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Conserved domains on  [gi|119614489|gb|EAW94083|]
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thioredoxin domain containing 3 (spermatozoa), isoform CRA_a [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 451-582 3.69e-57

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: 188.19  E-value: 3.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAVA 530
Cdd:cd04416    1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119614489 531 EWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:cd04416   81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 316-448 8.97e-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: 181.64  E-value: 8.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFHERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGLQ 395
Cdd:cd04416    1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119614489 396 YWKQLLGPRTVEEAIEYFPESLCAQFAMDSLpVNQLYGSDSLETAEREIQHFF 448
Cdd:cd04416   81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHL-SNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 3.46e-53

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: 176.37  E-value: 3.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  11 QTVINNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNeDEILHFAVAEADNIVTLQPFRDKCEPVFLFSV 90
Cdd:cd02948    1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                         90       100
                 ....*....|....*....|...
gi 119614489  91 NGKIIEKIQGANAPLVNKKVINL 113
Cdd:cd02948   80 NGELVAVIRGANAPLLNKTITEL 102
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 154-304 1.67e-46

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: 159.68  E-value: 1.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 154 LYSIAIIKPDAVISKKvLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVVSQGskh 233
Cdd:cd04416    1 EYTLALIKPDAVAEKK-DEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKE--- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489 234 NPPSEETEPQTDTEPNErsedqpeveaqvtpgMMKNKQDSLQEYLERQHLAQLCDIEEDAANVAKFMDAFF 304
Cdd:cd04416   77 NAVEEWRELMGPTDPEE---------------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
 
Name Accession Description Interval E-value
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 451-582 3.69e-57

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: 188.19  E-value: 3.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAVA 530
Cdd:cd04416    1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119614489 531 EWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:cd04416   81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 316-448 8.97e-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: 181.64  E-value: 8.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFHERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGLQ 395
Cdd:cd04416    1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119614489 396 YWKQLLGPRTVEEAIEYFPESLCAQFAMDSLpVNQLYGSDSLETAEREIQHFF 448
Cdd:cd04416   81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHL-SNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 3.46e-53

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: 176.37  E-value: 3.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  11 QTVINNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNeDEILHFAVAEADNIVTLQPFRDKCEPVFLFSV 90
Cdd:cd02948    1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                         90       100
                 ....*....|....*....|...
gi 119614489  91 NGKIIEKIQGANAPLVNKKVINL 113
Cdd:cd02948   80 NGELVAVIRGANAPLLNKTITEL 102
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 451-586 2.69e-50

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: 170.04  E-value: 2.69e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   451 QSTLGLIKPHATS-EQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:smart00562   1 ERTLAIIKPDAVQrGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119614489   530 AEWRRLMGPTDPEEAkllSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPESE 134
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 316-453 5.45e-48

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: 163.88  E-value: 5.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   316 EKTLALLRPNLF-HERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:smart00562   1 ERTLAIIKPDAVqRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 119614489   395 QYWKQLLGPRTveeAIEYFPESLCAQFAMDsLPVNQLYGSDSLETAEREIQHFFPLQST 453
Cdd:smart00562  81 KTWRTLMGPTD---PREAAPGTIRGDFGLD-IGRNAVHGSDSPESAEREIALFFPESEI 135
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 154-304 1.67e-46

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: 159.68  E-value: 1.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 154 LYSIAIIKPDAVISKKvLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVVSQGskh 233
Cdd:cd04416    1 EYTLALIKPDAVAEKK-DEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKE--- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489 234 NPPSEETEPQTDTEPNErsedqpeveaqvtpgMMKNKQDSLQEYLERQHLAQLCDIEEDAANVAKFMDAFF 304
Cdd:cd04416   77 NAVEEWRELMGPTDPEE---------------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK pfam00334
Nucleoside diphosphate kinase;
451-586 1.51e-35

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 129.91  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  451 QSTLGLIKPHATseQR---EQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWN 527
Cdd:pfam00334   1 ERTLAIIKPDAV--QRgliGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGEN 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119614489  528 AVAEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:pfam00334  79 AISKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPEEE 134
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 453-586 4.13e-30

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: 115.16  E-value: 4.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 453 TLGLIKPHATseQREQILKIVK---EAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:COG0105    5 TLVIIKPDAV--QRGLIGEIISrfeRKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENAV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119614489 530 AEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:COG0105   83 AVVRKLMGATNPAEAA---PGTIRGDFALSIGENAVHGSDSPESAEREIALFFSEEE 136
NDK pfam00334
Nucleoside diphosphate kinase;
316-449 4.13e-28

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 109.11  E-value: 4.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  316 EKTLALLRPNLFHERK-DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119614489  395 QYWKQLLGPRTVEEAIeyfPESLCAQFAMDsLPVNQLYGSDSLETAEREIQHFFP 449
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVS-IGRNAVHGSDSPESAEREIALFFP 131
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 451-584 1.75e-25

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 103.37  E-value: 1.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATS-EQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:PLN02931  30 ERTLAMIKPDGLSgNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAV 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119614489 530 AEWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFED 584
Cdd:PLN02931 110 SDWRTLIGPTDARKAKISHPNSIRAMCGLDSEKNCVHGSDSPESAEREISFFFGD 164
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 316-448 4.14e-22

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 93.74  E-value: 4.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPN-LFHERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:PLN02931  30 ERTLAMIKPDgLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAV 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119614489 395 QYWKQLLGPRTVEEAIEYFPESLCAQFAMDSlPVNQLYGSDSLETAEREIQHFF 448
Cdd:PLN02931 110 SDWRTLIGPTDARKAKISHPNSIRAMCGLDS-EKNCVHGSDSPESAEREISFFF 162
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 314-449 3.41e-17

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: 78.57  E-value: 3.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 314 KLEKTLALLRPNLFHERK-DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDN 392
Cdd:COG0105    1 AMERTLVIIKPDAVQRGLiGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGEN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119614489 393 GLQYWKQLLGPRTVEEAIeyfPESLCAQFAMdSLPVNQLYGSDSLETAEREIQHFFP 449
Cdd:COG0105   81 AVAVVRKLMGATNPAEAA---PGTIRGDFAL-SIGENAVHGSDSPESAEREIALFFS 133
NDK pfam00334
Nucleoside diphosphate kinase;
158-228 5.04e-13

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 66.36  E-value: 5.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489  158 AIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVVS 228
Cdd:pfam00334   5 AIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLE 75
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 159-227 5.62e-10

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: 57.77  E-value: 5.62e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119614489 159 IIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVV 227
Cdd:COG0105    8 IIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVL 76
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 20-102 8.01e-10

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: 56.09  E-value: 8.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   20 WDEMLQN-KGLTVIDVYQAWCGPCKAMQPLFRKLKNELNEDeiLHFAVAEAD-NIVTLQPFRDKCEPVFLFSVNGKIIEK 97
Cdd:pfam00085  10 FDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN--VVFAKVDVDeNPDLASKYGVRGYPTLIFFKNGQPVDD 87


                  ....*
gi 119614489   98 IQGAN 102
Cdd:pfam00085  88 YVGAR 92
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 125-227 4.31e-09

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 55.99  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 125 MARPQYPEIPLVDSDSEVSEESPCESVQELYSIAIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRI 204
Cdd:PLN02931   1 ISRSTLQPLFLLLLASFPIRCSSSGASEEERTLAMIKPDGLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEH 80

                         90       100
                 ....*....|....*....|...
gi 119614489 205 ADQCDFEEFVSFMTSGLSYILVV 227
Cdd:PLN02931  81 SSRSFFPSLVKYMTSGPVLVMVL 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 14-101 4.78e-09

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: 54.06  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNE---------DEilHFAVAEADNIVTLqpfrdkceP 84
Cdd:COG3118    5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkvkfvkvdvDE--NPELAAQFGVRSI--------P 74

                         90
                 ....*....|....*..
gi 119614489  85 VFLFSVNGKIIEKIQGA 101
Cdd:COG3118   75 TLLLFKDGQPVDRFVGA 91
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-103 8.26e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.56  E-value: 8.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNE--------LNEDEILHfaVAEADNIVTLqpfrdkcePV 85
Cdd:PTZ00051   5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEytkmvfvkVDVDELSE--VAEKENITSM--------PT 74

                         90
                 ....*....|....*...
gi 119614489  86 FLFSVNGKIIEKIQGANA 103
Cdd:PTZ00051  75 FKVFKNGSVVDTLLGAND 92
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-102 6.47e-06

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: 44.97  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNE---------LNEDEilHFAVAEADNIVTLqpfrdkceP 84
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyegkvkfvkLNVDE--NPDIAAKYGIRSI--------P 70

                          90
                  ....*....|....*...
gi 119614489   85 VFLFSVNGKIIEKIQGAN 102
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVGAL 88
 
Name Accession Description Interval E-value
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 451-582 3.69e-57

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: 188.19  E-value: 3.69e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAVA 530
Cdd:cd04416    1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119614489 531 EWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:cd04416   81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 316-448 8.97e-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: 181.64  E-value: 8.97e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFHERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGLQ 395
Cdd:cd04416    1 EYTLALIKPDAVAEKKDEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKENAVE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119614489 396 YWKQLLGPRTVEEAIEYFPESLCAQFAMDSLpVNQLYGSDSLETAEREIQHFF 448
Cdd:cd04416   81 EWRELMGPTDPEEAKEEKPDSLRAQFARDHL-SNAVHGSSSAEEAEKEIDFFF 132
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 11-113 3.46e-53

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: 176.37  E-value: 3.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  11 QTVINNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNeDEILHFAVAEADNIVTLQPFRDKCEPVFLFSV 90
Cdd:cd02948    1 QVEINNQEEWEELLSNKGLTVVDVYQEWCGPCKAVVSLFKKIKNELG-DDLLHFATAEADTIDTLKRYRGKCEPTFLFYK 79

                         90       100
                 ....*....|....*....|...
gi 119614489  91 NGKIIEKIQGANAPLVNKKVINL 113
Cdd:cd02948   80 NGELVAVIRGANAPLLNKTITEL 102
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 451-586 2.69e-50

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: 170.04  E-value: 2.69e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   451 QSTLGLIKPHATS-EQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:smart00562   1 ERTLAIIKPDAVQrGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119614489   530 AEWRRLMGPTDPEEAkllSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:smart00562  81 KTWRTLMGPTDPREA---APGTIRGDFGLDIGRNAVHGSDSPESAEREIALFFPESE 134
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 451-582 2.70e-48

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: 164.45  E-value: 2.70e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQR-EQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:cd00595    1 ERTLALIKPDAVAEGLlGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119614489 530 AEWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:cd00595   81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLRNAVHGSDSVESAAREIAFFF 133
NDK smart00562
Enzymes that catalyze nonsubstrate specific conversions of nucleoside diphosphates to ...
 316-453 5.45e-48

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: 163.88  E-value: 5.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   316 EKTLALLRPNLF-HERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:smart00562   1 ERTLAIIKPDAVqRGLIGEIISRFERKGFKIVAMKMLQLTEEQAEEFYAEHEGKPFFNDLVEFMTSGPVVAMVLEGEDAV 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 119614489   395 QYWKQLLGPRTveeAIEYFPESLCAQFAMDsLPVNQLYGSDSLETAEREIQHFFPLQST 453
Cdd:smart00562  81 KTWRTLMGPTD---PREAAPGTIRGDFGLD-IGRNAVHGSDSPESAEREIALFFPESEI 135
NDPk_TX cd04416
NDP kinase domain of thioredoxin domain-containing proteins (TXNDC3 and TXNDC6): Txl-2 ...
 154-304 1.67e-46

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: 159.68  E-value: 1.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 154 LYSIAIIKPDAVISKKvLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVVSQGskh 233
Cdd:cd04416    1 EYTLALIKPDAVAEKK-DEILEKIKEAGFEILAQKEMVLTEEQAREFYKEHEEEDYFEDLVEFMTSGPSLILVLSKE--- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489 234 NPPSEETEPQTDTEPNErsedqpeveaqvtpgMMKNKQDSLQEYLERQHLAQLCDIEEDAANVAKFMDAFF 304
Cdd:cd04416   77 NAVEEWRELMGPTDPEE---------------AKEEKPDSLRAQFARDHLSNAVHGSSSAEEAEKEIDFFF 132
NDK pfam00334
Nucleoside diphosphate kinase;
451-586 1.51e-35

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 129.91  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  451 QSTLGLIKPHATseQR---EQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWN 527
Cdd:pfam00334   1 ERTLAIIKPDAV--QRgliGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGEN 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 119614489  528 AVAEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:pfam00334  79 AISKWRELMGATNPAEAA---PGTIRGDFAVSIGRNAVHGSDSPESAEREIALFFPEEE 134
NDPk cd00595
Nucleoside diphosphate kinases (NDP kinases, NDPks): NDP kinases, responsible for the ...
 316-448 5.83e-35

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: 128.24  E-value: 5.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFHE-RKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:cd00595    1 ERTLALIKPDAVAEgLLGEIIMRIEDAGFEIVAMKELHLTEEQAEEFYVEHKGRPFFPDLVQFMSSGPVVAMILEKDNAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119614489 395 QYWKQLLGPRTVEEAIEYFPESLCAQFAMDSLPvNQLYGSDSLETAEREIQHFF 448
Cdd:cd00595   81 GEWREMLGPTNPEIARHLAPGSLRADFGTDVLR-NAVHGSDSVESAAREIAFFF 133
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 453-576 1.35e-32

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: 121.78  E-value: 1.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 453 TLGLIKPHATSeQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAVAEW 532
Cdd:cd04418    3 TLAIIKPDAVH-KAEEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAISYW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119614489 533 RRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGaSNAYEAKE 576
Cdd:cd04418   82 KELLGPTNSLKAKETHPDSLRAIYGTDDLRNAVHG-SDSFSSAE 124
NDPk5 cd04418
Nucleoside diphosphate kinase homolog 5 (NDP kinase homolog 5, NDPk5, NM23-H5; Inhibitor of ...
 316-449 1.18e-30

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: 116.38  E-value: 1.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFHeRKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGLQ 395
Cdd:cd04418    1 ERTLAIIKPDAVH-KAEEIEDIILESGFTIVQKRKLQLSPEQCSDFYAEHYGKMFFPHLVAYMSSGPIVAMVLARHNAIS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119614489 396 YWKQLLGPRTVEEAIEYFPESLCAQFAMDSLPvNQLYGSDSLETAEREIQHFFP 449
Cdd:cd04418   80 YWKELLGPTNSLKAKETHPDSLRAIYGTDDLR-NAVHGSDSFSSAEREIRFMFP 132
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 453-586 4.13e-30

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: 115.16  E-value: 4.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 453 TLGLIKPHATseQREQILKIVK---EAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:COG0105    5 TLVIIKPDAV--QRGLIGEIISrfeRKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGENAV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119614489 530 AEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:COG0105   83 AVVRKLMGATNPAEAA---PGTIRGDFALSIGENAVHGSDSPESAEREIALFFSEEE 136
NDK pfam00334
Nucleoside diphosphate kinase;
316-449 4.13e-28

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 109.11  E-value: 4.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  316 EKTLALLRPNLFHERK-DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:pfam00334   1 ERTLAIIKPDAVQRGLiGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLEGENAI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119614489  395 QYWKQLLGPRTVEEAIeyfPESLCAQFAMDsLPVNQLYGSDSLETAEREIQHFFP 449
Cdd:pfam00334  81 SKWRELMGATNPAEAA---PGTIRGDFAVS-IGRNAVHGSDSPESAEREIALFFP 131
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 451-577 2.22e-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: 107.10  E-value: 2.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQ--REQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNA 528
Cdd:cd04414    1 QLTLALIKPDAVAHPlaLEAVRQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHENA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119614489 529 VAEWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGA-SNAYEAKEV 577
Cdd:cd04414   81 IKTWRALMGPTKVFRARASAPDSIRGLYGLTDTRNATHGSdSPASAQREI 130
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 316-449 1.71e-26

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: 104.79  E-value: 1.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFheRKDDVL----RIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRD 391
Cdd:cd04414    1 QLTLALIKPDAV--AHPLALeavrQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILAHE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119614489 392 NGLQYWKQLLGPRTVEEAIEYFPESLCAQFAMDSLPvNQLYGSDSLETAEREIQHFFP 449
Cdd:cd04414   79 NAIKTWRALMGPTKVFRARASAPDSIRGLYGLTDTR-NATHGSDSPASAQREIALFFP 135
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 451-582 3.02e-26

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


Pssm-ID: 239878  Cd Length: 131  Bit Score: 104.06  E-value: 3.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQREqILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAVA 530
Cdd:cd04415    1 EKTLALIKPDAYSKIGK-IIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVGDDAIS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119614489 531 EWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:cd04415   80 EWRKLLGPTNSSVARSDAPNSIRALFGTDGTRNAAHGSDSVASAARELEFFF 131
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 451-584 1.75e-25

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 103.37  E-value: 1.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATS-EQREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:PLN02931  30 ERTLAMIKPDGLSgNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAV 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119614489 530 AEWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFED 584
Cdd:PLN02931 110 SDWRTLIGPTDARKAKISHPNSIRAMCGLDSEKNCVHGSDSPESAEREISFFFGD 164
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 451-582 3.99e-25

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: 100.79  E-value: 3.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 451 QSTLGLIKPHATSEQRE-QILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKD-FYKDLLEMLSVGPSMVMILTKWNA 528
Cdd:cd04412    1 NCTVCIIKPHAVSHGLLgEILQQILDEGFEITALQMFNLTRANAEEFLEVYKGVVpELPAMVDELTSGPCIALEIAGENA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119614489 529 VAEWRRLMGPTDPEEAKLLSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:cd04412   81 VKTFREFCGPFDPEIAKQLRPNTLRARYGKDKVQNAVHCTDLPEDGPLELKFFF 134
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 453-567 4.64e-25

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 100.57  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 453 TLGLIKPHATseQREQILKIVK---EAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAV 529
Cdd:PRK00668   4 TFSIIKPDAV--QRGLIGEIISrfeKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLEGENAI 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119614489 530 AEWRRLMGPTDPEEAkllSPDSIRAQFGISKLKNIVHG 567
Cdd:PRK00668  82 AKVRELMGATNPAEA---APGTIRGDFALSIGENVVHG 116
NDPk7A cd04415
Nucleoside diphosphate kinase 7 domain A (NDPk7A): The nm23-H7 class of nucleoside diphosphate ...
 316-448 1.67e-24

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: 99.06  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFhERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGLQ 395
Cdd:cd04415    1 EKTLALIKPDAY-SKIGKIIQIIEDAGFTITKAKMTKLSRKEAQDFYAEHQSKPFYNELVQFMTSGPIVAMELVGDDAIS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119614489 396 YWKQLLGPRTVEEAIEYFPESLCAQFAMDSLPvNQLYGSDSLETAEREIQHFF 448
Cdd:cd04415   80 EWRKLLGPTNSSVARSDAPNSIRALFGTDGTR-NAAHGSDSVASAARELEFFF 131
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 316-448 4.14e-22

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 93.74  E-value: 4.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPN-LFHERKDDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:PLN02931  30 ERTLAMIKPDgLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEHSSRSFFPSLVKYMTSGPVLVMVLEKENAV 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119614489 395 QYWKQLLGPRTVEEAIEYFPESLCAQFAMDSlPVNQLYGSDSLETAEREIQHFF 448
Cdd:PLN02931 110 SDWRTLIGPTDARKAKISHPNSIRAMCGLDS-EKNCVHGSDSPESAEREISFFF 162
PTZ00093 PTZ00093
nucleoside diphosphate kinase, cytosolic; Provisional
 449-587 5.23e-19

nucleoside diphosphate kinase, cytosolic; Provisional


Pssm-ID: 173387  Cd Length: 149  Bit Score: 84.00  E-value: 5.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 449 PLQSTLGLIKPHATseQREQILKIVK---EAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTK 525
Cdd:PTZ00093   1 SSERTFIMVKPDGV--QRGLVGEIIKrfeKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSGPVVCMVWEG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119614489 526 WNAVAEWRRLMGPTDPEEAkllSPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEdPEE 587
Cdd:PTZ00093  79 KNVVKQGRKLLGATNPLES---APGTIRGDFCVDVGRNVIHGSDSVESAKREIALWFK-PEE 136
NDPk_I cd04413
Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large ...
 316-448 9.81e-19

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: 82.52  E-value: 9.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPNLFHERK-DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGL 394
Cdd:cd04413    1 ERTLVIIKPDGVQRGLiGEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSGPVVAMVLEGENAV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119614489 395 QYWKQLLGPRTVEEAIeyfPESLCAQFAMdSLPVNQLYGSDSLETAEREIQHFF 448
Cdd:cd04413   81 KTVRKLMGATNPADAA---PGTIRGDFAL-SIGRNIVHGSDSVESAEREIALWF 130
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 450-575 4.88e-18

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 80.76  E-value: 4.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 450 LQSTLGLIKPHATSEQR-EQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNA 528
Cdd:PRK14541   1 MERTLTILKPDCVRKQLiGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEKENA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119614489 529 VAEWRRLMGPTDPEEAkllSPDSIRAQFGISKLKNIVHGASNAYEAK 575
Cdd:PRK14541  81 VADFRTLIGATDPAEA---AEGTVRKLYADSKGENIVHGSDSAENAA 124
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 315-449 3.31e-17

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 78.22  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 315 LEKTLALLRP-----NLFHErkddVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLL 389
Cdd:PRK00668   1 MERTFSIIKPdavqrGLIGE----IISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSGPVVVMVLE 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 390 RDNGLQYWKQLLGPRTVEEAIeyfPESLCAQFAMdSLPVNQLYGSDSLETAEREIQHFFP 449
Cdd:PRK00668  77 GENAIAKVRELMGATNPAEAA---PGTIRGDFAL-SIGENVVHGSDSPESAAREIALFFS 132
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 314-449 3.41e-17

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: 78.57  E-value: 3.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 314 KLEKTLALLRPNLFHERK-DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDN 392
Cdd:COG0105    1 AMERTLVIIKPDAVQRGLiGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVLEGEN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119614489 393 GLQYWKQLLGPRTVEEAIeyfPESLCAQFAMdSLPVNQLYGSDSLETAEREIQHFFP 449
Cdd:COG0105   81 AVAVVRKLMGATNPAEAA---PGTIRGDFAL-SIGENAVHGSDSPESAEREIALFFS 133
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 450-588 4.91e-17

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 77.79  E-value: 4.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 450 LQSTLGLIKPHATSEQR-EQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNA 528
Cdd:PRK14542   1 MSRTFIMIKPDGVKNKHvGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALERDNA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 529 VAEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEDPEEN 588
Cdd:PRK14542  81 VLHWREVIGATDPKEAA---AGTIRALYAESKEANAVHGSDSDANAALEISFFFKGNELF 137
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 453-568 3.54e-16

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 75.71  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 453 TLGLIKPHATSE-QREQILKIVKEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKWNAVAE 531
Cdd:PRK14545   6 TFTMIKPDAVENgHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRGPIVAAILEKENAVED 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119614489 532 WRRLMGPTDPEEAkllSPDSIRAQFGISKLKNIVHGA 568
Cdd:PRK14545  86 FRTLIGATNPADA---AEGTIRKKYAKSIGENAVHGS 119
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 450-582 4.00e-16

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 75.24  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 450 LQSTLGLIKPHATseQREQILKIVK---EAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMILTKW 526
Cdd:PRK14540   2 KERTFVALKPDAV--ERKLIGKIIQrfeNKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVIEGE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119614489 527 NAVAEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLF 582
Cdd:PRK14540  80 NAISTVRKMIGKTNPAEAE---PGTIRGDFGLYTPANIIHASDSKESAEREIKLFF 132
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 315-448 5.73e-16

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 74.86  E-value: 5.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 315 LEKTLALLRPNLFhERK--DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDN 392
Cdd:PRK14540   2 KERTFVALKPDAV-ERKliGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVIEGEN 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119614489 393 GLQYWKQLLGPRTVEEAieyFPESLCAQFAMdSLPVNQLYGSDSLETAEREIQHFF 448
Cdd:PRK14540  81 AISTVRKMIGKTNPAEA---EPGTIRGDFGL-YTPANIIHASDSKESAEREIKLFF 132
PRK14542 PRK14542
nucleoside diphosphate kinase; Provisional
 315-448 1.54e-15

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173008 [Multi-domain]  Cd Length: 137  Bit Score: 73.55  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 315 LEKTLALLRPNLFHERK-DDVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNG 393
Cdd:PRK14542   1 MSRTFIMIKPDGVKNKHvGNILQRIEKEGFKILGLKYLKLSLEDAKQFYKVHSARPFYNDLCNYMSSGPIVAAALERDNA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119614489 394 LQYWKQLLGPRTVEEAIEYFPESLCAQfamdSLPVNQLYGSDSLETAEREIQHFF 448
Cdd:PRK14542  81 VLHWREVIGATDPKEAAAGTIRALYAE----SKEANAVHGSDSDANAALEISFFF 131
NDK pfam00334
Nucleoside diphosphate kinase;
158-228 5.04e-13

Nucleoside diphosphate kinase;


Pssm-ID: 459766  Cd Length: 135  Bit Score: 66.36  E-value: 5.04e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489  158 AIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVVS 228
Cdd:pfam00334   5 AIIKPDAVQRGLIGEIISRFERKGFKIVALKMLQLTREQAEEHYAEHKGKPFFPDLVEFMTSGPVVAMVLE 75
PLN02619 PLN02619
nucleoside-diphosphate kinase
 446-587 1.14e-11

nucleoside-diphosphate kinase


Pssm-ID: 178228  Cd Length: 238  Bit Score: 64.87  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 446 HFFPLQSTLGLIKPHATseQREQILKIV---KEAGFDLTQVKKMFLTPEQIEKIYPKVTGKDFYKDLLEMLSVGPSMVMI 522
Cdd:PLN02619  84 HAAEMERTFIAIKPDGV--QRGLISEIIsrfERKGFKLVAIKVVVPSKEFAQKHYHDLKERPFFNGLCDFLSSGPVVAMV 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119614489 523 LTKWNAVAEWRRLMGPTDPEEAKllsPDSIRAQFGISKLKNIVHGASNAYEAKEVVNRLFEdPEE 587
Cdd:PLN02619 162 WEGEGVIKYGRKLIGATDPQKSE---PGTIRGDLAVVVGRNIIHGSDGPETAKDEINLWFK-PEE 222
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 20-104 2.52e-11

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


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 60.26  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  20 WDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNEDEIL------HFAVAEADNIVTLqpfrdkcePVFLFSVNGK 93
Cdd:cd02947    3 FEELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVkvdvdeNPELAEEYGVRSI--------PTFLFFKNGK 74

                         90
                 ....*....|.
gi 119614489  94 IIEKIQGANAP 104
Cdd:cd02947   75 EVDRVVGADPK 85
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 334-448 2.23e-10

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: 58.80  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 334 VLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENED-YFNKLIENMTSGPSLALVLLRDNGLQYWKQLLGPRTVEEAIEY 412
Cdd:cd04412   20 ILQQILDEGFEITALQMFNLTRANAEEFLEVYKGVVpELPAMVDELTSGPCIALEIAGENAVKTFREFCGPFDPEIAKQL 99

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119614489 413 FPESLCAQFAMDSLPvNQLYGSDSLETAEREIQHFF 448
Cdd:cd04412  100 RPNTLRARYGKDKVQ-NAVHCTDLPEDGPLELKFFF 134
Ndk COG0105
Nucleoside diphosphate kinase [Nucleotide transport and metabolism]; Nucleoside diphosphate ...
 159-227 5.62e-10

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: 57.77  E-value: 5.62e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119614489 159 IIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVV 227
Cdd:COG0105    8 IIKPDAVQRGLIGEIISRFERKGLKIVALKMLQLTREQAEEHYAEHKGKPFFGELVEFMTSGPVVAMVL 76
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 20-102 8.01e-10

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: 56.09  E-value: 8.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   20 WDEMLQN-KGLTVIDVYQAWCGPCKAMQPLFRKLKNELNEDeiLHFAVAEAD-NIVTLQPFRDKCEPVFLFSVNGKIIEK 97
Cdd:pfam00085  10 FDEVVQKsSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGN--VVFAKVDVDeNPDLASKYGVRGYPTLIFFKNGQPVDD 87


                  ....*
gi 119614489   98 IQGAN 102
Cdd:pfam00085  88 YVGAR 92
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 315-451 1.13e-09

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 56.88  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 315 LEKTLALLRPNLFheRKD---DVLRIIKDEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRD 391
Cdd:PRK14541   1 MERTLTILKPDCV--RKQligAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSGPCVPMILEKE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 392 NGLQYWKQLLGPRTVEEAIEYFPESLCAqfamDSLPVNQLYGSDSLETAEREIQHFFPLQ 451
Cdd:PRK14541  79 NAVADFRTLIGATDPAEAAEGTVRKLYA----DSKGENIVHGSDSAENAAIEAGFFFSAE 134
PRK14544 PRK14544
nucleoside diphosphate kinase; Provisional
 449-586 1.17e-09

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173010 [Multi-domain]  Cd Length: 183  Bit Score: 57.90  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 449 PLQSTLGLIKPHATSeqREQILKIV---KEAGFDLTQVKKMFLTPEQIEKIYPKV------------------------- 500
Cdd:PRK14544   2 PIERTLVILKPDAVK--RGLVGEIIsrfEKAGLKIVAMKMVKATPEQIERFYPSSeewyrsvgnkllkayqelgidprar 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 501 --------TGKDFYKDLLEMLSVGPSMVMILTKWNAVAEWRRLMGPTDPEEAKllsPDSIRAQFGISK----------LK 562
Cdd:PRK14544  80 lgtddpveVGKKVKESLVKYMTSGPIVAMVLKGNRAVEVVRKLVGPTSPHKAP---PGTIRGDYSIDSpdlaaeegrvVY 156

                        170       180
                 ....*....|....*....|....
gi 119614489 563 NIVHGASNAYEAKEVVNRLFEDPE 586
Cdd:PRK14544 157 NLVHASDSPEEAEREIKFWFREEE 180
PLN02931 PLN02931
nucleoside diphosphate kinase family protein
 125-227 4.31e-09

nucleoside diphosphate kinase family protein


Pssm-ID: 215503  Cd Length: 177  Bit Score: 55.99  E-value: 4.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 125 MARPQYPEIPLVDSDSEVSEESPCESVQELYSIAIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRI 204
Cdd:PLN02931   1 ISRSTLQPLFLLLLASFPIRCSSSGASEEERTLAMIKPDGLSGNYTERIKEVILESGFSIVKEMTTQLDEDRASLFYAEH 80

                         90       100
                 ....*....|....*....|...
gi 119614489 205 ADQCDFEEFVSFMTSGLSYILVV 227
Cdd:PLN02931  81 SSRSFFPSLVKYMTSGPVLVMVL 103
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 14-101 4.78e-09

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: 54.06  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNE---------DEilHFAVAEADNIVTLqpfrdkceP 84
Cdd:COG3118    5 LTDENFEEEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkvkfvkvdvDE--NPELAAQFGVRSI--------P 74

                         90
                 ....*....|....*..
gi 119614489  85 VFLFSVNGKIIEKIQGA 101
Cdd:COG3118   75 TLLLFKDGQPVDRFVGA 91
ndk PRK00668
mulitfunctional nucleoside diphosphate kinase/apyrimidinic endonuclease/3'-; Validated
 159-220 4.38e-08

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


Pssm-ID: 179085  Cd Length: 134  Bit Score: 52.03  E-value: 4.38e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119614489 159 IIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSG 220
Cdd:PRK00668   7 IIKPDAVQRGLIGEIISRFEKKGLKIVALKMMQLSRELAEGHYAEHKEKPFFGELVEFMTSG 68
NDPk_I cd04413
Nucleoside diphosphate kinase Group I (NDPk_I)-like: NDP kinase domains are present in a large ...
 159-220 4.69e-08

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: 52.09  E-value: 4.69e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119614489 159 IIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSG 220
Cdd:cd04413    6 IIKPDGVQRGLIGEIISRFERKGLKIVALKMLQLTEELAEEHYAEHKGKPFFPELVEFMTSG 67
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 20-65 5.92e-07

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: 47.99  E-value: 5.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119614489  20 WDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNEDEILHFA 65
Cdd:cd02961    8 FDELVKDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVA 53
PTZ00051 PTZ00051
thioredoxin; Provisional
 14-103 8.26e-07

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 47.56  E-value: 8.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNE--------LNEDEILHfaVAEADNIVTLqpfrdkcePV 85
Cdd:PTZ00051   5 VTSQAEFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEytkmvfvkVDVDELSE--VAEKENITSM--------PT 74

                         90
                 ....*....|....*...
gi 119614489  86 FLFSVNGKIIEKIQGANA 103
Cdd:PTZ00051  75 FKVFKNGSVVDTLLGAND 92
NDPk6 cd04414
Nucleoside diphosphate kinase 6 (NDP kinase 6, NDPk6, NM23-H6; NME6; Inhibitor of p53-induced ...
 156-228 1.00e-06

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: 48.16  E-value: 1.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119614489 156 SIAIIKPDAVISKKVLE-IKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVVS 228
Cdd:cd04414    3 TLALIKPDAVAHPLALEaVRQLILSNGFTIVRKKELRWTTEDAERFYAEHKGKFFYDRLVSFMTSGPSWALILA 76
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 17-110 1.01e-06

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


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 47.27  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  17 QSLWDEMLQNKG--LTVIDVYQAWCGPCKAMQPLFRKLKNELNEDeiLHFAVAEADNIVTL-QPFRDKCEPVFLFSVNGK 93
Cdd:cd02984    2 EEEFEELLKSDAskLLVLHFWAPWAEPCKQMNQVFEELAKEAFPS--VLFLSIEAEELPEIsEKFEITAVPTFVFFRNGT 79

                         90
                 ....*....|....*..
gi 119614489  94 IIEKIQGANAPLVNKKV 110
Cdd:cd02984   80 IVDRVSGADPKELAKKV 96
PTZ00093 PTZ00093
nucleoside diphosphate kinase, cytosolic; Provisional
 316-448 3.38e-06

nucleoside diphosphate kinase, cytosolic; Provisional


Pssm-ID: 173387  Cd Length: 149  Bit Score: 47.02  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 316 EKTLALLRPnlfherkDDVLR-----IIK---DEDFKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALV 387
Cdd:PTZ00093   3 ERTFIMVKP-------DGVQRglvgeIIKrfeKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSGPVVCMV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489 388 LLRDNGLQYWKQLLGprtVEEAIEYFPESLCAQFAMDsLPVNQLYGSDSLETAEREIQHFF 448
Cdd:PTZ00093  76 WEGKNVVKQGRKLLG---ATNPLESAPGTIRGDFCVD-VGRNVIHGSDSVESAKREIALWF 132
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 14-102 6.47e-06

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: 44.97  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489   14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNE---------LNEDEilHFAVAEADNIVTLqpfrdkceP 84
Cdd:TIGR01068   1 LTDANFDETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEyegkvkfvkLNVDE--NPDIAAKYGIRSI--------P 70

                          90
                  ....*....|....*...
gi 119614489   85 VFLFSVNGKIIEKIQGAN 102
Cdd:TIGR01068  71 TLLLFKNGKEVDRSVGAL 88
PRK14544 PRK14544
nucleoside diphosphate kinase; Provisional
 373-448 9.71e-06

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173010 [Multi-domain]  Cd Length: 183  Bit Score: 46.34  E-value: 9.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 373 KLIENMTSGPSLALVLLRDNGLQYWKQLLGPRTVEEAIeyfPESLCAQFAMDSLPV---------NQLYGSDSLETAERE 443
Cdd:PRK14544  95 SLVKYMTSGPIVAMVLKGNRAVEVVRKLVGPTSPHKAP---PGTIRGDYSIDSPDLaaeegrvvyNLVHASDSPEEAERE 171


                 ....*
gi 119614489 444 IQHFF 448
Cdd:PRK14544 172 IKFWF 176
PRK14541 PRK14541
nucleoside diphosphate kinase; Provisional
 156-220 1.72e-05

nucleoside diphosphate kinase; Provisional


Pssm-ID: 173007  Cd Length: 140  Bit Score: 44.94  E-value: 1.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119614489 156 SIAIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSG 220
Cdd:PRK14541   4 TLTILKPDCVRKQLIGAVIDKIERAGFRVVAMKKTRLTKETAGEFYAVHRERPFYGELVEFMSSG 68
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 12-57 2.70e-05

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: 43.43  E-value: 2.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 119614489  12 TVINNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELN 57
Cdd:cd03004    4 ITLTPEDFPELVLNRKEPWLVDFYAPWCGPCQALLPELRKAARALK 49
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 30-101 4.14e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 43.53  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  30 TVIDVYQAWCGPCKAMQPLFRKLKNELNEDEILhfAVAEADNIVTLQPFRDKCE---PV--------------------F 86
Cdd:COG0526   31 VLVNFWATWCPPCRAEMPVLKELAEEYGGVVFV--GVDVDENPEAVKAFLKELGlpyPVlldpdgelakaygvrgipttV 108

                         90
                 ....*....|....*
gi 119614489  87 LFSVNGKIIEKIQGA 101
Cdd:COG0526  109 LIDKDGKIVARHVGP 123
PRK14545 PRK14545
nucleoside diphosphate kinase; Provisional
 156-220 5.76e-05

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184734  Cd Length: 139  Bit Score: 43.36  E-value: 5.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119614489 156 SIAIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSG 220
Cdd:PRK14545   6 TFTMIKPDAVENGHIGGILDMITAAGFRIVAMKLTQLTVADAETFYAVHAERPFYGELVEFMSRG 70
PTZ00093 PTZ00093
nucleoside diphosphate kinase, cytosolic; Provisional
 160-220 2.68e-04

nucleoside diphosphate kinase, cytosolic; Provisional


Pssm-ID: 173387  Cd Length: 149  Bit Score: 41.63  E-value: 2.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119614489 160 IKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSG 220
Cdd:PTZ00093   9 VKPDGVQRGLVGEIIKRFEKKGYKLVALKMLQPTPEIAEEHYKEHKGKPFFPGLVKYISSG 69
trxA PRK09381
thioredoxin TrxA;
14-55 4.43e-04

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 40.05  E-value: 4.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119614489  14 INNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNE 55
Cdd:PRK09381   8 LTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADE 49
PLN02619 PLN02619
nucleoside-diphosphate kinase
 343-448 1.05e-03

nucleoside-diphosphate kinase


Pssm-ID: 178228  Cd Length: 238  Bit Score: 40.99  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489 343 FKILEQRQVVLSEKEAQALCKEYENEDYFNKLIENMTSGPSLALVLLRDNGLQYWKQLLG---PRTVEeaieyfPESLCA 419
Cdd:PLN02619 117 FKLVAIKVVVPSKEFAQKHYHDLKERPFFNGLCDFLSSGPVVAMVWEGEGVIKYGRKLIGatdPQKSE------PGTIRG 190

                         90       100
                 ....*....|....*....|....*....
gi 119614489 420 QFAMdSLPVNQLYGSDSLETAEREIQHFF 448
Cdd:PLN02619 191 DLAV-VVGRNIIHGSDGPETAKDEINLWF 218
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
30-101 1.32e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.08  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  30 TVIDVYQAWCGPCKAMQPLFRKLKNELNEDEILHFAVAeADNIVTLQPFRDK----------------------CEP-VF 86
Cdd:COG1225   24 VVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVS-SDSDEAHKKFAEKyglpfpllsdpdgevakaygvrGTPtTF 102

                         90
                 ....*....|....*
gi 119614489  87 LFSVNGKIIEKIQGA 101
Cdd:COG1225  103 LIDPDGKIRYVWVGP 117
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 21-103 1.40e-03

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


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 38.45  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  21 DEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNELNEDEILHFA---VAEADNIVTLQPFRDKCEPVFLFSVNGKIIEK 97
Cdd:cd02997   11 RKFLKKEKHVLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVLAavdCTKPEHDALKEEYNVKGFPTFKYFENGKFVEK 90


                 ....*.
gi 119614489  98 IQGANA 103
Cdd:cd02997   91 YEGERT 96
PRK10996 PRK10996
thioredoxin 2; Provisional
 21-101 3.55e-03

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 38.13  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119614489  21 DEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKLKNElNEDEILHFAV-AEADNIVTLQpFRDKCEPVFLFSVNGKIIEKIQ 99
Cdd:PRK10996  46 DKLLQDDLPVVIDFWAPWCGPCRNFAPIFEDVAAE-RSGKVRFVKVnTEAERELSAR-FRIRSIPTIMIFKNGQVVDMLN 123


                 ..
gi 119614489 100 GA 101
Cdd:PRK10996 124 GA 125
PRK14540 PRK14540
nucleoside diphosphate kinase; Provisional
 156-227 4.24e-03

nucleoside diphosphate kinase; Provisional


Pssm-ID: 184733  Cd Length: 134  Bit Score: 37.88  E-value: 4.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119614489 156 SIAIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFYSRIADQCDFEEFVSFMTSGLSYILVV 227
Cdd:PRK14540   5 TFVALKPDAVERKLIGKIIQRFENKGFEIVEMKMLKLTREMAEEYYEEHKGKEFYERLINFMTSGRIVAMVI 76
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 15-52 5.04e-03

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 38.22  E-value: 5.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 119614489   15 NNQSLWDEMLQNKGLTVIDVYQAWCGPCKAMQPLFRKL 52
Cdd:TIGR00385  51 PGQFYTADVLTQGKPVLLNVWASWCPPCRAEHPYLNEL 88
NDPk7B cd04412
Nucleoside diphosphate kinase 7 domain B (NDPk7B): The nm23-H7 class of nucleoside diphosphate ...
 156-229 9.66e-03

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: 36.84  E-value: 9.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119614489 156 SIAIIKPDAVISKKVLEIKRKITKAGFIIEAEHKTVLTEEQVVNFY----SRIAdqcDFEEFVSFMTSGLSYILVVSQ 229
Cdd:cd04412    3 TVCIIKPHAVSHGLLGEILQQILDEGFEITALQMFNLTRANAEEFLevykGVVP---ELPAMVDELTSGPCIALEIAG 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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