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Conserved domains on  [gi|515496824|ref|WP_016930078|]
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MULTISPECIES: NTP transferase domain-containing protein [Serratia]

Protein Classification

MocA family protein( domain architecture ID 10005267)

MocA family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-192 2.33e-47

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


:

Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 153.39  E-value: 2.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   1 MTTGIVITAAGRGERFiqaggQGNKLnagFADAAGeqRSLFEHTLRRALASGL-PVHVVARPDNLPVLAACAanQVPVTL 79
Cdd:COG2068    2 SKVAAIILAAGASSRM-----GRPKL---LLPLGG--KPLLERAVEAALAAGLdPVVVVLGADAEEVAAALA--GLGVRV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  80 L----ASAGLGDSIAAGVAATP-HWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPL 152
Cdd:COG2068   70 VvnpdWEEGMSSSLRAGLAALPaDADAVLVLLGDQPLVTAETLRRLLAAFRESPasIVAPTYDGRRGHPVLFSRRLFPEL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515496824 153 CQLRGDNGARELLQ--GAAVHLLPLEHPGVVRDIDLPSQLPA 192
Cdd:COG2068  150 LALTGDQGARALLRrhPDRVRLVPVDDPGVLLDIDTPEDLAR 191
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-192 2.33e-47

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 153.39  E-value: 2.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   1 MTTGIVITAAGRGERFiqaggQGNKLnagFADAAGeqRSLFEHTLRRALASGL-PVHVVARPDNLPVLAACAanQVPVTL 79
Cdd:COG2068    2 SKVAAIILAAGASSRM-----GRPKL---LLPLGG--KPLLERAVEAALAAGLdPVVVVLGADAEEVAAALA--GLGVRV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  80 L----ASAGLGDSIAAGVAATP-HWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPL 152
Cdd:COG2068   70 VvnpdWEEGMSSSLRAGLAALPaDADAVLVLLGDQPLVTAETLRRLLAAFRESPasIVAPTYDGRRGHPVLFSRRLFPEL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515496824 153 CQLRGDNGARELLQ--GAAVHLLPLEHPGVVRDIDLPSQLPA 192
Cdd:COG2068  150 LALTGDQGARALLRrhPDRVRLVPVDDPGVLLDIDTPEDLAR 191
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-190 1.04e-37

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 128.45  E-value: 1.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   3 TGIVITAAGRGERFiqaggQGNKLNAGFADaageqRSLFEHTLRRALASGL-PVHVVARPDNLPVLAACAANQVPVTLL- 80
Cdd:cd04182    1 IAAIILAAGRSSRM-----GGNKLLLPLDG-----KPLLRHALDAALAAGLsRVIVVLGAEADAVRAALAGLPVVVVINp 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  81 -ASAGLGDSIAAGV-AATPHWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPLCQLR 156
Cdd:cd04182   71 dWEEGMSSSLAAGLeALPADADAVLILLADQPLVTAETLRALIDAFREDGagIVAPVYQGRRGHPVLFPRSLFPELLALS 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515496824 157 GDNGARELLQGAAVHLL-PLEHPGVVRDIDLPSQL 190
Cdd:cd04182  151 GDKGARSLLRAHPDRVVvEVDDPGVLIDIDTPEDL 185
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
4-187 5.21e-32

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 113.97  E-value: 5.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824    4 GIVITAAGRGERFiqagGQgNKLNAGFAdaageQRSLFEHTLRRALAS-GLPVHVVARPDNLPVLAACAaNQVPVTL--- 79
Cdd:TIGR03310   1 DAIILAAGLSSRM----GQ-NKLLLPYK-----GKTILEHVVDNALRLfFDEVILVLGHEADELVALLA-NHSNITLvhn 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   80 -LASAGLGDSIAAGVAATPHWQGWLIHLADMPFVGADVFRQVADA--LRQHPIVRPSYAQQPGHPVGFSARLRKPLCQLR 156
Cdd:TIGR03310  70 pQYAEGQSSSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEAfaLKNDEIVVPLYKGKRGHPVLFPRKLFPELLALT 149
                         170       180       190
                  ....*....|....*....|....*....|...
gi 515496824  157 GDNGARELLQGAAVHLLPLE--HPGVVRDIDLP 187
Cdd:TIGR03310 150 GDTGGRQILRELPHEVKYVEvkDPGILFDIDTP 182
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
6-166 6.41e-23

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 89.56  E-value: 6.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824    6 VITAAGRGERFiqaggQGNKLNAGFADaageqRSLFEHTLRRALASGLPVHVVARPDnlPVLAACAANQVPVTLLASAGL 85
Cdd:pfam12804   2 VILAGGRSSRM-----GGDKALLPLGG-----KPLLERVLERLRPAGDEVVVVANDE--EVLAALAGLGVPVVPDPDPGQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   86 G--DSIAAGVAATPHWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPLCQLRGDNGA 161
Cdd:pfam12804  70 GplAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGadIVVPVYDGGRGHPLLYRRRLLPALEALLGDRGL 149

                  ....*
gi 515496824  162 RELLQ 166
Cdd:pfam12804 150 RRLLR 154
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-127 3.31e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.12  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   6 VITAAGRGERFiqaGGQGNKLnagFADAAGeqRSLFEHTLRRALASGL--PVHVVARPDNLPVLAACAANQVPVTLLASA 83
Cdd:PRK00155   7 IIPAAGKGSRM---GADRPKQ---YLPLGG--KPILEHTLEAFLAHPRidEIIVVVPPDDRPDFAELLLAKDPKVTVVAG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515496824  84 GL--GDSIAAGVAATPHwQGW-LIHLADMPFVGADVFRQVADALRQH 127
Cdd:PRK00155  79 GAerQDSVLNGLQALPD-DDWvLVHDAARPFLTPDDIDRLIEAAEET 124
 
Name Accession Description Interval E-value
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-192 2.33e-47

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 153.39  E-value: 2.33e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   1 MTTGIVITAAGRGERFiqaggQGNKLnagFADAAGeqRSLFEHTLRRALASGL-PVHVVARPDNLPVLAACAanQVPVTL 79
Cdd:COG2068    2 SKVAAIILAAGASSRM-----GRPKL---LLPLGG--KPLLERAVEAALAAGLdPVVVVLGADAEEVAAALA--GLGVRV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  80 L----ASAGLGDSIAAGVAATP-HWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPL 152
Cdd:COG2068   70 VvnpdWEEGMSSSLRAGLAALPaDADAVLVLLGDQPLVTAETLRRLLAAFRESPasIVAPTYDGRRGHPVLFSRRLFPEL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515496824 153 CQLRGDNGARELLQ--GAAVHLLPLEHPGVVRDIDLPSQLPA 192
Cdd:COG2068  150 LALTGDQGARALLRrhPDRVRLVPVDDPGVLLDIDTPEDLAR 191
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-190 1.04e-37

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 128.45  E-value: 1.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   3 TGIVITAAGRGERFiqaggQGNKLNAGFADaageqRSLFEHTLRRALASGL-PVHVVARPDNLPVLAACAANQVPVTLL- 80
Cdd:cd04182    1 IAAIILAAGRSSRM-----GGNKLLLPLDG-----KPLLRHALDAALAAGLsRVIVVLGAEADAVRAALAGLPVVVVINp 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  81 -ASAGLGDSIAAGV-AATPHWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPLCQLR 156
Cdd:cd04182   71 dWEEGMSSSLAAGLeALPADADAVLILLADQPLVTAETLRALIDAFREDGagIVAPVYQGRRGHPVLFPRSLFPELLALS 150
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515496824 157 GDNGARELLQGAAVHLL-PLEHPGVVRDIDLPSQL 190
Cdd:cd04182  151 GDKGARSLLRAHPDRVVvEVDDPGVLIDIDTPEDL 185
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
4-187 5.21e-32

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 113.97  E-value: 5.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824    4 GIVITAAGRGERFiqagGQgNKLNAGFAdaageQRSLFEHTLRRALAS-GLPVHVVARPDNLPVLAACAaNQVPVTL--- 79
Cdd:TIGR03310   1 DAIILAAGLSSRM----GQ-NKLLLPYK-----GKTILEHVVDNALRLfFDEVILVLGHEADELVALLA-NHSNITLvhn 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   80 -LASAGLGDSIAAGVAATPHWQGWLIHLADMPFVGADVFRQVADA--LRQHPIVRPSYAQQPGHPVGFSARLRKPLCQLR 156
Cdd:TIGR03310  70 pQYAEGQSSSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEAfaLKNDEIVVPLYKGKRGHPVLFPRKLFPELLALT 149
                         170       180       190
                  ....*....|....*....|....*....|...
gi 515496824  157 GDNGARELLQGAAVHLLPLE--HPGVVRDIDLP 187
Cdd:TIGR03310 150 GDTGGRQILRELPHEVKYVEvkDPGILFDIDTP 182
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
6-166 6.41e-23

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 89.56  E-value: 6.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824    6 VITAAGRGERFiqaggQGNKLNAGFADaageqRSLFEHTLRRALASGLPVHVVARPDnlPVLAACAANQVPVTLLASAGL 85
Cdd:pfam12804   2 VILAGGRSSRM-----GGDKALLPLGG-----KPLLERVLERLRPAGDEVVVVANDE--EVLAALAGLGVPVVPDPDPGQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   86 G--DSIAAGVAATPHWQGWLIHLADMPFVGADVFRQVADALRQHP--IVRPSYAQQPGHPVGFSARLRKPLCQLRGDNGA 161
Cdd:pfam12804  70 GplAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGadIVVPVYDGGRGHPLLYRRRLLPALEALLGDRGL 149

                  ....*
gi 515496824  162 RELLQ 166
Cdd:pfam12804 150 RRLLR 154
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
6-128 2.70e-10

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 57.45  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   6 VITAAGRGERFiqaGGQGNKLnagFADAAGeqRSLFEHTLRRALASGL--PVHVVARPDNLPVL-AACAANQVPVTLLAS 82
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQ---FLPLGG--KPVLEHTLEAFLAHPRidEIVVVVPPDDIEYFeELLAKYGIDKPVRVV 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515496824  83 AGlG----DSIAAGVAATPHWQGW-LIHLADMPFVGADVFRQVADALRQHP 128
Cdd:COG1211   73 AG-GatrqDSVRNGLEALPDDDDWvLVHDAARPLVSPELIDRVIEAAREYG 122
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
6-127 5.00e-08

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 50.99  E-value: 5.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   6 VITAAGRGERFiqaGGQGNKLnagFADAAGeqRSLFEHTLRRALASGL--PVHVVARPDNLPVLAACAANQVPVTLLASA 83
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQ---FLELGG--KPVLEHTLEAFLAHPAidEIVVVVPPDDIDLAKELAKYGLSKVVKIVE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515496824  84 GlG----DSIAAGVAATPHW-QGW-LIHLADMPFVGADVFRQVADALRQH 127
Cdd:cd02516   76 G-GatrqDSVLNGLKALPDAdPDIvLIHDAARPFVSPELIDRLIDALKEY 124
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
6-127 1.65e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 46.51  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824    6 VITAAGRGERFiqaggqGNKLNAGFADAAGeqRSLFEHTLRRALASGL--PVHVVARPDNLPVL-AACAANQVPVTLLAS 82
Cdd:TIGR00453   3 VIPAAGRGTRF------GSGVPKQYLELGG--RPLLEHALDAFLAHPAidEVVVVVSPDDTEFFqKYLVARAVPKIVAGG 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 515496824   83 AGLGDSIAAGVAATPHWQGWLIHLADMPFVGADVFRQVADALRQH 127
Cdd:TIGR00453  75 DTRQDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA 119
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-190 5.62e-06

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 44.80  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   1 MTTGI--VITAAGRGERFiqagGQgNKlnaGFADAAGeqRSLFEHTLRRALASGLPVHVVARPDnlpvlAACAANQVPVT 78
Cdd:COG0746    1 MTMPItgVILAGGRSRRM----GQ-DK---ALLPLGG--RPLLERVLERLRPQVDEVVIVANRP-----ERYAALGVPVV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  79 LLASAGLG--DSIAAGVAATPHwqGWLIHLA-DMPFVGADVFRQVADALRQ-HPIVRPSYAQQPgHPV-GF-SARLRKPL 152
Cdd:COG0746   66 PDDPPGAGplAGILAALEAAPA--EWVLVLAcDMPFLPPDLVRRLLEALEEgADAVVPRSGGRL-EPLfALyRRSLLPAL 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 515496824 153 CQL--RGDNGARELLQGAAVHLLPLE-HPGVVRDIDLPSQL 190
Cdd:COG0746  143 EAAlaEGERSLRALLERLDVVYVPFEdLDDAFFNVNTPEDL 183
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
2-190 2.52e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.87  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   2 TTGIVItAAGRGERFiqaggQGNKlnaGFADAAGeqRSLFEHTLRRALASGLPVHVVARPDnlpvLAACAANQVPVTLLA 81
Cdd:cd02503    1 ITGVIL-AGGKSRRM-----GGDK---ALLELGG--KPLLEHVLERLKPLVDEVVISANRD----QERYALLGVPVIPDE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824  82 SAGLGD--SIAAGVAATPHwQGWLIHLADMPFVGADVFRQVADALRQHP-IVRPSYAQQPgHP-VGF-SARLRKPLCQL- 155
Cdd:cd02503   66 PPGKGPlaGILAALRAAPA-DWVLVLACDMPFLPPELLERLLAAAEEGAdAVVPKSGGRL-QPlHALyHKSLLPALEELl 143
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515496824 156 -RGDNGARELLQGAAVHLLPLE--HPGVVRDIDLPSQL 190
Cdd:cd02503  144 eAGERRLRRLLEKLGVQYVEFEdeRLDAFFNINTPEDL 181
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-127 3.31e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.12  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   6 VITAAGRGERFiqaGGQGNKLnagFADAAGeqRSLFEHTLRRALASGL--PVHVVARPDNLPVLAACAANQVPVTLLASA 83
Cdd:PRK00155   7 IIPAAGKGSRM---GADRPKQ---YLPLGG--KPILEHTLEAFLAHPRidEIIVVVPPDDRPDFAELLLAKDPKVTVVAG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515496824  84 GL--GDSIAAGVAATPHwQGW-LIHLADMPFVGADVFRQVADALRQH 127
Cdd:PRK00155  79 GAerQDSVLNGLQALPD-DDWvLVHDAARPFLTPDDIDRLIEAAEET 124
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
102-187 3.27e-03

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 37.34  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824 102 WLIHLADMPFVGADVFRQVADalRQHPIvrpSYA-----QQPGHPVGFSA------RLRKPLCQLRGDNGARELLQGAAV 170
Cdd:PRK14490 262 WLVVACDLPFLDEATLQQLVE--GRNPF---RFAtafrhPDSGRPEPLCAiyepksRLRLLLRHAAGNNSLRSFLATSRI 336
                         90
                 ....*....|....*..
gi 515496824 171 HLLPLEHPGVVRDIDLP 187
Cdd:PRK14490 337 EELEPTDPEALQNINDP 353
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
1-132 6.47e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 36.36  E-value: 6.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515496824   1 MTTGIVITAAGRGERFiqaGGQGNK--LNAGfadaageQRSLFEHTLRRALASGL--PVHVVARPDNLPVLA-ACAANQV 75
Cdd:PRK09382   4 SDISLVIVAAGRSTRF---SAEVKKqwLRIG-------GKPLWLHVLENLSSAPAfkEIVVVIHPDDIAYMKkALPEIKF 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515496824  76 PVTLLASAGLGDSIAAGVAA--TPHwqgWLIHLADMPFVGADVFRQVADALRQHPIVRP 132
Cdd:PRK09382  74 VTLVTGGATRQESVRNALEAldSEY---VLIHDAARPFVPKELIDRLIEALDKADCVLP 129
 
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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