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Conserved domains on  [gi|1016713789|ref|XP_016076828|]
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PREDICTED: FAD synthase [Miniopterus natalensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 282-460 6.52e-108

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


:

Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 317.93  E-value: 6.52e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 282 KVANALQTIETALARYSLAQLCVGFNGGKDCTALLHLFHAAVQRKCPDTQEPLQILYIHSISPFPELEKFLQDTIKRYNL 361
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 362 RVLEAEGDMKQALSQLQARHPQLEAALMGTRRTDPYSRSLCPFSPTDPGWPSFMRINPLLDWTYRDIWDFLRQLFVPYCI 441
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 1016713789 442 LYDRGYTSLGSRENTVQNP 460
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 15-169 2.41e-55

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


:

Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 182.30  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  15 TAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKALGKEGW-------EKLSLVPSSARL---HYGTdphtgrpfrFPLVSVR----NVYLFPGI 160
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                  ....*....
gi 1016713789 161 PELLQRVLE 169
Cdd:cd00885   152 PSEMKPMLE 160
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 282-460 6.52e-108

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 317.93  E-value: 6.52e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 282 KVANALQTIETALARYSLAQLCVGFNGGKDCTALLHLFHAAVQRKCPDTQEPLQILYIHSISPFPELEKFLQDTIKRYNL 361
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 362 RVLEAEGDMKQALSQLQARHPQLEAALMGTRRTDPYSRSLCPFSPTDPGWPSFMRINPLLDWTYRDIWDFLRQLFVPYCI 441
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 1016713789 442 LYDRGYTSLGSRENTVQNP 460
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 15-169 2.41e-55

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 182.30  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  15 TAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKALGKEGW-------EKLSLVPSSARL---HYGTdphtgrpfrFPLVSVR----NVYLFPGI 160
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                  ....*....
gi 1016713789 161 PELLQRVLE 169
Cdd:cd00885   152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 15-251 3.64e-53

ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];


Pssm-ID: 440678  Cd Length: 249  Bit Score: 179.54  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  15 TAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:COG1058     1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKA-LGKEGWE------KLSLVPSSARL---HYGTDPhtGrpFRFPLVSVRnVYLFPGIPELL 164
Cdd:COG1058    81 AEALGVPLVLDPEALALIEErFAKRGREmtennlKQALLPEGAELlpnPVGTAP--G--FSIENNGKV-VIFLPGVPSEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 165 QRVLEG-----LKGLFQNTAVqfHLRELYVA-ADEASIAPILAEAQAHFgRRLGLGSYPDWGsnYYQVKLTLDSEEEGPL 238
Cdd:COG1058   156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYPSDG--EVRLRLTARGTDEEEA 230

                         250
                  ....*....|...
gi 1016713789 239 EECLAYLTARLPQ 251
Cdd:COG1058   231 EAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 301-458 1.27e-29

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 113.93  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 301 QLCVGFNGGKDCTALLHLFhaavqRKCpdtQEPLQILYIHSISPFPELEKFLQDTIKRYNLRVL-------EAEGD---- 369
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLA-----SKA---FPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKvylpedsFAEGInpeg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 370 -----------------MKQALSQLQARhpqleAALMGTRRTDPYSRSLCPFSPTDPGWPSFMRINPLLDWTYRDIWDFL 432
Cdd:pfam01507  73 ipsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170       180
                  ....*....|....*....|....*.
gi 1016713789 433 RQLFVPYCILYDRGYTSLGSRENTVQ 458
Cdd:pfam01507 148 LANNVPYNPLYDQGYRSIGCYPCTGP 173
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-108 6.38e-27

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 105.41  E-value: 6.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  17 GIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAVAQ 96
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 1016713789  97 AFGDELKPHPEL 108
Cdd:pfam00994  81 LGGRELPGFEEL 92
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 16-248 9.89e-25

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 102.95  E-value: 9.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  16 AGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLT-AGGIGPTHDDVTFEAV 94
Cdd:PRK03670    3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLViSGGLGPTHDDVTMLAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKA----LGKEGW----------EKLSLVPSSARLHYGTDphTGRPFRFPLVSVRNVYLFPGI 160
Cdd:PRK03670   83 AEALGRELVLCEDCLERIKEfyeeLYKKGLiddptlnearKKMAYLPEGAEPLENTE--GAAPGAYIEHKGTKIFVLPGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 161 PELLQRVLEG--LKGLFQNTAVQfhLRELYVAADEASIAPILAEAQAHFGRRL-----GLGSYpdwgsnyyqVKLTLDSE 233
Cdd:PRK03670  161 PREMKAMLEKevLPRLGERKFVQ--KKFLAEITDESKLAPILEEALERFNVKIhsspkGFGKY---------IGIIIFAE 229

                         250
                  ....*....|....*
gi 1016713789 234 EEGPLEECLAYLTAR 248
Cdd:PRK03670  230 DEEEIEKAVEFMEER 244
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-119 3.97e-24

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 97.66  E-value: 3.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789   17 GIIIVGDEVLKGHTQ-DTNTYFLCRTLRSLGVQVCRVSVV--PDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEA 93
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80

                           90       100
                   ....*....|....*....|....*.
gi 1016713789   94 VAQAFGDELKPHPEleaAIKALGKEG 119
Cdd:smart00852  81 LAELGGRELLGHGV---AMRPGGPPG 103
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 284-451 1.38e-17

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 81.82  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 284 ANALQTIETALARYSlAQLCVGFNGGKDCTALLHLfhAAVQRKcpdtqePLQILYI----HsispFPELEKFLQDTIKRY 359
Cdd:COG0175    19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHL--AAKFKP------PIPVLFLdtgyE----FPETYEFRDRLAERL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 360 NLRVLEAEGD------------------------------MKQALSQLQArhpqlEAALMGTRRTDPYSRSLCPFSPTDP 409
Cdd:COG0175    86 GLDLIVVRPEdafaeqlaefgpplfyrdprwcckirkvepLKRALAGYDF-----DAWITGLRRDESPTRAKEPVVEWDP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016713789 410 GwPSFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 451
Cdd:COG0175   161 V-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 14-118 1.45e-15

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 73.89  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  14 VTAGIIIVGDEVLKGHTQ-------DTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTH 86
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1016713789  87 DDVTFEAVAQAFGDELkphPELEAAIKALGKE 118
Cdd:TIGR00177  81 RDVTPEALEELGEKEI---PGFGEFRMLSSLP 109
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 253-451 6.70e-11

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 64.27  E-value: 6.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 253 SLVPYIPNAVEQASEAVYKLAKSGSSLGKKVANA--LQTIETALARYSlAQLCVGFNGGKDcTALLHLFHAavqrkcpdT 330
Cdd:TIGR00424  68 SIVPSAATTVAPEVEEKVVEVEDFEKLAKKLENAspLEIMDKALEKFG-NDIAIAFSGAED-VALIEYAHL--------T 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 331 QEPLQILYIHSISPFPELEKFLQDTIKRYNLRV-------LEAEG------------DMKQALSQLQARHPqLEAALMGT 391
Cdd:TIGR00424 138 GRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIeymfpdaVEVQAlvrskglfsfyeDGHQECCRVRKVRP-LRRALKGL 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016713789 392 R------RTD--PYSRSLCPFSPTDP-------GWPSFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 451
Cdd:TIGR00424 217 KawitgqRKDqsPGTRSEIPVVQVDPvfegldgGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIG 291
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
370-451 7.57e-09

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 56.38  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 370 MKQALSQLqarhpqlEAALMGTRRTDPYSRSLCPFSPTDPGwpsFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTS 449
Cdd:PRK02090  135 LNRALAGL-------DAWITGLRREQSGTRANLPVLEIDGG---RFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPS 204


                  ..
gi 1016713789 450 LG 451
Cdd:PRK02090  205 IG 206
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 282-460 6.52e-108

FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; Flavin adenine dinucleotide synthase (FADS); EC 2.7.7.2) is involved in the biochemical pathway for converting riboflavin into FAD. By sequence comparison, bacterial and eukaryotic FMNAT enzymes belong to two different protein superfamilies and apparently utilize different sets of active-site residues to accomplish the same chemistry. This subfamily includes eukaryotic FMNATs, which are members of the 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase-like family belonging to the adenine nucleotide alpha hydrolase superfamily, which has conserved motifs different from those of nucleotidylyl transferases.


Pssm-ID: 467513 [Multi-domain]  Cd Length: 179  Bit Score: 317.93  E-value: 6.52e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 282 KVANALQTIETALARYSLAQLCVGFNGGKDCTALLHLFHAAVQRKCPDTQEPLQILYIHSISPFPELEKFLQDTIKRYNL 361
Cdd:cd23948     1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRYNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 362 RVLEAEGDMKQALSQLQARHPQLEAALMGTRRTDPYSRSLCPFSPTDPGWPSFMRINPLLDWTYRDIWDFLRQLFVPYCI 441
Cdd:cd23948    81 DLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPYCS 160

                         170
                  ....*....|....*....
gi 1016713789 442 LYDRGYTSLGSRENTVQNP 460
Cdd:cd23948   161 LYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 15-169 2.41e-55

Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, where the domain is presumed to bind molybdopterin.


Pssm-ID: 238450 [Multi-domain]  Cd Length: 170  Bit Score: 182.30  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  15 TAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:cd00885     1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKALGKEGW-------EKLSLVPSSARL---HYGTdphtgrpfrFPLVSVR----NVYLFPGI 160
Cdd:cd00885    81 AKAFGRPLVLDEEALERIEARFARRGremteanLKQAMLPEGATLlpnPVGT---------APGFSVEhngkNVFLLPGV 151


                  ....*....
gi 1016713789 161 PELLQRVLE 169
Cdd:cd00885   152 PSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 15-251 3.64e-53

ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];


Pssm-ID: 440678  Cd Length: 249  Bit Score: 179.54  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  15 TAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:COG1058     1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKA-LGKEGWE------KLSLVPSSARL---HYGTDPhtGrpFRFPLVSVRnVYLFPGIPELL 164
Cdd:COG1058    81 AEALGVPLVLDPEALALIEErFAKRGREmtennlKQALLPEGAELlpnPVGTAP--G--FSIENNGKV-VIFLPGVPSEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 165 QRVLEG-----LKGLFQNTAVqfHLRELYVA-ADEASIAPILAEAQAHFgRRLGLGSYPDWGsnYYQVKLTLDSEEEGPL 238
Cdd:COG1058   156 KPMFEEevlprLKKLFSGEPI--VSRTLRTFgIGESDLAELLEDLEARF-PNVTIGSYPSDG--EVRLRLTARGTDEEEA 230

                         250
                  ....*....|...
gi 1016713789 239 EECLAYLTARLPQ 251
Cdd:COG1058   231 EAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 301-458 1.27e-29

Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).


Pssm-ID: 396201 [Multi-domain]  Cd Length: 173  Bit Score: 113.93  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 301 QLCVGFNGGKDCTALLHLFhaavqRKCpdtQEPLQILYIHSISPFPELEKFLQDTIKRYNLRVL-------EAEGD---- 369
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLA-----SKA---FPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKvylpedsFAEGInpeg 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 370 -----------------MKQALSQLQARhpqleAALMGTRRTDPYSRSLCPFSPTDPGWPSFMRINPLLDWTYRDIWDFL 432
Cdd:pfam01507  73 ipsslyrrccrlrkvepLKRALKELGFD-----AWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYI 147

                         170       180
                  ....*....|....*....|....*.
gi 1016713789 433 RQLFVPYCILYDRGYTSLGSRENTVQ 458
Cdd:pfam01507 148 LANNVPYNPLYDQGYRSIGCYPCTGP 173
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-108 6.38e-27

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerization.


Pssm-ID: 425979 [Multi-domain]  Cd Length: 143  Bit Score: 105.41  E-value: 6.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  17 GIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAVAQ 96
Cdd:pfam00994   1 AIITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAE 80

                          90
                  ....*....|..
gi 1016713789  97 AFGDELKPHPEL 108
Cdd:pfam00994  81 LGGRELPGFEEL 92
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 16-248 9.89e-25

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 102.95  E-value: 9.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  16 AGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLT-AGGIGPTHDDVTFEAV 94
Cdd:PRK03670    3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLViSGGLGPTHDDVTMLAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPELEAAIKA----LGKEGW----------EKLSLVPSSARLHYGTDphTGRPFRFPLVSVRNVYLFPGI 160
Cdd:PRK03670   83 AEALGRELVLCEDCLERIKEfyeeLYKKGLiddptlnearKKMAYLPEGAEPLENTE--GAAPGAYIEHKGTKIFVLPGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 161 PELLQRVLEG--LKGLFQNTAVQfhLRELYVAADEASIAPILAEAQAHFGRRL-----GLGSYpdwgsnyyqVKLTLDSE 233
Cdd:PRK03670  161 PREMKAMLEKevLPRLGERKFVQ--KKFLAEITDESKLAPILEEALERFNVKIhsspkGFGKY---------IGIIIFAE 229

                         250
                  ....*....|....*
gi 1016713789 234 EEGPLEECLAYLTAR 248
Cdd:PRK03670  230 DEEEIEKAVEFMEER 244
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
15-203 1.43e-24

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 102.78  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  15 TAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAV 94
Cdd:PRK01215    5 FAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  95 AQAFGDELKPHPEleaAIKALgKEGWEKLSLVPSSARLHYGTDPHTGRPFRFP-------LVSVRN--VYLFPGIPELLQ 165
Cdd:PRK01215   85 AKALGVELELNED---ALRMI-LEKYEKRGIPLTPERKKMAMMPPGAVPLENPvgtapgiLIEHGGkdIVALPGVPREME 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1016713789 166 RVLEG-LKGLFQNTA-VQFHLRELYVA-ADEASIAPILAEA 203
Cdd:PRK01215  161 AIFENfVEPLLKNRPpLKYYEDSILVEgVMESDLAPYVKEL 201
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 17-119 3.97e-24

Probable molybdopterin binding domain; This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor. The domain is presumed to bind molybdopterin. The structure of this domain is known, and it forms an alpha/beta structure. In the known structure of Gephyrin this domain mediates trimerisation.


Pssm-ID: 214856 [Multi-domain]  Cd Length: 138  Bit Score: 97.66  E-value: 3.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789   17 GIIIVGDEVLKGHTQ-DTNTYFLCRTLRSLGVQVCRVSVV--PDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEA 93
Cdd:smart00852   1 AIISTGDELLSGGQIrDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEA 80

                           90       100
                   ....*....|....*....|....*.
gi 1016713789   94 VAQAFGDELKPHPEleaAIKALGKEG 119
Cdd:smart00852  81 LAELGGRELLGHGV---AMRPGGPPG 103
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 284-451 1.38e-17

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 81.82  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 284 ANALQTIETALARYSlAQLCVGFNGGKDCTALLHLfhAAVQRKcpdtqePLQILYI----HsispFPELEKFLQDTIKRY 359
Cdd:COG0175    19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHL--AAKFKP------PIPVLFLdtgyE----FPETYEFRDRLAERL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 360 NLRVLEAEGD------------------------------MKQALSQLQArhpqlEAALMGTRRTDPYSRSLCPFSPTDP 409
Cdd:COG0175    86 GLDLIVVRPEdafaeqlaefgpplfyrdprwcckirkvepLKRALAGYDF-----DAWITGLRRDESPTRAKEPVVEWDP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016713789 410 GwPSFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 451
Cdd:COG0175   161 V-GGLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIG 201
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 16-182 4.33e-17

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 83.30  E-value: 4.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  16 AGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAVA 95
Cdd:PRK00549    3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKETVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  96 QAFGDELKPHPELEAAI----KALGK---EGWEKLSLVPSSARL---HYGTDPhtGRpfrfpLVSVRN--VYLFPGIP-E 162
Cdd:PRK00549   83 KFLGRELVLDEEALAKIedyfAKRGRemtENNRKQALIPEGATVlpnPVGTAP--GM-----IIEVDGktYIVLPGPPsE 155

                         170       180
                  ....*....|....*....|
gi 1016713789 163 llqrvlegLKGLFQNTAVQF 182
Cdd:PRK00549  156 --------LKPMFEEYVVPY 167
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 14-118 1.45e-15

molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein cnx1, and rat protein gephyrin each have one domain like MoeA and one like MoaB and Mog. These domains are, however, distantly related to each other, as captured by this model. Gephyrin is unusual in that it seems to be a tubulin-binding neuroprotein involved in the clustering of both blycine receptors and GABA receptors, rather than a protein of molybdenum cofactor biosynthesis.


Pssm-ID: 272944 [Multi-domain]  Cd Length: 148  Bit Score: 73.89  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  14 VTAGIIIVGDEVLKGHTQ-------DTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTH 86
Cdd:TIGR00177   1 PRVAVISVGDELVEGGQPlepgqiyDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGP 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1016713789  87 DDVTFEAVAQAFGDELkphPELEAAIKALGKE 118
Cdd:TIGR00177  81 RDVTPEALEELGEKEI---PGFGEFRMLSSLP 109
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 16-100 1.81e-13

MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.


Pssm-ID: 238387 [Multi-domain]  Cd Length: 133  Bit Score: 67.37  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  16 AGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAVA 95
Cdd:cd00758     2 VAIVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALA 81


                  ....*
gi 1016713789  96 qAFGD 100
Cdd:cd00758    82 -ELGE 85
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 303-452 5.09e-13

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 67.80  E-value: 5.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 303 CVGFNGGKDCTALLHLFHAAVQRKCPDtqepLQILYIHSISPFPELEKFLQDTIKRYNLRVLEAEGDMKQALSQLQA--- 379
Cdd:cd23947    16 IVSFSGGKDSLVLLHLALEALRRLRKD----VYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPLFLEWLTSNFqpq 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 380 ------------------------------RHPQLEAALM--GTRRTDPYSRSLCPFSPTDPGWPS-----FMRINPLLD 422
Cdd:cd23947    92 wdpiwdnpppprdyrwccdelklepftkwlKEKKPEGVLLlvGIRADESLNRAKRPRVYRKYGWRNstlpgQIVAYPIKD 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 1016713789 423 WTYRDIWDFLRQLFVPYCILYDRGYTSLGS 452
Cdd:cd23947   172 WSVEDVWLYILRHGLPYNPLYDLGFDRGGC 201
cinA_nterm TIGR00200
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ...
 16-170 6.48e-13

competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or competence-inducible protein that is polycistronic with recA in a number of species [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 161761 [Multi-domain]  Cd Length: 413  Bit Score: 70.32  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  16 AGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVV---PDEVATIAAEVtsfSSRFTHVLTAGGIGPTHDDVTFE 92
Cdd:TIGR00200   3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVgdnPERLKTIIRIA---SERADVLIFNGGLGPTSDDLTAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  93 AVAQAFGDELKPHPELEAAIKALGKE-------GWEKLSLVPSSARL---HYGTDP-----HTGRPFRFplvsvrnvyLF 157
Cdd:TIGR00200  80 TIATAKGEPLVLNEAWLKEIERYFHEtgrvmapNNRKQALLPAGAEFlanPVGTAPgmfavQLNRCLML---------FT 150

                         170
                  ....*....|...
gi 1016713789 158 PGIPELLQRVLEG 170
Cdd:TIGR00200 151 PGVPSEFRVMVEH 163
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 14-95 3.72e-11

MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF) an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MogA, together with MoeA, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes. In contrast, MoaB shows high similarity to MogA, but little is known about its physiological role. All well studied members of this family form highly stable trimers.


Pssm-ID: 238451 [Multi-domain]  Cd Length: 152  Bit Score: 61.34  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  14 VTAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTH--VLTAGGIGPTHDDVTF 91
Cdd:cd00886     1 LRAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEWADEDGVdlILTTGGTGLAPRDVTP 80


                  ....
gi 1016713789  92 EAVA 95
Cdd:cd00886    81 EATR 84
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 301-451 5.52e-11

Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8) is part of the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467510 [Multi-domain]  Cd Length: 183  Bit Score: 61.46  E-value: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 301 QLCVGFNGGKDCTALLHLFHAaVQRKCP----DTqeplqiLYIhsispFPELEKFLQDTIKRYNLRVLEAEGDMKQALSQ 376
Cdd:cd23945    15 KLVFATSFGAEDAVILDLLSK-VRPDIPvvflDT------GYL-----FPETYDLIDEVEARYGLNIEVYFPEGTEAEEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 377 LQARHPQ---------------------------LEAALMGTRRTDPYSRSLCPFSPTDPGWPSFmRINPLLDWTYRDIW 429
Cdd:cd23945    83 ALEGGLNefyledeerydccrkrkpfplalallgVKAWITGRRRDQSPTRANLPIVEVDEEGGLV-KINPLADWTWEDVW 161

                         170       180
                  ....*....|....*....|..
gi 1016713789 430 DFLRQLFVPYCILYDRGYTSLG 451
Cdd:cd23945   162 AYIREHDLPYNPLHDQGYPSIG 183
APS_reduc TIGR00424
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ...
 253-451 6.70e-11

5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273072 [Multi-domain]  Cd Length: 463  Bit Score: 64.27  E-value: 6.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 253 SLVPYIPNAVEQASEAVYKLAKSGSSLGKKVANA--LQTIETALARYSlAQLCVGFNGGKDcTALLHLFHAavqrkcpdT 330
Cdd:TIGR00424  68 SIVPSAATTVAPEVEEKVVEVEDFEKLAKKLENAspLEIMDKALEKFG-NDIAIAFSGAED-VALIEYAHL--------T 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 331 QEPLQILYIHSISPFPELEKFLQDTIKRYNLRV-------LEAEG------------DMKQALSQLQARHPqLEAALMGT 391
Cdd:TIGR00424 138 GRPFRVFSLDTGRLNPETYRFFDAVEKQYGIRIeymfpdaVEVQAlvrskglfsfyeDGHQECCRVRKVRP-LRRALKGL 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016713789 392 R------RTD--PYSRSLCPFSPTDP-------GWPSFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLG 451
Cdd:TIGR00424 217 KawitgqRKDqsPGTRSEIPVVQVDPvfegldgGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIG 291
MoaB COG0521
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ...
 6-95 1.50e-10

Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin biosynthesis enzyme MoaB/MogA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440287 [Multi-domain]  Cd Length: 169  Bit Score: 59.75  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789   6 SEPPPGRSVTAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTH--VLTAGGIG 83
Cdd:COG0521     2 SSARAFVPLRIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALRELIDDEGVdlVLTTGGTG 81

                          90
                  ....*....|..
gi 1016713789  84 PTHDDVTFEAVA 95
Cdd:COG0521    82 LSPRDVTPEATR 93
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
370-451 7.57e-09

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 56.38  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 370 MKQALSQLqarhpqlEAALMGTRRTDPYSRSLCPFSPTDPGwpsFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTS 449
Cdd:PRK02090  135 LNRALAGL-------DAWITGLRREQSGTRANLPVLEIDGG---RFKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPS 204


                  ..
gi 1016713789 450 LG 451
Cdd:PRK02090  205 IG 206
PRK03673 PRK03673
nicotinamide mononucleotide deamidase-related protein YfaY;
22-107 2.62e-08

nicotinamide mononucleotide deamidase-related protein YfaY;


Pssm-ID: 179629 [Multi-domain]  Cd Length: 396  Bit Score: 55.86  E-value: 2.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  22 GDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGPTHDDVTFEAVAQAFGDE 101
Cdd:PRK03673   10 GDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEG 89


                  ....*.
gi 1016713789 102 LKPHPE 107
Cdd:PRK03673   90 LVLHEE 95
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 350-456 3.26e-08

phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131112  Cd Length: 226  Bit Score: 54.07  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 350 KFLQD-TIKRYN-LRVLEAegdMKQALSQLQArhpqlEAALMGTRRTDPYSRSLCPFSPTDpGWPSFMRINPLLDWTYRD 427
Cdd:TIGR02057 102 KLLWQkDIEKYDyIAKVEP---MQRALKELNA-----SAWFTGRRRDQGSARANLPVIEID-EQNGILKVNPLIDWTFEQ 172

                          90       100
                  ....*....|....*....|....*....
gi 1016713789 428 IWDFLRQLFVPYCILYDRGYTSLGSRENT 456
Cdd:TIGR02057 173 VYQYLDAHNVPYNPLLDQGYRSIGDYHST 201
PLN02309 PLN02309
5'-adenylylsulfate reductase
 237-451 2.47e-07

5'-adenylylsulfate reductase


Pssm-ID: 215175 [Multi-domain]  Cd Length: 457  Bit Score: 52.87  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 237 PLEECLAYLTARLPQGSLVPYIPNAVEQASEAVYKLAKSGSSlgkkvANALQTIETALARYSlAQLCVGFNGGKDcTALL 316
Cdd:PLN02309   54 PLNAQPAARQAMIPSAATAVAEVPEEEGEVEDFEKLAKELEN-----ASPLEIMDKALEKFG-NDIAIAFSGAED-VALI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 317 HLFHAavqrkcpdTQEPLQILYIHSISPFPELEKFLQDTIKRYNLRV---------LEAEGDMKQALSQLQARHPQ---- 383
Cdd:PLN02309  127 EYAHL--------TGRPFRVFSLDTGRLNPETYRLFDAVEKHYGIRIeymfpdaveVQALVRNKGLFSFYEDGHQEccrv 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 384 -----LEAALMGTR------RTD--PYSRSLCPFSPTDP-------GWPSFMRINPLLDWTYRDIWDFLRQLFVPYCILY 443
Cdd:PLN02309  199 rkvrpLRRALKGLRawitgqRKDqsPGTRAEVPVVQVDPvfegldgGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLH 278


                  ....*...
gi 1016713789 444 DRGYTSLG 451
Cdd:PLN02309  279 AQGYVSIG 286
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 309-443 7.44e-07

Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in the sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN, coupled to ATP hydrolysis by CysD. CysD belongs to the ATP pyrophosphatase (ATP PPase) family of proteins, members of which include PAPS reductase, GMP synthetase, asparagine synthetase, and NAD(+) synthetase. This subunit is responsible for directly forming APS under control of the G protein. A modified version of the P loop (PP-loop), the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues.


Pssm-ID: 467511  Cd Length: 214  Bit Score: 49.80  E-value: 7.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 309 GKDCTALLHLFHAAVQRKCPdtqePLQILYIHSISPFPELEKFLQDTIKRYNL--------------------------R 362
Cdd:cd23946    30 GKDSSVMLHLARKAFYPGKP----PFPLLHVDTTWKFREMIEFRDRVAKEYGLdlivhvnpdgveaginpfthgsakhtD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789 363 VLEAEGdMKQALSQLQarhpqLEAALMGTRRTDPYSRS---LCPFSPTDPGW------PSF-------------MRINPL 420
Cdd:cd23946   106 IMKTEG-LKQALDKYG-----FDAAFGGARRDEEKSRAkerVYSFRDSNHRWdpknqrPELwnqyngrvkkgesIRVFPL 179

                         170       180
                  ....*....|....*....|...
gi 1016713789 421 LDWTYRDIWDFLRQLFVPYCILY 443
Cdd:cd23946   180 SNWTELDIWQYIYLENIPIVPLY 202
MoeA cd00887
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ...
 12-102 2.13e-05

MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor (MoCF), an essential cofactor of a diverse group of redox enzymes. MoCF biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes. MoCF contains a tricyclic pyranopterin, termed molybdopterin (MPT). MoeA, together with MoaB, is responsible for the metal incorporation into MPT, the third step in MoCF biosynthesis. The plant homolog Cnx1 is a MoeA-MogA fusion protein. The mammalian homolog gephyrin is a MogA-MoeA fusion protein, that plays a critical role in postsynaptic anchoring of inhibitory glycine receptors and major GABAa receptor subtypes.


Pssm-ID: 238452 [Multi-domain]  Cd Length: 394  Bit Score: 46.72  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  12 RSVTAGIIIVGDEVL-------KGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGP 84
Cdd:cd00887   167 RRPRVAIISTGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGVSV 246

                          90
                  ....*....|....*...
gi 1016713789  85 THDDVTFEAVAQAFGDEL 102
Cdd:cd00887   247 GDYDFVKEVLEELGGEVL 264
MoeA COG0303
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ...
 12-102 3.25e-05

Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; Molybdopterin Mo-transferase (molybdopterin biosynthesis) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440072 [Multi-domain]  Cd Length: 401  Bit Score: 46.24  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  12 RSVTAGIIIVGDEVL-------KGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRFTHVLTAGGIGP 84
Cdd:COG0303   171 RRPRVAILSTGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGVSV 250

                          90
                  ....*....|....*...
gi 1016713789  85 THDDVTFEAVAqAFGDEL 102
Cdd:COG0303   251 GDYDLVKEALE-ELGAEV 267
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 303-368 1.86e-04

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 39.74  E-value: 1.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016713789 303 CVGFNGGKDCTALLHLFHAAVQRKcpdtqePLQILYIHSISPFPELEKFLQDTIKRYNLRVLEAEG 368
Cdd:cd01986     2 VVGYSGGKDSSVALHLASRLGRKA------EVAVVHIDHGIGFKEEAESVASIARRSILKKLAEKG 61
MoeA_like cd03522
MoeA_like. This domain is similar to a domain found in a variety of proteins involved in ...
 10-100 4.53e-04

MoeA_like. This domain is similar to a domain found in a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. There this domain is presumed to bind molybdopterin. The exact function of this subgroup is unknown.


Pssm-ID: 239599  Cd Length: 312  Bit Score: 42.15  E-value: 4.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016713789  10 PGRSVTAGIIIVGDEVLKGHTQDTNTYFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSSRF--THVLTAGGI-GPth 86
Cdd:cd03522   156 PFRPLRVGLIVTGSEVYGGRIEDKFGPVLRARLAALGVELVEQVIVPHDEAAIAAAIAEALEAGaeLLILTGGASvDP-- 233

                          90
                  ....*....|....
gi 1016713789  87 DDVTFEAVAQAFGD 100
Cdd:cd03522   234 DDVTPAAIRAAGGE 247
 
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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