|
Name |
Accession |
Description |
Interval |
E-value |
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
296-476 |
3.01e-99 |
|
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: 296.35 E-value: 3.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 296 LKDSINKLQECFNRYSEEEVCLSFNGGKDCTVLLHLAYTVLLdwtVKEHIPVKPLKTLYIRPNDPFPELEDFIEQSVKRY 375
Cdd:cd23948 2 VKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALK---RKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 376 NLNVIKFSGNIKESLWKLHKEHSEIKAVLMGTRATDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHIPY 455
Cdd:cd23948 79 NLDLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPY 158
|
170 180
....*....|....*....|.
gi 1238882474 456 CSLYDCGYTSLGNQTNTRPNP 476
Cdd:cd23948 159 CSLYDQGYTSLGSVDNTLPNP 179
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
12-186 |
1.01e-48 |
|
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: 165.35 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGV 91
Cdd:cd00885 1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 92 AKAFNEELVVNSDLGNILGQWCEVNGLGKNVIH-KMSLVPQSSKLhyvwdNEHPDLIFPIVSVR----NVFIFPGIPayl 166
Cdd:cd00885 81 AKAFGRPLVLDEEALERIEARFARRGREMTEANlKQAMLPEGATL-----LPNPVGTAPGFSVEhngkNVFLLPGVP--- 152
|
170 180
....*....|....*....|
gi 1238882474 167 ehsfRLLEKIFSpTEAKPFF 186
Cdd:cd00885 153 ----SEMKPMLE-EEVLPRL 167
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
12-254 |
5.33e-47 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 163.36 E-value: 5.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGV 91
Cdd:COG1058 1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 92 AKAFNEELVVNSDLGNILGQWCEVNGLGKNVIH-KMSLVPQSSKlhyVWDNEH---PDLIFPIVSVRnVFIFPGIPAYLE 167
Cdd:COG1058 81 AEALGVPLVLDPEALALIEERFAKRGREMTENNlKQALLPEGAE---LLPNPVgtaPGFSIENNGKV-VIFLPGVPSEMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 168 HSFR--LLEKIFSPTEAKPFFHKILYLS-TTEFTVTEPLSQAVRKYEGrVSFGSYP---EVTLasyqnKITLEGDTEEIV 241
Cdd:COG1058 157 PMFEeeVLPRLKKLFSGEPIVSRTLRTFgIGESDLAELLEDLEARFPN-VTIGSYPsdgEVRL-----RLTARGTDEEEA 230
|
250
....*....|...
gi 1238882474 242 LEAEGFLRSLLPK 254
Cdd:COG1058 231 EAALEALEEELRE 243
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
317-474 |
5.19e-32 |
|
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: 120.86 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 317 LSFNGGKDCTVLLHLAYTVLldwtvkehipvKPLKTLYIRPNDPFPELEDFIEQSVKRYNLNVI--------KFSGNIKE 388
Cdd:pfam01507 4 VSFSGGKDSLVLLHLASKAF-----------PPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKvylpedsfAEGINPEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 389 SLWKLHKEHSEIK---------------AVLMGTRATDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHI 453
Cdd:pfam01507 73 IPSSLYRRCCRLRkveplkralkelgfdAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNV 152
|
170 180
....*....|....*....|.
gi 1238882474 454 PYCSLYDCGYTSLGNQTNTRP 474
Cdd:pfam01507 153 PYNPLYDQGYRSIGCYPCTGP 173
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-173 |
7.95e-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: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 15 IVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGVAKA 94
Cdd:pfam00994 2 IITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 95 FNEELVVNSDLgnilgqwcevnglgknvIHKMSLVPqssklhyvwdnEHPDLIFPIVSV----RNVFIFPGIPAYLEHSF 170
Cdd:pfam00994 82 GGRELPGFEEL-----------------FRGVSLKP-----------GKPVGTAPGAILsragKTVFGLPGSPVAAKVMF 133
|
...
gi 1238882474 171 RLL 173
Cdd:pfam00994 134 ELL 136
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-164 |
1.04e-22 |
|
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: 93.81 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 15 IVIIGDEILKGHT-RDTNSHFLCHGLYNIGVKVLRIVIV--PDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGV 91
Cdd:smart00852 2 IISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEAL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238882474 92 AKAFNEELVVnsdlgnilgqwcevnglgknviHKMSLVPQSSKLHYVWdnehPDLIFPIVSVRN-VFIFPGIPA 164
Cdd:smart00852 82 AELGGRELLG----------------------HGVAMRPGGPPGPLAN----LSGTAPGVRGKKpVFGLPGNPV 129
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
8-254 |
2.11e-22 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 96.62 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 8 MSRDTASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVT 87
Cdd:PRK01215 1 MDKWFAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 88 YAGVAKAFNEELVVNSD-LGNILGQWCEVNglgknvihkMSLVPQSSKLHYVWDN----EHPDLIFP--IVSVRN--VFI 158
Cdd:PRK01215 81 NEGFAKALGVELELNEDaLRMILEKYEKRG---------IPLTPERKKMAMMPPGavplENPVGTAPgiLIEHGGkdIVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 159 FPGIPAYLEHSFR-LLEKIFSPTEAKPFFHKILYLS-TTEFTVTEPLSQAVRKYEgRVSFGSYP----------EVTLAS 226
Cdd:PRK01215 152 LPGVPREMEAIFEnFVEPLLKNRPPLKYYEDSILVEgVMESDLAPYVKELVKKYD-RVYVKSHPkgyevskpilEIQIAG 230
|
250 260
....*....|....*....|....*...
gi 1238882474 227 YQNKitlEGDTEEIVLEAEGFLRSLLPK 254
Cdd:PRK01215 231 SGER---EEEAKVKVEKVLEELKELIKK 255
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
293-474 |
1.31e-20 |
|
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: 90.68 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 293 AGLLKDSINKLQECFNRYsEEEVCLSFNGGKDCTVLLHLAYTVLLDwtvkehIPVKPLKTLYIrpndpFPELEDFIEQSV 372
Cdd:COG0175 15 AELEAEAIEILREAAAEF-GGRVVVSSSGGKDSTVLLHLAAKFKPP------IPVLFLDTGYE-----FPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 373 KRYNLNVIKFSGniKESLWKLHKEHSEikavLMGTRATDPYSSRLKT---------------------------FQETDH 425
Cdd:COG0175 83 ERLGLDLIVVRP--EDAFAEQLAEFGP----PLFYRDPRWCCKIRKVeplkralagydfdawitglrrdesptrAKEPVV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238882474 426 GWPP---LMRISPLLDWGYHDVWGFLRTLHIPYCSLYDCGYTSLGNQTNTRP 474
Cdd:COG0175 157 EWDPvggLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRA 208
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
12-99 |
4.38e-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: 72.35 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHT-------RDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHD 84
Cdd:TIGR00177 2 RVAVISVGDELVEGGQplepgqiYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPR 81
|
90
....*....|....*
gi 1238882474 85 DVTYAGVAKAFNEEL 99
Cdd:TIGR00177 82 DVTPEALEELGEKEI 96
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
327-474 |
1.19e-12 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 67.56 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 327 VLLHLAytvlldWTVKEHIPVKPLKTLYIrpndpFPELEDFIEQSVKRYNLNVIKFSGNIKES--------LW----KLH 394
Cdd:PRK02090 55 VLLHLV------AQVDPDIPVIFLDTGYL-----FPETYRFIDELTERLLLNLKVYRPDASAAeqearyggLWeqsvEDR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 395 KEHSEIKAVLMGTRATDPYS---SRLKTFQ----------ETDHGwppLMRISPLLDWGYHDVWGFLRTLHIPYCSLYDC 461
Cdd:PRK02090 124 DECCRIRKVEPLNRALAGLDawiTGLRREQsgtranlpvlEIDGG---RFKINPLADWTNEDVWAYLKEHDLPYHPLVDQ 200
|
170
....*....|...
gi 1238882474 462 GYTSLGNQTNTRP 474
Cdd:PRK02090 201 GYPSIGCEPCTRP 213
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
327-504 |
1.16e-11 |
|
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: 64.04 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 327 VLLHLAYTVlldwtvKEHIPVKPLKTLYIrpndpFPELEDFIEQSVKRYNLNVIKFSGNIKES---------LWK----- 392
Cdd:TIGR00434 28 VLLDLVSKI------SPDIPVIFLDTGYH-----FPETYELIDELTERYPLNIKVYKPDLSLAeqaakygdkLWEqdpnk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 393 ---------LHKEHSE--IKAVLMGTRaTDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHIPYCSLYDC 461
Cdd:TIGR00434 97 ydylrkvepMHRALKElhASAWFTGLR-RDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1238882474 462 GYTSLGNQTNTRPnprllvqedncsryrpaymLKDPSEEREGR 504
Cdd:TIGR00434 176 GYPSIGDYHSTRP-------------------VKEGEDERAGR 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FAD_synthase |
cd23948 |
FAD synthase; FAD synthase (FMN:ATP adenylyl transferase (FMNAT); FAD pyrophosphorylase; ... |
296-476 |
3.01e-99 |
|
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: 296.35 E-value: 3.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 296 LKDSINKLQECFNRYSEEEVCLSFNGGKDCTVLLHLAYTVLLdwtVKEHIPVKPLKTLYIRPNDPFPELEDFIEQSVKRY 375
Cdd:cd23948 2 VKSALEVIEEALDKYGPEEIAISFNGGKDCTVLLHLLRAALK---RKYPSPLTPLKALYIKSPDPFPEVEEFVEDTAKRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 376 NLNVIKFSGNIKESLWKLHKEHSEIKAVLMGTRATDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHIPY 455
Cdd:cd23948 79 NLDLITIDGPMKEGLEELLKEHPIIKAVFMGTRRTDPHGENLKPFSPTDPGWPQFMRVNPILDWSYHDVWEFLRTLNLPY 158
|
170 180
....*....|....*....|.
gi 1238882474 456 CSLYDCGYTSLGNQTNTRPNP 476
Cdd:cd23948 159 CSLYDQGYTSLGSVDNTLPNP 179
|
|
| cinA |
cd00885 |
Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon ... |
12-186 |
1.01e-48 |
|
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: 165.35 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGV 91
Cdd:cd00885 1 TAEIIAIGDELLSGQIVDTNAAFLAKELAELGIEVYRVTVVGDDEDRIAEALRRASERADLVITTGGLGPTHDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 92 AKAFNEELVVNSDLGNILGQWCEVNGLGKNVIH-KMSLVPQSSKLhyvwdNEHPDLIFPIVSVR----NVFIFPGIPayl 166
Cdd:cd00885 81 AKAFGRPLVLDEEALERIEARFARRGREMTEANlKQAMLPEGATL-----LPNPVGTAPGFSVEhngkNVFLLPGVP--- 152
|
170 180
....*....|....*....|
gi 1238882474 167 ehsfRLLEKIFSpTEAKPFF 186
Cdd:cd00885 153 ----SEMKPMLE-EEVLPRL 167
|
|
| CinA |
COG1058 |
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA ... |
12-254 |
5.33e-47 |
|
ADP-ribose pyrophosphatase domain of DNA damage- and competence-inducible protein CinA [Replication, recombination and repair];
Pssm-ID: 440678 Cd Length: 249 Bit Score: 163.36 E-value: 5.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGV 91
Cdd:COG1058 1 KAEIITIGDELLSGRIVDTNAAWLARELAELGIDVYRITTVGDDPERIVEALREALARADLVITTGGLGPTPDDLTREAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 92 AKAFNEELVVNSDLGNILGQWCEVNGLGKNVIH-KMSLVPQSSKlhyVWDNEH---PDLIFPIVSVRnVFIFPGIPAYLE 167
Cdd:COG1058 81 AEALGVPLVLDPEALALIEERFAKRGREMTENNlKQALLPEGAE---LLPNPVgtaPGFSIENNGKV-VIFLPGVPSEMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 168 HSFR--LLEKIFSPTEAKPFFHKILYLS-TTEFTVTEPLSQAVRKYEGrVSFGSYP---EVTLasyqnKITLEGDTEEIV 241
Cdd:COG1058 157 PMFEeeVLPRLKKLFSGEPIVSRTLRTFgIGESDLAELLEDLEARFPN-VTIGSYPsdgEVRL-----RLTARGTDEEEA 230
|
250
....*....|...
gi 1238882474 242 LEAEGFLRSLLPK 254
Cdd:COG1058 231 EAALEALEEELRE 243
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
317-474 |
5.19e-32 |
|
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: 120.86 E-value: 5.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 317 LSFNGGKDCTVLLHLAYTVLldwtvkehipvKPLKTLYIRPNDPFPELEDFIEQSVKRYNLNVI--------KFSGNIKE 388
Cdd:pfam01507 4 VSFSGGKDSLVLLHLASKAF-----------PPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKvylpedsfAEGINPEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 389 SLWKLHKEHSEIK---------------AVLMGTRATDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHI 453
Cdd:pfam01507 73 IPSSLYRRCCRLRkveplkralkelgfdAWFTGLRRDESPSRAKLPIVSIDGDFPKVIKVFPLLNWTETDVWQYILANNV 152
|
170 180
....*....|....*....|.
gi 1238882474 454 PYCSLYDCGYTSLGNQTNTRP 474
Cdd:pfam01507 153 PYNPLYDQGYRSIGCYPCTGP 173
|
|
| MoCF_biosynth |
pfam00994 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-173 |
7.95e-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: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 15 IVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGVAKA 94
Cdd:pfam00994 2 IITTGDELLPGQIRDTNGPLLAALLREAGAEVIRYGIVPDDPEAIKEALRAAAEEADVVITTGGTGPGPDDVTPEALAEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 95 FNEELVVNSDLgnilgqwcevnglgknvIHKMSLVPqssklhyvwdnEHPDLIFPIVSV----RNVFIFPGIPAYLEHSF 170
Cdd:pfam00994 82 GGRELPGFEEL-----------------FRGVSLKP-----------GKPVGTAPGAILsragKTVFGLPGSPVAAKVMF 133
|
...
gi 1238882474 171 RLL 173
Cdd:pfam00994 134 ELL 136
|
|
| MoCF_biosynth |
smart00852 |
Probable molybdopterin binding domain; This domain is found a variety of proteins involved in ... |
15-164 |
1.04e-22 |
|
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: 93.81 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 15 IVIIGDEILKGHT-RDTNSHFLCHGLYNIGVKVLRIVIV--PDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGV 91
Cdd:smart00852 2 IISTGDELLSGGQiRDSNGPMLAALLRELGIEVVRVVVVggPDDPEAIREALREALAEADVVITTGGTGPGPDDLTPEAL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238882474 92 AKAFNEELVVnsdlgnilgqwcevnglgknviHKMSLVPQSSKLHYVWdnehPDLIFPIVSVRN-VFIFPGIPA 164
Cdd:smart00852 82 AELGGRELLG----------------------HGVAMRPGGPPGPLAN----LSGTAPGVRGKKpVFGLPGNPV 129
|
|
| PRK01215 |
PRK01215 |
nicotinamide mononucleotide deamidase-related protein; |
8-254 |
2.11e-22 |
|
nicotinamide mononucleotide deamidase-related protein;
Pssm-ID: 179250 [Multi-domain] Cd Length: 264 Bit Score: 96.62 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 8 MSRDTASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVT 87
Cdd:PRK01215 1 MDKWFAWIITIGNELLIGRTVNTNASWIARRLTYLGYTVRRITVVMDDIEEIVSAFREAIDRADVVVSTGGLGPTYDDKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 88 YAGVAKAFNEELVVNSD-LGNILGQWCEVNglgknvihkMSLVPQSSKLHYVWDN----EHPDLIFP--IVSVRN--VFI 158
Cdd:PRK01215 81 NEGFAKALGVELELNEDaLRMILEKYEKRG---------IPLTPERKKMAMMPPGavplENPVGTAPgiLIEHGGkdIVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 159 FPGIPAYLEHSFR-LLEKIFSPTEAKPFFHKILYLS-TTEFTVTEPLSQAVRKYEgRVSFGSYP----------EVTLAS 226
Cdd:PRK01215 152 LPGVPREMEAIFEnFVEPLLKNRPPLKYYEDSILVEgVMESDLAPYVKELVKKYD-RVYVKSHPkgyevskpilEIQIAG 230
|
250 260
....*....|....*....|....*...
gi 1238882474 227 YQNKitlEGDTEEIVLEAEGFLRSLLPK 254
Cdd:PRK01215 231 SGER---EEEAKVKVEKVLEELKELIKK 255
|
|
| CysD |
COG0175 |
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ... |
293-474 |
1.31e-20 |
|
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: 90.68 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 293 AGLLKDSINKLQECFNRYsEEEVCLSFNGGKDCTVLLHLAYTVLLDwtvkehIPVKPLKTLYIrpndpFPELEDFIEQSV 372
Cdd:COG0175 15 AELEAEAIEILREAAAEF-GGRVVVSSSGGKDSTVLLHLAAKFKPP------IPVLFLDTGYE-----FPETYEFRDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 373 KRYNLNVIKFSGniKESLWKLHKEHSEikavLMGTRATDPYSSRLKT---------------------------FQETDH 425
Cdd:COG0175 83 ERLGLDLIVVRP--EDAFAEQLAEFGP----PLFYRDPRWCCKIRKVeplkralagydfdawitglrrdesptrAKEPVV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238882474 426 GWPP---LMRISPLLDWGYHDVWGFLRTLHIPYCSLYDCGYTSLGNQTNTRP 474
Cdd:COG0175 157 EWDPvggLIKVNPLADWTELDVWAYIRREDLPYNPLYDQGYPSIGCAPCTRA 208
|
|
| PRK03670 |
PRK03670 |
competence damage-inducible protein A; Provisional |
13-250 |
1.73e-20 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 167581 Cd Length: 252 Bit Score: 90.63 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 13 ASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLT-SGGIGPTHDDVTYAGV 91
Cdd:PRK03670 3 AEIITVGDELLTGNTVDSNSAFIAQKLTEKGYWVRRITTVGDDVEEIKSVVLEILSRKPEVLViSGGLGPTHDDVTMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 92 AKAFNEELVVNSD-LGNILGQWCEVNGLG-------KNVIHKMSLVPQSSKLHYVWDNEHPDLIFPIVSVRnVFIFPGIP 163
Cdd:PRK03670 83 AEALGRELVLCEDcLERIKEFYEELYKKGliddptlNEARKKMAYLPEGAEPLENTEGAAPGAYIEHKGTK-IFVLPGMP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 164 AYLEhsfRLLEKIFSPTEAKPFFHKILYLS--TTEFTVTEPLSQAVRKYEGRV-----SFGSYPevtlasyqnKITLEGD 236
Cdd:PRK03670 162 REMK---AMLEKEVLPRLGERKFVQKKFLAeiTDESKLAPILEEALERFNVKIhsspkGFGKYI---------GIIIFAE 229
|
250
....*....|....
gi 1238882474 237 TEEIVLEAEGFLRS 250
Cdd:PRK03670 230 DEEEIEKAVEFMEE 243
|
|
| PAPS_reductase |
cd23945 |
Phosphoadenylyl-sulfate reductase (thioredoxin); Phosphoadenosine phosphosulfate (PAPS) ... |
313-467 |
3.60e-16 |
|
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: 76.48 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 313 EEVCLSFNGGKDCTVLLHLAytvlldWTVKEHIPVKPLKTLYIrpndpFPELEDFIEQSVKRYNLNVIKFSGNIKE---- 388
Cdd:cd23945 14 PKLVFATSFGAEDAVILDLL------SKVRPDIPVVFLDTGYL-----FPETYDLIDEVEARYGLNIEVYFPEGTEaeee 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 389 -------SLWK----------------LHKEHSEIKAVLMGTRAtDPYSSR--LKTFQETDHGwpPLMRISPLLDWGYHD 443
Cdd:cd23945 83 alegglnEFYLedeerydccrkrkpfpLALALLGVKAWITGRRR-DQSPTRanLPIVEVDEEG--GLVKINPLADWTWED 159
|
170 180
....*....|....*....|....
gi 1238882474 444 VWGFLRTLHIPYCSLYDCGYTSLG 467
Cdd:cd23945 160 VWAYIREHDLPYNPLHDQGYPSIG 183
|
|
| molyb_syn |
TIGR00177 |
molybdenum cofactor synthesis domain; The Drosophila protein cinnamon, the Arabidopsis protein ... |
12-99 |
4.38e-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: 72.35 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHT-------RDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHD 84
Cdd:TIGR00177 2 RVAVISVGDELVEGGQplepgqiYDSNGPLLAALLQEAGFNVVRLGIVPDDPEEIREILRKAVDEADVVLTTGGTGVGPR 81
|
90
....*....|....*
gi 1238882474 85 DVTYAGVAKAFNEEL 99
Cdd:TIGR00177 82 DVTPEALEELGEKEI 96
|
|
| PRK00549 |
PRK00549 |
competence damage-inducible protein A; Provisional |
13-163 |
4.01e-14 |
|
competence damage-inducible protein A; Provisional
Pssm-ID: 234789 [Multi-domain] Cd Length: 414 Bit Score: 74.05 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 13 ASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGVA 92
Cdd:PRK00549 3 AEIIAVGTELLLGQIVNTNAQFLSEKLAELGIDVYHQTVVGDNPERLLSALEIAEERSDLIITTGGLGPTKDDLTKETVA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238882474 93 KAFNEELVVNSDLGNILGQWceVNGLGKNV---IHKMSLVPQSSKlhyVWDNEH---PDLIFPIVSVrNVFIFPGIP 163
Cdd:PRK00549 83 KFLGRELVLDEEALAKIEDY--FAKRGREMtenNRKQALIPEGAT---VLPNPVgtaPGMIIEVDGK-TYIVLPGPP 153
|
|
| cinA_nterm |
TIGR00200 |
competence/damage-inducible protein CinA N-terminal domain; cinA is a DNA damage- or ... |
13-180 |
9.33e-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: 69.94 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 13 ASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGVA 92
Cdd:TIGR00200 3 AEIISVGDELLLGQIVNTNAQWLADFLAHQGLPLSRRTTVGDNPERLKTIIRIASERADVLIFNGGLGPTSDDLTAETIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 93 KAFNEELVVNSD-LGNILGQWCEVNGLGKNVIHKMSLVPQSSKLHYVWDNEHPDLIFPIVSVRNVFIFPGIPAYLEHSF- 170
Cdd:TIGR00200 83 TAKGEPLVLNEAwLKEIERYFHETGRVMAPNNRKQALLPAGAEFLANPVGTAPGMFAVQLNRCLMLFTPGVPSEFRVMVe 162
|
170
....*....|....*
gi 1238882474 171 -----RLLEKIFSPT 180
Cdd:TIGR00200 163 healpRLRERFSLPQ 177
|
|
| PRK02090 |
PRK02090 |
phosphoadenylyl-sulfate reductase; |
327-474 |
1.19e-12 |
|
phosphoadenylyl-sulfate reductase;
Pssm-ID: 234997 Cd Length: 241 Bit Score: 67.56 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 327 VLLHLAytvlldWTVKEHIPVKPLKTLYIrpndpFPELEDFIEQSVKRYNLNVIKFSGNIKES--------LW----KLH 394
Cdd:PRK02090 55 VLLHLV------AQVDPDIPVIFLDTGYL-----FPETYRFIDELTERLLLNLKVYRPDASAAeqearyggLWeqsvEDR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 395 KEHSEIKAVLMGTRATDPYS---SRLKTFQ----------ETDHGwppLMRISPLLDWGYHDVWGFLRTLHIPYCSLYDC 461
Cdd:PRK02090 124 DECCRIRKVEPLNRALAGLDawiTGLRREQsgtranlpvlEIDGG---RFKINPLADWTNEDVWAYLKEHDLPYHPLVDQ 200
|
170
....*....|...
gi 1238882474 462 GYTSLGNQTNTRP 474
Cdd:PRK02090 201 GYPSIGCEPCTRP 213
|
|
| PAPS_reductase-like_YbdN |
cd23947 |
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ... |
299-467 |
2.31e-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: 65.87 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 299 SINKLQECFNRYseEEVCLSFNGGKDCTVLLHLAYTVLLDWTvkehipvKPLKTLYIRPNDPFPELEDFIEQSVKRYNLN 378
Cdd:cd23947 1 ALERIRKVFEEF--DPVIVSFSGGKDSLVLLHLALEALRRLR-------KDVYVVFIDTGIEFPETIDFVEKLAETLGLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 379 VIKFSG----------------NIKESLWK-------------------LHKEHSEIKAVLMGTRAtdpYSS-------R 416
Cdd:cd23947 72 VEAARPplflewltsnfqpqwdPIWDNPPPprdyrwccdelklepftkwLKEKKPEGVLLLVGIRA---DESlnrakrpR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1238882474 417 LKTFQETDHGWPP-LMRISPLLDWGYHDVWGFLRTLHIPYCSLYDCGYTSLG 467
Cdd:cd23947 149 VYRKYGWRNSTLPgQIVAYPIKDWSVEDVWLYILRHGLPYNPLYDLGFDRGG 200
|
|
| cysH |
TIGR00434 |
phosophoadenylyl-sulfate reductase (thioredoxin); This enzyme, involved in the assimilation of ... |
327-504 |
1.16e-11 |
|
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: 64.04 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 327 VLLHLAYTVlldwtvKEHIPVKPLKTLYIrpndpFPELEDFIEQSVKRYNLNVIKFSGNIKES---------LWK----- 392
Cdd:TIGR00434 28 VLLDLVSKI------SPDIPVIFLDTGYH-----FPETYELIDELTERYPLNIKVYKPDLSLAeqaakygdkLWEqdpnk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 393 ---------LHKEHSE--IKAVLMGTRaTDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHIPYCSLYDC 461
Cdd:TIGR00434 97 ydylrkvepMHRALKElhASAWFTGLR-RDQGPSRANLSILNIDEKFGILKVLPLIDWTWKDVYQYIDAHNLPYNPLHDQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1238882474 462 GYTSLGNQTNTRPnprllvqedncsryrpaymLKDPSEEREGR 504
Cdd:TIGR00434 176 GYPSIGDYHSTRP-------------------VKEGEDERAGR 199
|
|
| MoCF_BD |
cd00758 |
MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of ... |
15-100 |
2.86e-10 |
|
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: 58.12 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 15 IVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGVAKA 94
Cdd:cd00758 4 IVTVSDELSQGQIEDTNGPALEALLEDLGCEVIYAGVVPDDADSIRAALIEASREADLVLTTGGTGVGRRDVTPEALAEL 83
|
....*.
gi 1238882474 95 FNEELV 100
Cdd:cd00758 84 GEREAH 89
|
|
| PRK08557 |
PRK08557 |
hypothetical protein; Provisional |
295-467 |
4.85e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181465 [Multi-domain] Cd Length: 417 Bit Score: 55.15 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 295 LLKDSINKLQECFNRYSEE--EVCLSFNGGKDCTVLLHLAYTVLLDwtvkehipvkpLKTLYIRPNDPFPELEDFIEQSV 372
Cdd:PRK08557 162 LEENSLSILKDYIEKYKNKgyAINASFSGGKDSSVSTLLAKEVIPD-----------LEVIFIDTGLEYPETINYVKDFA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 373 KRYNLNVIKFSGN------------IKESLW-----KLH------KEHSEIKAVLM--GTRATDPYSsRLKTFQETDHGW 427
Cdd:PRK08557 231 KKYDLNLDTLDGDnfwenlekegipTKDNRWcnsacKLMplkeylKKKYGNKKVLTidGSRKYESFT-RANLDYERKSGF 309
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1238882474 428 PPL-MRISPLLDWGYHDVWGFLRTLHIPYCSLYDCGYTSLG 467
Cdd:PRK08557 310 IDFqTNVFPILDWNSLDIWSYIYLNDILYNPLYDKGFERIG 350
|
|
| PLN02309 |
PLN02309 |
5'-adenylylsulfate reductase |
406-474 |
1.74e-07 |
|
5'-adenylylsulfate reductase
Pssm-ID: 215175 [Multi-domain] Cd Length: 457 Bit Score: 53.64 E-value: 1.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238882474 406 GTRATDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHIPYCSLYDCGYTSLGNQTNTRP 474
Cdd:PLN02309 225 GTRAEVPVVQVDPVFEGLDGGPGSLVKWNPLANVTGNEVWNFLRTMDVPVNSLHAQGYVSIGCEPCTRP 293
|
|
| MoeA |
COG0303 |
Molybdopterin Mo-transferase (molybdopterin biosynthesis) [Coenzyme transport and metabolism]; ... |
15-79 |
3.83e-07 |
|
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: 52.40 E-value: 3.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238882474 15 IVII--GDEIL-------KGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGI 79
Cdd:COG0303 175 VAILstGDELVepgeplgPGQIYDSNSYMLAALLREAGAEVVDLGIVPDDPEALRAALREALAEADLVITSGGV 248
|
|
| Sulfate_adenylyltransferase_2 |
cd23946 |
Sulfate adenylyltransferase subunit 2; Sulfate adenylyltransferase subunits 1 and 2 form ATP ... |
295-459 |
3.96e-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: 50.96 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 295 LLKDSINKLQECFNRYSEEEVCLSFngGKDCTVLLHLAytvlldwtVKEHIPVK-PLKTLYIRPNDPFPELEDFIEQSVK 373
Cdd:cd23946 5 LEAESIHIIREVAAEFSNPVMLYSI--GKDSSVMLHLA--------RKAFYPGKpPFPLLHVDTTWKFREMIEFRDRVAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 374 RYNLNVIKFSG--NIKESLWKLHK---EHSEI---------------KAVLMGTRaTDPYSSRLK----TFQETDHGWPP 429
Cdd:cd23946 75 EYGLDLIVHVNpdGVEAGINPFTHgsaKHTDImkteglkqaldkygfDAAFGGAR-RDEEKSRAKervySFRDSNHRWDP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1238882474 430 L-------------------MRISPLLDWGYHDVWGFLRTLHIPYCSLY 459
Cdd:cd23946 154 KnqrpelwnqyngrvkkgesIRVFPLSNWTELDIWQYIYLENIPIVPLY 202
|
|
| MogA_MoaB |
cd00886 |
MogA_MoaB family. Members of this family are involved in biosynthesis of the molybdenum ... |
12-99 |
4.25e-07 |
|
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: 49.40 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 12 TASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEIS-FCA-SRYSFVLTSGGIGPTHDDVTYA 89
Cdd:cd00886 2 RAAVLTVSDTRSAGEAEDRSGPALVELLEEAGHEVVAYEIVPDDKDEIREALIeWADeDGVDLILTTGGTGLAPRDVTPE 81
|
90
....*....|
gi 1238882474 90 GVAKAFNEEL 99
Cdd:cd00886 82 ATRPLLDKEL 91
|
|
| PRK03673 |
PRK03673 |
nicotinamide mononucleotide deamidase-related protein YfaY; |
19-100 |
8.81e-07 |
|
nicotinamide mononucleotide deamidase-related protein YfaY;
Pssm-ID: 179629 [Multi-domain] Cd Length: 396 Bit Score: 51.24 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 19 GDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGIGPTHDDVTYAGVAKAFNEE 98
Cdd:PRK03673 10 GDEVLHGQIVDTNAAWLADFFFHQGLPLSRRNTVGDNLDALVAILRERSQHADVLIVNGGLGPTSDDLSALAAATAAGEG 89
|
..
gi 1238882474 99 LV 100
Cdd:PRK03673 90 LV 91
|
|
| MoaB |
COG0521 |
Molybdopterin biosynthesis enzyme MoaB/MogA [Coenzyme transport and metabolism]; Molybdopterin ... |
1-88 |
1.19e-06 |
|
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: 48.57 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 1 MAASEERMSRdTASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEIS-FCA-SRYSFVLTSGG 78
Cdd:COG0521 1 MSSARAFVPL-RIAVLTVSDRRSRGEREDTSGPALVELLEEAGHEVVARRIVPDDKDAIRAALReLIDdEGVDLVLTTGG 79
|
90
....*....|
gi 1238882474 79 IGPTHDDVTY 88
Cdd:COG0521 80 TGLSPRDVTP 89
|
|
| APS_reduc |
TIGR00424 |
5'-adenylylsulfate reductase, thioredoxin-independent; This enzyme, involved in the ... |
406-474 |
1.39e-06 |
|
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: 50.78 E-value: 1.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238882474 406 GTRATDPYSSRLKTFQETDHGWPPLMRISPLLDWGYHDVWGFLRTLHIPYCSLYDCGYTSLGNQTNTRP 474
Cdd:TIGR00424 230 GTRSEIPVVQVDPVFEGLDGGVGSLVKWNPVANVEGKDVWNFLRTMDVPVNTLHAQGYVSIGCEPCTRP 298
|
|
| MoeA |
cd00887 |
MoeA family. Members of this family are involved in biosynthesis of the molybdenum cofactor ... |
15-79 |
2.27e-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: 2.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238882474 15 IVII--GDEIL-------KGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEISFCASRYSFVLTSGGI 79
Cdd:cd00887 171 VAIIstGDELVepgeplaPGQIYDSNSYMLAALLRELGAEVVDLGIVPDDPEALREALEEALEEADVVITSGGV 244
|
|
| moaC |
PRK03604 |
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional |
13-87 |
1.46e-04 |
|
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
Pssm-ID: 235138 [Multi-domain] Cd Length: 312 Bit Score: 43.78 E-value: 1.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238882474 13 ASIVIIGDEILKGHTRDTNSHFLCHGLYNIGVKVLRIVIVPDDLPAIAAEI-SFCASRYSFVLTSG--GIGPThdDVT 87
Cdd:PRK03604 158 AAVLVLSDSIAAGTKEDRSGKLIVEGLEEAGFEVSHYTIIPDEPAEIAAAVaAWIAEGYALIITTGgtGLGPR--DVT 233
|
|
| AANH-like |
cd01986 |
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ... |
315-380 |
1.12e-03 |
|
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: 37.82 E-value: 1.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238882474 315 VCLSFNGGKDCTVLLHLAytvlldwtvKEHIPVKPLKTLYIRPNDPFPELEDFIEQSVKRYNLNVI 380
Cdd:cd01986 1 VVVGYSGGKDSSVALHLA---------SRLGRKAEVAVVHIDHGIGFKEEAESVASIARRSILKKL 57
|
|
| PRK12563 |
PRK12563 |
sulfate adenylyltransferase subunit CysD; |
319-459 |
1.63e-03 |
|
sulfate adenylyltransferase subunit CysD;
Pssm-ID: 237138 Cd Length: 312 Bit Score: 40.54 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 319 FNGGKDCTVLLHLAytvlldwtVKEHIPVK-PLKTLYIRPNDPFPELEDFIEQSVKRY---------------NLNVIKF 382
Cdd:PRK12563 44 YSIGKDSVVMLHLA--------MKAFRPTRpPFPLLHVDTTWKFREMIDFRDRRAKELgldlvvhhnpdgiarGIVPFRH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 383 SGNIKESLWKLHK-----EHSEIKAVLMGTRaTDPYSSRLK----TFQETDHGWPPL-------------------MRIS 434
Cdd:PRK12563 116 GSALHTDVAKTQGlkqalDHHGFDAAIGGAR-RDEEKSRAKerifSFRSAFHRWDPKaqrpelwslynarlrrgesLRVF 194
|
170 180
....*....|....*....|....*
gi 1238882474 435 PLLDWGYHDVWGFLRTLHIPYCSLY 459
Cdd:PRK12563 195 PLSNWTELDVWQYIAREKIPLVPLY 219
|
|
| PRK13794 |
PRK13794 |
hypothetical protein; Provisional |
236-396 |
3.98e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237509 [Multi-domain] Cd Length: 479 Bit Score: 39.65 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 236 DTEEIVLEAEGFL----RSLLPKNS-VVSPYVPSSEDSKKKLFSladtnfNGSEQEKTEVQFAGLLKDSINKLqecfnry 310
Cdd:PRK13794 180 SYEEIVNMEKGMVvkvrKSEEPKNSnILSEYGPGEETWKDMVEA------NKNVLDKYERNSIGFIRNTAEKI------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238882474 311 sEEEVCLSFNGGKDCTVLLHLAYTVLldwtvKEHIPVkplktLYIRPNDPFPELEDFIEQSVKRYNLNVIKFSGnikESL 390
Cdd:PRK13794 247 -NKPVTVAYSGGKDSLATLLLALKAL-----GINFPV-----LFNDTGLEFPETLENVEDVEKHYGLEIIRTKS---EEF 312
|
....*.
gi 1238882474 391 WKLHKE 396
Cdd:PRK13794 313 WEKLEE 318
|
|
| |
