NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039744246|ref|XP_017171104|]
View 

thioredoxin domain-containing protein 3 isoform X1 [Mus musculus]

Protein Classification

TRX_NDPK and NDPk_TX domain-containing protein( domain architecture ID 10121458)

TRX_NDPK and NDPk_TX domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 1.77e-49

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: 164.43  E-value: 1.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  11 QSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNeDEILHFVVAEADNIVTLQPFRDKCEPVFLFSL 90
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                          90       100
                  ....*....|....*....|...
gi 1039744246  91 NGKIIAKIQGANAPLINRKVITL 113
Cdd:cd02948    80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 313-445 4.42e-49

NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance.


:

Pssm-ID: 239879  Cd Length: 132  Bit Score: 164.31  E-value: 4.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 313 QTTLALLHPDICEEEKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVE 392
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039744246 393 YWKTLIGPKTIEEAYASHPQSLCVQFASGNfPTNQFYGSSSKAAAEKEIAHFF 445
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDH-LSNAVHGSSSAEEAEKEIDFFF 132
NDPk super family cl00335
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 155-301 4.08e-41

Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the synthesis of nucleoside triphosphates (NTPs), are involved in numerous regulatory processes associated with proliferation, development, and differentiation. They are vital for DNA/RNA synthesis, cell division, macromolecular metabolism and growth. The enzymes generate NTPs or their deoxy derivatives by terminal (gamma) phosphotransfer from an NTP such as ATP or GTP to any nucleoside diphosphate (NDP) or its deoxy derivative. The sequence of NDPk has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes, which is involved in the catalytic mechanism. The first confirmed metastasis suppressor gene was the NDP kinase protein encoded by the nm23 gene. Unicellular organisms generally possess only one gene encoding NDP kinase, while most multicellular organisms possess not only an ortholog that provides most of the NDP kinase enzymatic activity but also multiple divergent paralogous genes. The human genome codes for at least nine NDP kinases and can be classified into two groups, Groups I and II, according to their genomic architecture and distinct enzymatic activity. Group I isoforms (A-D) are well-conserved, catalytically active, and share 58-88% identity between each other, while Group II are more divergent, with only NDPk6 shown to be active. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. The hexamer can be viewed as trimer of dimers, while tetramers are dimers of dimers, with the dimerization interface conserved.


The actual alignment was detected with superfamily member cd04416:

Pssm-ID: 469726  Cd Length: 132  Bit Score: 143.50  E-value: 4.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 155 YNMAIIKPDAVLMRKNiEVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQEDseV 234
Cdd:cd04416     2 YTLALIKPDAVAEKKD-EILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKEN--A 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 235 IQEETLPQTDTEEEPgvleephvrfapvMIKKKRDSLQEYMDRQHMSDYCDVEDDAVKVSKLIDILF 301
Cdd:cd04416    79 VEEWRELMGPTDPEE-------------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
 
Name Accession Description Interval E-value
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 1.77e-49

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: 164.43  E-value: 1.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  11 QSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNeDEILHFVVAEADNIVTLQPFRDKCEPVFLFSL 90
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                          90       100
                  ....*....|....*....|...
gi 1039744246  91 NGKIIAKIQGANAPLINRKVITL 113
Cdd:cd02948    80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 313-445 4.42e-49

NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance.


Pssm-ID: 239879  Cd Length: 132  Bit Score: 164.31  E-value: 4.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 313 QTTLALLHPDICEEEKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVE 392
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039744246 393 YWKTLIGPKTIEEAYASHPQSLCVQFASGNfPTNQFYGSSSKAAAEKEIAHFF 445
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDH-LSNAVHGSSSAEEAEKEIDFFF 132
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 155-301 4.08e-41

NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance.


Pssm-ID: 239879  Cd Length: 132  Bit Score: 143.50  E-value: 4.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 155 YNMAIIKPDAVLMRKNiEVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQEDseV 234
Cdd:cd04416     2 YTLALIKPDAVAEKKD-EILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKEN--A 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 235 IQEETLPQTDTEEEPgvleephvrfapvMIKKKRDSLQEYMDRQHMSDYCDVEDDAVKVSKLIDILF 301
Cdd:cd04416    79 VEEWRELMGPTDPEE-------------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 313-450 3.72e-30

Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to nucleoside triphosphates; These enzymes play important roles in bacterial growth, signal transduction and pathogenicity.


Pssm-ID: 197791  Cd Length: 135  Bit Score: 114.19  E-value: 3.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  313 QTTLALLHPDICEEE-KDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGV 391
Cdd:smart00562   1 ERTLAIIKPDAVQRGlIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039744246  392 EYWKTLIGPKTIEEAyasHPQSLCVQFASGNfPTNQFYGSSSKAAAEKEIAHFFPPQST 450
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDI-GRNAVHGSDSPESAEREIALFFPESEI 135
NDK pfam00334
Nucleoside diphosphate kinase;
315-447 1.42e-20

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 87.54  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 315 TLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVEY 393
Cdd:pfam00334   3 TLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAISK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039744246 394 WKTLIGPKTIEEAyasHPQSLCVQFASgNFPTNQFYGSSSKAAAEKEIAHFFPP 447
Cdd:pfam00334  83 WRELMGATNPAEA---APGTIRGDFAV-SIGRNAVHGSDSPESAEREIALFFPE 132
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 315-457 7.25e-19

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 84.11  E-value: 7.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 315 TLALLHPD-ICEEEKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVEY 393
Cdd:PLN02931   32 TLAMIKPDgLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAVSD 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 394 WKTLIGPKTIEEAYASHPQS---LCVQfasgNFPTNQFYGSSSKAAAEKEIAHFFPPQSTLALIKPH 457
Cdd:PLN02931  112 WRTLIGPTDARKAKISHPNSiraMCGL----DSEKNCVHGSDSPESAEREISFFFGDVSSGDVASQH 174
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 312-447 6.65e-11

Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439875  Cd Length: 140  Bit Score: 60.08  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 312 VQTTLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENG 390
Cdd:COG0105     2 MERTLVIIKPDAVQRGLiGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 391 VEYWKTLIGPKTIEEAyasHPQSLCVQFASGNFPtNQFYGSSSKAAAEKEIAHFFPP 447
Cdd:COG0105    82 VAVVRKLMGATNPAEA---APGTIRGDFALSIGE-NAVHGSDSPESAEREIALFFSE 134
NDK pfam00334
Nucleoside diphosphate kinase;
157-231 6.22e-10

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 57.11  E-value: 6.22e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 157 MAIIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQED 231
Cdd:pfam00334   4 LAIIKPDAV--QRGLigEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGEN 78
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 13-102 2.87e-08

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: 51.46  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  13 VVNSQNlWDEMLLN-KGLTVIDVYQAWCGPCKAVQSLFRKLKNELNEDeilhFVVAEAD---NIVTLQPFRDKCEPVFLF 88
Cdd:pfam00085   4 VLTDAN-FDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN----VVFAKVDvdeNPDLASKYGVRGYPTLIF 78

                          90
                  ....*....|....
gi 1039744246  89 SLNGKIIAKIQGAN 102
Cdd:pfam00085  79 FKNGQPVDDYVGAR 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 14-101 1.65e-06

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: 46.35  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNEDeilhFVVAEAD-----------NIVTLqpfrdkc 82
Cdd:COG3118     5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK----VKFVKVDvdenpelaaqfGVRSI------- 73

                          90
                  ....*....|....*....
gi 1039744246  83 ePVFLFSLNGKIIAKIQGA 101
Cdd:COG3118    74 -PTLLLFKDGQPVDRFVGA 91
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 159-231 2.16e-06

mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated


Pssm-ID: 179085  Cd Length: 134  Bit Score: 47.02  E-value: 2.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744246 159 IIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQED 231
Cdd:PRK00668    7 IIKPDAV--QRGLigEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLEGEN 79
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-103 7.05e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.48  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNE--------LNEDEILHfvVAEADNIVTLqpfrdkcePV 85
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEytkmvfvkVDVDELSE--VAEKENITSM--------PT 74

                          90
                  ....*....|....*...
gi 1039744246  86 FLFSLNGKIIAKIQGANA 103
Cdd:PTZ00051   75 FKVFKNGSVVDTLLGAND 92
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 159-227 1.18e-05

Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439875  Cd Length: 140  Bit Score: 45.06  E-value: 1.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039744246 159 IIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGlSCVLIV 227
Cdd:COG0105     8 IIKPDAV--QRGLigEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSG-PVVAMV 75
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-107 3.67e-04

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: 39.58  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNE---------LNEDEilHFVVAEADNIVTLqpfrdkceP 84
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyegkvkfvkLNVDE--NPDIAAKYGIRSI--------P 70

                          90       100
                  ....*....|....*....|....*
gi 1039744246  85 VFLFSLNGKIIAKIQGAN--APLIN 107
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVGALpkAALKQ 95
 
Name Accession Description Interval E-value
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 1.77e-49

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: 164.43  E-value: 1.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  11 QSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNeDEILHFVVAEADNIVTLQPFRDKCEPVFLFSL 90
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                          90       100
                  ....*....|....*....|...
gi 1039744246  91 NGKIIAKIQGANAPLINRKVITL 113
Cdd:cd02948    80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 313-445 4.42e-49

NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance.


Pssm-ID: 239879  Cd Length: 132  Bit Score: 164.31  E-value: 4.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 313 QTTLALLHPDICEEEKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVE 392
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039744246 393 YWKTLIGPKTIEEAYASHPQSLCVQFASGNfPTNQFYGSSSKAAAEKEIAHFF 445
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDH-LSNAVHGSSSAEEAEKEIDFFF 132
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 155-301 4.08e-41

NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 (TXNDC6) and Sptrx-2 (TXNDC3) are fusion proteins of Group II N-terminal thioredoxin domains followed by one or three NDP kinase domains, respectively. Sptrx-2, which has a tissue specific distribution in human testis, has been considered as a member of the nm23 family (nm23-H8) and exhibits a high homology with sea urchin IC1 (intermediate chain-1) protein, a component of the sperm axonemal outer dynein arm complex. Txl-2 is mainly represented in close association with microtubules within tissues with cilia and flagella such as seminiferous epithelium (spermatids) and lung airway epithelium, suggesting possible role in control of microtubule stability and maintenance.


Pssm-ID: 239879  Cd Length: 132  Bit Score: 143.50  E-value: 4.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 155 YNMAIIKPDAVLMRKNiEVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQEDseV 234
Cdd:cd04416     2 YTLALIKPDAVAEKKD-EILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKEN--A 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 235 IQEETLPQTDTEEEPgvleephvrfapvMIKKKRDSLQEYMDRQHMSDYCDVEDDAVKVSKLIDILF 301
Cdd:cd04416    79 VEEWRELMGPTDPEE-------------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 313-450 3.72e-30

Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to nucleoside triphosphates; These enzymes play important roles in bacterial growth, signal transduction and pathogenicity.


Pssm-ID: 197791  Cd Length: 135  Bit Score: 114.19  E-value: 3.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  313 QTTLALLHPDICEEE-KDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGV 391
Cdd:smart00562   1 ERTLAIIKPDAVQRGlIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039744246  392 EYWKTLIGPKTIEEAyasHPQSLCVQFASGNfPTNQFYGSSSKAAAEKEIAHFFPPQST 450
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDI-GRNAVHGSDSPESAEREIALFFPESEI 135
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 313-445 1.88e-26

Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the synthesis of nucleoside triphosphates (NTPs), are involved in numerous regulatory processes associated with proliferation, development, and differentiation. They are vital for DNA/RNA synthesis, cell division, macromolecular metabolism and growth. The enzymes generate NTPs or their deoxy derivatives by terminal (gamma) phosphotransfer from an NTP such as ATP or GTP to any nucleoside diphosphate (NDP) or its deoxy derivative. The sequence of NDPk has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes, which is involved in the catalytic mechanism. The first confirmed metastasis suppressor gene was the NDP kinase protein encoded by the nm23 gene. Unicellular organisms generally possess only one gene encoding NDP kinase, while most multicellular organisms possess not only an ortholog that provides most of the NDP kinase enzymatic activity but also multiple divergent paralogous genes. The human genome codes for at least nine NDP kinases and can be classified into two groups, Groups I and II, according to their genomic architecture and distinct enzymatic activity. Group I isoforms (A-D) are well-conserved, catalytically active, and share 58-88% identity between each other, while Group II are more divergent, with only NDPk6 shown to be active. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. The hexamer can be viewed as trimer of dimers, while tetramers are dimers of dimers, with the dimerization interface conserved.


Pssm-ID: 238335  Cd Length: 133  Bit Score: 103.97  E-value: 1.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 313 QTTLALLHPDICEE-EKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGV 391
Cdd:cd00595     1 ERTLALIKPDAVAEgLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039744246 392 EYWKTLIGPKTIEEAYASHPQSLCVQFASGNFpTNQFYGSSSKAAAEKEIAHFF 445
Cdd:cd00595    81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVL-RNAVHGSDSVESAAREIAFFF 133
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 315-446 1.71e-23

Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of p53-induced apoptosis-beta, IPIA-beta): In human, mRNA for NDPk5 is almost exclusively found in testis, especially in the flagella of spermatids and spermatozoa, in association with axoneme microtubules, and may play a role in spermatogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. It belongs to the nm23 Group II genes and appears to differ from the other human NDPks in that it lacks two important catalytic site residues, and thus does not appear to possess NDP kinase activity. NDPk5 confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes, including glutathione peroxidase 5 (Gpx5).


Pssm-ID: 239880  Cd Length: 132  Bit Score: 95.58  E-value: 1.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 315 TLALLHPDICEEEkDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVEYW 394
Cdd:cd04418     3 TLAIIKPDAVHKA-EEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAISYW 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039744246 395 KTLIGPKTIEEAYASHPQSLCVQFASGNFpTNQFYGSSSKAAAEKEIAHFFP 446
Cdd:cd04418    82 KELLGPTNSLKAKETHPDSLRAIYGTDDL-RNAVHGSDSFSSAEREIRFMFP 132
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 313-446 6.41e-23

Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced apoptosis-alpha, IPIA-alpha): The nm23-H6 gene encoding NDPk6 is expressed mainly in mitochondria, but also found at a lower level in most tissues. NDPk6 has all nine residues considered crucial for enzyme structure and activity, and has been found to have NDP kinase activity. It may play a role in cell growth and cell cycle progression. The nm23-H6 gene locus has been implicated in a variety of malignant tumors.


Pssm-ID: 239877  Cd Length: 135  Bit Score: 94.00  E-value: 6.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 313 QTTLALLHPDICEEEkdDVLNVIHN----EGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRE 388
Cdd:cd04414     1 QLTLALIKPDAVAHP--LALEAVRQlilsNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039744246 389 NGVEYWKTLIGPKTIEEAYASHPQSLCVQFASGNfPTNQFYGSSSKAAAEKEIAHFFP 446
Cdd:cd04414    79 NAIKTWRALMGPTKVFRARASAPDSIRGLYGLTD-TRNATHGSDSPASAQREIALFFP 135
NDK pfam00334
Nucleoside diphosphate kinase;
315-447 1.42e-20

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 87.54  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 315 TLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVEY 393
Cdd:pfam00334   3 TLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAISK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039744246 394 WKTLIGPKTIEEAyasHPQSLCVQFASgNFPTNQFYGSSSKAAAEKEIAHFFPP 447
Cdd:pfam00334  83 WRELMGATNPAEA---APGTIRGDFAV-SIGRNAVHGSDSPESAEREIALFFPE 132
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 315-457 7.25e-19

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 84.11  E-value: 7.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 315 TLALLHPD-ICEEEKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVEY 393
Cdd:PLN02931   32 TLAMIKPDgLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAVSD 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 394 WKTLIGPKTIEEAYASHPQS---LCVQfasgNFPTNQFYGSSSKAAAEKEIAHFFPPQSTLALIKPH 457
Cdd:PLN02931  112 WRTLIGPTDARKAKISHPNSiraMCGL----DSEKNCVHGSDSPESAEREISFFFGDVSSGDVASQH 174
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 313-445 1.95e-15

Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate kinase (NDPk7) consists of an N-terminal DM10 domain and two functional catalytic NDPk modules, NDPk7A and NDPk7B. The function of the DM10 domain, which also occurs in multiple copies in other proteins, is unknown. NDPk7 is predominantly expressed in testes, although appreciable amount are also found in liver, heart, brain, ovary, small intestine and spleen. The nm23-H7 gene is located in or near the hereditary prostrate cancer susceptibility locus. Nm23-H7 may be involved in the development of colon and gastric carcinoma, the latter possibly in a type-specific manner.


Pssm-ID: 239878  Cd Length: 131  Bit Score: 72.86  E-value: 1.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 313 QTTLALLHPDiCEEEKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVE 392
Cdd:cd04415     1 EKTLALIKPD-AYSKIGKIIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVGDDAIS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039744246 393 YWKTLIGPKTIEEAYASHPQSLCVQFASGNFpTNQFYGSSSKAAAEKEIAHFF 445
Cdd:cd04415    80 EWRKLLGPTNSSVARSDAPNSIRALFGTDGT-RNAAHGSDSVASAARELEFFF 131
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 312-445 1.03e-14

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 70.85  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 312 VQTTLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENG 390
Cdd:PRK14542    1 MSRTFIMIKPDGVKNKHvGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALERDNA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039744246 391 VEYWKTLIGPKTIEEAYASHPQSLcvqFASGNfPTNQFYGSSSKAAAEKEIAHFF 445
Cdd:PRK14542   81 VLHWREVIGATDPKEAAAGTIRAL---YAESK-EANAVHGSDSDANAALEISFFF 131
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 312-447 6.65e-11

Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439875  Cd Length: 140  Bit Score: 60.08  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 312 VQTTLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENG 390
Cdd:COG0105     2 MERTLVIIKPDAVQRGLiGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 391 VEYWKTLIGPKTIEEAyasHPQSLCVQFASGNFPtNQFYGSSSKAAAEKEIAHFFPP 447
Cdd:COG0105    82 VAVVRKLMGATNPAEA---APGTIRGDFALSIGE-NAVHGSDSPESAEREIALFFSE 134
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 312-445 2.05e-10

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 58.68  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 312 VQTTLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENG 390
Cdd:PRK14540    2 KERTFVALKPDAVERKLiGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVIEGENA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039744246 391 VEYWKTLIGPKTIEEAyasHPQSLCVQFASgNFPTNQFYGSSSKAAAEKEIAHFF 445
Cdd:PRK14540   82 ISTVRKMIGKTNPAEA---EPGTIRGDFGL-YTPANIIHASDSKESAEREIKLFF 132
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 312-447 5.07e-10

mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated


Pssm-ID: 179085  Cd Length: 134  Bit Score: 57.42  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 312 VQTTLALLHPD------ICEeekddVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLAL 385
Cdd:PRK00668    1 MERTFSIIKPDavqrglIGE-----IISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 386 RRENGVEYWKTLIG--------PKTIEEAYASHPQSlcvqfasgnfptNQFYGSSSKAAAEKEIAHFFPP 447
Cdd:PRK00668   76 EGENAIAKVRELMGatnpaeaaPGTIRGDFALSIGE------------NVVHGSDSPESAAREIALFFSE 133
NDK pfam00334
Nucleoside diphosphate kinase;
157-231 6.22e-10

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 57.11  E-value: 6.22e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 157 MAIIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQED 231
Cdd:pfam00334   4 LAIIKPDAV--QRGLigEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGEN 78
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 155-231 2.01e-09

Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the synthesis of nucleoside triphosphates (NTPs), are involved in numerous regulatory processes associated with proliferation, development, and differentiation. They are vital for DNA/RNA synthesis, cell division, macromolecular metabolism and growth. The enzymes generate NTPs or their deoxy derivatives by terminal (gamma) phosphotransfer from an NTP such as ATP or GTP to any nucleoside diphosphate (NDP) or its deoxy derivative. The sequence of NDPk has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes, which is involved in the catalytic mechanism. The first confirmed metastasis suppressor gene was the NDP kinase protein encoded by the nm23 gene. Unicellular organisms generally possess only one gene encoding NDP kinase, while most multicellular organisms possess not only an ortholog that provides most of the NDP kinase enzymatic activity but also multiple divergent paralogous genes. The human genome codes for at least nine NDP kinases and can be classified into two groups, Groups I and II, according to their genomic architecture and distinct enzymatic activity. Group I isoforms (A-D) are well-conserved, catalytically active, and share 58-88% identity between each other, while Group II are more divergent, with only NDPk6 shown to be active. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. The hexamer can be viewed as trimer of dimers, while tetramers are dimers of dimers, with the dimerization interface conserved.


Pssm-ID: 238335  Cd Length: 133  Bit Score: 55.82  E-value: 2.01e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744246 155 YNMAIIKPDAVLMRKNIEVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQED 231
Cdd:cd00595     2 RTLALIKPDAVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDN 78
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 315-445 1.29e-08

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 53.37  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 315 TLALLHPDICEE-EKDDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENGVEY 393
Cdd:PRK14545    6 TFTMIKPDAVENgHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRGPIVAAILEKENAVED 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039744246 394 WKTLIGPKTIEEAYASHPQSLcvqFASgNFPTNQFYGSSSKAAAEKEIAHFF 445
Cdd:PRK14545   86 FRTLIGATNPADAAEGTIRKK---YAK-SIGENAVHGSDSDENAQIEGAFHF 133
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 13-102 2.87e-08

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: 51.46  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  13 VVNSQNlWDEMLLN-KGLTVIDVYQAWCGPCKAVQSLFRKLKNELNEDeilhFVVAEAD---NIVTLQPFRDKCEPVFLF 88
Cdd:pfam00085   4 VLTDAN-FDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN----VVFAKVDvdeNPDLASKYGVRGYPTLIF 78

                          90
                  ....*....|....
gi 1039744246  89 SLNGKIIAKIQGAN 102
Cdd:pfam00085  79 FKNGQPVDDYVGAR 92
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 20-104 3.05e-08

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: 51.02  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  20 WDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNElnEDEILHFVVaeadNIVTLQPFRDKCE----PVFLFSLNGKII 95
Cdd:cd02947     3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEE--YPKVKFVKV----DVDENPELAEEYGvrsiPTFLFFKNGKEV 76


                  ....*....
gi 1039744246  96 AKIQGANAP 104
Cdd:cd02947    77 DRVVGADPK 85
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 312-452 6.91e-08

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 51.49  E-value: 6.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 312 VQTTLALLHPDICEEEK-DDVLNVIHNEGFTILMQRQIVLSEEEARTVCKIHENEEYFDNLIGHMTSNHSYVLALRRENG 390
Cdd:PRK14541    1 MERTLTILKPDCVRKQLiGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEKENA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039744246 391 VEYWKTLIGPKTIEEAYASHPQSLcvqFASGNfPTNQFYGSSSKAAAEKEIAHFFPPQSTLA 452
Cdd:PRK14541   81 VADFRTLIGATDPAEAAEGTVRKL---YADSK-GENIVHGSDSAENAAIEAGFFFSAEEVVR 138
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 29-110 1.38e-06

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: 46.50  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  29 LTVIDVYQAWCGPCKAVQSLFRKLKNELNEDeiLHFVVAEADNIVTL-QPFRDKCEPVFLFSLNGKIIAKIQGANAPLIN 107
Cdd:cd02984    16 LLVLHFWAPWAEPCKQMNQVFEELAKEAFPS--VLFLSIEAEELPEIsEKFEITAVPTFVFFRNGTIVDRVSGADPKELA 93


                  ...
gi 1039744246 108 RKV 110
Cdd:cd02984    94 KKV 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 14-101 1.65e-06

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: 46.35  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNEDeilhFVVAEAD-----------NIVTLqpfrdkc 82
Cdd:COG3118     5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK----VKFVKVDvdenpelaaqfGVRSI------- 73

                          90
                  ....*....|....*....
gi 1039744246  83 ePVFLFSLNGKIIAKIQGA 101
Cdd:COG3118    74 -PTLLLFKDGQPVDRFVGA 91
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 159-231 2.16e-06

mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated


Pssm-ID: 179085  Cd Length: 134  Bit Score: 47.02  E-value: 2.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744246 159 IIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQED 231
Cdd:PRK00668    7 IIKPDAV--QRGLigEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLEGEN 79
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-103 7.05e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.48  E-value: 7.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNE--------LNEDEILHfvVAEADNIVTLqpfrdkcePV 85
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEytkmvfvkVDVDELSE--VAEKENITSM--------PT 74

                          90
                  ....*....|....*...
gi 1039744246  86 FLFSLNGKIIAKIQGANA 103
Cdd:PTZ00051   75 FKVFKNGSVVDTLLGAND 92
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 159-227 1.18e-05

Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439875  Cd Length: 140  Bit Score: 45.06  E-value: 1.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039744246 159 IIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGlSCVLIV 227
Cdd:COG0105     8 IIKPDAV--QRGLigEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSG-PVVAMV 75
NDPk_I cd04413
Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large ...
 159-231 1.19e-05

Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large family of structurally and functionally conserved proteins from bacteria to humans that generally catalyze the transfer of gamma-phosphates of a nucleoside triphosphate (NTP) donor onto a nucleoside diphosphate (NDP) acceptor through a phosphohistidine intermediate. The mammalian nm23/NDP kinase gene family can be divided into two distinct groups. The group I genes encode proteins that generally have highly homologous counterparts in other organisms and possess the classic enzymatic activity of a kinase. This group includes vertebrate NDP kinases A-D (Nm23- H1 to -H4), and its counterparts in bacteria, archea and other eukaryotes. NDP kinases exist in two different quaternary structures; all known eukaryotic enzymes are hexamers, while some bacterial enzymes are tetramers, as in Myxococcus. They possess the NDP kinase active site motif (NXXH[G/A]SD) and the nine residues that are most essential for catalysis.


Pssm-ID: 239876  Cd Length: 130  Bit Score: 44.77  E-value: 1.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039744246 159 IIKPDAVLMRKNIEVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQED 231
Cdd:cd04413     6 IIKPDGVQRGLIGEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSGPVVAMVLEGEN 78
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 157-247 8.83e-05

Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of p53-induced apoptosis-beta, IPIA-beta): In human, mRNA for NDPk5 is almost exclusively found in testis, especially in the flagella of spermatids and spermatozoa, in association with axoneme microtubules, and may play a role in spermatogenesis by increasing the ability of late-stage spermatids to eliminate reactive oxygen species. It belongs to the nm23 Group II genes and appears to differ from the other human NDPks in that it lacks two important catalytic site residues, and thus does not appear to possess NDP kinase activity. NDPk5 confers protection from cell death by Bax and alters the cellular levels of several antioxidant enzymes, including glutathione peroxidase 5 (Gpx5).


Pssm-ID: 239880  Cd Length: 132  Bit Score: 42.43  E-value: 8.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 157 MAIIKPDAVLMRKNIEvrEKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGLSCVLIVSQEDSEVIQ 236
Cdd:cd04418     4 LAIIKPDAVHKAEEIE--DIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAISYW 81

                          90
                  ....*....|.
gi 1039744246 237 EETLPQTDTEE 247
Cdd:cd04418    82 KELLGPTNSLK 92
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 13-65 2.53e-04

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: 40.29  E-value: 2.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039744246  13 VVNSQNlWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNEDEILHFV 65
Cdd:cd02961     2 ELTDDN-FDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVA 53
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-107 3.67e-04

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: 39.58  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQSLFRKLKNE---------LNEDEilHFVVAEADNIVTLqpfrdkceP 84
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyegkvkfvkLNVDE--NPDIAAKYGIRSI--------P 70

                          90       100
                  ....*....|....*....|....*
gi 1039744246  85 VFLFSLNGKIIAKIQGAN--APLIN 107
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVGALpkAALKQ 95
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 157-240 1.27e-03

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 39.16  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 157 MAIIKPDAVlmRKNI--EVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFVVSMTNGlSCVLIVSQEDSEV 234
Cdd:PRK14541    5 LTILKPDCV--RKQLigAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSG-PCVPMILEKENAV 81


                  ....*.
gi 1039744246 235 IQEETL 240
Cdd:PRK14541   82 ADFRTL 87
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 25-116 1.63e-03

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 38.90  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  25 LNKGLTVIDVYQAWCGPCKAVQSLFRKLKNELNEdeiLHFV-VAEADNIVTLQPFRDKCE---PV--------------- 85
Cdd:COG0526    26 LKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG---VVFVgVDVDENPEAVKAFLKELGlpyPVlldpdgelakaygvr 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039744246  86 -----FLFSLNGKIIAKIQGA-NAPLINRKVITLIDE 116
Cdd:COG0526   103 gipttVLIDKDGKIVARHVGPlSPEELEEALEKLLAK 139
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 135-232 2.47e-03

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 39.04  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246 135 LVDAIDEEYGEVQYESAAEVYNMAIIKPDAVLMRKNIEVREKIAKEGFVIEIQENLILPEEVVREFYTHIADQPDFEEFV 214
Cdd:PLN02931   11 LLLLASFPIRCSSSGASEEERTLAMIKPDGLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLV 90

                          90
                  ....*....|....*...
gi 1039744246 215 VSMTNGLSCVLIVSQEDS 232
Cdd:PLN02931   91 KYMTSGPVLVMVLEKENA 108
trxA PRK09381
thioredoxin TrxA;
22-101 3.58e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 37.35  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  22 EMLLNKGLTVIDVYQAWCGPCKAVQSLFrklkNELNEDEILHFVVAEAD---NIVTLQPFRDKCEPVFLFSLNGKIIAKI 98
Cdd:PRK09381   16 DVLKADGAILVDFWAEWCGPCKMIAPIL----DEIADEYQGKLTVAKLNidqNPGTAPKYGIRGIPTLLLFKNGEVAATK 91


                  ...
gi 1039744246  99 QGA 101
Cdd:PRK09381   92 VGA 94
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 13-57 6.81e-03

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: 36.12  E-value: 6.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1039744246  13 VVNSQNLWdemllnkgltVIDVYQAWCGPCKAVQSLFRKLKNELN 57
Cdd:cd03004    15 VLNRKEPW----------LVDFYAPWCGPCQALLPELRKAARALK 49
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
30-132 9.40e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 36.38  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744246  30 TVIDVYQAWCGPCKAVQSLFRKLKNELNEDEIlHFVVAEADNIVTLQPFRDKCEPVF-LFSLNGKIIAKIQGANApliNR 108
Cdd:COG1225    24 VVLYFYATWCPGCTAELPELRDLYEEFKDKGV-EVLGVSSDSDEAHKKFAEKYGLPFpLLSDPDGEVAKAYGVRG---TP 99

                          90       100
                  ....*....|....*....|....*..
gi 1039744246 109 KVItLIDEERKIVA---GEMDRPQYVE 132
Cdd:COG1225   100 TTF-LIDPDGKIRYvwvGPVDPRPHLE 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH