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Conserved domains on  [gi|225579134|ref|NP_001139474|]
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thioredoxin domain-containing protein 2 isoform 1 [Mus musculus]

Protein Classification

thioredoxin( domain architecture ID 13312445)

thioredoxin is a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 454-546 3.12e-27

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: 104.95  E-value: 3.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 454 EEFEEVLKDAgeKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVGE 533
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....
gi 225579134 534 FSGAL-VGKLERSI 546
Cdd:cd02947   79 VVGADpKEELEEFL 92
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 126-395 6.71e-08

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 55.47  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 126 TQLKQEnISKSSGYSKQTNYSNTPKSLAKTTHPKQG---STLKPATNSTHYREDDIPKSSEDIIQPKKGDRPKSSEDIIQ 202
Cdd:PTZ00449 479 IQFTQE-IKKLIKKSKKKLAPIEEEDSDKHDEPPEGpeaSGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEV 557

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 203 SKK---EDRPKSSEDIIQSKKED---RPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSV 276
Cdd:PTZ00449 558 GKKpgpAKEHKPSKIPTLSKKPEfpkDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPP 637

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 277 PSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQS--KEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHRPLKDS---- 350
Cdd:PTZ00449 638 PPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPkfKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTpftt 717

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 225579134 351 ---VQSKESEEPKSSHESIQSKEDKIHKPLKDSIP--SKEGDIPKSPEDT 395
Cdd:PTZ00449 718 prpLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADT 767
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 454-546 3.12e-27

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: 104.95  E-value: 3.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 454 EEFEEVLKDAgeKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVGE 533
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....
gi 225579134 534 FSGAL-VGKLERSI 546
Cdd:cd02947   79 VVGADpKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 452-549 9.22e-23

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: 92.96  E-value: 9.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEE-VLKdaGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHED-VIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEE 529
Cdd:COG3118    6 TDENFEEeVLE--SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQ 83

                         90       100
                 ....*....|....*....|.
gi 225579134 530 KVGEFSGAL-VGKLERSISEL 549
Cdd:COG3118   84 PVDRFVGALpKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 449-537 3.02e-21

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: 88.44  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  449 VIKDKEEFEEVLKDAgEKLVAVDFSAAWCGPCRMMKPLFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKN 527
Cdd:pfam00085   3 VVLTDANFDEVVQKS-SKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90
                  ....*....|
gi 225579134  528 EEKVGEFSGA 537
Cdd:pfam00085  82 GQPVDDYVGA 91
PTZ00051 PTZ00051
thioredoxin; Provisional
 446-537 2.96e-19

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 83.00  E-value: 2.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 446 LVRVIKDKEEFEEVLkdAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFY 525
Cdd:PTZ00051   1 MVHIVTSQAEFESTL--SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVF 78

                         90
                 ....*....|..
gi 225579134 526 KNEEKVGEFSGA 537
Cdd:PTZ00051  79 KNGSVVDTLLGA 90
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 451-538 3.68e-15

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: 71.17  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  451 KDKEEFEEVLKDaGEKLVAVDFSAAWCGPCRMMKPLFHSLSLK-HEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEE 529
Cdd:TIGR01068   1 LTDANFDETIAS-SDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79


                  ....*....
gi 225579134  530 KVGEFSGAL 538
Cdd:TIGR01068  80 EVDRSVGAL 88
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 126-395 6.71e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 55.47  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 126 TQLKQEnISKSSGYSKQTNYSNTPKSLAKTTHPKQG---STLKPATNSTHYREDDIPKSSEDIIQPKKGDRPKSSEDIIQ 202
Cdd:PTZ00449 479 IQFTQE-IKKLIKKSKKKLAPIEEEDSDKHDEPPEGpeaSGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEV 557

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 203 SKK---EDRPKSSEDIIQSKKED---RPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSV 276
Cdd:PTZ00449 558 GKKpgpAKEHKPSKIPTLSKKPEfpkDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPP 637

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 277 PSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQS--KEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHRPLKDS---- 350
Cdd:PTZ00449 638 PPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPkfKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTpftt 717

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 225579134 351 ---VQSKESEEPKSSHESIQSKEDKIHKPLKDSIP--SKEGDIPKSPEDT 395
Cdd:PTZ00449 718 prpLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADT 767
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 74-444 1.45e-05

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 47.97  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134    74 SKEKAIASKVSNTLHMSTEESEFPQQvsstPMFSENTVHPRHEvspKPSSKNTQLKQENISKSSGYSKQTNYSNTPKSLA 153
Cdd:TIGR00600  308 SDDESLPSLSSQLDSNSEDLKSSPWE----KLKPESESIVEAE---PPSPRTLLAKQAAMSESSSEDSDESEWERQELKR 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   154 KTTHPKQGSTLKPATNSTHYR--EDDIPKSSEDIIQPKKGDRPKSSEDIIQS--KKEDRPKSSEDIIQSKKEDRPKSSED 229
Cdd:TIGR00600  381 NNVAFVDDGSLSPRTLQAIGQalDDDEDKKVSASSDDQASPSKKTKMLLISRieVEDDDLDYLDQGEGIPLMAALQLSSV 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   230 IIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSE-------DSVPSKKGDRPKSSEDSVQPKKEDRPKSS 302
Cdd:TIGR00600  461 NSKPEAVASTKIAREVTSSGHEAVPKAVQSLLLGATNDSPIPSEftildrkSELSIERTVKPVSSEFGLPSQREDKLAIP 540

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   303 EDSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKThrplkdsvqsKESEEPKSSHESIQSKEDKIHKPLKDSIP 382
Cdd:TIGR00600  541 TEGTQNLQGISDHPEQFEFQNELSPLETKNNESNLSSDAET----------EGSPNPEMPSWSSVTVPSEALDNYETTNP 610

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579134   383 SKEGDIPKSPEDTIQSQEEITASEEDTIQSQEGNTIKSSEEDVQLSESKLLGLGAEIETLEE 444
Cdd:TIGR00600  611 SNAKEVRNFAETGIQTTNVGESADLLLISNPMEVEPMESEKEESESDGSFIEVDSVSSTLEL 672
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 119-423 1.21e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.00  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 119 PKPSSKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQGST---LKPATNSTHYREDDIPKSSEDIIQPKKGDRPK 195
Cdd:NF033838 137 PGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESdveVKKAELELVKEEAKEPRDEEKIKQAKAKVESK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 196 SSEDIIQSK-KEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKssediiqsKKEDRPKSSEDIIQPKKEDRPKSSED 274
Cdd:NF033838 217 KAEATRLEKiKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPK--------RRAKRGVLGEPATPDKKENDAKSSDS 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 275 SV-----PS---KKGDRPKSSEDSVQP--------KKEDRP------------KSSEDSVQSKEGEVHKPLKDSIQSKET 326
Cdd:NF033838 289 SVgeetlPSpslKPEKKVAEAEKKVEEakkkakdqKEEDRRnyptntyktlelEIAESDVKVKEAELELVKEEAKEPRNE 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 327 KVPKSPQDSIQSKEDKTHR--PLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDTIQSQEEITA 404
Cdd:NF033838 369 EKIKQAKAKVESKKAEATRleKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPA 448

                        330
                 ....*....|....*....
gi 225579134 405 SEedtiQSQEGNTIKSSEE 423
Cdd:NF033838 449 DQ----QAEEDYARRSEEE 463
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 237-431 3.83e-03

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 39.91  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  237 DRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSVPSK-KGDRPKSSEDSVQPKKEDRPKSSEDSVQSKEGEVHK 315
Cdd:pfam07263 282 DDSNTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQsQEDSQNSQDPSSESSQEADLPSQESSSESQEEVVSE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  316 PLKDSIQSKETKVPKSPqDSIQSKEDKTHRPLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDT 395
Cdd:pfam07263 362 SRGDNPDNTSSSEEDQE-DSDSSEEDSLSTFSSSESESREEQADSESNESLRSSEESPESSEDENSSSQEGLQSHSASTE 440

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 225579134  396 IQSQE----EITASEEDTIQSQEGNTikSSEEDVQLSESK 431
Cdd:pfam07263 441 SQSEEsqseQDSQSEEDDESDSQDSS--RSKEDSNSTEST 478
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 454-546 3.12e-27

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: 104.95  E-value: 3.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 454 EEFEEVLKDAgeKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVGE 533
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                         90
                 ....*....|....
gi 225579134 534 FSGAL-VGKLERSI 546
Cdd:cd02947   79 VVGADpKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 452-549 9.22e-23

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: 92.96  E-value: 9.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEE-VLKdaGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHED-VIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEE 529
Cdd:COG3118    6 TDENFEEeVLE--SDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQ 83

                         90       100
                 ....*....|....*....|.
gi 225579134 530 KVGEFSGAL-VGKLERSISEL 549
Cdd:COG3118   84 PVDRFVGALpKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 449-537 3.02e-21

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: 88.44  E-value: 3.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  449 VIKDKEEFEEVLKDAgEKLVAVDFSAAWCGPCRMMKPLFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKN 527
Cdd:pfam00085   3 VVLTDANFDEVVQKS-SKPVLVDFYAPWCGPCKMLAPEYEELAQEYkGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKN 81

                          90
                  ....*....|
gi 225579134  528 EEKVGEFSGA 537
Cdd:pfam00085  82 GQPVDDYVGA 91
PTZ00051 PTZ00051
thioredoxin; Provisional
 446-537 2.96e-19

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 83.00  E-value: 2.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 446 LVRVIKDKEEFEEVLkdAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFY 525
Cdd:PTZ00051   1 MVHIVTSQAEFESTL--SQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVF 78

                         90
                 ....*....|..
gi 225579134 526 KNEEKVGEFSGA 537
Cdd:PTZ00051  79 KNGSVVDTLLGA 90
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 451-538 3.68e-15

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: 71.17  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  451 KDKEEFEEVLKDaGEKLVAVDFSAAWCGPCRMMKPLFHSLSLK-HEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEE 529
Cdd:TIGR01068   1 LTDANFDETIAS-SDKPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79


                  ....*....
gi 225579134  530 KVGEFSGAL 538
Cdd:TIGR01068  80 EVDRSVGAL 88
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 452-542 5.07e-14

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.


Pssm-ID: 239283  Cd Length: 103  Bit Score: 68.28  E-value: 5.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEEVLKDAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEV---DTEDCEQLVQDCEIFHLPTFQFYKNE 528
Cdd:cd02985    2 SVEELDEALKKAKGRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDG 81

                         90
                 ....*....|....
gi 225579134 529 EKVGEFSGALVGKL 542
Cdd:cd02985   82 EKIHEEEGIGPDEL 95
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 453-542 5.63e-12

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: 61.90  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 453 KEEFEEVLKDAGEKLVAVDFSAAWCGPCRMMKPLFHSLS-LKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKV 531
Cdd:cd02984    2 EEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAkEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIV 81

                         90
                 ....*....|.
gi 225579134 532 GEFSGALVGKL 542
Cdd:cd02984   82 DRVSGADPKEL 92
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 452-536 1.73e-11

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: 60.70  E-value: 1.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEEVLKDagEKLVAVDFSAAWCGPCRMMKPLFHSLSLK---HEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKN- 527
Cdd:cd02961    4 TDDNFDELVKD--SKDVLVEFYAPWCGHCKALAPEYEKLAKElkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNg 81


                 ....*....
gi 225579134 528 EEKVGEFSG 536
Cdd:cd02961   82 SKEPVKYEG 90
PRK10996 PRK10996
thioredoxin 2; Provisional
 454-538 7.04e-11

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 60.08  E-value: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 454 EEFEEVLKDagEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVI-FLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVG 532
Cdd:PRK10996  43 ETLDKLLQD--DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVrFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVD 120


                 ....*.
gi 225579134 533 EFSGAL 538
Cdd:PRK10996 121 MLNGAV 126
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 460-506 1.66e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 56.24  E-value: 1.66e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 225579134 460 LKDAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTED 506
Cdd:COG0526   23 LADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDE 69
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 450-549 5.22e-09

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 53.88  E-value: 5.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 450 IKDKEEFEEVLkdAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHED--VIFL--EVDT-EDCEQLVQDCEifhlPTFQF 524
Cdd:cd02948    4 INNQEEWEELL--SNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDdlLHFAtaEADTiDTLKRYRGKCE----PTFLF 77

                         90       100
                 ....*....|....*....|....*
gi 225579134 525 YKNEEKVGEFSGALVGKLERSISEL 549
Cdd:cd02948   78 YKNGELVAVIRGANAPLLNKTITEL 102
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 466-536 3.76e-08

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: 51.35  E-value: 3.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579134 466 KLVAVDFSAAWCGPCRMMKPLFHSLSLKH-EDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVGEFSG 536
Cdd:cd02949   14 RLILVLYTSPTCGPCRTLKPILNKVIDEFdGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 126-395 6.71e-08

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 55.47  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 126 TQLKQEnISKSSGYSKQTNYSNTPKSLAKTTHPKQG---STLKPATNSTHYREDDIPKSSEDIIQPKKGDRPKSSEDIIQ 202
Cdd:PTZ00449 479 IQFTQE-IKKLIKKSKKKLAPIEEEDSDKHDEPPEGpeaSGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEV 557

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 203 SKK---EDRPKSSEDIIQSKKED---RPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSV 276
Cdd:PTZ00449 558 GKKpgpAKEHKPSKIPTLSKKPEfpkDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPP 637

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 277 PSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQS--KEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHRPLKDS---- 350
Cdd:PTZ00449 638 PPQRPSSPERPEGPKIIKSPKPPKSPKPPFDPkfKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTpftt 717

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 225579134 351 ---VQSKESEEPKSSHESIQSKEDKIHKPLKDSIP--SKEGDIPKSPEDT 395
Cdd:PTZ00449 718 prpLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPpeEERTFFHETPADT 767
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 470-531 4.31e-07

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: 47.31  E-value: 4.31e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225579134 470 VDFSAAWCGPCRMMKPLFHSLSLKHEDVIFLEVDTEDC---EQLVQDCEIFHLPTFQFYKNEEKV 531
Cdd:cd01659    2 VLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDpalEKELKRYGVGGVPTLVVFGPGIGV 66
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 121-452 4.37e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 121 PSSKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQGSTLKPATNSTHYREDDIPKSSEDIIQPKKGDRPKssedi 200
Cdd:PTZ00449 524 PGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKKPK----- 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 201 iqskkedRPKSSEDIIQSKKEDRPKSSediiqskkeDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSVPskk 280
Cdd:PTZ00449 599 -------RPRSAQRPTRPKSPKLPELL---------DIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKP--- 659

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 281 gdrPKSSEDSVQPKKEDR--PKSSEDSVQSKEGEVHKPLKDSIQS-KETKVPKSPQDSIQSK----------EDKTHRPL 347
Cdd:PTZ00449 660 ---PKSPKPPFDPKFKEKfyDDYLDAAAKSKETKTTVVLDESFESiLKETLPETPGTPFTTPrplppklprdEEFPFEPI 736

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 348 KDSvqSKESEEPKSSHESIQSKEDKIHK-PLKDSIPSKEGDIPKSPEDTIQSQEEITASEEDTIQSQEGNTIKSSEEDVQ 426
Cdd:PTZ00449 737 GDP--DAEQPDDIEFFTPPEEERTFFHEtPADTPLPDILAEEFKEEDIHAETGEPDEAMKRPDSPSEHEDKPPGDHPSLP 814

                        330       340
                 ....*....|....*....|....*.
gi 225579134 427 LSESKLLGLGAEIETLEEGLVRVIKD 452
Cdd:PTZ00449 815 KKRHRLDGLALSTTDLESDAGRIAKD 840
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 107-372 5.84e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 49.30  E-value: 5.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 107 SENTVHPRHEVSPKPSSKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQ----GSTLKPATNSTHYRED------ 176
Cdd:PTZ00449 537 SKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDpeepKKPKRPRSAQRPTRPKspklpe 616

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 177 --DIPKSSEDIIQPKKGDRPKSSEDIIQSKKEDRP---KSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKE 251
Cdd:PTZ00449 617 llDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPkiiKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLD 696

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 252 DRPKSSEDIIQPKKEDRPKSSEDSVPSKkgdRPKSSEDSVQPKKEDRPKSSEDSvqskeGEVHKPLKDSIQSKETKvPKS 331
Cdd:PTZ00449 697 ESFESILKETLPETPGTPFTTPRPLPPK---LPRDEEFPFEPIGDPDAEQPDDI-----EFFTPPEEERTFFHETP-ADT 767

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 225579134 332 PQDSIQSKEDKTHrplKDSVQSKESEEPKSSHESIQSKEDK 372
Cdd:PTZ00449 768 PLPDILAEEFKEE---DIHAETGEPDEAMKRPDSPSEHEDK 805
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 470-550 1.40e-05

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: 43.81  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 470 VDFSAAWCGPCRMMKPLFHSLSLKHE----DVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVGEFSGAlvgkleRS 545
Cdd:cd03005   21 VKFFAPWCGHCKRLAPTWEQLAKKFNnenpSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT------RD 94


                 ....*
gi 225579134 546 ISELK 550
Cdd:cd03005   95 LDSLK 99
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 74-444 1.45e-05

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 47.97  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134    74 SKEKAIASKVSNTLHMSTEESEFPQQvsstPMFSENTVHPRHEvspKPSSKNTQLKQENISKSSGYSKQTNYSNTPKSLA 153
Cdd:TIGR00600  308 SDDESLPSLSSQLDSNSEDLKSSPWE----KLKPESESIVEAE---PPSPRTLLAKQAAMSESSSEDSDESEWERQELKR 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   154 KTTHPKQGSTLKPATNSTHYR--EDDIPKSSEDIIQPKKGDRPKSSEDIIQS--KKEDRPKSSEDIIQSKKEDRPKSSED 229
Cdd:TIGR00600  381 NNVAFVDDGSLSPRTLQAIGQalDDDEDKKVSASSDDQASPSKKTKMLLISRieVEDDDLDYLDQGEGIPLMAALQLSSV 460

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   230 IIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSE-------DSVPSKKGDRPKSSEDSVQPKKEDRPKSS 302
Cdd:TIGR00600  461 NSKPEAVASTKIAREVTSSGHEAVPKAVQSLLLGATNDSPIPSEftildrkSELSIERTVKPVSSEFGLPSQREDKLAIP 540

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   303 EDSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKThrplkdsvqsKESEEPKSSHESIQSKEDKIHKPLKDSIP 382
Cdd:TIGR00600  541 TEGTQNLQGISDHPEQFEFQNELSPLETKNNESNLSSDAET----------EGSPNPEMPSWSSVTVPSEALDNYETTNP 610

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579134   383 SKEGDIPKSPEDTIQSQEEITASEEDTIQSQEGNTIKSSEEDVQLSESKLLGLGAEIETLEE 444
Cdd:TIGR00600  611 SNAKEVRNFAETGIQTTNVGESADLLLISNPMEVEPMESEKEESESDGSFIEVDSVSSTLEL 672
PTZ00121 PTZ00121
MAEBL; Provisional
 189-466 2.39e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  189 KKGDRPKSSEDIIQSKKEDRPKSSEdiiqSKKEDRPKSSEDIIQSKKEDRPKSSEdiIQSKKEDRPKSSEdiIQPKKEDR 268
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADE----AKKKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEE--AKKKAEEA 1469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  269 PKSSE---DSVPSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHR 345
Cdd:PTZ00121 1470 KKADEakkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  346 PLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSK------EGDIPKSPEDTIQSQEEITASEEDTIQSQEgntIK 419
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE---LK 1626

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 225579134  420 SSEEDVQLSESKLLGLGAEIETLEEglvrviKDKEEFEEVLKDAGEK 466
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEE------LKKAEEENKIKAAEEA 1667
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 435-537 3.29e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 46.67  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 435 LGAEIETLEEGLVRVIKDkEEFEEVLKDagEKLVAVDFSAAWCGPCRMMKPLFHS----LSLKHEDVIFLEVDTEDCEQL 510
Cdd:PTZ00102  22 FGSAEEHFISEHVTVLTD-STFDKFITE--NEIVLVKFYAPWCGHCKRLAPEYKKaakmLKEKKSEIVLASVDATEEMEL 98

                         90       100
                 ....*....|....*....|....*..
gi 225579134 511 VQDCEIFHLPTFQFYKNEEKVgEFSGA 537
Cdd:PTZ00102  99 AQEFGVRGYPTIKFFNKGNPV-NYSGG 124
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 452-536 5.27e-05

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: 42.30  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEEVLKDagEKLVAVDFSAAWCGPCRMMKPLFH--SLSLKHE-DVIFLEVD-TEDCEQLVqdCEIFHL---PTFQF 524
Cdd:cd02997    6 TDEDFRKFLKK--EKHVLVMFYAPWCGHCKKMKPEFTkaATELKEDgKGVLAAVDcTKPEHDAL--KEEYNVkgfPTFKY 81

                         90
                 ....*....|..
gi 225579134 525 YKNEEKVGEFSG 536
Cdd:cd02997   82 FENGKFVEKYEG 93
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 452-537 9.44e-05

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: 41.85  E-value: 9.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEEVLKDAGeKLVAVDFSAAWCGPCRMMKPLFHSLS--LKHED-VIFLEVDTEDCEQLVqdCEIFHL---PTFQFY 525
Cdd:cd02998    6 TDSNFDKVVGDDK-KDVLVEFYAPWCGHCKNLAPEYEKLAavFANEDdVVIAKVDADEANKDL--AKKYGVsgfPTLKFF 82

                         90
                 ....*....|...
gi 225579134 526 -KNEEKVGEFSGA 537
Cdd:cd02998   83 pKGSTEPVKYEGG 95
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 119-423 1.21e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.00  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 119 PKPSSKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQGST---LKPATNSTHYREDDIPKSSEDIIQPKKGDRPK 195
Cdd:NF033838 137 PGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESdveVKKAELELVKEEAKEPRDEEKIKQAKAKVESK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 196 SSEDIIQSK-KEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKssediiqsKKEDRPKSSEDIIQPKKEDRPKSSED 274
Cdd:NF033838 217 KAEATRLEKiKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPK--------RRAKRGVLGEPATPDKKENDAKSSDS 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 275 SV-----PS---KKGDRPKSSEDSVQP--------KKEDRP------------KSSEDSVQSKEGEVHKPLKDSIQSKET 326
Cdd:NF033838 289 SVgeetlPSpslKPEKKVAEAEKKVEEakkkakdqKEEDRRnyptntyktlelEIAESDVKVKEAELELVKEEAKEPRNE 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 327 KVPKSPQDSIQSKEDKTHR--PLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDTIQSQEEITA 404
Cdd:NF033838 369 EKIKQAKAKVESKKAEATRleKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPA 448

                        330
                 ....*....|....*....
gi 225579134 405 SEedtiQSQEGNTIKSSEE 423
Cdd:NF033838 449 DQ----QAEEDYARRSEEE 463
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 456-538 1.95e-04

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 41.81  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 456 FEEVLKDAGE--KLVAVDFSAAWCGPC-RMMKPLFHSLSLKH---EDVIFLEVD-------------TEDCEQLVQDCEI 516
Cdd:COG2143   29 LEEDLALAKAegKPILLFFESDWCPYCkKLHKEVFSDPEVAAylkENFVVVQLDaegdkevtdfdgeTLTEKELARKYGV 108

                         90       100
                 ....*....|....*....|...
gi 225579134 517 FHLPTFQFY-KNEEKVGEFSGAL 538
Cdd:COG2143  109 RGTPTLVFFdAEGKEIARIPGYL 131
PRK08581 PRK08581
amidase domain-containing protein;
103-394 2.00e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.01  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 103 TPMFSENTVHPRHEVSPKPS---------SKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQGSTLKPATNSTHY 173
Cdd:PRK08581  17 LPTLTSPTAYADDPQKDSTAkttshdskkSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 174 REDDIPKSSEDIIQPKKGDRPKSSEDIIQSKKEDRP-KSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSE-DIIQSKKE 251
Cdd:PRK08581  97 KNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDiSDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKqDKADNQKA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 252 DrpkSSEDIIQPKKEDRPKSSEDSVPSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQskegevhkplkDSIQSketkvpks 331
Cdd:PRK08581 177 P---SSNNTKPSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSDSAL-----------DSILD-------- 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225579134 332 pqdsiQSKEDKTHRPlKDSVQSKESEEPKSSHES---IQSKEDKIHKplKDSIPSKEGDIPKSPED 394
Cdd:PRK08581 235 -----QYSEDAKKTQ-KDYASQSKKDKTETSNTKnpqLPTQDELKHK--SKPAQSFENDVNQSNTR 292
trxA PRK09381
thioredoxin TrxA;
458-544 2.88e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 40.43  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 458 EVLKDAGekLVAVDFSAAWCGPCRMMKPLFHSLSLKHE-DVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNeekvGEFSG 536
Cdd:PRK09381  16 DVLKADG--AILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKN----GEVAA 89


                 ....*...
gi 225579134 537 ALVGKLER 544
Cdd:PRK09381  90 TKVGALSK 97
rad2 TIGR00600
DNA excision repair protein (rad2); All proteins in this family for which functions are known ...
 148-429 3.18e-04

DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273166 [Multi-domain]  Cd Length: 1034  Bit Score: 43.73  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   148 TPKSLAKTTHPKQGSTLKPATNSTHyreDDIPKSSEDIIQPKKGDRPKSSEdiiqSKKEDRPKSS---EDIIQSKKEDRP 224
Cdd:TIGR00600  457 LSSVNSKPEAVASTKIAREVTSSGH---EAVPKAVQSLLLGATNDSPIPSE----FTILDRKSELsieRTVKPVSSEFGL 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   225 KSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSVPSKKGDRPKSSEDSVQPKKEDRPKSSED 304
Cdd:TIGR00600  530 PSQREDKLAIPTEGTQNLQGISDHPEQFEFQNELSPLETKNNESNLSSDAETEGSPNPEMPSWSSVTVPSEALDNYETTN 609

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   305 SVQSKEgeVHKPLKDSIQSKET---------KVPKSPQDSIQSKEDKTHRPLKDSVQSkESEEPKSSHESIQSKEDKIHK 375
Cdd:TIGR00600  610 PSNAKE--VRNFAETGIQTTNVgesadllliSNPMEVEPMESEKEESESDGSFIEVDS-VSSTLELQVPSKSQPTDESEE 686

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 225579134   376 PLKDSIPSKEGDIPKSPEDTIQSQEEITASEEDTIQSQEGNTIKSSEEDVQLSE 429
Cdd:TIGR00600  687 NAENKVASIEGEHRKEIEDLLFDESEEDNIVGMIEEEKDADDFKNEWQDISLEE 740
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 454-530 4.17e-04

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: 39.97  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 454 EEFEEVLKDAGEKLVaVDFSAAWCGPCRMMKPLFHSLS--LKHEdvifLEVDTEDC---EQLVQDCEIFHLPTFQFYKNE 528
Cdd:cd03004    9 EDFPELVLNRKEPWL-VDFYAPWCGPCQALLPELRKAAraLKGK----VKVGSVDCqkyESLCQQANIRAYPTIRLYPGN 83


                 ..
gi 225579134 529 EK 530
Cdd:cd03004   84 AS 85
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 470-546 4.69e-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: 40.78  E-value: 4.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 470 VDFSAAWCGPCRMMKPLFHSLSLKHED---VIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEekvGEFSGALVGKLERSI 546
Cdd:cd02950   25 VEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLNVDNPKWLPEIDRYRVDGIPHFVFLDRE---GNEEGQSIGLQPKQV 101
PHA02125 PHA02125
thioredoxin-like protein
 472-550 4.94e-04

thioredoxin-like protein


Pssm-ID: 133998 [Multi-domain]  Cd Length: 75  Bit Score: 38.81  E-value: 4.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225579134 472 FSAAWCGPCRMMKPLfhslsLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFqfyKNEEKVGEFSGalvgkLERSISELK 550
Cdd:PHA02125   5 FGAEWCANCKMVKPM-----LANVEYTYVDVDTDEGVELTAKHHIRSLPTL---VNTSTLDRFTG-----VPRNVAELK 70
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 122-348 1.49e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 41.60  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  122 SSKNTQLKQENISKSSGYSKQTNYSNTPKSLAKTTHPKQGSTL--KPATNSTHYRE--------DDIPKSSEDIIQPKKG 191
Cdd:PTZ00395  391 CAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTPynNPPNSNTPYSNppnsnppySNLPYSNTPYSNAPLS 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  192 DRPKSSediiqskKEDRPKSSEDIIQSKKEDRPKSSEDII-QSKKEDRPKSSEDIIQSKKEDRPKSSediiQPKKEDRPK 270
Cdd:PTZ00395  471 NAPPSS-------AKDHHSAYHAAYQHRAANQPAANLPTAnQPAANNFHGAAGNSVGNPFASRPFGS----APYGGNAAT 539

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  271 SSEDSVPSKKGDRP----------KSSEDSVQPKKEDRPKSSEDSVQSKEGEVHKPLKDSIQSKETKvpKSPQDSIQSKE 340
Cdd:PTZ00395  540 TADPNGIAKREDHPeggtnrqkyeQSDEESVESSSSENSSENENEVTDKGEEIYSLLKKTINRIDMN--KIPRPIINTQE 617


                  ....*...
gi 225579134  341 DKTHRPLK 348
Cdd:PTZ00395  618 KKKKKNLK 625
PTZ00121 PTZ00121
MAEBL; Provisional
 189-466 1.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  189 KKGDRPKSSEDIIQSKKEDRPKSSEdiiQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDIiqpKKEDR 268
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADE---AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK---KKADE 1550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  269 PKSSEDSvpsKKGDRPKSSEDSvQPKKEDRPKSSEDSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHRPLK 348
Cdd:PTZ00121 1551 LKKAEEL---KKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  349 DSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDTIQSQEEITASEEDTIQSQEGNTIKSSE----ED 424
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEakkaEE 1706

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 225579134  425 VQLSESKLLGLGAEIETLEEglVRVIK----------DKEEFEEVLKDAGEK 466
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEE--ENKIKaeeakkeaeeDKKKAEEAKKDEEEK 1756
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 237-431 3.83e-03

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 39.91  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  237 DRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRPKSSEDSVPSK-KGDRPKSSEDSVQPKKEDRPKSSEDSVQSKEGEVHK 315
Cdd:pfam07263 282 DDSNTMEEVKSDSTESTSSKEAGLSQSREDSKSESQEDSEESQsQEDSQNSQDPSSESSQEADLPSQESSSESQEEVVSE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  316 PLKDSIQSKETKVPKSPqDSIQSKEDKTHRPLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDT 395
Cdd:pfam07263 362 SRGDNPDNTSSSEEDQE-DSDSSEEDSLSTFSSSESESREEQADSESNESLRSSEESPESSEDENSSSQEGLQSHSASTE 440

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 225579134  396 IQSQE----EITASEEDTIQSQEGNTikSSEEDVQLSESK 431
Cdd:pfam07263 441 SQSEEsqseQDSQSEEDDESDSQDSS--RSKEDSNSTEST 478
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 460-506 3.87e-03

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: 37.22  E-value: 3.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225579134 460 LKDAGEKLVAVDFSAAWCGPCRMMKPLFHSLS--LKHEDVIFLEVDTED 506
Cdd:cd02966   14 LSDLKGKVVLVNFWASWCPPCRAEMPELEALAkeYKDDGVEVVGVNVDD 62
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 454-538 4.49e-03

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: 36.87  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 454 EEFEEVLKDAGEKLVAVDFSAAWCGPCRMMKPLFHSLSLKHED-VIFLEVDTEDCEQLVQDCEIFHLPTFQFYKNEEKVG 532
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGqFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80


                 ....*.
gi 225579134 533 EFSGAL 538
Cdd:cd02956   81 GFQGAQ 86
PDI_a_QSOX cd02992
PDIa family, Quiescin-sulfhydryl oxidase (QSOX) subfamily; QSOX is a eukaryotic protein ...
 469-526 7.10e-03

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: 36.48  E-value: 7.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225579134 469 AVDFSAAWCGPCRMMKPLFHSLS---LKHEDVIFLEVdtEDC-----EQLVQDCEIFHLPTFQFYK 526
Cdd:cd02992   23 LVEFYASWCGHCRAFAPTWKKLArdlRKWRPVVRVAA--VDCadeenVALCRDFGVTGYPTLRYFP 86
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 32-275 7.48e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 39.26  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134   32 EESDMTLNNGGKANERGSNENPLQALSKNEAFlvPEFLDTAQSKEKAIASKVSNTLHMSTEESEFPQQVSSTPMFSENTV 111
Cdd:PTZ00108 1154 KEQRLKSKTKGKASKLRKPKLKKKEKKKKKSS--ADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQ 1231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  112 HPRHEVSPKPSSKNTQLKQENISK--SSGYSKQTNYSNTPKSLAKTTHPKQGSTLKPATNSThyREDDIPKSSEDIIQPK 189
Cdd:PTZ00108 1232 KTKPKKSSVKRLKSKKNNSSKSSEdnDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPD--GESNGGSKPSSPTKKK 1309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  190 KGDRPKSSEDIIQSKKEDRPKSSEDiiqSKKEDRPKSSEDIIQSKKEDRP-----KSSEDiiqSKKEDRPKSSEDiiqpk 264
Cdd:PTZ00108 1310 VKKRLEGSLAALKKKKKSEKKTARK---KKSKTRVKQASASQSSRLLRRPrkkksDSSSE---DDDDSEVDDSED----- 1378

                         250
                  ....*....|.
gi 225579134  265 kEDRPKSSEDS 275
Cdd:PTZ00108 1379 -EDDEDDEDDD 1388
PTZ00121 PTZ00121
MAEBL; Provisional
 193-431 8.24e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  193 RPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEDII---QSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQPKKEDRP 269
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  270 KSSEDSvpsKKGDRPKSSEDSVQPKKEDRPKSSE------------DSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQ 337
Cdd:PTZ00121 1662 KAAEEA---KKAEEDKKKAEEAKKAEEDEKKAAEalkkeaeeakkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  338 SKEDK-------THRPLKDSVQSKESEEPKSSHESIQSKEDKIHKPLKDSIPSKEGDIPKSPEDTIQSQEEITASeedti 410
Cdd:PTZ00121 1739 AEEDKkkaeeakKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEG----- 1813

                         250       260
                  ....*....|....*....|.
gi 225579134  411 qSQEGNTIKSSEEDVQLSESK 431
Cdd:PTZ00121 1814 -GKEGNLVINDSKEMEDSAIK 1833
PTZ00121 PTZ00121
MAEBL; Provisional
 189-477 9.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  189 KKGDRPKSSEDIIQSKKEDRPKSSEdiiQSKKEDRPKSSEDIIQSKKEDRPKSSEDIIQSKKEDRPKSSEdiIQPKKEDR 268
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAE---ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE--AKKEAEED 1742

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  269 PKSSEDSVPSKKGDRPKSSEDSVQPKKEDRPKSSEDSVQSKEGEVHKPLKDSIQSKETKVPKSPQDSIQSKEDKTHRPLK 348
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  349 DSVQSKESEEPK----SSHESIQSKEDKIHKPLKDSIPSKEGDipkSPEDTIQSQEEITASEEDTIQSQEGNTIKSSEED 424
Cdd:PTZ00121 1823 DSKEMEDSAIKEvadsKNMQLEEADAFEKHKFNKNNENGEDGN---KEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 225579134  425 VQLSESKLLGLGAEIETLEEGLVRVIKD--KEEFEEVLKDAGEKLVAVDFSAAWC 477
Cdd:PTZ00121 1900 REIPNNNMAGKNNDIIDDKLDKDEYIKRdaEETREEIIKISKKDMCINDFSSKFC 1954
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 453-537 9.56e-03

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: 38.50  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134  453 KEEFEEVLKDAgeKLVAVDFSAAWCGPCRMMKPLFHS----LSLKHEDVIFLEVDTEDCEQLVQDCEIFHLPTFQFYKN- 527
Cdd:TIGR01130   8 KDNFDDFIKSH--EFVLVEFYAPWCGHCKSLAPEYEKaadeLKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNg 85

                          90
                  ....*....|
gi 225579134  528 EEKVGEFSGA 537
Cdd:TIGR01130  86 EDSVSDYNGP 95
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 452-527 9.73e-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: 36.21  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579134 452 DKEEFEEVLKDAGekLVAVDFSAAWCGPCRMMKPLFHSLSLKHED-------VIFLEVDTEDCEQLVQDCEIFHLPTFQF 524
Cdd:cd02996    7 TSGNIDDILQSAE--LVLVNFYADWCRFSQMLHPIFEEAAAKIKEefpdagkVVWGKVDCDKESDIADRYRINKYPTLKL 84


                 ...
gi 225579134 525 YKN 527
Cdd:cd02996   85 FRN 87
 
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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