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Conserved domains on  [gi|1224459568|ref|WP_092481715|]
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(d)CMP kinase [Desulfoscipio geothermicus]

Protein Classification

(d)CMP kinase( domain architecture ID 10785233)

(d)CMP kinase catalyzes the phosphorylation of cytidine monophosphate (CMP) or dCMP to produce cytidine diphosphate (CDP) or dCDP, using ATP as the preferred phosphoryl donor

CATH:  3.40.50.300
Gene Ontology:  GO:0036431|GO:0006220|GO:0005524
PubMed:  10218107

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
7-225 1.67e-118

Cytidylate kinase [Nucleotide transport and metabolism];


:

Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 336.23  E-value: 1.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALRVNEkGHTRVYLNSLD 86
Cdd:COG0283     3 IAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDP-GGQRVFLNGED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:COG0283    82 VTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEKG 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIVTRVSGRFN 225
Cdd:COG0283   162 ISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERLS 220
 
Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
7-225 1.67e-118

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 336.23  E-value: 1.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALRVNEkGHTRVYLNSLD 86
Cdd:COG0283     3 IAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDP-GGQRVFLNGED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:COG0283    82 VTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEKG 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIVTRVSGRFN 225
Cdd:COG0283   162 ISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERLS 220
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
1-218 4.91e-93

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 281.77  E-value: 4.91e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   1 MDNRVSIAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALRVNEKGHTRV 80
Cdd:PRK13477  281 MKRQPIIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIELKPSSGSPQRV 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  81 YLNSLDVSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHA 160
Cdd:PRK13477  361 WINGEDVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGEKGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRAL 440

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224459568 161 ELQERGYT-LSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIVT 218
Cdd:PRK13477  441 DLQAQGFPvIDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSIEEVVDKIID 499
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 7-217 4.59e-92

Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.


Pssm-ID: 280401 [Multi-domain]  Cd Length: 211  Bit Score: 268.79  E-value: 4.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALrvnekGHTRVYLNSLD 86
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISF-----GHTEVFLNGED 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:pfam02224  76 VSSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIV 217
Cdd:pfam02224 156 LSVDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKIL 206
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
 6-217 2.24e-85

cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 129128 [Multi-domain]  Cd Length: 217  Bit Score: 252.35  E-value: 2.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   6 SIAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALrVNEKGHTRVYLNSL 85
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRF-IPTNGEVEVFLNGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  86 DVSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQER 165
Cdd:TIGR00017  83 DVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1224459568 166 GYTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIV 217
Cdd:TIGR00017 163 GNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVVEKIL 214
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 7-203 8.98e-67

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 202.33  E-value: 8.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGamyravtlqalmdkinindetaltrvavdvdialrvnekghtrvylnsld 86
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAKKLGLPYLDTG-------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 vskEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:cd02020    32 ---GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKG 108

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIID 203
Cdd:cd02020   109 EGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVID 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 6-70 9.50e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.43  E-value: 9.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568    6 SIAIDGPAGAGKSTVARLVAERL-----GYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIAL 70
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELgppggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
 
Name Accession Description Interval E-value
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
7-225 1.67e-118

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 336.23  E-value: 1.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALRVNEkGHTRVYLNSLD 86
Cdd:COG0283     3 IAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRNGIDLDDEEALAALARNLDIEFETDP-GGQRVFLNGED 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:COG0283    82 VTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPGLVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEKG 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIVTRVSGRFN 225
Cdd:COG0283   162 ISVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTTDLSIEEVVEKILALVRERLS 220
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
1-218 4.91e-93

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 281.77  E-value: 4.91e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   1 MDNRVSIAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALRVNEKGHTRV 80
Cdd:PRK13477  281 MKRQPIIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRAVTWLVLQEGIDPQDEEALAELLSDLKIELKPSSGSPQRV 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  81 YLNSLDVSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHA 160
Cdd:PRK13477  361 WINGEDVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRIGEKGGLVAEGRDIGTHVFPDAELKIFLTASVEERARRRAL 440

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1224459568 161 ELQERGYT-LSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIVT 218
Cdd:PRK13477  441 DLQAQGFPvIDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDGLSIEEVVDKIID 499
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
 7-217 4.59e-92

Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.


Pssm-ID: 280401 [Multi-domain]  Cd Length: 211  Bit Score: 268.79  E-value: 4.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALrvnekGHTRVYLNSLD 86
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQKVDLTDEDALAELASEVDISF-----GHTEVFLNGED 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:pfam02224  76 VSSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEGRDIGTVVFPDAEVKIFLTASPEERAKRRYKQLQAKG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIV 217
Cdd:pfam02224 156 LSVDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTIEEVVEKIL 206
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
 6-217 2.24e-85

cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 129128 [Multi-domain]  Cd Length: 217  Bit Score: 252.35  E-value: 2.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   6 SIAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALrVNEKGHTRVYLNSL 85
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAALQNRVDLTSEDALAELISHLDIRF-IPTNGEVEVFLNGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  86 DVSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQER 165
Cdd:TIGR00017  83 DVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIADGRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIK 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1224459568 166 GYTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIV 217
Cdd:TIGR00017 163 GNEVNFEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSIDEVVEKIL 214
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 7-203 8.98e-67

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 202.33  E-value: 8.98e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGamyravtlqalmdkinindetaltrvavdvdialrvnekghtrvylnsld 86
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAKKLGLPYLDTG-------------------------------------------------- 31

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 vskEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:cd02020    32 ---GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLEGRDIGTVVFPDADLKIFLTASPEVRAKRRAKQLQAKG 108

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIID 203
Cdd:cd02020   109 EGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVID 145
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
7-223 3.17e-61

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 202.58  E-value: 3.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIALRvnekgHTRVYLNSLD 86
Cdd:PRK11860  445 ICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRAGVALDDEAAIAALARGLPVRFE-----GDRIWLGGED 519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERG 166
Cdd:PRK11860  520 VTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLVADGRDMGTVIFPDAALKVFLTASAEARAERRYKQLISKG 599

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1224459568 167 YTLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIIDCSIMTVEQVVNLIVTRVSGR 223
Cdd:PRK11860  600 ISANIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTIEQAVAQVLDWWQER 656
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
 7-217 1.79e-52

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 179.61  E-value: 1.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDV------DIALRVNEK-GHTR 79
Cdd:PRK09518    4 VAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAELVDEQVVTEAvgefftGLHFDISVDpDSPG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  80 VYLNSLDVSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAARCS----------VVMEGRDIGTHVLPDADMKFFLTA 149
Cdd:PRK09518   84 VFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLIAAQRAYIAREAsadsfsgglgIVAEGRDITTVVAPDAEVRILLTA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224459568 150 SVEERARRRHAELQERgytlSFAEIVEDIKQRDNIDaSRAVAPLKPAPDAEIIDCSIMTVEQVVNLIV 217
Cdd:PRK09518  164 REEVRQARRSGQDRSE----TPGVVLEDVAARDEAD-SKVTSFLSAADGVTTLDNSDLDFDETLDLLI 226
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
 5-223 2.62e-31

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 120.59  E-value: 2.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   5 VSIAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQAL------------------------------------- 47
Cdd:PRK12269   35 VIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALrrvselavqacspspdpdaavgcaavphatnldtsya 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  48 ----MDKININDETALTRVAVDVDIALRVNEkghtrVYLNSLDVSKEIRSPEVSRHVSLVSRVPGVRKRMTQLQREMAAR 123
Cdd:PRK12269  115 pltaQKKVALFDEAYWVSFARTVALSYRAGV-----MYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568 124 CSVVMEGRDIGTHVLPDADMKFFLTASVEERARRRHAELQERgytLSFAEIVEDIKQRDNIDASRAVAPLKPAPDAEIID 203
Cdd:PRK12269  190 ARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSR---LSKQELEQRMRARDAHDRARTVGGLRCAPDALYVD 266

                         250       260
                  ....*....|....*....|
gi 1224459568 204 CSIMTVEQVVNLIVTRVSGR 223
Cdd:PRK12269  267 TSCLTIEEVCERIAREAHRR 286
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
7-224 7.34e-15

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 69.85  E-value: 7.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDtgamyRAVtLQALMDKININDEtaltrvavdvdIALRVNEKGHTRVYLNSLD 86
Cdd:COG1102     3 ITISREPGSGGTTIAKRLAEKLGLPLYD-----GEI-LREAAKERGLSEE-----------EFEKLDEKAPSLLYRDTAE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSKeirspevsrhvslvsrvpgVRKRMTQLQREMAARCSVVMEGRdIGTHVLPD--ADMKFFLTASVEERARRrhaeLQE 164
Cdd:COG1102    66 EDE-------------------IDRALDKVIRELARKGNCVIVGR-LADWILRDrpNVLKVFLTAPLEVRVKR----IAE 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224459568 165 RgYTLSFAEIVEDIKQRD-----------NIDASravaplkpapDAE----IIDCSIMTVEQVVNLIVTRVSGRF 224
Cdd:COG1102   122 R-EGISEEEAEKEIKKRDksrakyykyyyGIDWG----------DPSnydlVINTSRLGIEEAVDLILAAIEARE 185
PRK04182 PRK04182
cytidylate kinase; Provisional
 7-223 7.14e-13

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 64.44  E-value: 7.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRavtlqalmdkinindetaltrvavdvDIAlrvNEKGHTRVYLNSLD 86
Cdd:PRK04182    3 ITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFR--------------------------ELA---KERGMSLEEFNKYA 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 VSkeirSPEVSRHVSlvsrvpgvrkrmtQLQREMA-ARCSVVMEGRDIGTHVLPDADMKFFLTASVEERARRrhaeLQER 165
Cdd:PRK04182   54 EE----DPEIDKEID-------------RRQLEIAeKEDNVVLEGRLAGWMAKDYADLKIWLKAPLEVRAER----IAER 112

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568 166 GYTlSFAEIVEDIKQRDNIDASR------------AVAPLkpapdaeIIDCSIMTVEQVVNLIVTRVSGR 223
Cdd:PRK04182  113 EGI-SVEEALEETIEREESEAKRykeyygididdlSIYDL-------VINTSRWDPEGVFDIILTAIDKL 174
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 7-176 9.29e-10

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 55.89  E-value: 9.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVTLQALMDKININDETAltrvavdvdialrvnekghtrvylnsld 86
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKLISAGDIFRELAAKMGLDLIEFLNYAE---------------------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  87 vskeiRSPEVSRHVSlvsrvpgvrkrmtQLQREMAARC-SVVMEGRDIGTHVLPDADMKFFLTASVEERARRRhAELQER 165
Cdd:TIGR02173  55 -----ENPEIDKKID-------------RRIHEIALKEkNVVLESRLAGWIVREYADVKIWLKAPLEVRARRI-AKREGK 115

                         170
                  ....*....|.
gi 1224459568 166 GYTLSFAEIVE 176
Cdd:TIGR02173 116 SLTVARSETIE 126
aroK PRK00131
shikimate kinase; Reviewed
 1-35 2.47e-07

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 49.03  E-value: 2.47e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1224459568   1 MDNRVSIAIDGPAGAGKSTVARLVAERLGYIYIDT 35
Cdd:PRK00131    1 MLKGPNIVLIGFMGAGKSTIGRLLAKRLGYDFIDT 35
Cytidylate_kin2 pfam13189
Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.
 7-157 6.68e-07

Cytidylate kinase-like family; This family includes enzymes related to cytidylate kinase.


Pssm-ID: 433023 [Multi-domain]  Cd Length: 176  Bit Score: 47.62  E-value: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDTGAMYRAVtlqalmDKININDETAltrvavdvdialrvnEKGHTRVYLNSLd 86
Cdd:pfam13189   2 ITISRQYGSGGTTIAKKLAEKLGYPFYDREILDEIA------KELGISEEEF---------------ELFDEKSRLSSF- 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224459568  87 VSKEIRSPEVSRHVSLVSrvpgVRKRMTQLQREMAARCSVVMEGRDiGTHVLPDAD--MKFFLTASVEERARR 157
Cdd:pfam13189  60 LYSLAGGRVRGDALSDDR----LFDAQSKVIRELAAEDNCVIVGRG-ADYILKDIPnvLRVFLTAPLEDRVKR 127
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 6-35 2.65e-06

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 45.62  E-value: 2.65e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1224459568   6 SIAIDGPAGAGKSTVARLVAERLGYIYIDT 35
Cdd:cd00464     1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDL 30
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 11-41 3.46e-06

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 46.27  E-value: 3.46e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAMYRA 41
Cdd:COG0563     7 GPPGAGKGTQAKRLAEKYGIPHISTGDMLRA 37
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 7-34 8.20e-06

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 44.17  E-value: 8.20e-06
                          10        20
                  ....*....|....*....|....*...
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYID 34
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFID 29
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 11-35 1.49e-05

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 43.58  E-value: 1.49e-05
                          10        20
                  ....*....|....*....|....*
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDT 35
Cdd:COG0703     5 GMMGAGKSTVGRLLAKRLGLPFVDT 29
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 1-169 2.90e-05

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 43.29  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568   1 MDNRVSIAIDGPAGAGKSTVARLVAERLGY-----IYIDtgAMYRAVTLQALMDKININDETALtrvAVDVDI------A 69
Cdd:COG0572     4 SGKPRIIGIAGPSGSGKTTFARRLAEQLGAdkvvvISLD--DYYKDREHLPLDERGKPNFDHPE---AFDLDLlnehleP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568  70 LRVNEKGHTRVYlnslDVSKEIRSPEVsrhvslvsrvpgvrkrmtqlqREMAARCSVVMEGrdIGTH----VLPDADMKF 145
Cdd:COG0572    79 LKAGESVELPVY----DFATGTRSGET---------------------VKVEPADVIIVEG--IHALndelLRDLLDLKI 131

                         170       180
                  ....*....|....*....|....*
gi 1224459568 146 FLTASVEERARRRHA-ELQERGYTL 169
Cdd:COG0572   132 YVDADTDVRLIRRIVrDGEERGRTA 156
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
7-30 5.23e-05

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 42.47  E-value: 5.23e-05
                          10        20
                  ....*....|....*....|....
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGY 30
Cdd:COG1428     6 IAVEGNIGAGKTTLARLLAEHLGA 29
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 11-41 1.21e-04

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 41.45  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAMYRA 41
Cdd:cd01428     6 GPPGSGKGTQAERLAKKYGLPHISTGDLLRE 36
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 11-34 1.30e-04

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 40.88  E-value: 1.30e-04
                          10        20
                  ....*....|....*....|....
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYID 34
Cdd:COG3265     8 GVSGSGKSTVGQALAERLGWPFID 31
PRK03839 PRK03839
putative kinase; Provisional
 7-34 2.63e-04

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 40.47  E-value: 2.63e-04
                          10        20
                  ....*....|....*....|....*...
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYID 34
Cdd:PRK03839    3 IAITGTPGVGKTTVSKLLAEKLGYEYVD 30
SKI pfam01202
Shikimate kinase;
14-35 3.92e-04

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 39.49  E-value: 3.92e-04
                          10        20
                  ....*....|....*....|..
gi 1224459568  14 GAGKSTVARLVAERLGYIYIDT 35
Cdd:pfam01202   2 GAGKSTIGRLLAKALGLPFIDT 23
AAA_17 pfam13207
AAA domain;
11-65 4.03e-04

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 39.14  E-value: 4.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAMYRA-------VTLQALMDKININDETALTRVAVD 65
Cdd:pfam13207   2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLREeakerglVEDRDEMRKLPLEPQKELQKLAAE 63
dNK cd01673
Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to ...
 7-33 4.09e-04

Deoxyribonucleoside kinase (dNK) catalyzes the phosphorylation of deoxyribonucleosides to yield corresponding monophosphates (dNMPs). This family consists of various deoxynucleoside kinases including deoxyribo- cytidine (EC 2.7.1.74), guanosine (EC 2.7.1.113), adenosine (EC 2.7.1.76), and thymidine (EC 2.7.1.21) kinases. They are key enzymes in the salvage of deoxyribonucleosides originating from extra- or intracellular breakdown of DNA.


Pssm-ID: 238836  Cd Length: 193  Bit Score: 39.90  E-value: 4.09e-04
                          10        20
                  ....*....|....*....|....*..
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYI 33
Cdd:cd01673     2 IVVEGNIGAGKSTLAKELAEHLGYEVV 28
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
7-35 4.70e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.51  E-value: 4.70e-04
                          10        20
                  ....*....|....*....|....*....
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYIDT 35
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERLGAVRLRS 30
ADK pfam00406
Adenylate kinase;
11-50 6.54e-04

Adenylate kinase;


Pssm-ID: 395329 [Multi-domain]  Cd Length: 184  Bit Score: 39.21  E-value: 6.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAMYRA---------VTLQALMDK 50
Cdd:pfam00406   3 GPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAeiksgtelgKEAKEYMDK 51
adk PRK00279
adenylate kinase; Reviewed
 11-41 7.41e-04

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 39.36  E-value: 7.41e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAMYRA 41
Cdd:PRK00279    7 GPPGAGKGTQAKFIAEKYGIPHISTGDMLRA 37
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
7-34 9.61e-04

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 38.64  E-value: 9.61e-04
                          10        20
                  ....*....|....*....|....*...
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYIYID 34
Cdd:COG1936     3 IAITGTPGTGKTTVAKLLAERLGLEVIH 30
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 7-31 9.85e-04

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 36.55  E-value: 9.85e-04
                          10        20
                  ....*....|....*....|....*
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGYI 31
Cdd:cd02019     2 IAITGGSGSGKSTVAKKLAEQLGGR 26
aroL PRK03731
shikimate kinase AroL;
11-38 1.76e-03

shikimate kinase AroL;


Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 38.00  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|....*...
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAM 38
Cdd:PRK03731    9 GARGCGKTTVGMALAQALGYRFVDTDQW 36
PRK14526 PRK14526
adenylate kinase; Provisional
 11-59 3.66e-03

adenylate kinase; Provisional


Pssm-ID: 172992 [Multi-domain]  Cd Length: 211  Bit Score: 37.14  E-value: 3.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1224459568  11 GPAGAGKSTVARLVAERLGYIYIDTGAMYRAvtlqalmdkiNINDETAL 59
Cdd:PRK14526    7 GPPGSGKGTIAKILSNELNYYHISTGDLFRE----------NILNSTPL 45
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 6-53 4.06e-03

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 37.21  E-value: 4.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1224459568   6 SIAIDGPAGAGKSTVARL------VAErlGYIYIDtGAMYRAVTLQALMDKINI 53
Cdd:cd03253    29 KVAIVGPSGSGKSTILRLlfrfydVSS--GSILID-GQDIREVTLDSLRRAIGV 79
PRK06547 PRK06547
hypothetical protein; Provisional
 9-30 4.22e-03

hypothetical protein; Provisional


Pssm-ID: 235825  Cd Length: 172  Bit Score: 36.64  E-value: 4.22e-03
                          10        20
                  ....*....|....*....|..
gi 1224459568   9 IDGPAGAGKSTVARLVAERLGY 30
Cdd:PRK06547   20 IDGRSGSGKTTLAGALAARTGF 41
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 7-53 4.48e-03

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 37.49  E-value: 4.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1224459568   7 IAIDGPAGAGKSTVARLVAeRL-----GYIYIDtGAMYRAVTLQALMDKINI 53
Cdd:COG5265   387 VAIVGPSGAGKSTLARLLF-RFydvtsGRILID-GQDIRDVTQASLRAAIGI 436
AAA_18 pfam13238
AAA domain;
7-30 5.18e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 35.87  E-value: 5.18e-03
                          10        20
                  ....*....|....*....|....
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERLGY 30
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGF 24
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 7-28 7.24e-03

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 36.48  E-value: 7.24e-03
                          10        20
                  ....*....|....*....|..
gi 1224459568   7 IAIDGPAGAGKSTVARLVAERL 28
Cdd:cd01672     3 IVFEGIDGAGKTTLIELLAERL 24
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
7-51 9.40e-03

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 36.68  E-value: 9.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1224459568   7 IAIDGPAGAGKSTVARLVAeRL-----GYIYIDtGAMYRAVTLQALMDKI 51
Cdd:COG1132   369 VALVGPSGSGKSTLVNLLL-RFydptsGRILID-GVDIRDLTLESLRRQI 416
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 6-70 9.50e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.43  E-value: 9.50e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224459568    6 SIAIDGPAGAGKSTVARLVAERL-----GYIYIDTGAMYRAVTLQALMDKININDETALTRVAVDVDIAL 70
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELgppggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
 
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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