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Conserved domains on  [gi|18414227|ref|NP_568117|]
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phosphoadenosine phosphosulfate (PAPS) reductase family protein [Arabidopsis thaliana]

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; ...
 18-203 3.30e-93

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: 280.56  E-value: 3.30e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  18 KYNNAIFVIKRALALYSIEEVAFSFNGGKDSTVLLHLLRAGYFLHKKEQtcsngglsSFPVRTIYFESPSAFTEINAFTY 97
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSP--------LTPLKALYIKSPDPFPEVEEFVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  98 DAAQTYNLQLDIIRQDFKSGLEALLKANP-IRAIFLGVRIGDPTAVGQEQFSPSSPGWPPFMRVNPILDWSYRDVWAFLL 176
Cdd:cd23948  73 DTAKRYNLDLITIDGPMKEGLEELLKEHPiIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLR 152

                       170       180
                ....*....|....*....|....*..
gi 18414227 177 TCKVKYCSLYDQGYTSIGSIHDTVPNS 203
Cdd:cd23948 153 TLNLPYCSLYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 255-408 3.59e-46

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: 158.42  E-value: 3.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVA 334
Cdd:cd00885   2 AEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 335 KAFGVRLAPDEEFEEYLRHLISDQC---TGDRNEMAQLPEGITELLHHEKlSVPLIKCRN---VIVLAATNTEELEKEWE 408
Cdd:cd00885  82 KAFGRPLVLDEEALERIEARFARRGremTEANLKQAMLPEGATLLPNPVG-TAPGFSVEHngkNVFLLPGVPSEMKPMLE 160
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 18-203 3.30e-93

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: 280.56  E-value: 3.30e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  18 KYNNAIFVIKRALALYSIEEVAFSFNGGKDSTVLLHLLRAGYFLHKKEQtcsngglsSFPVRTIYFESPSAFTEINAFTY 97
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSP--------LTPLKALYIKSPDPFPEVEEFVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  98 DAAQTYNLQLDIIRQDFKSGLEALLKANP-IRAIFLGVRIGDPTAVGQEQFSPSSPGWPPFMRVNPILDWSYRDVWAFLL 176
Cdd:cd23948  73 DTAKRYNLDLITIDGPMKEGLEELLKEHPiIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLR 152

                       170       180
                ....*....|....*....|....*..
gi 18414227 177 TCKVKYCSLYDQGYTSIGSIHDTVPNS 203
Cdd:cd23948 153 TLNLPYCSLYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 255-408 3.59e-46

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: 158.42  E-value: 3.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVA 334
Cdd:cd00885   2 AEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 335 KAFGVRLAPDEEFEEYLRHLISDQC---TGDRNEMAQLPEGITELLHHEKlSVPLIKCRN---VIVLAATNTEELEKEWE 408
Cdd:cd00885  82 KAFGRPLVLDEEALERIEARFARRGremTEANLKQAMLPEGATLLPNPVG-TAPGFSVEHngkNVFLLPGVPSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 255-490 5.27e-30

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 117.52  E-value: 5.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVA 334
Cdd:COG1058   2 AEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 335 KAFGVRLAPDEEFEEYLRHLISD---QCTGDRNEMAQLPEGiTELLHHEKLSVPLIKCRN----VIVLA---AtnteELE 404
Cdd:COG1058  82 EALGVPLVLDPEALALIEERFAKrgrEMTENNLKQALLPEG-AELLPNPVGTAPGFSIENngkvVIFLPgvpS----EMK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 405 K--EWECLTELTKLGGGSLIEysSRRLMT-----SltdvEVAEPLSKLGLEFPDIYLGCYrkSRQGPIIICLT--GKDNA 475
Cdd:COG1058 157 PmfEEEVLPRLKKLFSGEPIV--SRTLRTfgigeS----DLAELLEDLEARFPNVTIGSY--PSDGEVRLRLTarGTDEE 228

                       250
                ....*....|....*
gi 18414227 476 RMDSAAQALRKKFKK 490
Cdd:COG1058 229 EAEAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 37-201 5.01e-25

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: 101.22  E-value: 5.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227    37 EVAFSFNGGKDSTVLLHLLRagyflhkkeqtcsnggLSSFPVRTIYFESPSAFTEINAFTYDAAQTYNLQLDII------ 110
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLAS----------------KAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYlpedsf 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   111 -RQDFKSG--------------LEALLKA---NPIRAIFLGVRIGDPTAVGQEQFSPSSPGWPPFMRVNPILDWSYRDVW 172
Cdd:pfam01507  65 aEGINPEGipsslyrrccrlrkVEPLKRAlkeLGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVW 144

                         170       180
                  ....*....|....*....|....*....
gi 18414227   173 AFLLTCKVKYCSLYDQGYTSIGSIHDTVP 201
Cdd:pfam01507 145 QYILANNVPYNPLYDQGYRSIGCYPCTGP 173
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 20-242 1.02e-19

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: 87.98  E-value: 1.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  20 NNAIFVIKRALALYSiEEVAFSFNGGKDSTVLLHLLRAgyflHKKEqtcsngglssFPVRTIY--FEspsaFTEINAFTY 97
Cdd:COG0175  19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHLAAK----FKPP----------IPVLFLDtgYE----FPETYEFRD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  98 DAAQTYNLQLDIIR--QDFKSGLE---------------ALLKANPIR---------AIFLGVRigdptavgQEQfSPS- 150
Cdd:COG0175  80 RLAERLGLDLIVVRpeDAFAEQLAefgpplfyrdprwccKIRKVEPLKralagydfdAWITGLR--------RDE-SPTr 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 151 --SP--GWPPF---MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGSIHDTVPnsllsvndtsskekfkpaylLS 223
Cdd:COG0175 151 akEPvvEWDPVgglIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRA--------------------VE 210

                       250
                ....*....|....*....
gi 18414227 224 DGRLERAGRVKKIASLKKD 242
Cdd:COG0175 211 SGEDERAGRWWDEEKERKE 229
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 253-487 1.67e-17

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 82.15  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  253 LLASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDS----VSEEVDRQrstSDMVFIYGGVGPLHSDV 328
Cdd:PRK03670   1 MFAEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEiksvVLEILSRK---PEVLVISGGLGPTHDDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  329 TLAGVAKAFGVRLAPDEE--------FEE-YLRHLISDQCTGD-RNEMAQLPEGiTELLHHEKLSVP--LIKCRNV--IV 394
Cdd:PRK03670  78 TMLAVAEALGRELVLCEDclerikefYEElYKKGLIDDPTLNEaRKKMAYLPEG-AEPLENTEGAAPgaYIEHKGTkiFV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  395 LAATNTE---ELEKEwecltELTKLGGGSLIEyssRRLMTSLTDVEVAEPLSKLGLEFPDIYLGCYRKSRQGPIIICLTG 471
Cdd:PRK03670 157 LPGMPREmkaMLEKE-----VLPRLGERKFVQ---KKFLAEITDESKLAPILEEALERFNVKIHSSPKGFGKYIGIIIFA 228

                        250
                 ....*....|....*.
gi 18414227  472 KDNARMDSAAQALRKK 487
Cdd:PRK03670 229 EDEEEIEKAVEFMEER 244
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 257-354 2.52e-16

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: 75.75  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   257 VIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVAKA 336
Cdd:pfam00994   2 IITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAEL 81

                          90
                  ....*....|....*...
gi 18414227   337 FGVRLapdEEFEEYLRHL 354
Cdd:pfam00994  82 GGREL---PGFEELFRGV 96
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 257-341 1.87e-14

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: 70.31  E-value: 1.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227    257 VIAVGDEILSG-TVEDQLGLSLCKKLTSVGWSVQQTTVLRN--DIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGV 333
Cdd:smart00852   2 IISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGGpdDPEAIREALREALAEADVVITTGGTGPGPDDLTPEAL 81


                   ....*...
gi 18414227    334 AKAFGVRL 341
Cdd:smart00852  82 AELGGREL 89
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
158-201 2.85e-10

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 60.62  E-value: 2.85e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 18414227  158 MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGSIHDTVP 201
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRP 213
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 255-352 2.52e-09

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: 55.79  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   255 ASVIAVGDEILSGT-------VEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSD 327
Cdd:TIGR00177   3 VAVISVGDELVEGGqplepgqIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRD 82

                          90       100
                  ....*....|....*....|....*
gi 18414227   328 VTLAGVAKAFGVRLapdEEFEEYLR 352
Cdd:TIGR00177  83 VTPEALEELGEKEI---PGFGEFRM 104
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 158-201 9.19e-09

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: 56.00  E-value: 9.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 18414227   158 MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGSIHDTVP 201
Cdd:TIGR02057 160 LKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRK 203
 
Name Accession Description Interval E-value
FAD_synthase cd23948
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ...
 18-203 3.30e-93

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: 280.56  E-value: 3.30e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  18 KYNNAIFVIKRALALYSIEEVAFSFNGGKDSTVLLHLLRAGYFLHKKEQtcsngglsSFPVRTIYFESPSAFTEINAFTY 97
Cdd:cd23948   1 KVKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALKRKYPSP--------LTPLKALYIKSPDPFPEVEEFVE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  98 DAAQTYNLQLDIIRQDFKSGLEALLKANP-IRAIFLGVRIGDPTAVGQEQFSPSSPGWPPFMRVNPILDWSYRDVWAFLL 176
Cdd:cd23948  73 DTAKRYNLDLITIDGPMKEGLEELLKEHPiIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLR 152

                       170       180
                ....*....|....*....|....*..
gi 18414227 177 TCKVKYCSLYDQGYTSIGSIHDTVPNS 203
Cdd:cd23948 153 TLNLPYCSLYDQGYTSLGSVDNTLPNP 179
cinA cd00885
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ...
 255-408 3.59e-46

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: 158.42  E-value: 3.59e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVA 334
Cdd:cd00885   2 AEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 335 KAFGVRLAPDEEFEEYLRHLISDQC---TGDRNEMAQLPEGITELLHHEKlSVPLIKCRN---VIVLAATNTEELEKEWE 408
Cdd:cd00885  82 KAFGRPLVLDEEALERIEARFARRGremTEANLKQAMLPEGATLLPNPVG-TAPGFSVEHngkNVFLLPGVPSEMKPMLE 160
CinA COG1058
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ...
 255-490 5.27e-30

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


Pssm-ID: 440678  Cd Length: 249  Bit Score: 117.52  E-value: 5.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVA 334
Cdd:COG1058   2 AEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAVA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 335 KAFGVRLAPDEEFEEYLRHLISD---QCTGDRNEMAQLPEGiTELLHHEKLSVPLIKCRN----VIVLA---AtnteELE 404
Cdd:COG1058  82 EALGVPLVLDPEALALIEERFAKrgrEMTENNLKQALLPEG-AELLPNPVGTAPGFSIENngkvVIFLPgvpS----EMK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 405 K--EWECLTELTKLGGGSLIEysSRRLMT-----SltdvEVAEPLSKLGLEFPDIYLGCYrkSRQGPIIICLT--GKDNA 475
Cdd:COG1058 157 PmfEEEVLPRLKKLFSGEPIV--SRTLRTfgigeS----DLAELLEDLEARFPNVTIGSY--PSDGEVRLRLTarGTDEE 228

                       250
                ....*....|....*
gi 18414227 476 RMDSAAQALRKKFKK 490
Cdd:COG1058 229 EAEAALEALEEELRE 243
PAPS_reduct pfam01507
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ...
 37-201 5.01e-25

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: 101.22  E-value: 5.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227    37 EVAFSFNGGKDSTVLLHLLRagyflhkkeqtcsnggLSSFPVRTIYFESPSAFTEINAFTYDAAQTYNLQLDII------ 110
Cdd:pfam01507   1 ELVVSFSGGKDSLVLLHLAS----------------KAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYlpedsf 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   111 -RQDFKSG--------------LEALLKA---NPIRAIFLGVRIGDPTAVGQEQFSPSSPGWPPFMRVNPILDWSYRDVW 172
Cdd:pfam01507  65 aEGINPEGipsslyrrccrlrkVEPLKRAlkeLGFDAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVW 144

                         170       180
                  ....*....|....*....|....*....
gi 18414227   173 AFLLTCKVKYCSLYDQGYTSIGSIHDTVP 201
Cdd:pfam01507 145 QYILANNVPYNPLYDQGYRSIGCYPCTGP 173
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 20-242 1.02e-19

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: 87.98  E-value: 1.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  20 NNAIFVIKRALALYSiEEVAFSFNGGKDSTVLLHLLRAgyflHKKEqtcsngglssFPVRTIY--FEspsaFTEINAFTY 97
Cdd:COG0175  19 AEAIEILREAAAEFG-GRVVVSSSGGKDSTVLLHLAAK----FKPP----------IPVLFLDtgYE----FPETYEFRD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  98 DAAQTYNLQLDIIR--QDFKSGLE---------------ALLKANPIR---------AIFLGVRigdptavgQEQfSPS- 150
Cdd:COG0175  80 RLAERLGLDLIVVRpeDAFAEQLAefgpplfyrdprwccKIRKVEPLKralagydfdAWITGLR--------RDE-SPTr 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 151 --SP--GWPPF---MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGSIHDTVPnsllsvndtsskekfkpaylLS 223
Cdd:COG0175 151 akEPvvEWDPVgglIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRA--------------------VE 210

                       250
                ....*....|....*....
gi 18414227 224 DGRLERAGRVKKIASLKKD 242
Cdd:COG0175 211 SGEDERAGRWWDEEKERKE 229
PRK03670 PRK03670
competence damage-inducible protein A; Provisional
 253-487 1.67e-17

competence damage-inducible protein A; Provisional


Pssm-ID: 167581  Cd Length: 252  Bit Score: 82.15  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  253 LLASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDS----VSEEVDRQrstSDMVFIYGGVGPLHSDV 328
Cdd:PRK03670   1 MFAEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEiksvVLEILSRK---PEVLVISGGLGPTHDDV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  329 TLAGVAKAFGVRLAPDEE--------FEE-YLRHLISDQCTGD-RNEMAQLPEGiTELLHHEKLSVP--LIKCRNV--IV 394
Cdd:PRK03670  78 TMLAVAEALGRELVLCEDclerikefYEElYKKGLIDDPTLNEaRKKMAYLPEG-AEPLENTEGAAPgaYIEHKGTkiFV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  395 LAATNTE---ELEKEwecltELTKLGGGSLIEyssRRLMTSLTDVEVAEPLSKLGLEFPDIYLGCYRKSRQGPIIICLTG 471
Cdd:PRK03670 157 LPGMPREmkaMLEKE-----VLPRLGERKFVQ---KKFLAEITDESKLAPILEEALERFNVKIHSSPKGFGKYIGIIIFA 228

                        250
                 ....*....|....*.
gi 18414227  472 KDNARMDSAAQALRKK 487
Cdd:PRK03670 229 EDEEEIEKAVEFMEER 244
PRK01215 PRK01215
nicotinamide mononucleotide deamidase-related protein;
255-372 2.80e-17

nicotinamide mononucleotide deamidase-related protein;


Pssm-ID: 179250 [Multi-domain]  Cd Length: 264  Bit Score: 81.60  E-value: 2.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVA 334
Cdd:PRK01215   6 AWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKTNEGFA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18414227  335 KAFGVRLAPDEEFEEYLRHLISDQ---CTGDRNEMAQLPEG 372
Cdd:PRK01215  86 KALGVELELNEDALRMILEKYEKRgipLTPERKKMAMMPPG 126
MoCF_biosynth pfam00994
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 257-354 2.52e-16

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: 75.75  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   257 VIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVAKA 336
Cdd:pfam00994   2 IITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAEL 81

                          90
                  ....*....|....*...
gi 18414227   337 FGVRLapdEEFEEYLRHL 354
Cdd:pfam00994  82 GGREL---PGFEELFRGV 96
MoCF_biosynth smart00852
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ...
 257-341 1.87e-14

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: 70.31  E-value: 1.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227    257 VIAVGDEILSG-TVEDQLGLSLCKKLTSVGWSVQQTTVLRN--DIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGV 333
Cdd:smart00852   2 IISTGDELLSGgQIRDSNGPMLAALLRELGIEVVRVVVVGGpdDPEAIREALREALAEADVVITTGGTGPGPDDLTPEAL 81


                   ....*...
gi 18414227    334 AKAFGVRL 341
Cdd:smart00852  82 AELGGREL 89
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 36-195 5.02e-12

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: 65.10  E-value: 5.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  36 EEVAFSFNGGKDSTVLLHL-LRAGYFLHKKeqtcsngglssfpVRTIYFESPSAFTEINAFTYDAAQTYNLQLDIIRQDF 114
Cdd:cd23947  13 DPVIVSFSGGKDSLVLLHLaLEALRRLRKD-------------VYVVFIDTGIEFPETIDFVEKLAETLGLDVEAARPPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 115 ---KSGLEAL----------------------LKANPIR-----------AIFLGVRigdptavGQEQF-------SPSS 151
Cdd:cd23947  80 fleWLTSNFQpqwdpiwdnpppprdyrwccdeLKLEPFTkwlkekkpegvLLLVGIR-------ADESLnrakrprVYRK 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18414227 152 PGW-----PPFMRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGS 195
Cdd:cd23947 153 YGWrnstlPGQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGGC 201
PAPS_reductase cd23945
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ...
 159-194 3.00e-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: 62.23  E-value: 3.00e-11
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18414227 159 RVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIG 194
Cdd:cd23945 148 KINPLADWTWEDVWAYIREHDLPYNPLHDQGYPSIG 183
PRK02090 PRK02090
phosphoadenylyl-sulfate reductase;
158-201 2.85e-10

phosphoadenylyl-sulfate reductase;


Pssm-ID: 234997  Cd Length: 241  Bit Score: 60.62  E-value: 2.85e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 18414227  158 MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGSIHDTVP 201
Cdd:PRK02090 170 FKINPLADWTNEDVWAYLKEHDLPYHPLVDQGYPSIGCEPCTRP 213
molyb_syn TIGR00177
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ...
 255-352 2.52e-09

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: 55.79  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   255 ASVIAVGDEILSGT-------VEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSD 327
Cdd:TIGR00177   3 VAVISVGDELVEGGqplepgqIYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPRD 82

                          90       100
                  ....*....|....*....|....*
gi 18414227   328 VTLAGVAKAFGVRLapdEEFEEYLR 352
Cdd:TIGR00177  83 VTPEALEELGEKEI---PGFGEFRM 104
PAPS_reductase TIGR02057
phosphoadenosine phosphosulfate reductase, thioredoxin dependent; Requiring thioredoxin as an ...
 158-201 9.19e-09

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: 56.00  E-value: 9.19e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 18414227   158 MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIGSIHDTVP 201
Cdd:TIGR02057 160 LKVNPLIDWTFEQVYQYLDAHNVPYNPLLDQGYRSIGDYHSTRK 203
cysH TIGR00434
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ...
 122-201 2.24e-08

phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129526  Cd Length: 212  Bit Score: 54.41  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   122 LKANPIRAIFLGVRigdptavgQEQfSPSSPGWPPF--------MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSI 193
Cdd:TIGR00434 110 LKELHASAWFTGLR--------RDQ-GPSRANLSILnidekfgiLKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQGYPSI 180


                  ....*...
gi 18414227   194 GSIHDTVP 201
Cdd:TIGR00434 181 GDYHSTRP 188
MoCF_BD cd00758
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ...
 257-342 4.92e-08

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: 51.58  E-value: 4.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 257 VIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDRQRSTSDMVFIYGGVGPLHSDVTLAGVAKA 336
Cdd:cd00758   4 IVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALAEL 83


                ....*.
gi 18414227 337 FGVRLA 342
Cdd:cd00758  84 GEREAH 89
PRK00549 PRK00549
competence damage-inducible protein A; Provisional
 255-372 3.12e-07

competence damage-inducible protein A; Provisional


Pssm-ID: 234789 [Multi-domain]  Cd Length: 414  Bit Score: 52.48  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSV-QQTTVLRN--DIDSVSEEVDrQRStsDMVFIYGGVGPLHSDVTLA 331
Cdd:PRK00549   3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVyHQTVVGDNpeRLLSALEIAE-ERS--DLIITTGGLGPTKDDLTKE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 18414227  332 GVAKAFGVRLAPDEE----FEEYLRHLisDQCTGDRNE-MAQLPEG 372
Cdd:PRK00549  80 TVAKFLGRELVLDEEalakIEDYFAKR--GREMTENNRkQALIPEG 123
Sulfate_adenylyltransferase_2 cd23946
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ...
 20-186 2.42e-06

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: 48.26  E-value: 2.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  20 NNAIFVIKRALALYSIEEVAFSFngGKDSTVLLHLLRAGYFlhkkeqtcsnGGLSSFPVrtIYFESPSAFTEINAFTYDA 99
Cdd:cd23946   7 AESIHIIREVAAEFSNPVMLYSI--GKDSSVMLHLARKAFY----------PGKPPFPL--LHVDTTWKFREMIEFRDRV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227 100 AQTYNLQL------------------------DIIRQDfksGLEALLKANPIRAIFLGVRIGDPTAVGQEQ---FSPSSP 152
Cdd:cd23946  73 AKEYGLDLivhvnpdgveaginpfthgsakhtDIMKTE---GLKQALDKYGFDAAFGGARRDEEKSRAKERvysFRDSNH 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18414227 153 GWPP-------------------FMRVNPILDWSYRDVWAFLLTCKVKYCSLY 186
Cdd:cd23946 150 RWDPknqrpelwnqyngrvkkgeSIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
PRK08557 PRK08557
hypothetical protein; Provisional
 9-194 4.31e-05

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 45.90  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227    9 ESDDKRLKTKYNNAIFVIKRALALYSIEEVAF--SFNGGKDSTVLLHLlragyflhkkeqtcSNGGLSSFPVrtIYFESP 86
Cdd:PRK08557 153 EKNKERIEKLEENSLSILKDYIEKYKNKGYAInaSFSGGKDSSVSTLL--------------AKEVIPDLEV--IFIDTG 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227   87 SAFTEINAFTYDAAQTYNLQLDIIR-QDFKSGLE-------------ALLKANPIRAiFLGVRIGDP---TAVGQEQFSP 149
Cdd:PRK08557 217 LEYPETINYVKDFAKKYDLNLDTLDgDNFWENLEkegiptkdnrwcnSACKLMPLKE-YLKKKYGNKkvlTIDGSRKYES 295

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18414227  150 SS---------PGWPPF-MRVNPILDWSYRDVWAFLLTCKVKYCSLYDQGYTSIG 194
Cdd:PRK08557 296 FTranldyerkSGFIDFqTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
MogA_MoaB cd00886
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ...
 255-329 1.60e-03

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: 39.00  E-value: 1.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18414227 255 ASVIAVGDEILSGTVEDQLGLSLCKKLTSVGWSVQQTTVLRNDIDSVSEEVDR--QRSTSDMVFIYGGVGPLHSDVT 329
Cdd:cd00886   3 AAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIEwaDEDGVDLILTTGGTGLAPRDVT 79
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 38-133 2.56e-03

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 39.11  E-value: 2.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414227  38 VAFSfnGGKDSTVLLHLLRAgyfLHKKEQtcsngglssFPVRTIYF------ESpsafTEINAFTYDAAQTYNLQLDIIR 111
Cdd:cd01992   4 VAVS--GGPDSMALLHLLKE---LRPKLG---------LKLVAVHVdhglreES----AEEAQFVAKLCKKLGIPLHILT 65

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18414227 112 QDF----KSGLEA------------LLKANPIRAIFLG 133
Cdd:cd01992  66 VTEapksGGNLEAaarearyaflerAAKEHGIDVLLTA 103
 
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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