|
Name |
Accession |
Description |
Interval |
E-value |
| YcbX |
COG3217 |
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ... |
1-264 |
2.69e-111 |
|
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];
Pssm-ID: 442450 [Multi-domain] Cd Length: 240 Bit Score: 324.45 E-value: 2.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 1 MATLTRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPVHDG-LHLTAPDSSSAYVR 79
Cdd:COG3217 1 MGRVSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGgLTLTAPGGESLTVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 80 FADfatqdaptevwgthftarIAPEAINKWLSGFFSREVQLRWVGPQMTRrvkrhnTVPLSFADGYPYLLANEASLRDLQ 159
Cdd:COG3217 81 LDD------------------DAGDAAAAWLSEYLGRPVRLVRLPPESRR------GPPVGFADGYPVLLISTASLADLN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 160 QRCPASVKMEQFRPNLVVSGASAWEEDSW--KVIRIGDVVFDVVKPCSRCIFTTVSPEKGQKHPagEPLKTLQSFRtaQD 237
Cdd:COG3217 137 ARLGAPVDMRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETGERDP--EPLRTLARYR--GA 212
|
250 260
....*....|....*....|....*..
gi 15830285 238 NGDVDFGQNLIARNSGVIRVGDEVEIL 264
Cdd:COG3217 213 DGHVDFGVNAIVLEGGTIRVGDEVEVL 239
|
|
| MOSC_N |
pfam03476 |
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The ... |
1-117 |
2.50e-45 |
|
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The function of this domain is unknown, however it is predicted to adopt a beta barrel fold.
Pssm-ID: 281474 Cd Length: 118 Bit Score: 151.36 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 1 MATLTRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPS-PVHDGLHLTAPDSSSAYVR 79
Cdd:pfam03476 1 MARVSSLYVYPIKSCRGESLSRAELTAAGLAWDRRFMVVDSDGKFVTARREPRLVLIRTTlDEDGGLTLTAPGMPDLSVP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15830285 80 FADFATQDAPTEVWGTHFTARIAPEAINKWLSGFFSRE 117
Cdd:pfam03476 81 LADNKFDLRGVLVWGLSFSGRDCGDAAADWFSDFLGKP 118
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
4-261 |
1.60e-29 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 119.97 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 4 LTRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPS-PVHDG-LHLTAPD-SSSAYVRF 80
Cdd:PLN02724 520 LKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGEILTQKKVPEMCLITTFiDLESGkLVVRAPRcDHKLEIPL 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 81 AD--FATQDAPTEVWGTHFTARIAPEAINKWLSGFFSREVQLRWVGPQMTRRVKRHNTVP---------LSFADGYPYLL 149
Cdd:PLN02724 600 ESdsQHEESGEVILCGNRAESMSYGTEINEWFTNALGRRCTLVRKSSSNTRVCRNRNPSHspcgddesrLSFANEGQFLL 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 150 ANEASLRDLQQRC-----PASVKME--QFRPNLVVSGASAWEEDSWKVIRIGDVVFDVVKPCSRCIFTTVSPEKGQKHPA 222
Cdd:PLN02724 680 ISEASVEDLNRRLatgqeDAKIRLDptRFRPNLVVSGGEAYAEDEWQSLSIGDAEFTVLGGCNRCQMINIDQETGLVNPS 759
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15830285 223 GEPLKTLQSFRTAQdnGDVDFG----QNLIARNSGVIRVGDEV 261
Cdd:PLN02724 760 NEPLATLASYRRVK--GKILFGillrYEISDKRDQWIAVGSRV 800
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
289-367 |
2.46e-20 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 84.13 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 289 ANVDIDWQGQAFRGNNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGD----DGTILCCSCVPKTA 364
Cdd:COG0633 2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDeeraAGSRLACQARPTSD 81
|
...
gi 15830285 365 LKL 367
Cdd:COG0633 82 LVV 84
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
290-367 |
4.46e-17 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 75.12 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 290 NVDIDWQGQAFRGNNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSCVPKTAL 365
Cdd:cd00207 2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEeaegGYVLACQTRVTDGL 81
|
..
gi 15830285 366 KL 367
Cdd:cd00207 82 VI 83
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
291-362 |
3.84e-14 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 66.78 E-value: 3.84e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830285 291 VDIDWQGQAFRGN-NQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEV----TPLKKSAMGDDGTILCCSCVPK 362
Cdd:pfam00111 1 VTINGKGVTIEVPdGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDqsdqSFLEDDELAAGYVVLACQTYPK 77
|
|
| PRK10713 |
PRK10713 |
2Fe-2S ferredoxin-like protein; |
308-367 |
5.98e-13 |
|
2Fe-2S ferredoxin-like protein;
Pssm-ID: 182668 [Multi-domain] Cd Length: 84 Bit Score: 63.98 E-value: 5.98e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830285 308 LLEQLENQGIRIPYSCRAGICGSCRVQLLEGEV----TPLkksAMGDDGTILCCSCVPKTALKL 367
Cdd:PRK10713 22 LLAALESHNVAVEYQCREGYCGSCRTRLVAGQVdwiaEPL---AFIQPGEILPCCCRAKGDIEI 82
|
|
| fdx_plant |
TIGR02008 |
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ... |
306-367 |
5.47e-09 |
|
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.
Pssm-ID: 273926 [Multi-domain] Cd Length: 97 Bit Score: 52.84 E-value: 5.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830285 306 QVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSCVPKTALKL 367
Cdd:TIGR02008 23 QYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDqmeaGYVLTCVAYPTSDCTI 88
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YcbX |
COG3217 |
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ... |
1-264 |
2.69e-111 |
|
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];
Pssm-ID: 442450 [Multi-domain] Cd Length: 240 Bit Score: 324.45 E-value: 2.69e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 1 MATLTRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPVHDG-LHLTAPDSSSAYVR 79
Cdd:COG3217 1 MGRVSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGgLTLTAPGGESLTVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 80 FADfatqdaptevwgthftarIAPEAINKWLSGFFSREVQLRWVGPQMTRrvkrhnTVPLSFADGYPYLLANEASLRDLQ 159
Cdd:COG3217 81 LDD------------------DAGDAAAAWLSEYLGRPVRLVRLPPESRR------GPPVGFADGYPVLLISTASLADLN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 160 QRCPASVKMEQFRPNLVVSGASAWEEDSW--KVIRIGDVVFDVVKPCSRCIFTTVSPEKGQKHPagEPLKTLQSFRtaQD 237
Cdd:COG3217 137 ARLGAPVDMRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETGERDP--EPLRTLARYR--GA 212
|
250 260
....*....|....*....|....*..
gi 15830285 238 NGDVDFGQNLIARNSGVIRVGDEVEIL 264
Cdd:COG3217 213 DGHVDFGVNAIVLEGGTIRVGDEVEVL 239
|
|
| MOSC_N |
pfam03476 |
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The ... |
1-117 |
2.50e-45 |
|
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The function of this domain is unknown, however it is predicted to adopt a beta barrel fold.
Pssm-ID: 281474 Cd Length: 118 Bit Score: 151.36 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 1 MATLTRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPS-PVHDGLHLTAPDSSSAYVR 79
Cdd:pfam03476 1 MARVSSLYVYPIKSCRGESLSRAELTAAGLAWDRRFMVVDSDGKFVTARREPRLVLIRTTlDEDGGLTLTAPGMPDLSVP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15830285 80 FADFATQDAPTEVWGTHFTARIAPEAINKWLSGFFSRE 117
Cdd:pfam03476 81 LADNKFDLRGVLVWGLSFSGRDCGDAAADWFSDFLGKP 118
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
4-261 |
1.60e-29 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 119.97 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 4 LTRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPS-PVHDG-LHLTAPD-SSSAYVRF 80
Cdd:PLN02724 520 LKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGEILTQKKVPEMCLITTFiDLESGkLVVRAPRcDHKLEIPL 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 81 AD--FATQDAPTEVWGTHFTARIAPEAINKWLSGFFSREVQLRWVGPQMTRRVKRHNTVP---------LSFADGYPYLL 149
Cdd:PLN02724 600 ESdsQHEESGEVILCGNRAESMSYGTEINEWFTNALGRRCTLVRKSSSNTRVCRNRNPSHspcgddesrLSFANEGQFLL 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 150 ANEASLRDLQQRC-----PASVKME--QFRPNLVVSGASAWEEDSWKVIRIGDVVFDVVKPCSRCIFTTVSPEKGQKHPA 222
Cdd:PLN02724 680 ISEASVEDLNRRLatgqeDAKIRLDptRFRPNLVVSGGEAYAEDEWQSLSIGDAEFTVLGGCNRCQMINIDQETGLVNPS 759
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15830285 223 GEPLKTLQSFRTAQdnGDVDFG----QNLIARNSGVIRVGDEV 261
Cdd:PLN02724 760 NEPLATLASYRRVK--GKILFGillrYEISDKRDQWIAVGSRV 800
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
289-367 |
2.46e-20 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 84.13 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 289 ANVDIDWQGQAFRGNNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGD----DGTILCCSCVPKTA 364
Cdd:COG0633 2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDeeraAGSRLACQARPTSD 81
|
...
gi 15830285 365 LKL 367
Cdd:COG0633 82 LVV 84
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
290-367 |
4.46e-17 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 75.12 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 290 NVDIDWQGQAFRGNNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSCVPKTAL 365
Cdd:cd00207 2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEeaegGYVLACQTRVTDGL 81
|
..
gi 15830285 366 KL 367
Cdd:cd00207 82 VI 83
|
|
| MOSC |
pfam03473 |
MOSC domain; The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich ... |
138-262 |
2.83e-16 |
|
MOSC domain; The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. These MOSC domains contain an absolutely conserved cysteine and occur either as stand-alone forms such as Swiss:P32157, or fused to other domains such as NifS-like catalytic domain in Molybdenum cofactor sulfurase. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters.
Pssm-ID: 460936 Cd Length: 116 Bit Score: 74.15 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 138 PLSFADGYPYLLANEASLRDLQQRCPAS-VKMEQFRPNLVVSGASaweedsWKVIRIGDVvFDVVKPCSRcifTTVSPek 216
Cdd:pfam03473 3 KHHGGDDKAVLLYSRESYDAWNAELGRGpLDPGRFRENLVVSGGT------WKEVCIGDR-FRIGGACLR---LEVTQ-- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15830285 217 gqkhpAGEPLKTLQSfRTAQDNGD------VDFGQNLIARNSGVIRVGDEVE 262
Cdd:pfam03473 71 -----PREPCKTLAK-RFGERRVDkrfkgsGRFGWYLRVLEEGTVRVGDEVE 116
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
291-362 |
3.84e-14 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 66.78 E-value: 3.84e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830285 291 VDIDWQGQAFRGN-NQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEV----TPLKKSAMGDDGTILCCSCVPK 362
Cdd:pfam00111 1 VTINGKGVTIEVPdGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDqsdqSFLEDDELAAGYVVLACQTYPK 77
|
|
| PRK10713 |
PRK10713 |
2Fe-2S ferredoxin-like protein; |
308-367 |
5.98e-13 |
|
2Fe-2S ferredoxin-like protein;
Pssm-ID: 182668 [Multi-domain] Cd Length: 84 Bit Score: 63.98 E-value: 5.98e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830285 308 LLEQLENQGIRIPYSCRAGICGSCRVQLLEGEV----TPLkksAMGDDGTILCCSCVPKTALKL 367
Cdd:PRK10713 22 LLAALESHNVAVEYQCREGYCGSCRTRLVAGQVdwiaEPL---AFIQPGEILPCCCRAKGDIEI 82
|
|
| PTZ00038 |
PTZ00038 |
ferredoxin; Provisional |
308-363 |
1.66e-11 |
|
ferredoxin; Provisional
Pssm-ID: 240237 [Multi-domain] Cd Length: 191 Bit Score: 62.55 E-value: 1.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 308 LLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSCVPKT 363
Cdd:PTZ00038 117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEqlkkGYCLLCTCYPKS 176
|
|
| petF |
CHL00134 |
ferredoxin; Validated |
303-363 |
5.31e-11 |
|
ferredoxin; Validated
Pssm-ID: 177056 [Multi-domain] Cd Length: 99 Bit Score: 58.96 E-value: 5.31e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830285 303 NNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSCVPKT 363
Cdd:CHL00134 22 PDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDqleaGFVLTCVAYPTS 86
|
|
| fdx_plant |
TIGR02008 |
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ... |
306-367 |
5.47e-09 |
|
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.
Pssm-ID: 273926 [Multi-domain] Cd Length: 97 Bit Score: 52.84 E-value: 5.47e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830285 306 QVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSCVPKTALKL 367
Cdd:TIGR02008 23 QYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDqmeaGYVLTCVAYPTSDCTI 88
|
|
| PRK07609 |
PRK07609 |
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated |
282-367 |
5.99e-09 |
|
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
Pssm-ID: 181058 [Multi-domain] Cd Length: 339 Bit Score: 56.80 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 282 NITQQPdanvdidwQGQAFRGNNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVT--PLKKSAMGDD----GTIL 355
Cdd:PRK07609 4 QVTLQP--------SGRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEqgPHQASALSGEeraaGEAL 75
|
90
....*....|..
gi 15830285 356 CCSCVPKTALKL 367
Cdd:PRK07609 76 TCCAKPLSDLVL 87
|
|
| PRK10684 |
PRK10684 |
HCP oxidoreductase, NADH-dependent; Provisional |
308-368 |
2.88e-07 |
|
HCP oxidoreductase, NADH-dependent; Provisional
Pssm-ID: 236735 [Multi-domain] Cd Length: 332 Bit Score: 51.63 E-value: 2.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830285 308 LLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGD----DGTILCCSCVPKTALKLA 368
Cdd:PRK10684 268 LLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPaeiaQGYVLACSCHPQGDLVLA 332
|
|
| PLN03136 |
PLN03136 |
Ferredoxin; Provisional |
308-363 |
4.82e-06 |
|
Ferredoxin; Provisional
Pssm-ID: 178681 [Multi-domain] Cd Length: 148 Bit Score: 45.90 E-value: 4.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 308 LLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGD----DGTILCCSCVPKT 363
Cdd:PLN03136 76 VLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDeqisEGYVLTCVAYPTS 135
|
|
| PRK05713 |
PRK05713 |
iron-sulfur-binding ferredoxin reductase; |
308-359 |
4.91e-06 |
|
iron-sulfur-binding ferredoxin reductase;
Pssm-ID: 235575 [Multi-domain] Cd Length: 312 Bit Score: 47.80 E-value: 4.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15830285 308 LLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDD----GTILCCSC 359
Cdd:PRK05713 19 LLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEkreqGWRLACQC 74
|
|
| YiiM |
COG2258 |
N-hydroxylaminopurine reductase YiiM, contains MOSC domain [Nucleotide transport and ... |
147-264 |
4.60e-04 |
|
N-hydroxylaminopurine reductase YiiM, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];
Pssm-ID: 441859 Cd Length: 162 Bit Score: 40.54 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830285 147 YLLANEaSLRDLQQRCPASVKMEQFRPNLVVSGasaWEEDSWKV---IRIGDVVFDVV---KPCSR-CIFTTVspekgqk 219
Cdd:COG2258 50 TLYAAE-HYDAWAAELGRDLPPGAFGENLTTEG---LDLSDLPIgdrLRIGEALLEVTqprKPCHKlEARLGG------- 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15830285 220 hpAGEPLKTLQSFRTaqdngdvdfGQNLIARNSGVIRVGDEVEIL 264
Cdd:COG2258 119 --PGLAKAMCQMGRG---------GIYARVLEGGEVRAGDEVELL 152
|
|
| COG3894 |
COG3894 |
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ... |
308-361 |
6.49e-04 |
|
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];
Pssm-ID: 443101 [Multi-domain] Cd Length: 621 Bit Score: 41.71 E-value: 6.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830285 308 LLEQLENQGIRIPYSCR-AGICGSCRVQLLEGEVTPLKKSAMG-------DDGTILCCSCVP 361
Cdd:COG3894 23 LLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEFSPVTEEERRllspeelAEGYRLACQARV 84
|
|
|