDYVGARPKDALAAFLKA 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 2291-2389 3.31e-37

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 136.26  E-value: 3.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDD-VVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLKIFRK 2369
Cdd:cd03001      5 LTDSNFDKkVLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI---VKVGAVDADVHQSLAQQYGVRGFPTIKVFGA 81

                           90       100
                   ....*....|....*....|..
gi 1564305953 2370 GK--AFDYNGPREKFGIVDYMS 2389
Cdd:cd03001     82 GKnsPQDYQGGRTAKAIVSAAL 103
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 2172-2273 2.13e-36

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 133.95  E-value: 2.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2172 GVLVLTDENFDTF-MEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVAKVDATKASALGSRFEVSGYPTIK 2250
Cdd:cd03001      1 DVVELTDSNFDKKvLNSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGI---VKVGAVDADVHQSLAQQYGVRGFPTIK 77

                           90       100
                   ....*....|....*....|....*
gi 1564305953 2251 ILKKG--EPVDYDGDRSEQAIVERV 2273
Cdd:cd03001     78 VFGAGknSPQDYQGGRTAKAIVSAA 102
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2172-2275 2.36e-34

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 128.12  E-value: 2.36e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2172 GVLVLTDENFDTF-MEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVAKVDATKASALGSRFEVSGYPTIK 2250
Cdd:pfam00085    1 VVVVLTDANFDEVvQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN---VVFAKVDVDENPDLASKYGVRGYPTLI 77

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2251 ILKKGEPVD-YDGDRSEQAIVERVKE 2275
Cdd:pfam00085   78 FFKNGQPVDdYVGARPKDALAAFLKA 103
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 2289-2380 6.31e-34

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 126.98  E-value: 6.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2289 LVLTKDNFDDVVNN-ADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtPPIPLAKVDATAE-SELATRFGVSGYPTLKI 2366
Cdd:cd02998      3 VELTDSNFDKVVGDdKKDVLVEFYAPWCGHCKNLAPEYEKLAAVFANE-DDVVIAKVDADEAnKDLAKKYGVSGFPTLKF 81

                           90
                   ....*....|....*.
gi 1564305953 2367 FRKG--KAFDYNGPRE 2380
Cdd:cd02998     82 FPKGstEPVKYEGGRD 97
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 2637-2740 2.87e-33

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; 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 and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 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 usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 125.03  E-value: 2.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2637 KVVVGKTFDEIVMDtKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDATAN-DIPhDSYKAEGFPTIYFA 2715
Cdd:cd02961      1 VELTDDNFDELVKD-SKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKVDCTANnDLC-SEYGVRGYPTIKLF 78

                           90       100
                   ....*....|....*....|....*
gi 1564305953 2716 PSNKKqNPVKFEGGkRDVEELSKFV 2740
Cdd:cd02961     79 PNGSK-EPVKYEGP-RTLESLVEFI 101
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 2291-2389 1.26e-31

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 120.54  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVV-NNADIILVEFYAPWCGHCKRLAPEYEKAAKELSnrtPPIPLAKVDATAES--ELATRFGVSGYPTLKIF 2367
Cdd:cd03002      5 LTPKNFDKVVhNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELD---GLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKVF 81

                           90       100
                   ....*....|....*....|....*...
gi 1564305953 2368 RKGKAF------DYNGPREKFGIVDYMS 2389
Cdd:cd03002     82 RPPKKAskhaveDYNGERSAKAIVDFVL 109
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 2168-2285 1.57e-31

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: 130.95  E-value: 1.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2168 EEENGVLVLTDENFD--TFMEGKDtVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDPPIPVAKVDATKASAlgSRFEVSG 2245
Cdd:TIGR01130  343 DDEGPVKVLVGKNFDeiVLDETKD-VLVEFYAPWCGHCKNLAPIYEELAEKYKDAESDVVIAKMDATANDV--PPFEVEG 419

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1564305953 2246 YPTIKILKKG---EPVDYDGDRSEQAIVERVKEVAQPDWKPPP 2285
Cdd:TIGR01130  420 FPTIKFVPAGkksEPVPYDGDRTLEDFSKFIAKHATFPLEGKA 462
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 2173-2271 4.05e-31

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 118.96  E-value: 4.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKEnDPPIPVAKVDATKA--SALGSRFEVSGYPTIK 2250
Cdd:cd02997      2 VVHLTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKE-DGKGVLAAVDCTKPehDALKEEYNVKGFPTFK 80

                           90       100
                   ....*....|....*....|..
gi 1564305953 2251 ILKKGEPV-DYDGDRSEQAIVE 2271
Cdd:cd02997     81 YFENGKFVeKYEGERTAEDIIE 102
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 2294-2387 8.75e-31

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 117.94  E-value: 8.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2294 DNFDDVVNNaDIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLKIFRKGKAF 2373
Cdd:cd03000      7 DSFKDVRKE-DIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAY 85

                           90
                   ....*....|....
gi 1564305953 2374 DYNGPREKFGIVDY 2387
Cdd:cd03000     86 NYRGPRTKDDIVEF 99
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 2287-2379 2.94e-30

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 116.23  E-value: 2.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2287 ATLVLTKDNFDDVVNNAdIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAESELATRFGVSGYPTLKI 2366
Cdd:cd03005      1 GVLELTEDNFDHHIAEG-NHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                           90
                   ....*....|....
gi 1564305953 2367 FRKG-KAFDYNGPR 2379
Cdd:cd03005     80 FKDGeKVDKYKGTR 93
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 2291-2388 3.23e-29

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 113.57  E-value: 3.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELsNRTPPIPLAKVDATAESE--LATRFGVSGYPTLKIFR 2368
Cdd:cd02997      5 LTDEDFRKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATEL-KEDGKGVLAAVDCTKPEHdaLKEEYNVKGFPTFKYFE 83

                           90       100
                   ....*....|....*....|.
gi 1564305953 2369 KGK-AFDYNGPREKFGIVDYM 2388
Cdd:cd02997     84 NGKfVEKYEGERTAEDIIEFM 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2635-2742 3.74e-29

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 113.48  E-value: 3.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2635 PVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNekNLVIAKMDATANDIPHDSYKAEGFPTIYF 2714
Cdd:pfam00085    1 VVVVLTDANFDEVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKG--NVVFAKVDVDENPDLASKYGVRGYPTLIF 78

                           90       100
                   ....*....|....*....|....*...
gi 1564305953 2715 APsnKKQNPVKFEGGkRDVEELSKFVEK 2742
Cdd:pfam00085   79 FK--NGQPVDDYVGA-RPKDALAAFLKA 103
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 2173-2271 6.35e-29

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 112.65  E-value: 6.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFD-TFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDPPIpVAKVDATkASALGSRFEVSGYPTIKI 2251
Cdd:cd02995      2 VKVVVGKNFDeVVLDSDKDVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVV-IAKMDAT-ANDVPSEFVVDGFPTILF 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2252 LKKG---EPVDYDGDRSEQAIVE 2271
Cdd:cd02995     80 FPAGdksNPIKYEGDRTLEDLIK 102
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 1484-1601 7.83e-28

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 110.34  E-value: 7.83e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1484 YAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTREL-SSSHSKLFTCNSRNTFILSSPeSLGRVWKVHLWHDNGGSSPSWY 1562
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLkKSNNKNKFERGQTDKFTVEAV-DLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1564305953 1563 LSHVVVKDLVQGSCWFFLGQCWLAVDEGDGRVERSLVAS 1601
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 2173-2274 4.47e-27

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 107.45  E-value: 4.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDTFMEGKD-TVLVEFYAPWCGHCKQFAPEYEKIAKTLkenDPPIPVAKVDATKAS--ALGSRFEVSGYPTI 2249
Cdd:cd03002      2 VYELTPKNFDKVVHNTNyTTLVEFYAPWCGHCKNLKPEYAKAAKEL---DGLVQVAAVDCDEDKnkPLCGKYGVQGFPTL 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564305953 2250 KILKKGEPV------DYDGDRSEQAIVERVK 2274
Cdd:cd03002     79 KVFRPPKKAskhaveDYNGERSAKAIVDFVL 109
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 2182-2277 5.52e-27

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 107.15  E-value: 5.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2182 DTFMEGK--DTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKGEPVD 2259
Cdd:cd03000      7 DSFKDVRkeDIWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN 86

                           90
                   ....*....|....*...
gi 1564305953 2260 YDGDRSEQAIVERVKEVA 2277
Cdd:cd03000     87 YRGPRTKDDIVEFANRVA 104
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 2290-2388 1.22e-26

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are 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. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 106.10  E-value: 1.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2290 VLTKDNFDDVVNNADI-ILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIpLAKVDATAeSELATRFGVSGYPTLKIFR 2368
Cdd:cd02995      4 VVVGKNFDEVVLDSDKdVLVEFYAPWCGHCKALAPIYEELAEKLKGDDNVV-IAKMDATA-NDVPSEFVVDGFPTILFFP 81

                           90       100
                   ....*....|....*....|...
gi 1564305953 2369 KGKAF---DYNGPREKFGIVDYM 2388
Cdd:cd02995     82 AGDKSnpiKYEGDRTLEDLIKFI 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2173-2276 2.76e-26

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 105.29  E-value: 2.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDT-FMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKI 2251
Cdd:COG3118      2 VVELTDENFEEeVLESDKPVLVDFWAPWCGPCKMLAPVLEELA---AEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLL 78

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2252 LKKGEPVD-YDGDRSEQAIVERVKEV 2276
Cdd:COG3118     79 FKDGQPVDrFVGALPKEQLREFLDKV 104
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2287-2374 2.29e-25

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 102.59  E-value: 2.29e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2287 ATLVLTKDNFD-DVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLK 2365
Cdd:COG3118      1 AVVELTDENFEeEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK---VKFVKVDVDENPELAAQFGVRSIPTLL 77


                   ....*....
gi 1564305953 2366 IFRKGKAFD 2374
Cdd:COG3118     78 LFKDGQPVD 86
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 2172-2273 3.14e-25

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 101.98  E-value: 3.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2172 GVLVLTDENFDTFMEGKDTvLVEFYAPWCGHCKQFAPEYEKIAKTLKENDPPIPVAKVDATKASALGSRFEVSGYPTIKI 2251
Cdd:cd03005      1 GVLELTEDNFDHHIAEGNH-FVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLL 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2252 LKKGEPVD-YDGDRSEQAIVERV 2273
Cdd:cd03005     80 FKDGEKVDkYKGTRDLDSLKEFV 102
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 2166-2303 6.72e-25

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 105.48  E-value: 6.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2166 DSEEENGVLVLTDENFDTFMEGKD-----TVLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVAKVDATKASALGSR 2240
Cdd:PTZ00443    25 DAEDANALVLLNDKNFEKLTQASTgattgPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKR 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1564305953 2241 FEVSGYPTIKILKKGEPVDYD-GDRSeqaiVERVKEVAQPDWK-------PPPEATLVLTKDNFDDVVNNA 2303
Cdd:PTZ00443   102 FAIKGYPTLLLFDKGKMYQYEgGDRS----TEKLAAFALGDFKkalgapvPAPLSFFALTIDFFVSGTNEA 168
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 2179-2274 1.02e-21

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 91.85  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2179 ENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTlkenDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKGEPV 2258
Cdd:cd02947      1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE----YPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                           90
                   ....*....|....*..
gi 1564305953 2259 D-YDGDRSEQAIVERVK 2274
Cdd:cd02947     77 DrVVGADPKEELEEFLE 93
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 2294-2371 3.48e-21

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 90.31  E-value: 3.48e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1564305953 2294 DNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNrtppIPLAKVDATAESELATRFGVSGYPTLKIFRKGK 2371
Cdd:cd02947      1 EEFEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK----VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGK 74
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 2291-2387 3.78e-21

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 90.53  E-value: 3.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRTP---PIPLAKVDATAESELATRFGVSGYPTLKIF 2367
Cdd:cd02996      6 LTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPdagKVVWGKVDCDKESDIADRYRINKYPTLKLF 85

                           90       100
                   ....*....|....*....|..
gi 1564305953 2368 RKGKAF--DYNGPREKFGIVDY 2387
Cdd:cd02996     86 RNGMMMkrEYRGQRSVEALAEF 107
PDI_b_family cd02981
Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of ...
 2396-2487 1.24e-20

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: 88.93  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2396 SKQVQTLKQVQELIRDgDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKFMHTFNNEVAKFLKASPGQVVMLQP-EKFRS 2474
Cdd:cd02981      1 VKELTSKEELEKFLDK-DDVVVVGFFKDEESEEYKTFEKVAESLRDDYGFGHTSDKEVAKKLKVKPGSVVLFKPfEEEPV 79

                           90
                   ....*....|...
gi 1564305953 2475 KYEPASHSLTLKD 2487
Cdd:cd02981     80 EYDGEFTEESLVE 92
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 402-621 2.84e-20

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 96.80  E-value: 2.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  402 QCNISRGLLYRWTIYDMSG----QQLLLPHIDTGRQYiNLPKYLLHYGTYKAIAKVQITGSV-VYSNYSVLIEVIRSHPV 476
Cdd:pfam02010    7 GCFSAYTIDYLWSVFTVSSnlnlQTISSPKDLVLPQL-TIPSGTLPYGTYVFTLTVSLSSTPsLAGTDIITVTVQPSPLV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  477 SVISEATNIFINRQSStiVTLDGRKSHDPDYPNNT---ISYSWSCRPVNTEESSCFNRNIV------------TTSAVLT 541
Cdd:pfam02010   86 AVIDGGSSRVVGYNQD--LTLDGSESYDPDVDPGSssgLTYLWSCRRSSSGDNPLLNNDPVcfsdqnegtllqSTSSSLT 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  542 FPALALKSDFDlLKFTLTVYSGHRSSAS-NMFITVTSKPVSNVHMYCEHCQGNSVNWNEQFSVSA-FCEDCGLNAKSVTY 619
Cdd:pfam02010  164 IPASTLQANVT-YTFKLTVSKGSRNSAStTQTILVVDGNPPIIILSCISNCNRKNNPVDRLVLLAsTCLNCSSDLSDVTY 242


                   ..
gi 1564305953  620 YW 621
Cdd:pfam02010  243 RW 244
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2173-2271 3.70e-20

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 87.73  E-value: 3.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENF-DTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVAKVDATKASALGSRFEVSGYPTIKI 2251
Cdd:cd03004      3 VITLTPEDFpELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKGK---VKVGSVDCQKYESLCQQANIRAYPTIRL 79

                           90       100
                   ....*....|....*....|...
gi 1564305953 2252 L--KKGEPVDYDGD-RSEQAIVE 2271
Cdd:cd03004     80 YpgNASKYHSYNGWhRDADSILE 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2291-2371 1.21e-19

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 86.19  E-value: 1.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVVNNADI-ILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLKIFRK 2369
Cdd:TIGR01068    1 LTDANFDETIASSDKpVLVDFWAPWCGPCKMIAPILEELAKEYEGK---VKFVKLNVDENPDIAAKYGIRSIPTLLLFKN 77


                   ..
gi 1564305953 2370 GK 2371
Cdd:TIGR01068   78 GK 79
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 2635-2740 2.04e-19

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 85.42  E-value: 2.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2635 PVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTalgKKYKNEKNLV-IAKMDATANDIPHDSYKAEGFPTIY 2713
Cdd:cd03001      1 DVVELTDSNFDKKVLNSDDVWLVEFYAPWCGHCKNLAPEWK---KAAKALKGIVkVGAVDADVHQSLAQQYGVRGFPTIK 77

                           90       100
                   ....*....|....*....|....*..
gi 1564305953 2714 FAPSNKKQnPVKFEGGkRDVEELSKFV 2740
Cdd:cd03001     78 VFGAGKNS-PQDYQGG-RTAKAIVSAA 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2176-2259 2.77e-19

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 85.03  E-value: 2.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2176 LTDENFDTFMEGKDT-VLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKILKK 2254
Cdd:TIGR01068    1 LTDANFDETIASSDKpVLVDFWAPWCGPCKMIAPILEELA---KEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKN 77


                   ....*
gi 1564305953 2255 GEPVD 2259
Cdd:TIGR01068   78 GKEVD 82
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2290-2377 1.16e-18

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 83.50  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2290 VLTKDNFDD-VVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSnrtPPIPLAKVDATAESELATRFGVSGYPTLKIF- 2367
Cdd:cd03004      5 TLTPEDFPElVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALK---GKVKVGSVDCQKYESLCQQANIRAYPTIRLYp 81

                           90
                   ....*....|.
gi 1564305953 2368 -RKGKAFDYNG 2377
Cdd:cd03004     82 gNASKYHSYNG 92
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 2173-2275 2.64e-18

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 82.43  E-value: 2.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDTFMEGKdtVLVEFYAPWCGHCKQFAPEYEKIAKtlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKIL 2252
Cdd:cd02994      3 VVELTDSNWTLVLEGE--WMIEFYAPWCPACQQLQPEWEEFAD--WSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHA 78

                           90       100
                   ....*....|....*....|...
gi 1564305953 2253 KKGEPVDYDGDRSEQAIVERVKE 2275
Cdd:cd02994     79 KDGVFRRYQGPRDKEDLISFIEE 101
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 2287-2394 1.24e-17

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 84.29  E-value: 1.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2287 ATLVLTKDNFDDVVN-----NADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGY 2361
Cdd:PTZ00443    31 ALVLLNDKNFEKLTQastgaTTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ---VNVADLDATRALNLAKRFAIKGY 107

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1564305953 2362 PTLKIFRKGKAFDY-NGPR--EK---FGIVDYMSDQAGP 2394
Cdd:PTZ00443   108 PTLLLFDKGKMYQYeGGDRstEKlaaFALGDFKKALGAP 146
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 316-610 1.29e-17

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 90.91  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  316 VSYIWNFGDGT--ERNGSSTEHHVYDRTGEYIVQVIMSNLVSSASLTGHIFVVEESCQPPPVKNMGPNKIQVWQYQTVRL 393
Cdd:TIGR00864 2073 MACHWDFGDGSagQDTDEPRAEHEYLHPGDYRVQVNASNLVSFFSAHAEINVQVLACEEPEVDVVLALQLAIRRSQPNLL 2152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  394 avtfEAHIQCN--ISRGLLYRWTIYD--------------MSGQQLLLP------HIDTGRQYINLPKYLLHYGTYKAIA 451
Cdd:TIGR00864 2153 ----EAHVDLKdcLRYGAEYLWEILRaascdndghfargaLNGATRSFPviplpaEVDVQRLQLSLPKLALAAGHYCFVF 2228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  452 KVQITGSVVYSNYSVLIEVIRSHPVSVISEATNIFINRQSStiVTLDGRKSHDPDY-PNNT--ISYSWSCRPVNTEESSC 528
Cdd:TIGR00864 2229 SLSFEDTPLKKAACANLGVAAARLMPIIEGGSYRVWSDTQD--LQLDAEESYDPNLdDDDQslLHFHWACQASSKGEAGC 2306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  529 --FNRNIVTTSAVLTFPALALKSDFDlLKFTLTVY-SGHRSSASNMFITVTSKPVSNVHMYCEHCQGNS---VNWNEQFS 602
Cdd:TIGR00864 2307 caLNFGLGGKGPTLGIPGEELAAGIE-YTFKLSIGkAGMKEEATNQTVLIQSGHIPIVSLECVSCKAQAlyeVSQNSYVY 2385


                   ....*...
gi 1564305953  603 VSAFCEDC 610
Cdd:TIGR00864 2386 LEGRCLNC 2393
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 2636-2740 1.86e-17

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 80.02  E-value: 1.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2636 VKVVVGKTFDEIVmdTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLV-IAKMDATANDIPHDSYKAEGFPTIYF 2714
Cdd:cd03005      2 VLELTEDNFDHHI--AEGNHFVKFFAPWCGHCKRLAPTWEQLAKKFNNENPSVkIAKVDCTQHRELCSEFQVRGYPTLLL 79

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2715 APSNKKqnPVKFEgGKRDVEELSKFV 2740
Cdd:cd03005     80 FKDGEK--VDKYK-GTRDLDSLKEFV 102
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 2165-2275 2.21e-17

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 87.88  E-value: 2.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2165 PDSEEENG-VLVLTDENFD--TFMEGKDtVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDpPIPVAKVDATKASALGSRF 2241
Cdd:PTZ00102   350 PIPEEQDGpVKVVVGNTFEeiVFKSDKD-VLLEIYAPWCGHCKNLEPVYNELGEKYKDND-SIIVAKMNGTANETPLEEF 427

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1564305953 2242 EVSGYPTIKILKKGE--PVDYDGDRSEQAIVERVKE 2275
Cdd:PTZ00102   428 SWSAFPTILFVKAGErtPIPYEGERTVEGFKEFVNK 463
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 2172-2273 4.83e-17

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 78.97  E-value: 4.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2172 GVLVLTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDP---PIPVAKVDATKASALGSRFEVSGYPT 2248
Cdd:cd02996      2 EIVSLTSGNIDDILQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEFPdagKVVWGKVDCDKESDIADRYRINKYPT 81

                           90       100
                   ....*....|....*....|....*..
gi 1564305953 2249 IKILKKGEPV--DYDGDRSEQAIVERV 2273
Cdd:cd02996     82 LKLFRNGMMMkrEYRGQRSVEALAEFV 108
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 2635-2740 5.59e-17

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 78.94  E-value: 5.59e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2635 PVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDATANDIPHDSYKAEGFPTI-Y 2713
Cdd:cd03002      1 PVYELTPKNFDKVVHNTNYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKNKPLCGKYGVQGFPTLkV 80

                           90       100
                   ....*....|....*....|....*...
gi 1564305953 2714 FAPSNKKQNP-VKFEGGKRDVEELSKFV 2740
Cdd:cd03002     81 FRPPKKASKHaVEDYNGERSAKAIVDFV 108
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 2636-2743 8.81e-17

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 77.94  E-value: 8.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2636 VKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEknLVIAKMDATAN-DIPhDSYKAEGFPTIYF 2714
Cdd:COG3118      2 VVELTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK--VKFVKVDVDENpELA-AQFGVRSIPTLLL 78

                           90       100
                   ....*....|....*....|....*....
gi 1564305953 2715 ApsnKKQNPVKFEGGKRDVEELSKFVEKH 2743
Cdd:COG3118     79 F---KDGQPVDRFVGALPKEQLREFLDKV 104
PTZ00051 PTZ00051
thioredoxin; Provisional
 2290-2374 9.78e-17

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 77.61  E-value: 9.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2290 VLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELsnrtPPIPLAKVDATAESELATRFGVSGYPTLKIFRK 2369
Cdd:PTZ00051     5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEY----TKMVFVKVDVDELSEVAEKENITSMPTFKVFKN 80


                   ....*
gi 1564305953 2370 GKAFD 2374
Cdd:PTZ00051    81 GSVVD 85
PDI_b'_family cd02982
Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of ...
 2507-2615 1.03e-16

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: 77.70  E-value: 1.03e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2507 GHRKQSNDAKRytARPLVVVYYGVDFSfdyrvATQFWRSKVLEVAKDF-PEYTFAIADEEDYSDELKSLGLSEsgEEVNV 2585
Cdd:cd02982      1 NAETFFNYEES--GKPLLVLFYNKDDS-----ESEELRERFKEVAKKFkGKLLFVVVDADDFGRHLEYFGLKE--EDLPV 71

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1564305953 2586 GIL--GEGGKKYAMEPEEFDSDVLRSFVMAFK 2615
Cdd:cd02982     72 IAIinLSDGKKYLMPEEELTAESLEEFVEDFL 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 2175-2259 1.20e-16

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 77.61  E-value: 1.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2175 VLTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLkendPPIPVAKVDATKASALGSRFEVSGYPTIKILKK 2254
Cdd:PTZ00051     5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEY----TKMVFVKVDVDELSEVAEKENITSMPTFKVFKN 80


                   ....*
gi 1564305953 2255 GEPVD 2259
Cdd:PTZ00051    81 GSVVD 85
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 2286-2368 1.28e-16

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 78.08  E-value: 1.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2286 EATLVLTKDNFDDVVNNADI-ILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPIPLAKVDATAES--ELATRFGVSGYP 2362
Cdd:cd02992      1 DPVIVLDAASFNSALLGSPSaWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDCADEEnvALCRDFGVTGYP 80


                   ....*.
gi 1564305953 2363 TLKIFR 2368
Cdd:cd02992     81 TLRYFP 86
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 1826-1997 7.08e-16

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 78.62  E-value: 7.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1826 SFHSIQKHEDWWNWTTTTFLERLYDNANCHDKrvkNETDFSSPLSLIGSPVIRKIKSTyNSSCQILNLLGKNNIKCSDNH 1905
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHSNKTPSGL---PGSFIAYESLLLGVPRLRQLRVR-NSSCLVHDKFVREINECHAGY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1906 TVE---KRHSLC----------------------------GKLGCYEGESVSVNLGKTRSEAIKSIKTLLDAGWMTPFTQ 1954
Cdd:pfam20519   77 SPPsedRKLYSAlpykpvhygskywfiytppgllmgydhwGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1564305953 1955 IVMIQFILYNGPSNLFTAVTILVEQTSTGALMPSASIQSTRLY 1997
Cdd:pfam20519  157 AVFVDFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 2173-2250 1.98e-15

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 74.61  E-value: 1.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENF-DTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDPPIPVAKVD--ATKASALGSRFEVSGYPTI 2249
Cdd:cd02992      3 VIVLDAASFnSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVRVAAVDcaDEENVALCRDFGVTGYPTL 82


                   .
gi 1564305953 2250 K 2250
Cdd:cd02992     83 R 83
PRK10996 PRK10996
thioredoxin 2; Provisional
 2292-2382 1.99e-15

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 75.49  E-value: 1.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2292 TKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKElsnRTPPIPLAKVDATAESELATRFGVSGYPTLKIFRKGK 2371
Cdd:PRK10996    41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE---RSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQ 117

                           90
                   ....*....|....
gi 1564305953 2372 AFD-YNG--PREKF 2382
Cdd:PRK10996   118 VVDmLNGavPKAPF 131
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 2652-2740 7.04e-15

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 72.87  E-value: 7.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2652 KKDVLIEFYAPWCGHCKKLEPDYTALGKKYkNEKNLVIAKMDATANDIPHDsyKAEG----FPTIYFAPSNKKQnPVKFE 2727
Cdd:cd02993     21 NQSTLVVLYAPWCPFCQAMEASYEELAEKL-AGSNVKVAKFNADGEQREFA--KEELqlksFPTILFFPKNSRQ-PIKYP 96

                           90
                   ....*....|...
gi 1564305953 2728 GGKRDVEELSKFV 2740
Cdd:cd02993     97 SEQRDVDSLLMFV 109
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 2639-2741 8.47e-15

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 72.35  E-value: 8.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2639 VVGKTFDEIVMDtKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDAT--ANDIPHDSYKAEGFPTI-YFa 2715
Cdd:cd02997      5 LTDEDFRKFLKK-EKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAAVDCTkpEHDALKEEYNVKGFPTFkYF- 82

                           90       100
                   ....*....|....*....|....*.
gi 1564305953 2716 psNKKQNPVKFEGGKRDveelSKFVE 2741
Cdd:cd02997     83 --ENGKFVEKYEGERTA----EDIIE 102
PRK10996 PRK10996
thioredoxin 2; Provisional
 2177-2259 1.66e-14

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 72.79  E-value: 1.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2177 TDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKGE 2256
Cdd:PRK10996    41 TGETLDKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVA---AERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQ 117


                   ...
gi 1564305953 2257 PVD 2259
Cdd:PRK10996   118 VVD 120
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
2421-2612 2.34e-14

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 73.55  E-value: 2.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2421 FSSEEDAVYEIYQEACNSLREDYKFMHTFNNEVAKFLKASPGQVVMLQP-EKFRSKYEPashsltlkDSTPASEVQEFFK 2499
Cdd:pfam13848    1 FEDKDSPLYEIFRKAAKELKGDVRFGITFSKEVADKYNIKEPAILLFRKfDEETVHYPG--------DSINFEDLKKFIQ 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2500 KHILPLVGHRKQSNdAKRYTARPLVVVYygVDFSFDYRVATQFWRSKVLEVAKDFP-EYTFAIADEEDYSDELKSLGLSE 2578
Cdd:pfam13848   73 KNCLPLVREFTPEN-AEELFEEGIPPLL--LLFLKKDDESTEEFKKALEKVAKKFRgKINFALVDAKSFGRPLEYFGLSE 149

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1564305953 2579 SGEEVNVGILGEGGKKYAMEPEEFDSDVLRSFVM 2612
Cdd:pfam13848  150 SDLPVIVIVDSFSHMYKYFPSDEFSPESLKEFIN 183
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 1484-1599 7.44e-13

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 67.07  E-value: 7.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1484 YAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTcNSRNTFILSSPESLGRVWKVHLWHDNGGSSPSWYL 1563
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESAQLEITLDNPDFER-GAEDSFEIDTDWDVGAILKINLHWDNNGLSDEWFL 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1564305953 1564 SHVVV-KDLVQGSCWFFLGQCWLAVDEgDGRVERSLV 1599
Cdd:pfam01477   80 KSITVeVPGETGGKYTFPCNSWVYGSK-KYKETRVFF 115
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 2290-2390 8.78e-13

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 66.63  E-value: 8.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2290 VLTKDNFDDVVNnaDIILVEFYAPWCGHCKRLAPEYEKAA---KELSnrtppIPLAKVDATAESELATRFGVSGYPTL-- 2364
Cdd:cd02994      5 ELTDSNWTLVLE--GEWMIEFYAPWCPACQQLQPEWEEFAdwsDDLG-----INVAKVDVTQEPGLSGRFFVTALPTIyh 77

                           90       100
                   ....*....|....*....|....*....
gi 1564305953 2365 ---KIFRKgkafdYNGPREKFGIVDYMSD 2390
Cdd:cd02994     78 akdGVFRR-----YQGPRDKEDLISFIEE 101
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 861-1050 1.15e-12

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 72.92  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  861 VFESYTLTGLTSSDVTFKPFMLKPKSLYLLEVSAISEKRL-QGKSQLFFHTQAVPEGMSCQVQPNTGYEIHTHFSIFCSS 939
Cdd:pfam02010  258 QLNSQTSTGRSGPYLVIKAGVLQSGVSYRFTLIVTVYPGLvSGLASISFITNAPPTGGTCSVTPTEGTALETKFTVTCQG 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  940 GKED---LVFE---YSFSVGNNVRKLLYEG-RDFQHYFSLPSGDPNDDYKVTIYIEIKNRFGAATKpCPVKVTVLPsfqr 1012
Cdd:pfam02010  338 WTDDdlpLTYQfgdISFREASEEWFLLYEGsSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATS-VSLTITVTP---- 412

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1564305953 1013 ssssQLKPDQELYMY-GVGNLTSLSKIGSNQDIVNYISL 1050
Cdd:pfam02010  413 ----PSSSDELLYFLlGTTSDLSALLQSGDPQQAAQLIL 447
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2285-2387 1.21e-12

PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 66.01  E-value: 1.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2285 PEATlVLTKDNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTL 2364
Cdd:cd03003      1 PEIV-TLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFAKEMDGV---IRIGAVNCGDDRMLCRSQGVNSYPSL 76

                           90       100
                   ....*....|....*....|....
gi 1564305953 2365 KIFRKG-KAFDYNGPREKFGIVDY 2387
Cdd:cd03003     77 YVFPSGmNPEKYYGDRSKESLVKF 100
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 2645-2714 1.69e-12

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 65.94  E-value: 1.69e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564305953 2645 DEIVMDTKKD--VLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLV-IAKMDATANDIPHDSYKAEGFPTIYF 2714
Cdd:cd03000      6 DDSFKDVRKEdiWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGSPVrVGKLDATAYSSIASEFGVRGYPTIKL 78
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 2642-2741 3.01e-11

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 61.81  E-value: 3.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2642 KTFDEIVmDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYkneKNLVIAKMDATAN-DIPhDSYKAEGFPTIYFapsnkk 2720
Cdd:cd02947      1 EEFEELI-KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEY---PKVKFVKVDVDENpELA-EEYGVRSIPTFLF------ 69

                           90       100
                   ....*....|....*....|....*....
gi 1564305953 2721 qnpvkFEGGK--------RDVEELSKFVE 2741
Cdd:cd02947     70 -----FKNGKevdrvvgaDPKEELEEFLE 93
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 2635-2736 3.45e-11

PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein containing an N-terminal redox active TRX domain, similar to that of PDI, and a small C-terminal flavin adenine dinucleotide (FAD)-binding domain homologous to the yeast ERV1p protein. QSOX oxidizes thiol groups to disulfides like PDI, however, unlike PDI, this oxidation is accompanied by the reduction of oxygen to hydrogen peroxide. QSOX is localized in high concentrations in cells with heavy secretory load and prefers peptides and proteins as substrates, not monothiols like glutathione. Inside the cell, QSOX is found in the endoplasmic reticulum and Golgi. The flow of reducing equivalents in a QSOX-catalyzed reaction goes from the dithiol substrate -> dithiol of the QSOX TRX domain -> dithiols of the QSOX ERV1p domain -> FAD -> oxygen.


Pssm-ID: 239290 [Multi-domain]  Cd Length: 114  Bit Score: 62.29  E-value: 3.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2635 PVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLV-IAKMD--ATANDIPHDSYKAEGFPT 2711
Cdd:cd02992      2 PVIVLDAASFNSALLGSPSAWLVEFYASWCGHCRAFAPTWKKLARDLRKWRPVVrVAAVDcaDEENVALCRDFGVTGYPT 81

                           90       100
                   ....*....|....*....|....*..
gi 1564305953 2712 IYFAPSNKKQNPV--KFEGGKRDVEEL 2736
Cdd:cd02992     82 LRYFPPFSKEATDglKQEGPERDVNEL 108
PDI_b_ERp57 cd03069
PDIb family, ERp57 subfamily, first redox inactive TRX-like domain b; ERp57 (or ERp60) ...
 2396-2502 3.99e-11

PDIb family, ERp57 subfamily, first redox inactive TRX-like domain b; ERp57 (or ERp60) 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. ERp57 contains two redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. It shares the same domain arrangement of abb'a' as PDI, but lacks the C-terminal acid-rich region (c domain) that is present in PDI. ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins. Similar to PDI, the b domain of ERp57 is likely involved in binding to substrates.


Pssm-ID: 239367  Cd Length: 104  Bit Score: 61.96  E-value: 3.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2396 SKQVQTLKQVQELIrDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKFMHTFNNEVAKflKASPGQ-VVMLQPEKFRS 2474
Cdd:cd03069      2 SVELRTEAEFEKFL-SDDDASVVGFFEDEDSKLLSEFLKAADTLRESFRFAHTSDKQLLE--KYGYGEgVVLFRPPRLSN 78

                           90       100
                   ....*....|....*....|....*...
gi 1564305953 2475 KYEPASHSLTlkDSTPASEVQEFFKKHI 2502
Cdd:cd03069     79 KFEDSSVKFD--GDLDSSKIKKFIRENI 104
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 2656-2739 6.30e-11

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 64.65  E-value: 6.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2656 LIEFYAPWCGHCKKLEPDYTALGKKYKNEKNlvIAKMDATANDIPHDSYKAEGFPTIYFAPSNKKqnpVKFEGGKRDVEE 2735
Cdd:PTZ00443    56 FVKFYAPWCSHCRKMAPAWERLAKALKGQVN--VADLDATRALNLAKRFAIKGYPTLLLFDKGKM---YQYEGGDRSTEK 130


                   ....
gi 1564305953 2736 LSKF 2739
Cdd:PTZ00443   131 LAAF 134
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 2301-2379 7.93e-11

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 60.84  E-value: 7.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2301 NNADIILVEFYAPWCGHCKRLAPEYEKaakeLSNRTPPIPLAKVDAT-AESELATRFGVSGYPTLKIFRKGKAFDYNGPR 2379
Cdd:cd02999     16 NREDYTAVLFYASWCPFSASFRPHFNA----LSSMFPQIRHLAIEESsIKPSLLSRYGVVGFPTILLFNSTPRVRYNGTR 91
trxA PRK09381
thioredoxin TrxA;
2291-2371 1.05e-10

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 60.85  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVVNNAD-IILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLKIFRK 2369
Cdd:PRK09381     8 LTDDSFDTDVLKADgAILVDFWAEWCGPCKMIAPILDEIADEYQGK---LTVAKLNIDQNPGTAPKYGIRGIPTLLLFKN 84


                   ..
gi 1564305953 2370 GK 2371
Cdd:PRK09381    85 GE 86
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 2642-2744 1.36e-10

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 60.38  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2642 KTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEknLVIAKMDATANDIPHDSYKAEGFPTIYFApsnKKQ 2721
Cdd:TIGR01068    4 ANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGK--VKFVKLNVDENPDIAAKYGIRSIPTLLLF---KNG 78

                           90       100
                   ....*....|....*....|...
gi 1564305953 2722 NPVKFEGGKRDVEELSKFVEKHA 2744
Cdd:TIGR01068   79 KEVDRSVGALPKAALKQLINKNL 101
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 2294-2374 2.63e-10

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 59.21  E-value: 2.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2294 DNFDDVVNNAD--IILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLKIFRKGK 2371
Cdd:cd02956      1 QNFQQVLQESTqvPVVVDFWAPRSPPSKELLPLLERLAEEYQGQ---FVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ 77


                   ...
gi 1564305953 2372 AFD 2374
Cdd:cd02956     78 PVD 80
Calsequestrin pfam01216
Calsequestrin;
2291-2504 4.77e-10

Calsequestrin;


Pssm-ID: 395972 [Multi-domain]  Cd Length: 350  Bit Score: 63.88  E-value: 4.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2291 LTKDNFDDVVNNADIILVEFYAPwcghckrlaPEYEKAAK----------ELSNRT---PPIPLAKVDATAESELATRFG 2357
Cdd:pfam01216   16 LNAKNFKNVFKKYDVLALLYHEP---------PEDDKAAQkqfeleeiilELAAQVledKDIGFGLVDAEKDAALAKKLG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2358 VSGYPTLKIFRKGKAFDYNGPREKFGIVDYMSDQAGPPSKQVQTLKQVQELIRDGDDAVIVGVFSSEEDAVYEIYQEACN 2437
Cdd:pfam01216   87 FDEEDSLYVFKGDETIEFDGEFAADTIVEFLLDLIEDPVEIIEGELELQAFENIEDEIKLIGFFKSEDSEHYKAFEDAAE 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1564305953 2438 SLREDYKFMHTFNNEVAKFLKASPGQVVMLQPekFRSkyEPashsLTLKDStPAS--EVQEFFKKHILP 2504
Cdd:pfam01216  167 EFHPYIKFFATFDKGVAKKLSLKLNEIDFYEA--FMD--EP----IAIPDK-PNSeeEIVEFVEEHQRP 226
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
 305-359 1.23e-09

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 56.63  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1564305953  305 NFTCRISSGTDVSYIWNFGDGTERNGSSTE-HHVYDRTGEYIVQVIMSNLVSSASL 359
Cdd:pfam00801   15 TFTATLADGSNVTYTWDFGDSPGTSGSGPTvTHTYLSPGTYTVTLTASNAVGSANA 70
trxA PRK09381
thioredoxin TrxA;
2173-2256 1.59e-09

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 57.77  E-value: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDT-FMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKI 2251
Cdd:PRK09381     5 IIHLTDDSFDTdVLKADGAILVDFWAEWCGPCKMIAPILDEIA---DEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLL 81


                   ....*
gi 1564305953 2252 LKKGE 2256
Cdd:PRK09381    82 FKNGE 86
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2642-2740 1.80e-09

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 57.30  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2642 KTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNekNLVIAKMDATANDIPHDSYKAEGFPTIYFAPSNKKq 2721
Cdd:cd03004      9 EDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALKG--KVKVGSVDCQKYESLCQQANIRAYPTIRLYPGNAS- 85

                           90
                   ....*....|....*....
gi 1564305953 2722 NPVKFEGGKRDVEELSKFV 2740
Cdd:cd03004     86 KYHSYNGWHRDADSILEFI 104
PLN02309 PLN02309
5'-adenylylsulfate reductase
 2652-2741 2.29e-09

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 62.50  E-value: 2.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2652 KKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNeKNLVIAKMDAtanDIPHDSYKAE-----GFPTIYFAPSNKKQnPVKF 2726
Cdd:PLN02309   365 KEPWLVVLYAPWCPFCQAMEASYEELAEKLAG-SGVKVAKFRA---DGDQKEFAKQelqlgSFPTILLFPKNSSR-PIKY 439

                           90
                   ....*....|....*
gi 1564305953 2727 EGGKRDVEELSKFVE 2741
Cdd:PLN02309   440 PSEKRDVDSLLSFVN 454
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 1484-1594 2.34e-09

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 57.35  E-value: 2.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1484 YAVTVDTGLRSRTRMTAKVHIVLYGDKSvSQTRELSSSHSKLFTCNSRNTFILSSPESLGRVWKVHLWHDNGGSSPSWYL 1563
Cdd:cd00113      3 YTVTIKTGDKKGAGTDSNISLALYGENG-NSSDIPILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWYC 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1564305953 1564 SHVVVKDLVQGSCWFFLGQCWLAVDEGDGRV 1594
Cdd:cd00113     82 ESITVQALGTKKVYTFPVNRWVLGGKWYTSV 112
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2173-2271 2.54e-09

PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 56.76  E-value: 2.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDTFMEGKDTVLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKIL 2252
Cdd:cd03003      3 IVTLDRGDFDAAVNSGEIWFVNFYSPRCSHCHDLAPTWREFA---KEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVF 79

                           90       100
                   ....*....|....*....|
gi 1564305953 2253 KKG-EPVDYDGDRSEQAIVE 2271
Cdd:cd03003     80 PSGmNPEKYYGDRSKESLVK 99
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 2656-2742 4.06e-09

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 56.23  E-value: 4.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2656 LIEFYAPWCGHCKKLEPDYTALGKKyKNEKNLVIAKMDATANDIPHDSYKAEGFPTIYFApsnkKQNPVKFEGGKRDVEE 2735
Cdd:cd02994     20 MIEFYAPWCPACQQLQPEWEEFADW-SDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHA----KDGVFRRYQGPRDKED 94


                   ....*..
gi 1564305953 2736 LSKFVEK 2742
Cdd:cd02994     95 LISFIEE 101
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 2179-2273 8.52e-09

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 54.97  E-value: 8.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2179 ENFDTFMEGKDT--VLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKILKKGE 2256
Cdd:cd02956      1 QNFQQVLQESTQvpVVVDFWAPRSPPSKELLPLLERLA---EEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQ 77

                           90
                   ....*....|....*...
gi 1564305953 2257 PVD-YDGDRSEQAIVERV 2273
Cdd:cd02956     78 PVDgFQGAQPEEQLRQML 95
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 2307-2376 9.35e-09

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 54.24  E-value: 9.35e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564305953 2307 LVEFYAPWCGHCKRLAPEYEKAAKELSNrtppIPLAKVDATAESEL---ATRFGVSGYPTLKIFRKGKAFDYN 2376
Cdd:cd01659      1 LVLFYAPWCPFCQALRPVLAELALLNKG----VKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVKYG 69
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 2173-2266 1.93e-08

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 54.38  E-value: 1.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2173 VLVLTDENFDTFMEG----KDTVLVeFYAPWCGHCKQFAPEYEKIAKTLKENDppIPVAKVDATKASALGSRFE--VSGY 2246
Cdd:cd02993      3 VVTLSRAEIEALAKGerrnQSTLVV-LYAPWCPFCQAMEASYEELAEKLAGSN--VKVAKFNADGEQREFAKEElqLKSF 79

                           90       100
                   ....*....|....*....|..
gi 1564305953 2247 PTIKILKKG--EPVDYDGDRSE 2266
Cdd:cd02993     80 PTILFFPKNsrQPIKYPSEQRD 101
PKD smart00089
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ...
 312-366 2.05e-08

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.


Pssm-ID: 214510 [Multi-domain]  Cd Length: 79  Bit Score: 53.22  E-value: 2.05e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1564305953   312 SGTDVSYIWNFGDGTERNGSSTEhHVYDRTGEYIVQVIMSNLVSSASLTGHIFVV 366
Cdd:smart00089   26 DGSIVSYTWDFGDGTSSTGPTVT-HTYTKPGTYTVTLTVTNAVGSASATVTVVVQ 79
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 2192-2261 4.47e-08

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 52.32  E-value: 4.47e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564305953 2192 LVEFYAPWCGHCKQFAPeyekIAKTLKENDPPIPVAKVDATKASAL---GSRFEVSGYPTIKILKKGEPVDYD 2261
Cdd:cd01659      1 LVLFYAPWCPFCQALRP----VLAELALLNKGVKFEAVDVDEDPALekeLKRYGVGGVPTLVVFGPGIGVKYG 69
PDI_a_ERp44_like cd02999
PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of ...
 2189-2264 5.57e-08

PDIa family, endoplasmic reticulum protein 44 (ERp44)-like subfamily; composed of uncharacterized PDI-like eukaryotic proteins containing only one redox active TRX (a) domain with a CXXS motif, similar to ERp44. CXXS is still a redox active motif; however, the mixed disulfide formed with the substrate is more stable than those formed by CXXC motif proteins. PDI-related proteins are usually involved in the oxidative protein folding in the ER by acting as catalysts and folding assistants. ERp44 is involved in thiol-mediated retention in the ER.


Pssm-ID: 239297 [Multi-domain]  Cd Length: 100  Bit Score: 52.75  E-value: 5.57e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953 2189 DTVLVEFYAPWCGHCKQFAPEYEKIAKTLkendPPIPVAKVDATKA-SALGSRFEVSGYPTIKILKKGEPVDYDGDR 2264
Cdd:cd02999     19 DYTAVLFYASWCPFSASFRPHFNALSSMF----PQIRHLAIEESSIkPSLLSRYGVVGFPTILLFNSTPRVRYNGTR 91
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 2656-2740 7.61e-08

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 57.72  E-value: 7.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2656 LIEFYAPWCGHCKKLEPDYTALGKKYKNeKNLVIAKM--DATANDIPHDSYKAEGFPTIYFAPSNKKQnPVKFEGGKRDV 2733
Cdd:TIGR00424  375 LVVLYAPWCPFCQAMEASYLELAEKLAG-SGVKVAKFraDGDQKEFAKQELQLGSFPTILFFPKHSSR-PIKYPSEKRDV 452


                   ....*..
gi 1564305953 2734 EELSKFV 2740
Cdd:TIGR00424  453 DSLMSFV 459
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 219-417 1.18e-07

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 57.78  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  219 DIKFVAVTEGPDPLYFYWQFGDGPEIKTTSRIYK--KRYRLPDKYSITVSVSNGLtSISSDVYLVRIQRAVqpnrLLYSS 296
Cdd:TIGR00864 1358 EAQFQACAEPEFNYRYEWDFGGEEAAPLPAAGAEvtFIYNDPGCYLVTVAASNNI-SAANDSALIEVLEPV----GATSF 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  297 SVLLHSSVNFTCR-------ISSGTDVSYIWNFGDGTERNGSSTEhHVYDRTGEYIVQVIMSNLVSSASLTGHIFVVEEs 369
Cdd:TIGR00864 1433 KHNGSHGNNLELGqpylfsaFGRARNASYLWDFGDGGLLEGPEIL-HAFNSPGDFNIRLAAANEVGKNEATLNVAVKAR- 1510

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1564305953  370 cqpppVKNMGPNKIQVwqyqTVRL--AVTFEAHIQCNISrgLLYRWTIYD 417
Cdd:TIGR00864 1511 -----VRGLTINASLT----NVPLngSVHFEAHLDAGDD--VRFSWILCD 1549
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 2185-2276 3.24e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.00  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2185 MEGKdTVLVEFYAPWCGHCKQFAPEYEKIAKT---------------------LKENDPPIPVAkVDATkaSALGSRFEV 2243
Cdd:COG0526     26 LKGK-PVLVNFWATWCPPCRAEMPVLKELAEEyggvvfvgvdvdenpeavkafLKELGLPYPVL-LDPD--GELAKAYGV 101

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1564305953 2244 SGYPTIKIL-KKGEPVDYD-GDRSEQAIVERVKEV 2276
Cdd:COG0526    102 RGIPTTVLIdKDGKIVARHvGPLSPEELEEALEKL 136
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 2653-2746 3.27e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 52.00  E-value: 3.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2653 KDVLIEFYAPWCGHCKKLEPDYTALGKKYKN----------EKNLVIAKMDATANDIPH---------DSYKAEGFPTIY 2713
Cdd:COG0526     29 KPVLVNFWATWCPPCRAEMPVLKELAEEYGGvvfvgvdvdeNPEAVKAFLKELGLPYPVlldpdgelaKAYGVRGIPTTV 108

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564305953 2714 FApsNKKQNPVKFEGGKRDVEELSKFVEKHATK 2746
Cdd:COG0526    109 LI--DKDGKIVARHVGPLSPEELEEALEKLLAK 139
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 2292-2374 3.35e-07

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 50.35  E-value: 3.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2292 TKDNFDDVVNNA--DIILVEFYAPWCGHCKRLAPEYEKAAKElsnRTPPIPLAKVDATAESELATRFGVSGYPTLKIFRK 2369
Cdd:cd02984      1 SEEEFEELLKSDasKLLVLHFWAPWAEPCKQMNQVFEELAKE---AFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRN 77


                   ....*
gi 1564305953 2370 GKAFD 2374
Cdd:cd02984     78 GTIVD 82
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 2177-2259 4.23e-07

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 50.35  E-value: 4.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2177 TDENFDTFMEG--KDTVLVEFYAPWCGHCKQFAPEYEKIAktlKENDPPIPVAKVDATKASALGSRFEVSGYPTIKILKK 2254
Cdd:cd02984      1 SEEEFEELLKSdaSKLLVLHFWAPWAEPCKQMNQVFEELA---KEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRN 77


                   ....*
gi 1564305953 2255 GEPVD 2259
Cdd:cd02984     78 GTIVD 82
PKD pfam00801
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ...
 215-276 4.78e-07

PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold.


Pssm-ID: 395646 [Multi-domain]  Cd Length: 70  Bit Score: 49.31  E-value: 4.78e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564305953  215 ATETDIKFVAVTEGPDPLYFYWQFGDGPEIKTTSRIYKKRYRLPDKYSITVSVSNGLTSISS 276
Cdd:pfam00801    9 AAGQPVTFTATLADGSNVTYTWDFGDSPGTSGSGPTVTHTYLSPGTYTVTLTASNAVGSANA 70
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 2282-2371 6.41e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.84  E-value: 6.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2282 KPPPEATLvltKDNFDDVVNNAD----IILVEFYAPWCGHCKRLAPEYEKAAKELSN---------RTPPIPLAKVDAT- 2347
Cdd:COG0526      6 KPAPDFTL---TDLDGKPLSLADlkgkPVLVNFWATWCPPCRAEMPVLKELAEEYGGvvfvgvdvdENPEAVKAFLKELg 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564305953 2348 --------AESELATRFGVSGYPTLKIF-RKGK 2371
Cdd:COG0526     83 lpypvlldPDGELAKAYGVRGIPTTVLIdKDGK 115
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
1484-1578 6.89e-07

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 49.95  E-value: 6.89e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  1484 YAVTVDTGLRSRTRMTAKVHIVLYGDKSVSQTRELSSSHSKLFTCNSRNTFILSSPESLGRVWKVHLWHDNggSSPSWYL 1563
Cdd:smart00308    3 YKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEH--RHPEWFL 80

                            90
                    ....*....|....*.
gi 1564305953  1564 SHVVVKDLV-QGSCWF 1578
Cdd:smart00308   81 KSITVKDLPtGGKYHF 96
PTZ00051 PTZ00051
thioredoxin; Provisional
 2635-2693 7.92e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 46.79  E-value: 7.92e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1564305953 2635 PVKVVVGKTFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYkneKNLVIAKMD 2693
Cdd:PTZ00051     1 MVHIVTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEY---TKMVFVKVD 56
PDI_a_APS_reductase cd02993
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ...
 2307-2381 9.08e-06

PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly.


Pssm-ID: 239291 [Multi-domain]  Cd Length: 109  Bit Score: 46.68  E-value: 9.08e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953 2307 LVEFYAPWCGHCKRLAPEYEKAAKELSNRTppIPLAKVDATAESELATR--FGVSGYPTLKIFRKGKAFDYNGPREK 2381
Cdd:cd02993     25 LVVLYAPWCPFCQAMEASYEELAEKLAGSN--VKVAKFNADGEQREFAKeeLQLKSFPTILFFPKNSRQPIKYPSEQ 99
PKD_4 pfam18911
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.
 311-352 1.72e-05

PKD domain; This entry is composed of PKD domains found in bacterial surface proteins.


Pssm-ID: 436824 [Multi-domain]  Cd Length: 85  Bit Score: 45.34  E-value: 1.72e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564305953  311 SSGTDVSYIWNFGDGTERNGSSTEhHVYDRTGEYIVQVIMSN 352
Cdd:pfam18911   30 PDGDILSYRWDFGDGTTATGANVS-HTYAAPGTYTVTLTVTD 70
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 2656-2714 1.96e-05

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 44.61  E-value: 1.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1564305953 2656 LIEFYAPWCGHCKKLEPDYTALGKKYkneKNLVIAKMDATANDIPHDS---YKAEGFPTIYF 2714
Cdd:cd01659      1 LVLFYAPWCPFCQALRPVLAELALLN---KGVKFEAVDVDEDPALEKElkrYGVGGVPTLVV 59
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 311-366 2.16e-05

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 44.79  E-value: 2.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953  311 SSGTDVSYIWNFGDGTER-NGSSTEHHVYDRTGEYIVQVIMSNLVSSASLTGHIFVV 366
Cdd:cd00146     25 SGGSIVSYKWDFGDGEVSsSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 2305-2368 2.19e-05

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 45.57  E-value: 2.19e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564305953 2305 IILVEFYAPWCGHCKRLAPEYEKAAKELSNRtppIPLAKVDATAESELATRFGVSGYPTLKIFR 2368
Cdd:cd02949     15 LILVLYTSPTCGPCRTLKPILNKVIDEFDGA---VHFVEIDIDEDQEIAEAAGIMGTPTVQFFK 75
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 2187-2276 2.63e-05

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 46.56  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2187 GKDTvLVEFYAPWCGHCKQFAPEYEKIAKTLKENdppIPVA--KVDATKASALGSRFEVSGYPTIKILkkgepvDYDGDR 2264
Cdd:cd02950     20 GKPT-LVEFYADWCTVCQEMAPDVAKLKQKYGDQ---VNFVmlNVDNPKWLPEIDRYRVDGIPHFVFL------DREGNE 89

                           90
                   ....*....|..
gi 1564305953 2265 SEQAIVERVKEV 2276
Cdd:cd02950     90 EGQSIGLQPKQV 101
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 2306-2367 2.82e-05

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 46.44  E-value: 2.82e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1564305953 2306 ILVEFYAPWCGHCKRL------APEYEKAAKE--------LSNRTPPIPLAKVdATAESELATRFGVSGYPTLKIF 2367
Cdd:COG2143     43 ILLFFESDWCPYCKKLhkevfsDPEVAAYLKEnfvvvqldAEGDKEVTDFDGE-TLTEKELARKYGVRGTPTLVFF 117
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 229-419 3.55e-05

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 49.70  E-value: 3.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  229 PDP--LYFYWQFGDGPEIKTTSR-----IYKKRyrlpDKYSITVSVSNGLTSISSDVYlVRIQRAVQPNRLLYSSSVLLH 301
Cdd:TIGR00864 1113 PSPggIHYEWDFGDGSALLQGRQpaaahTFAKR----GPFHVCLEVNNTISGAAACAD-MFAFEEIEGLSADMSLATELG 1187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  302 SSVNFTCRISSGTDVSYIWNFGDGTERNGS-STEHHVYDRTGEYIVQVIMSNLVSSASLTGHIFV-VEESCQPPPVKNMG 379
Cdd:TIGR00864 1188 AATTVRAALQSGDNITWTFDMGDGKSLSGPeATVEHKYAKAGNCTVNIGAANAAGHGARIIHVEVfVFEVAGIEPAACIG 1267

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1564305953  380 PNKIqvwqyqtvrlaVTFEAHIQCNISRgLLYRWTIYDMS 419
Cdd:TIGR00864 1268 EHAD-----------ANFRARVSGNAAH-YLFDWSFGDGS 1295
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
2186-2249 4.27e-05

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 44.72  E-value: 4.27e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953 2186 EGKDTVLVeFYAPWCGHCKQFAPE---YEKIAKTLKENDPPIPV----------AKVDATKASALGSRFEVSGYPTI 2249
Cdd:pfam13098    3 NGKPVLVV-FTDPDCPYCKKLKKElleDPDVTVYLGPNFVFIAVniwcakevakAFTDILENKELGRKYGVRGTPTI 78
COG3291 COG3291
Uncharacterized conserved protein, PKD repeat domain [Function unknown];
311-583 4.65e-05

Uncharacterized conserved protein, PKD repeat domain [Function unknown];


Pssm-ID: 442520 [Multi-domain]  Cd Length: 333  Bit Score: 48.13  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  311 SSGTDVSYIWNFGDGTerngSSTEH---HVYDRTGEYIVQVIMSNLV-SSASLTGHIFVVEESCQPPPVKNMG-PNKIQV 385
Cdd:COG3291     20 SSGNATSYEWDFGDGT----TSTEAnpsHTYTTPGTYTVTLTVTDAAgCSDTTTKTITVGAPNPGVTTVTTSTtVTTLAN 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  386 WQYQTVRLAVTFEAHIQCNISRGLLYRWTIYDMSGQQlllpHIDTGRQYINLPKYLLHYGTYKAIAKVQITGSVVYSNYS 465
Cdd:COG3291     96 TANGGATTVVAGSTVGTGVATSTTTAAAPGGGGGTGT----TTTTGTDTGLTGSTGTASDTATVTTSVSTTDVTSDGTTS 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  466 VLIEVIRSHPVSVISEATNIFINRQSSTIVTLDGRKSHDPDYPNNTISYSWSCRPVNTEESSCFNRNIVTTSAVLTFPAL 545
Cdd:COG3291    172 ASTNPSVTTDTVTTLTGSYTGTIVGGSGSGTVTSGTAGVTTGATSGTSGTGSATSGVAVTDVTLTGISTGDAGTPGTNTV 251

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1564305953  546 ALKSDFDLLKFTLTVYSGHRSSASNMFITVTSKPVSNV 583
Cdd:COG3291    252 TTSGANTAGTSTITGGTSGVVTTSAATGTSTNGTGGLG 289
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 2186-2255 4.95e-05

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 44.52  E-value: 4.95e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953 2186 EGKdTVLVEFYAPWCGHCKQFAPEY---EKIAKTLKENdppIPVAKVDATKAS----ALGSRFEVSGYPTIKILKKG 2255
Cdd:cd02953     10 QGK-PVFVDFTADWCVTCKVNEKVVfsdPEVQAALKKD---VVLLRADWTKNDpeitALLKRFGVFGPPTYLFYGPG 82
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 2646-2741 5.25e-05

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 45.40  E-value: 5.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2646 EIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEKNLVIAKMDATANDIPHDSYKAEGFPTIYFApsNKKQNPVK 2725
Cdd:cd02950     14 EVALSNGKPTLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFVMLNVDNPKWLPEIDRYRVDGIPHFVFL--DREGNEEG 91

                           90
                   ....*....|....*.
gi 1564305953 2726 FEGGKRDVEELSKFVE 2741
Cdd:cd02950     92 QSIGLQPKQVLAQNLD 107
trxA PRK09381
thioredoxin TrxA;
2643-2712 5.82e-05

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 44.67  E-value: 5.82e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2643 TFDEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEknLVIAKMDATANDIPHDSYKAEGFPTI 2712
Cdd:PRK09381    12 SFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGK--LTVAKLNIDQNPGTAPKYGIRGIPTL 79
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 2174-2258 6.84e-05

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 44.53  E-value: 6.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2174 LVLTDENFDTF----MEGKdTVLVEFYAPWCGHCKQFAPEYEKIAKT------------------------LKENDPPIP 2225
Cdd:cd02966      2 FSLPDLDGKPVslsdLKGK-VVLVNFWASWCPPCRAEMPELEALAKEykddgvevvgvnvddddpaavkafLKKYGITFP 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1564305953 2226 VAkVDATkaSALGSRFEVSGYPTIKIL-KKGEPV 2258
Cdd:cd02966     81 VL-LDPD--GELAKAYGVRGLPTTFLIdRDGRIR 111
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
2302-2382 1.73e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 43.18  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2302 NADIILVEFYAPWCGHCKRLAPE---YEKAAKELSNRTPPIPL----------AKVDATAESELATRFGVSGYPTLKIF- 2367
Cdd:pfam13098    3 NGKPVLVVFTDPDCPYCKKLKKElleDPDVTVYLGPNFVFIAVniwcakevakAFTDILENKELGRKYGVRGTPTIVFFd 82

                           90
                   ....*....|....*..
gi 1564305953 2368 RKGKAFDYNG--PREKF 2382
Cdd:pfam13098   83 GKGELLRLPGyvPAEEF 99
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 2656-2739 2.51e-04

PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 42.51  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2656 LIEFYAPWCGHCKKLEPDYTALGKKYknEKNLVIAKMDATANDIPHDSYKAEGFPTIYFAPSNkkQNPVKFEgGKRDVEE 2735
Cdd:cd03003     22 FVNFYSPRCSHCHDLAPTWREFAKEM--DGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSG--MNPEKYY-GDRSKES 96


                   ....
gi 1564305953 2736 LSKF 2739
Cdd:cd03003     97 LVKF 100
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 2305-2371 2.63e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 42.99  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2305 IILVEFYAPWCGHCKRLAPEYEKAAKELSNRTPPI--------PLAKVDATAE-------------SELATRFGVSGYPT 2363
Cdd:cd02966     21 VVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVvgvnvdddDPAAVKAFLKkygitfpvlldpdGELAKAYGVRGLPT 100


                   ....*....
gi 1564305953 2364 LKIF-RKGK 2371
Cdd:cd02966    101 TFLIdRDGR 109
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 2176-2260 3.83e-04

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 42.67  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2176 LTDENFDTF-MEGKdTVLVEFYAPWCGHCK-------QFAPEY------------EKIAKTLKENDPPIPVAkvdATKAS 2235
Cdd:cd03011      8 LDGEQFDLEsLSGK-PVLVYFWATWCPVCRftsptvnQLAADYpvvsvalrsgddGAVARFMQKKGYGFPVI---NDPDG 83

                           90       100
                   ....*....|....*....|....*
gi 1564305953 2236 ALGSRFEVSGYPTIKILKKGEPVDY 2260
Cdd:cd03011     84 VISARWGVSVTPAIVIVDPGGIVFV 108
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 2186-2262 4.79e-04

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 42.60  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2186 EGKdTVLVEFYAPWCGHCKQFAPE----YEKIAKT---------------------LKENDPPIPVAKVDATKASALGSR 2240
Cdd:cd02964     16 EGK-TVGLYFSASWCPPCRAFTPKlvefYEKLKEEgknfeivfvsrdrseesfneyFSEMPPWLAVPFEDEELRELLEKQ 94

                           90       100
                   ....*....|....*....|...
gi 1564305953 2241 FEVSGYPTIKILK-KGEPVDYDG 2262
Cdd:cd02964     95 FKVEGIPTLVVLKpDGDVVTTNA 117
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 2307-2372 5.37e-04

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 42.71  E-value: 5.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953 2307 LVEFYAPWCGHCKRLAPEYEKAAKELSNRTpPIPLAKVDATAESELATRFGVSGYPTLKIF-RKGKA 2372
Cdd:cd02950     24 LVEFYADWCTVCQEMAPDVAKLKQKYGDQV-NFVMLNVDNPKWLPEIDRYRVDGIPHFVFLdREGNE 89
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 2645-2730 5.62e-04

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 41.49  E-value: 5.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2645 DEIVMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNEknLVIAKMDATANDIPHDSYKAEGFPTIYFApsnKKQNPV 2724
Cdd:cd02956      5 QVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQ--FVLAKVNCDAQPQIAQQFGVQALPTVYLF---AAGQPV 79


                   ....*..
gi 1564305953 2725 K-FEGGK 2730
Cdd:cd02956     80 DgFQGAQ 86
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 2302-2331 5.71e-04

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 42.97  E-value: 5.71e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1564305953 2302 NADIILVEFYAPWCGHCKRLAPEYEKAAKE 2331
Cdd:cd03023      4 NGDVTIVEFFDYNCGYCKKLAPELEKLLKE 33
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 2306-2372 6.26e-04

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 41.43  E-value: 6.26e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1564305953 2306 ILVEFYAPWCGHCK---RLAPEYEKAAKELSNRtppIPLAKVDATAES----ELATRFGVSGYPTLKIFRKGKA 2372
Cdd:cd02953     14 VFVDFTADWCVTCKvneKVVFSDPEVQAALKKD---VVLLRADWTKNDpeitALLKRFGVFGPPTYLFYGPGGE 84
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 2278-2371 7.30e-04

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 42.37  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2278 QPDWKPPPEATLVLTKDNFDDVVNNADII-LVEFYAPWCGHCKRLAPEYekaaKELSNR--TPPIPLAKVDATAESELAT 2354
Cdd:cd02962     21 QPLYMGPEHIKYFTPKTLEEELERDKRVTwLVEFFTTWSPECVNFAPVF----AELSLKynNNNLKFGKIDIGRFPNVAE 96

                           90       100
                   ....*....|....*....|...
gi 1564305953 2355 RFGVSGY------PTLKIFRKGK 2371
Cdd:cd02962     97 KFRVSTSplskqlPTIILFQGGK 119
PDI_b_Calsequestrin_N cd03065
PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major ...
 2165-2271 8.35e-04

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: 41.65  E-value: 8.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2165 PDSEEENGVLVLTDENFDTFMEGKDTVLVEFYAPWCGHC---KQFAPE---YEKIAKTLKENDppIPVAKVDATKASALG 2238
Cdd:cd03065      3 PEYDGKDRVIDLNEKNYKQVLKKYDVLCLLYHEPVESDKeaqKQFQMEelvLELAAQVLEDKG--IGFGLVDSKKDAKVA 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1564305953 2239 SRFEVSGYPTIKILKKGEPVDYDGDRSEQAIVE 2271
Cdd:cd03065     81 KKLGLDEEDSIYVFKDDEVIEYDGEFAADTLVE 113
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 224-433 1.04e-03

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 45.07  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  224 AVTEGPDPLyFYWQFGDGPEIKTTSRIYKKRYRLPDKYSITVSVSNGLTSISSDvYLVRIQRaVQPNRLLYSSSVLLHSS 303
Cdd:TIGR00864  917 SVEAGSDMT-FKWTIDDKPFFTFQNTVFNVIYQHAAVFKLSLTAMNHVSNLTED-FNVTVDR-LNPMQGLQVKGVPAVLP 993

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  304 VNFTCRISSG------TDVSYIWNFGDGTER--------NGSST-----------EH---HVYDRTGEYIVQVIMSNlvS 355
Cdd:TIGR00864  994 PGATLALTAGvlidmaVEAAFLWSFGDGEQAlfefkppyNESFPcpdpspaqvllEHnvmHIYAAPGEYLATVLASN--A 1071

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  356 SASLTGHIFVVEESCQPppvknmgpnKIQVWQYQTVRLA---VTFEAHiQCNISRGLLYRWTIYDmsGQQLLlphidTGR 432
Cdd:TIGR00864 1072 FENISQQINMSVRAILP---------RVAIGTEDGLLLAgkpADFEAH-PLPSPGGIHYEWDFGD--GSALL-----QGR 1134


                   .
gi 1564305953  433 Q 433
Cdd:TIGR00864 1135 Q 1135
PDI_a_EFP1_N cd03006
PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase ...
 2294-2335 1.04e-03

PDIa family, N-terminal EFP1 subfamily; EFP1 is a binding partner protein of thyroid oxidase (ThOX), also called Duox. ThOX proteins are responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. EFP1 was isolated through a yeast two-hybrid method using the EF-hand fragment of dog Duox1 as a bait. It could be one of the partners in the assembly of a multiprotein complex constituting the thyroid hydrogen peroxide generating system. EFP1 contains two TRX domains related to the redox active TRX domains of protein disulfide isomerase (PDI). This subfamily is composed of the N-terminal TRX domain of EFP1, which contains a CXXS sequence in place of the typical CXXC motif, similar to ERp44. The CXXS motif allows the formation of stable mixed disulfides, crucial for the ER-retention function of ERp44.


Pssm-ID: 239304  Cd Length: 113  Bit Score: 40.92  E-value: 1.04e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1564305953 2294 DNFDDVVNNADIILVEFYAPWCGHCKRLAPEYEKAAKELSNR 2335
Cdd:cd03006     20 DYAEELRTDAEVSLVMYYAPWDAQSQAARQEFEQVAQKLSDQ 61
PDI_b_Calsequestrin_middle cd03066
PDIb family, Calsequestrin subfamily, Middle TRX-fold domain; Calsequestrin is the major ...
 2404-2501 1.54e-03

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: 40.10  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2404 QVQELIRDGDDAVIVGVFSSEEDAVYEIYQEACNSLREDYKFMHTFNNEVAKFLKASPGQVVMLQPekFRSkyEPashsL 2483
Cdd:cd03066     10 ELQAFENIEDDIKLIGYFKSEDSEHYKAFEEAAEEFHPYIKFFATFDSKVAKKLGLKMNEVDFYEP--FME--EP----V 81

                           90       100
                   ....*....|....*....|
gi 1564305953 2484 TLKDStPAS--EVQEFFKKH 2501
Cdd:cd03066     82 TIPDK-PYSeeELVDFVEEH 100
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 2644-2740 1.64e-03

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 40.45  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2644 FDEIvMDTKKDVLIEFYAPWCGHCKKLEPDYTALGKKYKNE----KNLVIAKMDATANDIPHDSYKAEGFPTIyfapsnk 2719
Cdd:cd02996     11 IDDI-LQSAELVLVNFYADWCRFSQMLHPIFEEAAAKIKEEfpdaGKVVWGKVDCDKESDIADRYRINKYPTL------- 82

                           90       100
                   ....*....|....*....|....*....
gi 1564305953 2720 kqnPVKFEG--------GKRDVEELSKFV 2740
Cdd:cd02996     83 ---KLFRNGmmmkreyrGQRSVEALAEFV 108
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 2189-2255 2.36e-03

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 39.60  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2189 DTVLVEFYAPWCGHCKQFAPEYEKIAKTLKENDPPIPVA------------------------KVDATKASALGSRFEVS 2244
Cdd:pfam13905    2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIVFvsldrdleefkdylkkmpkdwlsvPFDDDERNELKRKYGVN 81

                           90
                   ....*....|.
gi 1564305953 2245 GYPTIKILKKG 2255
Cdd:pfam13905   82 AIPTLVLLDPN 92
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 2171-2280 3.26e-03

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 42.23  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2171 NGVLVLTDENFDTFMEGKD--TVLVEFYAPW----CGHCKQFAPEYEKIA----KTLKENDPPIPVAKVDATKASALGSR 2240
Cdd:pfam04756   11 NGVIKLNDSNYKRLLSGPRdySVVVLLTALDprfgCQLCREFQPEFELVAkswfKDHKAGSSKLFFATLDFDDGKDVFQS 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1564305953 2241 FEVSGYPTI--------KILKKGEPVDYD---GDRSEQAIVERVKEVAQPD 2280
Cdd:pfam04756   91 LGLQTAPHLllfpptggPKISDSEPDQYDftrGGFSAEQLAAFLSRHTGVP 141
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 1484-1595 3.73e-03

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 39.60  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 1484 YAVTVDTG--LRSRTRmtAKVHIVLYGDKSVSQTRELSSShSKLFTCNSRNTFILSSPESLG-----RVWKVHLWHDNgg 1556
Cdd:cd01753      3 YKVTVATGssLFAGTD--DYIYLTLVGTAGESEKQLLDRP-GYDFERGAVDEYKVKVPEDLGelllvRLRKRKYLLFD-- 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1564305953 1557 sspSWYLSHVVVKDLvQGSCWFFLGQCWLavdEGDGRVE 1595
Cdd:cd01753     78 ---AWFCNYITVTGP-GGDEYHFPCYRWI---EGYGTLE 109
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 2186-2258 3.91e-03

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 40.27  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953 2186 EGKdTVLVEFYAPWCGHCKQ-----FAPeyEKIAKTLKENdppIPVAKVDA-------------TKASALGSRFEVSGYP 2247
Cdd:COG2143     39 EGK-PILLFFESDWCPYCKKlhkevFSD--PEVAAYLKEN---FVVVQLDAegdkevtdfdgetLTEKELARKYGVRGTP 112

                           90
                   ....*....|..
gi 1564305953 2248 TIKIL-KKGEPV 2258
Cdd:COG2143    113 TLVFFdAEGKEI 124
PKD cd00146
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ...
 208-283 4.45e-03

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.


Pssm-ID: 238084 [Multi-domain]  Cd Length: 81  Bit Score: 38.25  E-value: 4.45e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1564305953  208 FSDTRAYATETDIKFVA-VTEGPDPLYFYWQFGDGPEIKTTSRIYKKRYRLPDKYSITVSVSNGLTSISSDVYLVRI 283
Cdd:cd00146      5 VSAPPVAELGASVTFSAsDSSGGSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTVTNAVGSSSTKTTTVVV 81
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 216-521 6.95e-03

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 41.99  E-value: 6.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  216 TETDIKFVA-VTEGPDPLYFYWQFGDGPEIKT------TSRIYKKRYRLPDKYSIT--VSVSNGLTSISSDVYLVRIqrA 286
Cdd:TIGR00864 1268 EHADANFRArVSGNAAHYLFDWSFGDGSPNEThhgcpgISHNFRGNGTFPLALTISsgVNKAHFFTQICVEPELGKI--S 1345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  287 VQPNRLLYSSSVLLHssvnFTCRISSGTDVSYIWNFG---DGTERNGSSTEHHVYDRTGEYIVQVIMSNLVSSASLTGHI 363
Cdd:TIGR00864 1346 LQAEKQFFALGDEAQ----FQACAEPEFNYRYEWDFGgeeAAPLPAAGAEVTFIYNDPGCYLVTVAASNNISAANDSALI 1421

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  364 FVVEescqppPVknmGPNKIQV--WQYQTVRLAVT--FEAhiqcnISRG--LLYRWTIYD---MSGQQLLLPHIDTGrqy 434
Cdd:TIGR00864 1422 EVLE------PV---GATSFKHngSHGNNLELGQPylFSA-----FGRArnASYLWDFGDgglLEGPEILHAFNSPG--- 1484

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564305953  435 inlpkyllHYgtykaiaKVQITGSVvysnysvliEVIRSH---PVSVISEATNIFINrQSSTIVTLDGRKSHDPDY-PNN 510
Cdd:TIGR00864 1485 --------DF-------NIRLAAAN---------EVGKNEatlNVAVKARVRGLTIN-ASLTNVPLNGSVHFEAHLdAGD 1539

                          330
                   ....*....|....*
gi 1564305953  511 TISYSW----SCRPV 521
Cdd:TIGR00864 1540 DVRFSWilcdHCTPI 1554
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 2191-2221 8.79e-03

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 39.21  E-value: 8.79e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1564305953 2191 VLVEFYAPWCGHCKQFAPEYEKIAKTLKEND 2221
Cdd:COG1651      3 TVVEFFDYQCPYCARFHPELPELLKKYVDGK 33
 
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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