|
Name |
Accession |
Description |
Interval |
E-value |
| NorV |
COG0426 |
Flavorubredoxin [Energy production and conversion]; |
3-390 |
1.09e-172 |
|
Flavorubredoxin [Energy production and conversion];
Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 487.03 E-value: 1.09e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 3 HAVKVKPDVYWVGGIDWNERNFHG-YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVE 81
Cdd:COG0426 1 QAVEIAHGVYWVGVLDWDRRLFEGeYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 82 QDHSGAVPAISYLAPRAKIYASgPHGVNGLTAHYG--DRGYVPVKTGDTLRIGKRTLSFTQTMMVHWPDNMATYSEYDRI 159
Cdd:COG0426 81 PDHSGSLPELLELAPNAKIVCS-KKAARFLPHFYGipDFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 160 LFSNDAFGQHFASSKHFDDEVGlPEVLAQAKKYYANIVMPYSRHVQKALKSFEGCEVDMIAPSHGVIWRSHVAEILGEYG 239
Cdd:COG0426 160 LFSGDAFGSHGASDELFDDEVD-EHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 240 RWSSLAPDDSAIVVYDSMWHTTEDMALEIVEAFIECGVPTRLFDLKANHISDIMTDLLSAKFVAVGSPTLNNGMMPTVAA 319
Cdd:COG0426 239 KWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIAD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664115 320 FLCYLKGLSPKagweGRVGIPFGSYGWGTNGPDEVAAALEACGFDLPLGTLSHQWIEDEDHLARLQETIKQ 390
Cdd:COG0426 319 LLGYLKGLAPK----NKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFEPLRVKFKPTEEDLKKCEELGTD 385
|
|
| PRK11921 |
PRK11921 |
anaerobic nitric oxide reductase flavorubredoxin; |
5-386 |
2.99e-126 |
|
anaerobic nitric oxide reductase flavorubredoxin;
Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 369.41 E-value: 2.99e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 5 VKVKPDVYWVGGIDWNERNFHG--YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVEQ 82
Cdd:PRK11921 1 FKINDNVTWVGKIDWELRKFHGeeYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 83 DHSGAVPAISYLAPRAKIYASGpHGVNGLTAHY-GDRGYVPVKTGDTLRIGKRTLSFTQTMMVHWPDNMATYSEYDRILF 161
Cdd:PRK11921 81 DHSGALPELMKEIPDTPIYCTK-NGAKSLKGHYhQDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 162 SNDAFGQHFASSKHFDDEVGLPEVLAQAKKYYANIVMPYSRHVQKALKSFEGCE--VDMIAPSHGVIWRSHVAEILGEYG 239
Cdd:PRK11921 160 SNDAFGQHYASELMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEILSLNlpVDMICPSHGVIWRDNPLQIVEKYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 240 RWSSLAPDDSAIVVYDSMWHTTEDMALEIVEAFIEC--GVPTRLFDLKANHISDIMTDLLSAKFVAVGSPTLNNGMMPTV 317
Cdd:PRK11921 240 EWAANYQENQVTILYDTMWNSTRRMAEAIAEGIKKAnkDVTVKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGILSST 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664115 318 AAFLCYLKGLspkaGWEGRVGIPFGSYGWGTNGPDEVAAALEACGFDLPLGTLSHQWIEDEDHLARLQE 386
Cdd:PRK11921 320 AAILEEIKGL----GFKNKKAAAFGSYGWSGESVKIITERLKKAGFEIVNDGIRELWNPDDEALDRCRS 384
|
|
| flavodiiron_proteins_MBL-fold |
cd07709 |
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
5-242 |
2.44e-107 |
|
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.
Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 315.20 E-value: 2.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 5 VKVKPDVYWVGGIDWNERNFHG-YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVEQD 83
Cdd:cd07709 1 VEIADDIYWVGVNDWDLRLFEGeYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 84 HSGAVPAISYLAPRAKIYASGPhGVNGLTAHYGDRG--YVPVKTGDTLRIGKRTLSFTQTMMVHWPDNMATYSEYDRILF 161
Cdd:cd07709 81 HSGSLPELLELAPNAKIVCSKK-AARFLKHFYPGIDerFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 162 SNDAFGQHFASSKHFDDEVGlpEVLAQAKKYYANIVMPYSRHVQKALKSFEGCEVDMIAPSHGVIWRSHVAEILGEYGRW 241
Cdd:cd07709 160 SGDAFGAHGASGELFDDEVE--DYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLYRDW 237
|
.
gi 496664115 242 S 242
Cdd:cd07709 238 S 238
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
36-177 |
1.86e-15 |
|
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 73.74 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 36 NAYLIMDE-QVTLIDTcKPAFAGELIERISEVVDPAcIEHVIVNHVEQDHSGAVPAISYlAPRAKIYAS----------G 104
Cdd:smart00849 1 NSYLVRDDgGAILIDT-GPGEAEDLLAELKKLGPKK-IDAIILTHGHPDHIGGLPELLE-APGAPVYAPegtaellkdlL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664115 105 PHGVNGLTAHYGDRGYVPVKTGDTLRIGKRTLSFTQTMMvHWPDNMATYSEYDRILFSNDAFGQHFASSKHFD 177
Cdd:smart00849 78 ALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVD 149
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
252-387 |
6.70e-09 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 53.91 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 252 VVYDSMWHTTEDMALEIVEAFIECGVPTRLFDLKanHISDIMTDLLSAKFVAVGSPTLNNGMMPTVAAFLCYLKGL--SP 329
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLD--DVDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLfgTL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664115 330 KAGWEGRVGIP---FGSYGWGT--NGPDEVAAALEACGFD--LPLGTLshqwieDEDHLARLQET 387
Cdd:pfam00258 79 EDGDLSGLKYAvfgLGDSGYEGfcGAAKKLDEKLSELGASrvGPLGEG------DEDPQEDGLEE 137
|
|
| flav_short |
TIGR01753 |
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
250-390 |
6.03e-08 |
|
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]
Pssm-ID: 273789 [Multi-domain] Cd Length: 140 Bit Score: 51.18 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 250 AIVVYDSMWHTTEDMALEIVEAFIECGVPTRLFDlkANHISDimTDLLSAKFVAVGSPTLNNGMMPTvAAFLCYLKGLSp 329
Cdd:TIGR01753 1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLE--VADADA--EDLLSYDAVLLGCSTWGDEDLEQ-DDFEPFFEELE- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664115 330 KAGWEGRVGIPFGSYGWGTNG---PDEVAAALEACGFDLPLGTLSHQWIEDEDHLARLQETIKQ 390
Cdd:TIGR01753 75 DIDLGGKKVALFGSGDWGYEFceaVDDWEERLKEAGATIIAEGLKVDGDPEEEDLDKCREFAKD 138
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NorV |
COG0426 |
Flavorubredoxin [Energy production and conversion]; |
3-390 |
1.09e-172 |
|
Flavorubredoxin [Energy production and conversion];
Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 487.03 E-value: 1.09e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 3 HAVKVKPDVYWVGGIDWNERNFHG-YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVE 81
Cdd:COG0426 1 QAVEIAHGVYWVGVLDWDRRLFEGeYPTPRGTTYNSYLIVDEKTALIDTVGESFFEEFLENLSKVIDPKKIDYIIVNHQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 82 QDHSGAVPAISYLAPRAKIYASgPHGVNGLTAHYG--DRGYVPVKTGDTLRIGKRTLSFTQTMMVHWPDNMATYSEYDRI 159
Cdd:COG0426 81 PDHSGSLPELLELAPNAKIVCS-KKAARFLPHFYGipDFRFIVVKEGDTLDLGGHTLQFIPAPMLHWPDTMFTYDPEDKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 160 LFSNDAFGQHFASSKHFDDEVGlPEVLAQAKKYYANIVMPYSRHVQKALKSFEGCEVDMIAPSHGVIWRSHVAEILGEYG 239
Cdd:COG0426 160 LFSGDAFGSHGASDELFDDEVD-EHLEEEARRYYANIMMPFSKQVLKALKKVRGLDIDMIAPSHGPIWRGNPKEILDWYR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 240 RWSSLAPDDSAIVVYDSMWHTTEDMALEIVEAFIECGVPTRLFDLKANHISDIMTDLLSAKFVAVGSPTLNNGMMPTVAA 319
Cdd:COG0426 239 KWSSYQPEKKVVIVYASMYGNTEKMAEAIAEGLTEEGVKVKLYDLEKTDPSEIITEIFDAKGIVIGSPTYNGGAFPPIAD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664115 320 FLCYLKGLSPKagweGRVGIPFGSYGWGTNGPDEVAAALEACGFDLPLGTLSHQWIEDEDHLARLQETIKQ 390
Cdd:COG0426 319 LLGYLKGLAPK----NKLAGAFGSYGWSGEAVKLLEEKLEDAGFEVVFEPLRVKFKPTEEDLKKCEELGTD 385
|
|
| PRK11921 |
PRK11921 |
anaerobic nitric oxide reductase flavorubredoxin; |
5-386 |
2.99e-126 |
|
anaerobic nitric oxide reductase flavorubredoxin;
Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 369.41 E-value: 2.99e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 5 VKVKPDVYWVGGIDWNERNFHG--YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVEQ 82
Cdd:PRK11921 1 FKINDNVTWVGKIDWELRKFHGeeYSTHRGSSYNSYLIKDEKTVLIDTVWQPFAKEFVENLKKEIDLDKIDYIVANHGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 83 DHSGAVPAISYLAPRAKIYASGpHGVNGLTAHY-GDRGYVPVKTGDTLRIGKRTLSFTQTMMVHWPDNMATYSEYDRILF 161
Cdd:PRK11921 81 DHSGALPELMKEIPDTPIYCTK-NGAKSLKGHYhQDWNFVVVKTGDRLEIGSNELIFIEAPMLHWPDSMFTYLTGDNILF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 162 SNDAFGQHFASSKHFDDEVGLPEVLAQAKKYYANIVMPYSRHVQKALKSFEGCE--VDMIAPSHGVIWRSHVAEILGEYG 239
Cdd:PRK11921 160 SNDAFGQHYASELMYNDLVDQGELYQEAIKYYANILTPFSPLVIKKIEEILSLNlpVDMICPSHGVIWRDNPLQIVEKYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 240 RWSSLAPDDSAIVVYDSMWHTTEDMALEIVEAFIEC--GVPTRLFDLKANHISDIMTDLLSAKFVAVGSPTLNNGMMPTV 317
Cdd:PRK11921 240 EWAANYQENQVTILYDTMWNSTRRMAEAIAEGIKKAnkDVTVKLYNSAKSDKNDIITEVFKSKAILVGSSTINRGILSST 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664115 318 AAFLCYLKGLspkaGWEGRVGIPFGSYGWGTNGPDEVAAALEACGFDLPLGTLSHQWIEDEDHLARLQE 386
Cdd:PRK11921 320 AAILEEIKGL----GFKNKKAAAFGSYGWSGESVKIITERLKKAGFEIVNDGIRELWNPDDEALDRCRS 384
|
|
| flavodiiron_proteins_MBL-fold |
cd07709 |
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
5-242 |
2.44e-107 |
|
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.
Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 315.20 E-value: 2.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 5 VKVKPDVYWVGGIDWNERNFHG-YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVEQD 83
Cdd:cd07709 1 VEIADDIYWVGVNDWDLRLFEGeYPTPRGTSYNSYLIKDEKTALIDTVKEPFFDEFLENLEEVIDPRKIDYIVVNHQEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 84 HSGAVPAISYLAPRAKIYASGPhGVNGLTAHYGDRG--YVPVKTGDTLRIGKRTLSFTQTMMVHWPDNMATYSEYDRILF 161
Cdd:cd07709 81 HSGSLPELLELAPNAKIVCSKK-AARFLKHFYPGIDerFVVVKDGDTLDLGKHTLKFIPAPMLHWPDTMVTYDPEDKILF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 162 SNDAFGQHFASSKHFDDEVGlpEVLAQAKKYYANIVMPYSRHVQKALKSFEGCEVDMIAPSHGVIWRSHVAEILGEYGRW 241
Cdd:cd07709 160 SGDAFGAHGASGELFDDEVE--DYLEEARRYYANIMGPFSKQVRKALEKLEALDIKMIAPSHGPIWRKDPGEIIDLYRDW 237
|
.
gi 496664115 242 S 242
Cdd:cd07709 238 S 238
|
|
| PRK05452 |
PRK05452 |
anaerobic nitric oxide reductase flavorubredoxin; Provisional |
4-386 |
2.07e-101 |
|
anaerobic nitric oxide reductase flavorubredoxin; Provisional
Pssm-ID: 235475 [Multi-domain] Cd Length: 479 Bit Score: 309.00 E-value: 2.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 4 AVKVKPDVYWVGGIDWNERNFHG--YTTDRGSTYNAYLIMDEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVE 81
Cdd:PRK05452 2 SIHVKNNIHWVGQRDWEVRDFHGteYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 82 QDHSGAVPAISYLAPRAKIYASgPHGVNGLTAHY--GDRGYVPVKTGDTLRIGK-RTLSFTQTMMVHWPDNMATYSEYDR 158
Cdd:PRK05452 82 EDHAGALTELMAQIPDTPIYCT-ANAIDSINGHHhhPEWNFNVVKTGDTLDIGNgKQLIFVETPMLHWPDSMMTYLTGDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 159 ILFSNDAFGQHFASSKHFDDEVGLPEVLAQAKKYYANIVMPYSRHVQKALK---SFeGCEVDMIAPSHGVIWRSHVAEIL 235
Cdd:PRK05452 161 VLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITeilGF-NLPVDMIATSHGVVWRDNPTQIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 236 GEYGRWSSLAPDDSAIVVYDSMWHTTEDMALEIVEAF--IECGVPTRLFDLKANHISDIMTDLLSAKFVAVGSPTLNNGM 313
Cdd:PRK05452 240 ELYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIaeVDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGSSTMNNVM 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664115 314 MPTVAAFLCYLKGLSpkagWEGRVGIPFGSYGWGTNGPDEVAAALEACGFDLPLGtLSHQWIEDEDHLARLQE 386
Cdd:PRK05452 320 MPKIAGLLEEITGLR----FRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLS-LKAKWRPDQDALELCRE 387
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
36-177 |
1.86e-15 |
|
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 73.74 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 36 NAYLIMDE-QVTLIDTcKPAFAGELIERISEVVDPAcIEHVIVNHVEQDHSGAVPAISYlAPRAKIYAS----------G 104
Cdd:smart00849 1 NSYLVRDDgGAILIDT-GPGEAEDLLAELKKLGPKK-IDAIILTHGHPDHIGGLPELLE-APGAPVYAPegtaellkdlL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496664115 105 PHGVNGLTAHYGDRGYVPVKTGDTLRIGKRTLSFTQTMMvHWPDNMATYSEYDRILFSNDAFGQHFASSKHFD 177
Cdd:smart00849 78 ALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPG-HTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVD 149
|
|
| ST1585-like_MBL-fold |
cd07726 |
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ... |
17-167 |
6.14e-10 |
|
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293812 [Multi-domain] Cd Length: 215 Bit Score: 58.66 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 17 IDWNERNFHGYTTdrgstynAYLIMDE-QVTLIDTCkPAFAGELIERISEV--VDPACIEHVIVNHVEQDHSGAVPAISY 93
Cdd:cd07726 5 IDLGFLGFPGRIA-------SYLLDGEgRPALIDTG-PSSSVPRLLAALEAlgIAPEDVDYIILTHIHLDHAGGAGLLAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 94 LAPRAKIYA--SG-PHGVN------GLTAHYGDR----GY----------VPVKTGDTLRIGKRTLSFTQTMMvHWPDNM 150
Cdd:cd07726 77 ALPNAKVYVhpRGaRHLIDpsklwaSARAVYGDEadrlGGeilpvpeervIVLEDGETLDLGGRTLEVIDTPG-HAPHHL 155
|
170
....*....|....*..
gi 496664115 151 ATYSEYDRILFSNDAFG 167
Cdd:cd07726 156 SFLDEESDGLFTGDAAG 172
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
252-387 |
6.70e-09 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 53.91 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 252 VVYDSMWHTTEDMALEIVEAFIECGVPTRLFDLKanHISDIMTDLLSAKFVAVGSPTLNNGMMPTVAAFLCYLKGL--SP 329
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLD--DVDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLfgTL 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496664115 330 KAGWEGRVGIP---FGSYGWGT--NGPDEVAAALEACGFD--LPLGTLshqwieDEDHLARLQET 387
Cdd:pfam00258 79 EDGDLSGLKYAvfgLGDSGYEGfcGAAKKLDEKLSELGASrvGPLGEG------DEDPQEDGLEE 137
|
|
| flav_short |
TIGR01753 |
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
250-390 |
6.03e-08 |
|
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport]
Pssm-ID: 273789 [Multi-domain] Cd Length: 140 Bit Score: 51.18 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 250 AIVVYDSMWHTTEDMALEIVEAFIECGVPTRLFDlkANHISDimTDLLSAKFVAVGSPTLNNGMMPTvAAFLCYLKGLSp 329
Cdd:TIGR01753 1 ILIVYASMTGNTEEMANIIAEGLKEAGAEVDLLE--VADADA--EDLLSYDAVLLGCSTWGDEDLEQ-DDFEPFFEELE- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496664115 330 KAGWEGRVGIPFGSYGWGTNG---PDEVAAALEACGFDLPLGTLSHQWIEDEDHLARLQETIKQ 390
Cdd:TIGR01753 75 DIDLGGKKVALFGSGDWGYEFceaVDDWEERLKEAGATIIAEGLKVDGDPEEEDLDKCREFAKD 138
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
250-390 |
1.13e-06 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 47.59 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 250 AIVVYDSMWHTTEDMALEIVEAFIECGVptRLFDLKANHISdimtDLLSAKFVAVGSPTLNNGMMPTVAAFLCYLKG-LS 328
Cdd:COG0716 1 ILIVYGSTTGNTEKVAEAIAEALGAAGV--DLFEIEDADLD----DLEDYDLLILGTPTWAGELPDDWEDFLEELKEdLS 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496664115 329 PKagwegRVGiPFGSYGWGTNGP--DEVAAALEACGFDLpLGTLSHQWI---EDEDHLARLQETIKQ 390
Cdd:COG0716 75 GK-----KVA-LFGTGDSSGYGDalGELKELLEEKGAKV-VGGYDFEGSkapDAEDTEERAEEWLKQ 134
|
|
| GloB |
COG0491 |
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ... |
24-178 |
1.56e-06 |
|
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
Pssm-ID: 440257 [Multi-domain] Cd Length: 215 Bit Score: 48.53 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 24 FHGYTTDRGSTYNAYLIMD-EQVTLIDT-CKPAFAGELIERISEVVDPacIEHVIVNHVEQDHSGAVPAISYlAPRAKIY 101
Cdd:COG0491 4 LPGGTPGAGLGVNSYLIVGgDGAVLIDTgLGPADAEALLAALAALGLD--IKAVLLTHLHPDHVGGLAALAE-AFGAPVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 102 ASgPHGVNGLT-----AHYGDRGYVP---VKTGDTLRIGKRTLsftQTMMV--HWPDNMATYSEYDRILFSNDAFGQHFA 171
Cdd:COG0491 81 AH-AAEAEALEapaagALFGREPVPPdrtLEDGDTLELGGPGL---EVIHTpgHTPGHVSFYVPDEKVLFTGDALFSGGV 156
|
....*..
gi 496664115 172 SSKHFDD 178
Cdd:COG0491 157 GRPDLPD 163
|
|
| yflN-like_MBL-fold |
cd07721 |
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ... |
36-166 |
2.31e-06 |
|
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293807 [Multi-domain] Cd Length: 202 Bit Score: 47.99 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 36 NAYLIMDE-QVTLIDTCKPAFAGELIERISEV-VDPACIEHVIVNHVEQDHSGAVPAISYlAPRAKIYAS---------- 103
Cdd:cd07721 12 NAYLIEDDdGLTLIDTGLPGSAKRILKALRELgLSPKDIRRILLTHGHIDHIGSLAALKE-APGAPVYAHereapylege 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496664115 104 -GPHGVNGLTAHYGDRGYVPVKTGDTLRI--GKRTLSFTQTMMV-----HWPDNMATYSEYDRILFSNDAF 166
Cdd:cd07721 91 kPYPPPVRLGLLGLLSPLLPVKPVPVDRTleDGDTLDLAGGLRVihtpgHTPGHISLYLEEDGVLIAGDAL 161
|
|
| metallo-hydrolase-like_MBL-fold |
cd06262 |
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ... |
36-164 |
2.95e-05 |
|
mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.
Pssm-ID: 293792 [Multi-domain] Cd Length: 188 Bit Score: 44.58 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 36 NAYLIMDE--QVTLIDTckpafAGELIERISEVVD--PACIEHVIVNHVEQDHSGAVPAISyLAPRAKIYAS-------- 103
Cdd:cd06262 11 NCYLVSDEegEAILIDP-----GAGALEKILEAIEelGLKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHeadaelle 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496664115 104 ---GPHGVNGLTAHYGDRGYVPVKTGDTLRIGKRTLSftqtmmV-----HWPDNMATYSEYDRILFSND 164
Cdd:cd06262 85 dpeLNLAFFGGGPLPPPEPDILLEDGDTIELGGLELE------VihtpgHTPGSVCFYIEEEGVLFTGD 147
|
|
| Lactamase_B |
pfam00753 |
Metallo-beta-lactamase superfamily; |
36-223 |
5.00e-05 |
|
Metallo-beta-lactamase superfamily;
Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 43.90 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 36 NAYLIM-DEQVTLIDTCKPAFAGELIERISEVVDPACIEHVIVNHVEQDHSGAVPAI------SYLAPRAKIYASGPHGV 108
Cdd:pfam00753 7 NSYLIEgGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaeatdvPVIVVAEEARELLDEEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 109 NGLTAHYGDRGYVPVKT--------GDTLRIGKRTLSFTQTMmVHWPDNMATYSEYDRILFSNDAFGQHfaSSKHFDDEV 180
Cdd:pfam00753 87 GLAASRLGLPGPPVVPLppdvvleeGDGILGGGLGLLVTHGP-GHGPGHVVVYYGGGKVLFTGDLLFAG--EIGRLDLPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 496664115 181 GLPEVLAqakkyyanivMPYSRHVQKALKSFEGCEVDMIAPSH 223
Cdd:pfam00753 164 GGLLVLH----------PSSAESSLESLLKLAKLKAAVIVPGH 196
|
|
| hydroxyacylglutathione_hydrolase_MBL-fold |
cd07723 |
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ... |
37-132 |
9.81e-05 |
|
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293809 [Multi-domain] Cd Length: 165 Bit Score: 42.45 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 37 AYLIMDE---QVTLIDtckPAFAGELIERISEvvDPACIEHVIVNHVEQDHSGAVPAISYLAPRAKIYASGPHGVNGLTa 113
Cdd:cd07723 11 IYLIVDEatgEAAVVD---PGEAEPVLAALEK--NGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIPGLD- 84
|
90
....*....|....*....
gi 496664115 114 hygdrgyVPVKTGDTLRIG 132
Cdd:cd07723 85 -------HPVKDGDEIKLG 96
|
|
| PRK05569 |
PRK05569 |
flavodoxin; Provisional |
252-350 |
9.68e-04 |
|
flavodoxin; Provisional
Pssm-ID: 135442 [Multi-domain] Cd Length: 141 Bit Score: 39.05 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 252 VVYDSMWHTTEDMALEIVEAFIECGVptrlfDLKANHISDI-MTDLLSAKFVAVGSPTLNNGMMPT--VAAFLCYLKGLS 328
Cdd:PRK05569 6 IIYWSCGGNVEVLANTIADGAKEAGA-----EVTIKHVADAkVEDVLEADAVAFGSPSMDNNNIEQeeMAPFLDQFKLTP 80
|
90 100
....*....|....*....|..
gi 496664115 329 PkagwEGRVGIPFGSYGWgTNG 350
Cdd:PRK05569 81 N----ENKKCILFGSYGW-DNG 97
|
|
| YSH1 |
COG1236 |
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ... |
24-105 |
2.11e-03 |
|
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440849 [Multi-domain] Cd Length: 404 Bit Score: 39.78 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496664115 24 FHGYTtdRGSTYNAYLI-MDEQVTLIDtCKPAFAGELIERISEVVDPACIEHVIVNHVEQDHSGAVPAISYLAPRAKIYA 102
Cdd:COG1236 5 FLGAA--GEVTGSCYLLeTGGTRILID-CGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFRGPIYA 81
|
...
gi 496664115 103 SGP 105
Cdd:COG1236 82 TPA 84
|
|
| |
