|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
4-530 |
0e+00 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 1053.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918 1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918 81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918 161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 305
Cdd:PLN02918 241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 306 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 385
Cdd:PLN02918 320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 386 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 465
Cdd:PLN02918 400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695795 466 EYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN02918 480 EYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
|
|
| PdxH |
COG0259 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ... |
316-530 |
9.74e-114 |
|
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440029 Cd Length: 212 Bit Score: 335.62 E-value: 9.74e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 316 DISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESK 395
Cdd:COG0259 3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 396 KGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYS 475
Cdd:COG0259 83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30695795 476 DGSViPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNgnpaWKIHRLAP 530
Cdd:COG0259 163 GGDV-PRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGG----WTIERLAP 212
|
|
| pdxH |
TIGR00558 |
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ... |
337-530 |
2.02e-113 |
|
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273138 Cd Length: 190 Bit Score: 334.08 E-value: 2.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:TIGR00558 1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSViPKPKNWGGFRLKPNLF 496
Cdd:TIGR00558 81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEV-PRPEFWGGYRVVPDEI 159
|
170 180 190
....*....|....*....|....*....|....
gi 30695795 497 EFWQGQPSRLHDRLQYSLQDVNGnpaWKIHRLAP 530
Cdd:TIGR00558 160 EFWQGRPSRLHDRFRYRRDGDGS---WRIERLAP 190
|
|
| phena_PhzG |
NF038138 |
phenazine biosynthesis FMN-dependent oxidase PhzG; |
337-530 |
3.42e-52 |
|
phenazine biosynthesis FMN-dependent oxidase PhzG;
Pssm-ID: 468380 Cd Length: 205 Bit Score: 176.40 E-value: 3.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:NF038138 19 EPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRETS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQysdGSVIPKPKNWGGFRLKPNLF 496
Cdd:NF038138 99 QQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAEA---GGPLPRPARFVGYRLVPEEV 175
|
170 180 190
....*....|....*....|....*....|....
gi 30695795 497 EFWQGQPSRLHDRLQYslqDVNGnPAWKIHRLAP 530
Cdd:NF038138 176 EFWAAGPDRLHRRLRY---DRDG-DGWTHVRLQP 205
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
97-269 |
1.99e-41 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 146.60 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 97 DQLMELAGLSVAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFICYPkrtaKPLYTGLV-TQLDSL 173
Cdd:pfam03853 2 AVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGP----EEKLSEDArRQLDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 174 S------VPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqtLQKHPVIVSVDIPSGWHVEE 247
Cdd:pfam03853 77 KklggkiVTDNPDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALIEWI---------NQSGAPVLAVDIPSGLDADT 146
|
170 180
....*....|....*....|..
gi 30695795 248 GDHEDGGIKPDMLVSLTAPKLC 269
Cdd:pfam03853 147 GAVLGTAVRADHTVTFGAPKPG 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
4-530 |
0e+00 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 1053.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 4 VIRRVTTMTFTFLLQSPPLPISP-SPPQFSLSSSPLSKTQRFITPSQG----SRLRTLCTKV-------------IIPNM 65
Cdd:PLN02918 1 NIKSTATMTFTFLLQSLLPLPISpPPPHSSSLSSSPSPTQRFLTPSQGsrlpPRRRALCTKSqdprwrramaslaVIPNM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 66 QDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHH 145
Cdd:PLN02918 81 QDSGSPPLSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARHLHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 146 FGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 225
Cdd:PLN02918 161 FGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 226 QTLqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSM 305
Cdd:PLN02918 241 QTL-KHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 306 CVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENG 385
Cdd:PLN02918 320 CVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDKNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 386 FVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYD 465
Cdd:PLN02918 400 FVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695795 466 EYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN02918 480 EYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
60-530 |
0e+00 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 854.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 60 VIIPNMQDSGSppLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVA 139
Cdd:PLN03049 1 VAVQHLHNPDS--ISYLSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEYRRVLALCGPGNNGGDGLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 140 ARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLV 219
Cdd:PLN03049 79 ARHLHHFGYKPSICYPKRTDKPLYNGLVTQLESLSVPFLSVEDLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 220 SLQNyeqtlqkHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPS 299
Cdd:PLN03049 159 RAAG-------PPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKLCAKMFKGPHHFLGGRFVPPAIVEKFKLHLPP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 300 YPGTSMCVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLK 379
Cdd:PLN03049 232 YPGTSMCVRIGKTPSVDIAALRENYVGPELLEEQVNADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 380 GFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPG 459
Cdd:PLN03049 312 GVDKRGFVWYTNYDSRKAHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPG 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695795 460 RHVLYDEYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP 530
Cdd:PLN03049 392 RHILDQSYKELEAKYADSSAIPKPKHWGGYRLKPELIEFWQGRESRLHDRLQYTREEINGKSVWKIDRLAP 462
|
|
| PdxH |
COG0259 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ... |
316-530 |
9.74e-114 |
|
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440029 Cd Length: 212 Bit Score: 335.62 E-value: 9.74e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 316 DISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESK 395
Cdd:COG0259 3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 396 KGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYS 475
Cdd:COG0259 83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30695795 476 DGSViPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNgnpaWKIHRLAP 530
Cdd:COG0259 163 GGDV-PRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTREDGG----WTIERLAP 212
|
|
| pdxH |
TIGR00558 |
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ... |
337-530 |
2.02e-113 |
|
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273138 Cd Length: 190 Bit Score: 334.08 E-value: 2.02e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:TIGR00558 1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSViPKPKNWGGFRLKPNLF 496
Cdd:TIGR00558 81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPDGEV-PRPEFWGGYRVVPDEI 159
|
170 180 190
....*....|....*....|....*....|....
gi 30695795 497 EFWQGQPSRLHDRLQYSLQDVNGnpaWKIHRLAP 530
Cdd:TIGR00558 160 EFWQGRPSRLHDRFRYRRDGDGS---WRIERLAP 190
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
65-309 |
2.36e-113 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 336.08 E-value: 2.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 65 MQDSGsppLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYK-------PEEYSRVLAICGPGNNGGDGL 137
Cdd:PLN03050 1 MSNIQ---TGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADgekasnpPGRHPRVLLVCGPGNNGGDGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 138 VAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSV----EDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDD 213
Cdd:PLN03050 78 VAARHLAHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAiggtNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 214 LIRRLVSLQNyeqtlqKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGpHHFLGGRFVPPSVAEKY 293
Cdd:PLN03050 158 LLAQMVQQQK------SPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEG-RHFVGGRFLPPAIAEKY 230
|
250
....*....|....*.
gi 30695795 294 KLELPSYPGTSMCVRI 309
Cdd:PLN03050 231 GLQKPPYPGVSQVMEV 246
|
|
| PRK05679 |
PRK05679 |
pyridoxal 5'-phosphate synthase; |
331-530 |
2.49e-98 |
|
pyridoxal 5'-phosphate synthase;
Pssm-ID: 235555 Cd Length: 195 Bit Score: 295.59 E-value: 2.49e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 331 EEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLF 410
Cdd:PRK05679 1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 411 YWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSViPKPKNWGGFR 490
Cdd:PRK05679 81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFAQGEV-PRPPHWGGYR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30695795 491 LKPNLFEFWQGQPSRLHDRLQYSLQDvngnPAWKIHRLAP 530
Cdd:PRK05679 160 VVPESIEFWQGRPSRLHDRILYRRDD----GGWKIERLAP 195
|
|
| phena_PhzG |
NF038138 |
phenazine biosynthesis FMN-dependent oxidase PhzG; |
337-530 |
3.42e-52 |
|
phenazine biosynthesis FMN-dependent oxidase PhzG;
Pssm-ID: 468380 Cd Length: 205 Bit Score: 176.40 E-value: 3.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 337 DPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILN 416
Cdd:NF038138 19 EPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWASGVLYWRETS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 417 RQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQysdGSVIPKPKNWGGFRLKPNLF 496
Cdd:NF038138 99 QQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAEA---GGPLPRPARFVGYRLVPEEV 175
|
170 180 190
....*....|....*....|....*....|....
gi 30695795 497 EFWQGQPSRLHDRLQYslqDVNGnPAWKIHRLAP 530
Cdd:NF038138 176 EFWAAGPDRLHRRLRY---DRDG-DGWTHVRLQP 205
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
81-287 |
5.22e-45 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 157.19 E-value: 5.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 81 AAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEysRVLAICGPGNNGGDGLVAARHLHhfGYKPFICYPKRTAK 160
Cdd:TIGR00197 8 DMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAG--HVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLLKKEKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 161 -PLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIrrlvslqnyeQTLQKHPV-IVSVD 238
Cdd:TIGR00197 84 iECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIV----------ESINELPApIVSVD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30695795 239 IPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPH---HFLGGRFVPP 287
Cdd:TIGR00197 154 IPSGLDVDTGAIEGPAVNADLTITFHAIKPCLLSDRADVtgeLKVGGIGIPP 205
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
97-269 |
1.99e-41 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 146.60 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 97 DQLMELAGLSVAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARHLHHFGYK--PFICYPkrtaKPLYTGLV-TQLDSL 173
Cdd:pfam03853 2 AVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGP----EEKLSEDArRQLDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 174 S------VPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLvslqnyeqtLQKHPVIVSVDIPSGWHVEE 247
Cdd:pfam03853 77 KklggkiVTDNPDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALIEWI---------NQSGAPVLAVDIPSGLDADT 146
|
170 180
....*....|....*....|..
gi 30695795 248 GDHEDGGIKPDMLVSLTAPKLC 269
Cdd:pfam03853 147 GAVLGTAVRADHTVTFGAPKPG 168
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
76-281 |
2.20e-41 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 155.41 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 76 LTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYkPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYP 155
Cdd:COG0062 4 LTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRF-PSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 156 KRTAKplYTGL----VTQLDSLSVPFVSVEDLPDDLSkDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYeqtlqkh 231
Cdd:COG0062 83 GDPEK--LSGDaaanLERLKAAGIPILELDDELPELA-EADLIVDALFGTGLSRPLRGPYAELIEAINASGAP------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 30695795 232 pvIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCakrfrgphHFLG 281
Cdd:COG0062 153 --VLAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPG--------LLLG 192
|
|
| Putative_PNPOx |
pfam01243 |
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ... |
346-432 |
7.10e-26 |
|
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Swiss:Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.
Pssm-ID: 426149 [Multi-domain] Cd Length: 88 Bit Score: 101.17 E-value: 7.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 346 FDEAVAAGLRETNAMALSTANKDKKPSSRMVLLK-GFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGP 424
Cdd:pfam01243 1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLKyGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80
|
....*...
gi 30695795 425 VERIPESE 432
Cdd:pfam01243 81 AEIVTDGE 88
|
|
| PNP_phzG_C |
pfam10590 |
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ... |
486-530 |
9.01e-21 |
|
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of the two dimerization regions of the protein, located at the edge of the dimer interface, at the C-terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In Swiss:P21159, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule.To date, the only time functional oxidase or phenazine biosynthesis activities have been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. It is unknown the role performed by each domain in bringing about molecular functions of either oxidase or phenazine activity.
Pssm-ID: 463161 Cd Length: 42 Bit Score: 85.25 E-value: 9.01e-21
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 30695795 486 WGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDvngNPAWKIHRLAP 530
Cdd:pfam10590 1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTREG---DGGWTIERLAP 42
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
72-267 |
8.30e-12 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 67.39 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 72 PLSYLTQREAAEIDEtlmgpLGFSIDQLMELAGLSvAASIAEVYKPEEySRVLAICGPGNNGGDGLVAARhlhhfgykpf 151
Cdd:PRK10565 19 PADDIRRGEREAADA-----LGLTLYELMLRAGEA-AFQVARSAYPDA-RHWLVLCGHGNNGGDGYVVAR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 152 icypkrtakplytglVTQLDSLSVPFVSVED---LPDD---------------------LSKDFDVIVDAMFGFSFHGAP 207
Cdd:PRK10565 82 ---------------LAQAAGIDVTLLAQESdkpLPEEaalareawlnaggeihaadivWPESVDLIVDALLGTGLRQAP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695795 208 RPPFDDLIRRlvslqnyeqtLQKHPV-IVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPK 267
Cdd:PRK10565 147 REPYAALIDQ----------ANAHPApVVALDIPSGLLAETGATPGAVINADHTVTFIALK 197
|
|
| YzzA |
COG3871 |
General stress protein 26 (function unknown) [Function unknown]; |
348-428 |
8.31e-04 |
|
General stress protein 26 (function unknown) [Function unknown];
Pssm-ID: 443080 [Multi-domain] Cd Length: 132 Bit Score: 39.53 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695795 348 EAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWF-TNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVE 426
Cdd:COG3871 9 EKLWELLEDIRTAMLATVDADGRPHSRPMWFQVDVDDGTLWFfTSRDSAKVRNIRRDPRVSLSFADPGDDRYVSVEGTAE 88
|
..
gi 30695795 427 RI 428
Cdd:COG3871 89 IV 90
|
|
| |
