NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046866160|ref|XP_017456125|]
View 

thioredoxin domain-containing protein 3 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 458-589 9.05e-64

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: 205.67  E-value: 9.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:cd00595     1 ERTLALIKPDaVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 537 GEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:cd00595    81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF 133
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 323-455 6.15e-55

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: 182.41  E-value: 6.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVE 402
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 403 RWKELIGPKTVEEAYASHPDSLCVRFASGNfPVNQFYGSSSKAAAETEIEHFF 455
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDH-LSNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 8.05e-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: 164.82  E-value: 8.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  11 QSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNeDELLHFVVAEADSIVTLQPFRDKCEPVFLFSL 90
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                          90       100
                  ....*....|....*....|...
gi 1046866160  91 NGKIIAKIQGANAPLINRKVIAL 113
Cdd:cd02948    80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 155-311 1.53e-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: 146.59  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 155 YNMAVINPDAVLMRKnLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIISQGedtE 234
Cdd:cd04416     2 YTLALIKPDAVAEKK-DEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKE---N 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 235 VIEEEALPQSDDeeeeeeeevveepDPLEephvrfapmLVKKKRDSLQEYMDRQHMSDYCHVEDDAVKVSKFIDILF 311
Cdd:cd04416    78 AVEEWRELMGPT-------------DPEE---------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
 
Name Accession Description Interval E-value
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 458-589 9.05e-64

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: 205.67  E-value: 9.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:cd00595     1 ERTLALIKPDaVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 537 GEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:cd00595    81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF 133
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 323-455 6.15e-55

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: 182.41  E-value: 6.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVE 402
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 403 RWKELIGPKTVEEAYASHPDSLCVRFASGNfPVNQFYGSSSKAAAETEIEHFF 455
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDH-LSNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 8.05e-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: 164.82  E-value: 8.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  11 QSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNeDELLHFVVAEADSIVTLQPFRDKCEPVFLFSL 90
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                          90       100
                  ....*....|....*....|...
gi 1046866160  91 NGKIIAKIQGANAPLINRKVIAL 113
Cdd:cd02948    80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 155-311 1.53e-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: 146.59  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 155 YNMAVINPDAVLMRKnLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIISQGedtE 234
Cdd:cd04416     2 YTLALIKPDAVAEKK-DEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKE---N 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 235 VIEEEALPQSDDeeeeeeeevveepDPLEephvrfapmLVKKKRDSLQEYMDRQHMSDYCHVEDDAVKVSKFIDILF 311
Cdd:cd04416    78 AVEEWRELMGPT-------------DPEE---------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 458-592 5.52e-40

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: 142.30  E-value: 5.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:smart00562   1 ERTLAIIKPDaVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160  537 GEWRRMMGPVDPEEAkllSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTES 592
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPES 133
NDK pfam00334
Nucleoside diphosphate kinase;
458-594 4.94e-35

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 128.76  E-value: 4.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPHVSHKER-MEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046866160 537 GEWRRMMGPVDPEEAKllsPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTESNF 594
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPEEEI 135
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 323-460 7.18e-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: 7.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  323 QRTLGLLYPE-VCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:smart00562   1 ERTLAIIKPDaVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046866160  402 ERWKELIGPKTVEEAyasHPDSLCVRFASGNfPVNQFYGSSSKAAAETEIEHFFPPQST 460
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDI-GRNAVHGSDSPESAEREIALFFPESEI 135
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 460-592 9.23e-26

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: 102.84  E-value: 9.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 460 TLALIKPHVSHKERM-EILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVGE 538
Cdd:COG0105     5 TLVIIKPDAVQRGLIgEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENAVAV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046866160 539 WRRMMGPVDPEEAKllsPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTES 592
Cdd:COG0105    85 VRKLMGATNPAEAA---PGTIRGDFALSIGENAVHGSDSPESAEREIALFFSEE 135
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 439-591 2.99e-24

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 99.90  E-value: 2.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 439 YGSSSKAAAETEiehffppqSTLALIKPH-VSHKERMEILKAIRDARFELtqMKEM--HLTPEHASKVYFKITGKDFYKN 515
Cdd:PLN02931   19 IRCSSSGASEEE--------RTLAMIKPDgLSGNYTERIKEVILESGFSI--VKEMttQLDEDRASLFYAEHSSRSFFPS 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 516 VLDVLSSGMSVVMILTKWNAVGEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTE 591
Cdd:PLN02931   89 LVKYMTSGPVLVMVLEKENAVSDWRTLIGPTDARKAKISHPNSIRAMCGLDSEKNCVHGSDSPESAEREISFFFGD 164
NDK pfam00334
Nucleoside diphosphate kinase;
323-457 2.01e-20

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 87.54  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 402 ERWKELIGPKTVEEAyasHPDSLCVRFASgNFPVNQFYGSSSKAAAETEIEHFFPP 457
Cdd:pfam00334  81 SKWRELMGATNPAEA---APGTIRGDFAV-SIGRNAVHGSDSPESAEREIALFFPE 132
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 323-467 7.22e-17

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 78.71  E-value: 7.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPE-VCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:PLN02931   30 ERTLAMIKPDgLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAV 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 402 ERWKELIGPKTVEEAYASHPDSlcVRFASG-NFPVNQFYGSSSKAAAETEIEHFFPPQSTLALIKPH 467
Cdd:PLN02931  110 SDWRTLIGPTDARKAKISHPNS--IRAMCGlDSEKNCVHGSDSPESAEREISFFFGDVSSGDVASQH 174
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 322-457 4.79e-12

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: 63.55  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 322 VQRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHS 400
Cdd:COG0105     2 MERTLVIIKPDAVQRGLiGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 401 VERWKELIGPKTVEEAyasHPDSLCVRFASGNFpVNQFYGSSSKAAAETEIEHFFPP 457
Cdd:COG0105    82 VAVVRKLMGATNPAEA---APGTIRGDFALSIG-ENAVHGSDSPESAEREIALFFSE 134
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 13-102 1.05e-07

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: 50.31  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  13 VVNSQNlWDEMLLN-KGLTVIDVYQAWCGPCKAVQALFRKLKNELNEDelLHFVVAEADSIVTL-QPFRDKCEPVFLFSL 90
Cdd:pfam00085   4 VLTDAN-FDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN--VVFAKVDVDENPDLaSKYGVRGYPTLIFFK 80

                          90
                  ....*....|..
gi 1046866160  91 NGKIIAKIQGAN 102
Cdd:pfam00085  81 NGQPVDDYVGAR 92
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 158-232 2.22e-07

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: 50.24  E-value: 2.22e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160  158 AVINPDAVLMRKNLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIIsQGED 232
Cdd:smart00562   5 AIIKPDAVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVL-EGED 78
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 14-101 4.70e-07

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: 48.28  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNEDellhFVVAEAD--------------SIvtlqpfr 79
Cdd:COG3118     5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK----VKFVKVDvdenpelaaqfgvrSI------- 73

                          90       100
                  ....*....|....*....|..
gi 1046866160  80 dkcePVFLFSLNGKIIAKIQGA 101
Cdd:COG3118    74 ----PTLLLFKDGQPVDRFVGA 91
NDK pfam00334
Nucleoside diphosphate kinase;
157-232 1.30e-06

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 47.87  E-value: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046866160 157 MAVINPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIIsQGED 232
Cdd:pfam00334   4 LAIIKPDAV--QRGLigEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVL-EGEN 78
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-103 1.97e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 43.71  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNE--------LNEDELLHfvVAEADSIVTLqpfrdkcePV 85
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEytkmvfvkVDVDELSE--VAEKENITSM--------PT 74

                          90
                  ....*....|....*...
gi 1046866160  86 FLFSLNGKIIAKIQGANA 103
Cdd:PTZ00051   75 FKVFKNGSVVDTLLGAND 92
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 160-218 4.76e-05

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 43.56  E-value: 4.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046866160 160 INPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMT 218
Cdd:PRK00668    8 IKPDAV--QRGLigEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMT 66
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 160-232 2.65e-04

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: 41.21  E-value: 2.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 160 INPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRlSCVLIISQGED 232
Cdd:COG0105     9 IKPDAV--QRGLigEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSG-PVVAMVLEGEN 80
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-107 5.78e-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: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNE---------LNEDEllHFVVAEADSIVTLqpfrdkceP 84
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyegkvkfvkLNVDE--NPDIAAKYGIRSI--------P 70

                          90       100
                  ....*....|....*....|....*
gi 1046866160  85 VFLFSLNGKIIAKIQGAN--APLIN 107
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVGALpkAALKQ 95
 
Name Accession Description Interval E-value
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 458-589 9.05e-64

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: 205.67  E-value: 9.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:cd00595     1 ERTLALIKPDaVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 537 GEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:cd00595    81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF 133
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 458-589 6.76e-56

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: 184.72  E-value: 6.76e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPHVSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVG 537
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046866160 538 EWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 323-455 6.15e-55

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: 182.41  E-value: 6.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVE 402
Cdd:cd04416     1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 403 RWKELIGPKTVEEAYASHPDSLCVRFASGNfPVNQFYGSSSKAAAETEIEHFF 455
Cdd:cd04416    81 EWRELMGPTDPEEAKEEKPDSLRAQFARDH-LSNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 8.05e-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: 164.82  E-value: 8.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  11 QSVVNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNeDELLHFVVAEADSIVTLQPFRDKCEPVFLFSL 90
Cdd:cd02948     1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                          90       100
                  ....*....|....*....|...
gi 1046866160  91 NGKIIAKIQGANAPLINRKVIAL 113
Cdd:cd02948    80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 155-311 1.53e-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: 146.59  E-value: 1.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 155 YNMAVINPDAVLMRKnLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIISQGedtE 234
Cdd:cd04416     2 YTLALIKPDAVAEKK-DEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKE---N 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 235 VIEEEALPQSDDeeeeeeeevveepDPLEephvrfapmLVKKKRDSLQEYMDRQHMSDYCHVEDDAVKVSKFIDILF 311
Cdd:cd04416    78 AVEEWRELMGPT-------------DPEE---------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 458-592 5.52e-40

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: 142.30  E-value: 5.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:smart00562   1 ERTLAIIKPDaVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160  537 GEWRRMMGPVDPEEAkllSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTES 592
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPES 133
NDK pfam00334
Nucleoside diphosphate kinase;
458-594 4.94e-35

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 128.76  E-value: 4.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPHVSHKER-MEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046866160 537 GEWRRMMGPVDPEEAKllsPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTESNF 594
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPEEEI 135
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 460-589 1.39e-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: 124.47  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 460 TLALIKPHVSHKERmEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVGEW 539
Cdd:cd04418     3 TLAIIKPDAVHKAE-EIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAISYW 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046866160 540 RRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:cd04418    82 KELLGPTNSLKAKETHPDSLRAIYGTDDLRNAVHGSDSFSSAEREIRFMF 131
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 323-460 7.18e-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: 7.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  323 QRTLGLLYPE-VCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:smart00562   1 ERTLAIIKPDaVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046866160  402 ERWKELIGPKTVEEAyasHPDSLCVRFASGNfPVNQFYGSSSKAAAETEIEHFFPPQST 460
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDI-GRNAVHGSDSPESAEREIALFFPESEI 135
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 458-581 5.23e-28

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: 108.88  E-value: 5.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYfkitgkDFYKNVL-------DVLSSGMSVVMI 529
Cdd:cd04412     1 NCTVCIIKPHaVSHGLLGEILQQILDEGFEITALQMFNLTRANAEEFL------EVYKGVVpelpamvDELTSGPCIALE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046866160 530 LTKWNAVGEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEA 581
Cdd:cd04412    75 IAGENAVKTFREFCGPFDPEIAKQLRPNTLRARYGKDKVQNAVHCTDLPEDG 126
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 458-589 8.68e-27

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: 105.56  E-value: 8.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPHV-SHKERMEILKA-IRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNA 535
Cdd:cd04414     1 QLTLALIKPDAvAHPLALEAVRQlILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHENA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046866160 536 VGEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:cd04414    81 IKTWRALMGPTKVFRARASAPDSIRGLYGLTDTRNATHGSDSPASAQREIALFF 134
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 323-455 4.56e-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: 103.59  E-value: 4.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPE-VCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:cd00595     1 ERTLALIKPDaVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046866160 402 ERWKELIGPKTVEEAYASHPDSLCVRFASGNFPvNQFYGSSSKAAAETEIEHFF 455
Cdd:cd00595    81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLR-NAVHGSDSVESAAREIAFFF 133
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 460-592 9.23e-26

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: 102.84  E-value: 9.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 460 TLALIKPHVSHKERM-EILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVGE 538
Cdd:COG0105     5 TLVIIKPDAVQRGLIgEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENAVAV 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046866160 539 WRRMMGPVDPEEAKllsPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTES 592
Cdd:COG0105    85 VRKLMGATNPAEAA---PGTIRGDFALSIGENAVHGSDSPESAEREIALFFSEE 135
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 323-456 3.19e-25

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: 100.98  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEkDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVE 402
Cdd:cd04418     1 ERTLAIIKPDAVHKA-EEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAIS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046866160 403 RWKELIGPKTVEEAYASHPDSLCVRFASGNFPvNQFYGSSSKAAAETEIEHFFP 456
Cdd:cd04418    80 YWKELLGPTNSLKAKETHPDSLRAIYGTDDLR-NAVHGSDSFSSAEREIRFMFP 132
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 458-582 5.66e-25

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: 100.21  E-value: 5.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPHVSHKERmEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVG 537
Cdd:cd04415     1 EKTLALIKPDAYSKIG-KIIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVGDDAIS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1046866160 538 EWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAA 582
Cdd:cd04415    80 EWRKLLGPTNSSVARSDAPNSIRALFGTDGTRNAAHGSDSVASAA 124
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 439-591 2.99e-24

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 99.90  E-value: 2.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 439 YGSSSKAAAETEiehffppqSTLALIKPH-VSHKERMEILKAIRDARFELtqMKEM--HLTPEHASKVYFKITGKDFYKN 515
Cdd:PLN02931   19 IRCSSSGASEEE--------RTLAMIKPDgLSGNYTERIKEVILESGFSI--VKEMttQLDEDRASLFYAEHSSRSFFPS 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 516 VLDVLSSGMSVVMILTKWNAVGEWRRMMGPVDPEEAKLLSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTE 591
Cdd:PLN02931   89 LVKYMTSGPVLVMVLEKENAVSDWRTLIGPTDARKAKISHPNSIRAMCGLDSEKNCVHGSDSPESAEREISFFFGD 164
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 323-456 1.41e-20

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: 87.84  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEE--KDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHS 400
Cdd:cd04414     1 QLTLALIKPDAVAHPlaLEAVRQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHENA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 401 VERWKELIGPKTVEEAYASHPDSLCVRFASGNfPVNQFYGSSSKAAAETEIEHFFP 456
Cdd:cd04414    81 IKTWRALMGPTKVFRARASAPDSIRGLYGLTD-TRNATHGSDSPASAQREIALFFP 135
NDK pfam00334
Nucleoside diphosphate kinase;
323-457 2.01e-20

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 87.54  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 402 ERWKELIGPKTVEEAyasHPDSLCVRFASgNFPVNQFYGSSSKAAAETEIEHFFPP 457
Cdd:pfam00334  81 SKWRELMGATNPAEA---APGTIRGDFAV-SIGRNAVHGSDSPESAEREIALFFPE 132
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 460-574 8.62e-19

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 82.85  E-value: 8.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 460 TLALIKP------HVShkermEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKW 533
Cdd:PRK00668    4 TFSIIKPdavqrgLIG-----EIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLEGE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1046866160 534 NAVGEWRRMMGPVDPEEAkllSPNSLRARYGIDVLRNAVHG 574
Cdd:PRK00668   79 NAIAKVRELMGATNPAEA---APGTIRGDFALSIGENVVHG 116
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 323-455 9.93e-18

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: 79.80  E-value: 9.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEKDnVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVE 402
Cdd:cd04415     1 EKTLALIKPDAYSKIGK-IIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVGDDAIS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 403 RWKELIGPKTVEEAYASHPDSLCVRFASGNFPvNQFYGSSSKAAAETEIEHFF 455
Cdd:cd04415    80 EWRKLLGPTNSSVARSDAPNSIRALFGTDGTR-NAAHGSDSVASAARELEFFF 131
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 323-467 7.22e-17

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 78.71  E-value: 7.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPE-VCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSV 401
Cdd:PLN02931   30 ERTLAMIKPDgLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAV 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 402 ERWKELIGPKTVEEAYASHPDSlcVRFASG-NFPVNQFYGSSSKAAAETEIEHFFPPQSTLALIKPH 467
Cdd:PLN02931  110 SDWRTLIGPTDARKAKISHPNS--IRAMCGlDSEKNCVHGSDSPESAEREISFFFGDVSSGDVASQH 174
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 458-591 3.36e-15

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 72.55  E-value: 3.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:PRK14540    3 ERTFVALKPDaVERKLIGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVIEGENAI 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 537 GEWRRMMGPVDPEEAKllsPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFTE 591
Cdd:PRK14540   83 STVRKMIGKTNPAEAE---PGTIRGDFGLYTPANIIHASDSKESAEREIKLFFGE 134
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 458-589 4.00e-15

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 72.39  E-value: 4.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:PRK14542    2 SRTFIMIKPDgVKNKHVGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALERDNAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 537 GEWRRMMGPVDPEEAKllsPNSLRARYGIDVLRNAVHGASNMSEAATAISNVF 589
Cdd:PRK14542   82 LHWREVIGATDPKEAA---AGTIRALYAESKEANAVHGSDSDANAALEISFFF 131
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 458-582 1.95e-14

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 70.75  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 458 QSTLALIKPHVSHKERM-EILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAV 536
Cdd:PRK14541    2 ERTLTILKPDCVRKQLIgAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEKENAV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1046866160 537 GEWRRMMGPVDPEEAkllSPNSLRARYGIDVLRNAVHGASNMSEAA 582
Cdd:PRK14541   82 ADFRTLIGATDPAEA---AEGTVRKLYADSKGENIVHGSDSAENAA 124
PTZ00093 PTZ00093
nucleoside diphosphate kinase, cytosolic; Provisional
 456-590 2.59e-14

nucleoside diphosphate kinase, cytosolic; Provisional


Pssm-ID: 173387  Cd Length: 149  Bit Score: 70.52  E-value: 2.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 456 PPQSTLALIKPHVSHKERM-EILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWN 534
Cdd:PTZ00093    1 SSERTFIMVKPDGVQRGLVgEIIKRFEKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSGPVVCMVWEGKN 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 535 AVGEWRRMMGPVDPEEAkllSPNSLRARYGIDVLRNAVHGASNMSEAATAISNVFT 590
Cdd:PTZ00093   81 VVKQGRKLLGATNPLES---APGTIRGDFCVDVGRNVIHGSDSVESAKREIALWFK 133
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 460-582 1.72e-13

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 68.01  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 460 TLALIKPHVSHKERM-EILKAIRDARFELTQMKEMHLTPEHASKVYFKITGKDFYKNVLDVLSSGMSVVMILTKWNAVGE 538
Cdd:PRK14545    6 TFTMIKPDAVENGHIgGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRGPIVAAILEKENAVED 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1046866160 539 WRRMMGPVDPEEAkllSPNSLRARYGIDVLRNAVHGASNMSEAA 582
Cdd:PRK14545   86 FRTLIGATNPADA---AEGTIRKKYAKSIGENAVHGSDSDENAQ 126
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 322-457 4.79e-12

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: 63.55  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 322 VQRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHS 400
Cdd:COG0105     2 MERTLVIIKPDAVQRGLiGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046866160 401 VERWKELIGPKTVEEAyasHPDSLCVRFASGNFpVNQFYGSSSKAAAETEIEHFFPP 457
Cdd:COG0105    82 VAVVRKLMGATNPAEA---APGTIRGDFALSIG-ENAVHGSDSPESAEREIALFFSE 134
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 322-455 5.45e-12

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 63.54  E-value: 5.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 322 VQRTLGLLYPE-VCEEEKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHS 400
Cdd:PRK14542    1 MSRTFIMIKPDgVKNKHVGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALERDNA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 401 VERWKELIGPKTVEEAYASHPDSLcvrFASGNfPVNQFYGSSSKAAAETEIEHFF 455
Cdd:PRK14542   81 VLHWREVIGATDPKEAAAGTIRAL---YAESK-EANAVHGSDSDANAALEISFFF 131
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 322-455 9.83e-10

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 56.75  E-value: 9.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 322 VQRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHS 400
Cdd:PRK14540    2 KERTFVALKPDAVERKLiGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVIEGENA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 401 VERWKELIGPKTVEEAyasHPDSLCVRFASgNFPVNQFYGSSSKAAAETEIEHFF 455
Cdd:PRK14540   82 ISTVRKMIGKTNPAEA---EPGTIRGDFGL-YTPANIIHASDSKESAEREIKLFF 132
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 323-455 1.20e-08

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: 53.79  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 323 QRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDN-LIGYMCSNNSYILVLMREHS 400
Cdd:cd04412     1 NCTVCIIKPHAVSHGLlGEILQQILDEGFEITALQMFNLTRANAEEFLEVYKGVVPELPaMVDELTSGPCIALEIAGENA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046866160 401 VERWKELIGPKTVEEAYASHPDSLCVRFasGNFPV-NQFYGSSSKAAAETEIEHFF 455
Cdd:cd04412    81 VKTFREFCGPFDPEIAKQLRPNTLRARY--GKDKVqNAVHCTDLPEDGPLELKFFF 134
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 20-104 7.65e-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: 50.25  E-value: 7.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  20 WDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNEdelLHFVVAEADsivTLQPFRDKCE----PVFLFSLNGKII 95
Cdd:cd02947     3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPK---VKFVKVDVD---ENPELAEEYGvrsiPTFLFFKNGKEV 76


                  ....*....
gi 1046866160  96 AKIQGANAP 104
Cdd:cd02947    77 DRVVGADPK 85
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 13-102 1.05e-07

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: 50.31  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  13 VVNSQNlWDEMLLN-KGLTVIDVYQAWCGPCKAVQALFRKLKNELNEDelLHFVVAEADSIVTL-QPFRDKCEPVFLFSL 90
Cdd:pfam00085   4 VLTDAN-FDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN--VVFAKVDVDENPDLaSKYGVRGYPTLIFFK 80

                          90
                  ....*....|..
gi 1046866160  91 NGKIIAKIQGAN 102
Cdd:pfam00085  81 NGQPVDDYVGAR 92
PRK14544 PRK14544
nucleoside diphosphate kinase; Provisional
 456-591 1.99e-07

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173010 [Multi-domain]  Cd Length: 183  Bit Score: 51.35  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 456 PPQSTLALIKPH-VSHKERMEILKAIRDARFELTQMKEMHLTPEHASKVY--------------FKI------------- 507
Cdd:PRK14544    2 PIERTLVILKPDaVKRGLVGEIISRFEKAGLKIVAMKMVKATPEQIERFYpsseewyrsvgnklLKAyqelgidprarlg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 508 ------TGKDFYKNVLDVLSSGMSVVMILTKWNAVGEWRRMMGPVDPEEAKllsPNSLRARYGID----------VLRNA 571
Cdd:PRK14544   82 tddpveVGKKVKESLVKYMTSGPIVAMVLKGNRAVEVVRKLVGPTSPHKAP---PGTIRGDYSIDspdlaaeegrVVYNL 158

                         170       180
                  ....*....|....*....|
gi 1046866160 572 VHGASNMSEAATAISNVFTE 591
Cdd:PRK14544  159 VHASDSPEEAEREIKFWFRE 178
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 158-232 2.22e-07

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: 50.24  E-value: 2.22e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160  158 AVINPDAVLMRKNLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIIsQGED 232
Cdd:smart00562   5 AIIKPDAVQRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVL-EGED 78
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 324-455 2.57e-07

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 50.29  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 324 RTLGLLYPEVCEE-EKDNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHSVE 402
Cdd:PRK14545    5 RTFTMIKPDAVENgHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRGPIVAAILEKENAVE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160 403 RWKELIGPKTVEEAYAShpdSLCVRFASgNFPVNQFYGSSSKAAAETEIEHFF 455
Cdd:PRK14545   85 DFRTLIGATNPADAAEG---TIRKKYAK-SIGENAVHGSDSDENAQIEGAFHF 133
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 14-101 4.70e-07

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: 48.28  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNEDellhFVVAEAD--------------SIvtlqpfr 79
Cdd:COG3118     5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK----VKFVKVDvdenpelaaqfgvrSI------- 73

                          90       100
                  ....*....|....*....|..
gi 1046866160  80 dkcePVFLFSLNGKIIAKIQGA 101
Cdd:COG3118    74 ----PTLLLFKDGQPVDRFVGA 91
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 322-462 4.71e-07

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 49.56  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160 322 VQRTLGLLYPEVCEEEK-DNVLDIIQNEGFTILMQRQVVLSEEEARAVCHVHEDEDYFDNLIGYMCSNNSYILVLMREHS 400
Cdd:PRK14541    1 MERTLTILKPDCVRKQLiGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEKENA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046866160 401 VERWKELIGPKTVEEAYASHPDSLcvrFASGNFPvNQFYGSSSKAAAETEIEHFFPPQSTLA 462
Cdd:PRK14541   81 VADFRTLIGATDPAEAAEGTVRKL---YADSKGE-NIVHGSDSAENAAIEAGFFFSAEEVVR 138
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 29-110 6.06e-07

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


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 47.65  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  29 LTVIDVYQAWCGPCKAVQALFRKLKNELNEDELLHFVVAEADSIVTLQpFRDKCEPVFLFSLNGKIIAKIQGANAPLINR 108
Cdd:cd02984    16 LLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEK-FEITAVPTFVFFRNGTIVDRVSGADPKELAK 94


                  ..
gi 1046866160 109 KV 110
Cdd:cd02984    95 KV 96
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 155-229 6.85e-07

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: 48.89  E-value: 6.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 155 YNMAVINPDAVLMRKNLEIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIISQ 229
Cdd:cd00595     2 RTLALIKPDAVAEGLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEK 76
NDK pfam00334
Nucleoside diphosphate kinase;
157-232 1.30e-06

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 47.87  E-value: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046866160 157 MAVINPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRLSCVLIIsQGED 232
Cdd:pfam00334   4 LAIIKPDAV--QRGLigEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVL-EGEN 78
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-103 1.97e-05

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 43.71  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNE--------LNEDELLHfvVAEADSIVTLqpfrdkcePV 85
Cdd:PTZ00051    5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEytkmvfvkVDVDELSE--VAEKENITSM--------PT 74

                          90
                  ....*....|....*...
gi 1046866160  86 FLFSLNGKIIAKIQGANA 103
Cdd:PTZ00051   75 FKVFKNGSVVDTLLGAND 92
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 160-218 4.76e-05

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 43.56  E-value: 4.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046866160 160 INPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMT 218
Cdd:PRK00668    8 IKPDAV--QRGLigEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMT 66
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 13-65 1.61e-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: 41.06  E-value: 1.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1046866160  13 VVNSQNlWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNEDELLHFV 65
Cdd:cd02961     2 ELTDDN-FDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVA 53
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 160-232 2.65e-04

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: 41.21  E-value: 2.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 160 INPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRlSCVLIISQGED 232
Cdd:COG0105     9 IKPDAV--QRGLigEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSG-PVVAMVLEGEN 80
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-107 5.78e-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: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  14 VNSQNLWDEMLLNKGLTVIDVYQAWCGPCKAVQALFRKLKNE---------LNEDEllHFVVAEADSIVTLqpfrdkceP 84
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyegkvkfvkLNVDE--NPDIAAKYGIRSI--------P 70

                          90       100
                  ....*....|....*....|....*
gi 1046866160  85 VFLFSLNGKIIAKIQGAN--APLIN 107
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVGALpkAALKQ 95
NDPk_I cd04413
Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large ...
 160-232 7.60e-04

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: 39.76  E-value: 7.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046866160 160 INPDAVlmRKNL--EIKEKITKEGFIIEIQENMLLPEEVAREFYNHMIDEPDFEEFVYSMTNRlSCVLIISQGED 232
Cdd:cd04413     7 IKPDGV--QRGLigEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSG-PVVAMVLEGEN 78
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 25-116 1.77e-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: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046866160  25 LNKGLTVIDVYQAWCGPCKAVQALFRKLKNELNEdelLHFV-VAEADSIVTLQPFRDKCE---PV--------------- 85
Cdd:COG0526    26 LKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGG---VVFVgVDVDENPEAVKAFLKELGlpyPVlldpdgelakaygvr 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1046866160  86 -----FLFSLNGKIIAKIQGA-NAPLINRKVIALIDE 116
Cdd:COG0526   103 gipttVLIDKDGKIVARHVGPlSPEELEEALEKLLAK 139
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 13-57 8.49e-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: 8.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1046866160  13 VVNSQNLWdemllnkgltVIDVYQAWCGPCKAVQALFRKLKNELN 57
Cdd:cd03004    15 VLNRKEPW----------LVDFYAPWCGPCQALLPELRKAARALK 49
 
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