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Conserved domains on  [gi|1150561082|ref|NP_001335954|]
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thioredoxin domain-containing protein 6 isoform g [Homo sapiens]

Protein Classification

NME8/NME9 family nucleoside-diphosphate kinase; nucleoside-diphosphate kinase( domain architecture ID 10121450)

NME8/NME9 family nucleoside-diphosphate kinase similar to thioredoxin domain-containing proteins, TXNDC3/NME8/SPTRX2 and TXNDC6/NME9/TXL2| nucleoside-diphosphate kinase catalyzes the exchange of phosphate groups between different nucleoside diphosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 120-256 6.02e-63

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: 194.74  E-value: 6.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 120 TCTLAIIKPDAVAHgKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegf 199
Cdd:cd04416     1 EYTLALIKPDAVAE-KKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSK---- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 200 EDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd04416    76 ENAVEEWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-89 2.39e-47

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: 153.65  E-value: 2.39e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150561082  11 QVNISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFYA 89
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79
 
Name Accession Description Interval E-value
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 120-256 6.02e-63

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: 194.74  E-value: 6.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 120 TCTLAIIKPDAVAHgKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegf 199
Cdd:cd04416     1 EYTLALIKPDAVAE-KKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSK---- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 200 EDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd04416    76 ENAVEEWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 121-261 1.32e-56

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: 178.51  E-value: 1.32e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082  121 CTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfE 200
Cdd:smart00562   2 RTLAIIKPDAVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEG----E 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150561082  201 DVVTTWRTVMGPRDPnvaRREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFPSLKF 261
Cdd:smart00562  78 DAVKTWRTLMGPTDP---REAAPGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPESEI 135
NDK pfam00334
Nucleoside diphosphate kinase;
118-261 2.92e-49

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 159.57  E-value: 2.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:pfam00334   1 ERT--LAIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVL---E 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFPSLKF 261
Cdd:pfam00334  76 G-ENAISKWRELMGATNPAEA---APGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPEEEI 135
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-89 2.39e-47

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: 153.65  E-value: 2.39e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150561082  11 QVNISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFYA 89
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 118-257 9.66e-33

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: 117.48  E-value: 9.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:COG0105     3 ERT--LVIIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVL---E 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFP 257
Cdd:COG0105    78 G-ENAVAVVRKLMGATNPAEA---APGTIRGDFALSIGENAVHGSDSPESAEREIALFFS 133
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 118-257 1.89e-30

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 111.35  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:PRK00668    2 ERT--FSIIKPDAVQRGLIGEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVL---E 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFP 257
Cdd:PRK00668   77 G-ENAIAKVRELMGATNPAEA---APGTIRGDFALSIGENVVHGSDSPESAAREIALFFS 132
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-88 3.58e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.56  E-value: 3.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150561082  14 ISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGldLLHFALAEADRL-DVLEKYRGKCEPTFLFY 88
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYT--KMVFVKVDVDELsEVAEKENITSMPTFKVF 78
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-46 2.80e-05

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: 42.11  E-value: 2.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1150561082  12 VNISTQELWEEMLSSKGLTVVDVYQGWCGPCK---PVV 46
Cdd:COG3118     3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKmlaPVL 40
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-88 1.28e-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: 40.35  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082  14 ISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFY 88
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 21-88 1.91e-03

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: 37.21  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150561082  21 EEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLhFALAEADRL-DVLEKYRGKCEPTFLFY 88
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVV-FAKVDVDENpDLASKYGVRGYPTLIFF 79
 
Name Accession Description Interval E-value
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 120-256 6.02e-63

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: 194.74  E-value: 6.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 120 TCTLAIIKPDAVAHgKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegf 199
Cdd:cd04416     1 EYTLALIKPDAVAE-KKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSK---- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 200 EDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd04416    76 ENAVEEWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 121-261 1.32e-56

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: 178.51  E-value: 1.32e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082  121 CTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfE 200
Cdd:smart00562   2 RTLAIIKPDAVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEG----E 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150561082  201 DVVTTWRTVMGPRDPnvaRREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFPSLKF 261
Cdd:smart00562  78 DAVKTWRTLMGPTDP---REAAPGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPESEI 135
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 121-256 1.05e-53

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: 171.00  E-value: 1.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 121 CTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfE 200
Cdd:cd00595     2 RTLALIKPDAVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEK----D 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1150561082 201 DVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd00595    78 NAVGEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF 133
NDK pfam00334
Nucleoside diphosphate kinase;
118-261 2.92e-49

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 159.57  E-value: 2.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:pfam00334   1 ERT--LAIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVL---E 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFPSLKF 261
Cdd:pfam00334  76 G-ENAISKWRELMGATNPAEA---APGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPEEEI 135
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-89 2.39e-47

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: 153.65  E-value: 2.39e-47
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150561082  11 QVNISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFYA 89
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELGDDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 122-257 5.08e-36

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: 125.59  E-value: 5.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIM-KIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfE 200
Cdd:cd04414     3 TLALIKPDAVAHPLALEAVRqLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAH----E 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 201 DVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFP 257
Cdd:cd04414    79 NAIKTWRALMGPTKVFRARASAPDSIRGLYGLTDTRNATHGSDSPASAQREIALFFP 135
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 121-257 1.62e-33

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: 119.08  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 121 CTLAIIKPDAVAhgKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfE 200
Cdd:cd04418     2 RTLAIIKPDAVH--KAEEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLAR----H 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 201 DVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFP 257
Cdd:cd04418    76 NAISYWKELLGPTNSLKAKETHPDSLRAIYGTDDLRNAVHGSDSFSSAEREIRFMFP 132
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 118-257 9.66e-33

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: 117.48  E-value: 9.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:COG0105     3 ERT--LVIIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVL---E 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFP 257
Cdd:COG0105    78 G-ENAVAVVRKLMGATNPAEA---APGTIRGDFALSIGENAVHGSDSPESAEREIALFFS 133
NDPk_I cd04413
Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large ...
 118-256 2.33e-32

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: 116.03  E-value: 2.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:cd04413     1 ERT--LVIIKPDGVQRGLIGEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSGPVVAMVL---E 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd04413    76 G-ENAVKTVRKLMGATNPADA---APGTIRGDFALSIGRNIVHGSDSVESAEREIALWF 130
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 118-257 1.89e-30

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 111.35  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 118 ERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILtrtE 197
Cdd:PRK00668    2 ERT--FSIIKPDAVQRGLIGEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVL---E 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 198 GfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLFP 257
Cdd:PRK00668   77 G-ENAIAKVRELMGATNPAEA---APGTIRGDFALSIGENVVHGSDSPESAAREIALFFS 132
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 121-256 2.91e-30

Nucleoside diphosphate kinase 7 domain B (NDPk7B): 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: 239875  Cd Length: 134  Bit Score: 110.80  E-value: 2.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 121 CTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEA-FEKLVHHMCSGPSHLLILTRtegf 199
Cdd:cd04412     2 CTVCIIKPHAVSHGLLGEILQQILDEGFEITALQMFNLTRANAEEFLEVYKGVVPeLPAMVDELTSGPCIALEIAG---- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 200 EDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd04412    78 ENAVKTFREFCGPFDPEIAKQLRPNTLRARYGKDKVQNAVHCTDLPEDGPLELKFFF 134
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 122-256 4.97e-28

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: 104.83  E-value: 4.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAhgKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfED 201
Cdd:cd04415     3 TLALIKPDAYS--KIGKIIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVG----DD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082 202 VVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:cd04415    77 AISEWRKLLGPTNSSVARSDAPNSIRALFGTDGTRNAAHGSDSVASAARELEFFF 131
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 115-256 7.95e-26

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 100.67  E-value: 7.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 115 VSSERTCTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILT 194
Cdd:PLN02931   25 GASEEERTLAMIKPDGLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLE 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150561082 195 RtegfEDVVTTWRTVMGPRDPNVARREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PLN02931  105 K----ENAVSDWRTLIGPTDARKAKISHPNSIRAMCGLDSEKNCVHGSDSPESAEREISFFF 162
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 122-256 4.33e-18

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 78.71  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPshlLILTRTEGfED 201
Cdd:PRK14540    5 TFVALKPDAVERKLIGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGR---IVAMVIEG-EN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082 202 VVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PRK14540   81 AISTVRKMIGKTNPAEA---EPGTIRGDFGLYTPANIIHASDSKESAEREIKLFF 132
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 122-256 2.24e-16

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 74.17  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRTEGFED 201
Cdd:PRK14545    6 TFTMIKPDAVENGHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRGPIVAAILEKENAVED 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082 202 vvttWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PRK14545   86 ----FRTLIGATNPADA---AEGTIRKKYAKSIGENAVHGSDSDENAQIEGAFHF 133
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 122-256 2.95e-16

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 73.94  E-value: 2.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfED 201
Cdd:PRK14542    4 TFIMIKPDGVKNKHVGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALER----DN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082 202 VVTTWRTVMGPRDPNVARreqPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PRK14542   80 AVLHWREVIGATDPKEAA---AGTIRALYAESKEANAVHGSDSDANAALEISFFF 131
PTZ00093 PTZ00093
nucleoside diphosphate kinase, cytosolic; Provisional
 116-256 1.45e-15

nucleoside diphosphate kinase, cytosolic; Provisional


Pssm-ID: 173387  Cd Length: 149  Bit Score: 72.06  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 116 SSERTctLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPshlLILTR 195
Cdd:PTZ00093    1 SSERT--FIMVKPDGVQRGLVGEIIKRFEKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSGP---VVCMV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150561082 196 TEGfEDVVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PTZ00093   76 WEG-KNVVKQGRKLLGATNPLES---APGTIRGDFCVDVGRNVIHGSDSVESAKREIALWF 132
PRK14544 PRK14544
nucleoside diphosphate kinase; Provisional
 122-256 1.67e-12

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173010 [Multi-domain]  Cd Length: 183  Bit Score: 64.45  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQH-------------------------------- 169
Cdd:PRK14544    6 TLVILKPDAVKRGLVGEIISRFEKAGLKIVAMKMVKATPEQIERFYPSseewyrsvgnkllkayqelgidprarlgtddp 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 170 -KAGEEAFEKLVHHMCSGPSHLLILTRTEGFEDVvttwRTVMGPRDPNVArreQPESLRAQYGTEMP----------FNA 238
Cdd:PRK14544   86 vEVGKKVKESLVKYMTSGPIVAMVLKGNRAVEVV----RKLVGPTSPHKA---PPGTIRGDYSIDSPdlaaeegrvvYNL 158

                         170
                  ....*....|....*...
gi 1150561082 239 VHGSRDREDADRELALLF 256
Cdd:PRK14544  159 VHASDSPEEAEREIKFWF 176
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 122-256 3.52e-12

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 62.66  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPSHLLILTRtegfED 201
Cdd:PRK14541    4 TLTILKPDCVRKQLIGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEK----EN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082 202 VVTTWRTVMGPRDPNVArreQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PRK14541   80 AVADFRTLIGATDPAEA---AEGTVRKLYADSKGENIVHGSDSAENAAIEAGFFF 131
PRK14543 PRK14543
nucleoside diphosphate kinase; Provisional
 122-256 3.20e-07

nucleoside diphosphate kinase; Provisional


Pssm-ID: 237749  Cd Length: 169  Bit Score: 49.12  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 122 TLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNE----ERTMteAEVRLFYQHKA---GEEAFEKLVHHMCSGPSHLLILT 194
Cdd:PRK14543    8 TLCIIKPDGVRRGLIGNVVSRFERVGLKIVAAKmllvDRSM--AEKHYLYDDIAvrhGEAVWKSLIKFISSSPVFVFVVE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150561082 195 RTEGFEDVvttwRTVMGPRDPNVArreQPESLRA-------QYGTEMPF---NAVHGSRDREDADRELALLF 256
Cdd:PRK14543   86 GVESVEVV----RKFCGSTEPKLA---IPGTIRGdfsyhsfNYANEKGFsvyNVIHASANEDDALREIPIWF 150
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-88 3.58e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.56  E-value: 3.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150561082  14 ISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGldLLHFALAEADRL-DVLEKYRGKCEPTFLFY 88
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYT--KMVFVKVDVDELsEVAEKENITSMPTFKVF 78
PLN02619 PLN02619
nucleoside-diphosphate kinase
 110-256 2.05e-06

nucleoside-diphosphate kinase


Pssm-ID: 178228  Cd Length: 238  Bit Score: 47.92  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150561082 110 EDEDMVSSERTCTLAIIKPDAVAHGKTDEIIMKIQEAGFEILTNEERTMTEAEVRLFYQHKAGEEAFEKLVHHMCSGPsh 189
Cdd:PLN02619   79 QEQEAHAAEMERTFIAIKPDGVQRGLISEIISRFERKGFKLVAIKVVVPSKEFAQKHYHDLKERPFFNGLCDFLSSGP-- 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082 190 lLILTRTEGfEDVVTTWRTVMGPRDPnvaRREQPESLRAQYGTEMPFNAVHGSRDREDADRELALLF 256
Cdd:PLN02619  157 -VVAMVWEG-EGVIKYGRKLIGATDP---QKSEPGTIRGDLAVVVGRNIIHGSDGPETAKDEINLWF 218
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 20-88 1.03e-05

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: 43.32  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150561082  20 WEEMLSSKGLTVVDVYQGWCGPCK---PVVSLFQKMRIEVgldllHFALAEADRL-DVLEKYRGKCEPTFLFY 88
Cdd:cd02947     3 FEELIKSAKPVVVDFWAPWCGPCKaiaPVLEELAEEYPKV-----KFVKVDVDENpELAEEYGVRSIPTFLFF 70
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 12-46 2.80e-05

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: 42.11  E-value: 2.80e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1150561082  12 VNISTQELWEEMLSSKGLTVVDVYQGWCGPCK---PVV 46
Cdd:COG3118     3 VELTDENFEEEVLESDKPVLVDFWAPWCGPCKmlaPVL 40
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-88 1.28e-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: 40.35  E-value: 1.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082  14 ISTQELWEEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFY 88
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLF 75
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 16-87 6.48e-04

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: 38.41  E-value: 6.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150561082  16 TQELWEEMLSSKG--LTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLhFALAEADRL-DVLEKYRGKCEPTFLF 87
Cdd:cd02984     1 SEEEFEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVL-FLSIEAEELpEISEKFEITAVPTFVF 74
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 21-88 1.91e-03

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: 37.21  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150561082  21 EEMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLhFALAEADRL-DVLEKYRGKCEPTFLFY 88
Cdd:pfam00085  12 EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVV-FAKVDVDENpDLASKYGVRGYPTLIFF 79
trxA PRK09381
thioredoxin TrxA;
22-88 6.36e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 35.81  E-value: 6.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150561082  22 EMLSSKGLTVVDVYQGWCGPCKPVVSLFQKMRIEVGLDLLHFALAEADRLDVLEKYRGKCEPTFLFY 88
Cdd:PRK09381   16 DVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLF 82
 
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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