|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11709 |
PRK11709 |
putative L-ascorbate 6-phosphate lactonase; Provisional |
1-357 |
0e+00 |
|
putative L-ascorbate 6-phosphate lactonase; Provisional
Pssm-ID: 236958 Cd Length: 355 Bit Score: 693.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 1 MAKattIQEATRENWIQNTFPEWGTWLNEEIEQSKVPEKNFRMWWLANNGIWLKTHEDTNILVDLWNGTGKQTHGSGLMK 80
Cdd:PRK11709 1 MSK---VKEITRESWILSTFPEWGTWLNEEIEQEVVPPGTFAMWWLGCTGIWLKTEGGTNVCVDLWCGTGKQTHGNPLMK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 81 QGHQMMRMSGVQKMQPNLRLQPFVIDPYAVKNVDALLVTHIHSDHLDINTAAAVLQNSGPETKFIGPQAVVDIWKGWGVP 160
Cdd:PRK11709 78 RGHQMARMAGVRKLQPNLRTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQNCADHVKFIGPQACVDLWIGWGVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 161 EERTIVVHPGDEVTVKSVTIKALEAFDRTVLLTVDNDVTIKD-SLPQDMDEIAVNYLFKTSGGNLYHAADSHMSNMFAKH 239
Cdd:PRK11709 158 KERCIVVKPGDVVKVKDIKIHALDSFDRTALVTLPADGKAAGgVLPDDMDRRAVNYLFKTPGGNIYHSGDSHYSNYFAKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 240 GNENHVDVEIINYGENPRGITDKVTSIDVLRSAEDLKAKVVIPVHYDIWSNFDADPQEIVKLWEMKKDTLNYQFHPFVWR 319
Cdd:PRK11709 238 GNDHQIDVALGSYGENPRGITDKMTSIDILRMAESLNAKVVIPVHHDIWSNFQADPQEILVLWKMRKDRLQYGFHPFIWQ 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 1905566313 320 VGGSYTFPEDQNKIQYHYDRGFSDVFSKDNDVPFPSFL 357
Cdd:PRK11709 318 VGGKFTYPQDKDRFEYHYPRGFDDCFTIEPDLPFKSFL 355
|
|
| UlaG-like_MBL-fold |
cd16284 |
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase ... |
41-252 |
4.91e-86 |
|
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain; UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. 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.
Pssm-ID: 293842 Cd Length: 178 Bit Score: 257.39 E-value: 4.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 41 FRMWWLANNGIWLKTHEDTNILVDLWNgtgkqthgsglmkqghqmmrmsgvqkmqpnlrlqpFVIDPYAVKNVDALLVTH 120
Cdd:cd16284 2 FAMWWLGCTGIWLKSEGNTNICIDFWC-----------------------------------FVLDPFAIKQIDAVLATH 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 121 IHSDHLDINTAAAVLQNSGPETKFIGPQAVVDIWKGWGVPEERTIVVHPGDEVTVKSVTIKALEAFDRTVLLTVDNDVTI 200
Cdd:cd16284 47 DHNDHIDVNVAAAVLQNCAPDVPFIGPQACVDLWIGWGVPKERCIVVKPGDVVKIKDIEIHVLDSFDRTALVTLPADQKL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1905566313 201 KDSLPQDMDEIAVNYLFKTSGGNLYHAADSHMSNMFAKHGNENHVDVEIINY 252
Cdd:cd16284 127 AGKMPDDMDERAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNDHKIDVALGSY 178
|
|
| UlaG |
COG2220 |
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
40-297 |
5.66e-40 |
|
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];
Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 140.82 E-value: 5.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 40 NFRMWWLANNGIWLKThEDTNILVDLWNGtgkqthgsglmkqghqmmrmsgvqkmQPNLRLQPFVIDPYAVKNVDALLVT 119
Cdd:COG2220 3 GMKITWLGHATFLIET-GGKRILIDPVFS--------------------------GRASPVNPLPLDPEDLPKIDAVLVT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 120 HIHSDHLDINTAAAVLQNSgpeTKFIGPQAVVDIWKGWGVPeeRTIVVHPGDEVTVKSVTIKALEAFDRTvlltvdndvt 199
Cdd:COG2220 56 HDHYDHLDDATLRALKRTG---ATVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSS---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 200 ikdSLPQDMDEIAVNYLFKTSGGNLYHAADSHMSNMFAKHGNENHVDVEIINYGenprGITDKVTSIDVLRSAEDLKAKV 279
Cdd:COG2220 121 ---GRPDRNGGLWVGFVIETDGKTIYHAGDTGYFPEMKEIGERFPIDVALLPIG----AYPFTMGPEEAAEAARDLKPKV 193
|
250
....*....|....*...
gi 1905566313 280 VIPVHYDIWSNFDADPQE 297
Cdd:COG2220 194 VIPIHYGTFPLLDEDPLE 211
|
|
| Lactamase_B_2 |
pfam12706 |
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
113-285 |
5.95e-06 |
|
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.
Pssm-ID: 432732 [Multi-domain] Cd Length: 196 Bit Score: 46.53 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 113 VDALLVTHIHSDHL-DINTAAAvlqnsGPETKFIGPQAVVDIWKGWGVPE-------ERTIVVHPGDEVTVKSVTIKaLE 184
Cdd:pfam12706 29 IDAVLLTHDHYDHLaGLLDLRE-----GRPRPLYAPLGVLAHLRRNFPYLfllehygVRVHEIDWGESFTVGDGGLT-VT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 185 AFdrTVLLTVDNDVTIKDSLpqdmdeiAVNYLFKTSGGNLYHAADSHM--SNMFAKHGNenhVDVEIIN---YGENPRGI 259
Cdd:pfam12706 103 AT--PARHGSPRGLDPNPGD-------TLGFRIEGPGKRVYYAGDTGYfpDEIGERLGG---ADLLLLDggaWRDDEMIH 170
|
170 180
....*....|....*....|....*.
gi 1905566313 260 TDKVTSIDVLRSAEDLKAKVVIPVHY 285
Cdd:pfam12706 171 MGHMTPEEAVEAAADLGARRKVLIHI 196
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
110-185 |
1.41e-05 |
|
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: 44.85 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 110 VKNVDALLVTHIHSDHldINTAAAVLQNsgPETKFIGPQAVVDIWKG----------WGVPEERTIVVHPGDEVTVKSVT 179
Cdd:smart00849 33 PKKIDAIILTHGHPDH--IGGLPELLEA--PGAPVYAPEGTAELLKDllallgelgaEAEPAPPDRTLKDGDELDLGGGE 108
|
....*.
gi 1905566313 180 IKALEA 185
Cdd:smart00849 109 LEVIHT 114
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11709 |
PRK11709 |
putative L-ascorbate 6-phosphate lactonase; Provisional |
1-357 |
0e+00 |
|
putative L-ascorbate 6-phosphate lactonase; Provisional
Pssm-ID: 236958 Cd Length: 355 Bit Score: 693.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 1 MAKattIQEATRENWIQNTFPEWGTWLNEEIEQSKVPEKNFRMWWLANNGIWLKTHEDTNILVDLWNGTGKQTHGSGLMK 80
Cdd:PRK11709 1 MSK---VKEITRESWILSTFPEWGTWLNEEIEQEVVPPGTFAMWWLGCTGIWLKTEGGTNVCVDLWCGTGKQTHGNPLMK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 81 QGHQMMRMSGVQKMQPNLRLQPFVIDPYAVKNVDALLVTHIHSDHLDINTAAAVLQNSGPETKFIGPQAVVDIWKGWGVP 160
Cdd:PRK11709 78 RGHQMARMAGVRKLQPNLRTQPFVLDPFAIREIDAVLATHDHSDHIDVNVAAAVLQNCADHVKFIGPQACVDLWIGWGVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 161 EERTIVVHPGDEVTVKSVTIKALEAFDRTVLLTVDNDVTIKD-SLPQDMDEIAVNYLFKTSGGNLYHAADSHMSNMFAKH 239
Cdd:PRK11709 158 KERCIVVKPGDVVKVKDIKIHALDSFDRTALVTLPADGKAAGgVLPDDMDRRAVNYLFKTPGGNIYHSGDSHYSNYFAKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 240 GNENHVDVEIINYGENPRGITDKVTSIDVLRSAEDLKAKVVIPVHYDIWSNFDADPQEIVKLWEMKKDTLNYQFHPFVWR 319
Cdd:PRK11709 238 GNDHQIDVALGSYGENPRGITDKMTSIDILRMAESLNAKVVIPVHHDIWSNFQADPQEILVLWKMRKDRLQYGFHPFIWQ 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 1905566313 320 VGGSYTFPEDQNKIQYHYDRGFSDVFSKDNDVPFPSFL 357
Cdd:PRK11709 318 VGGKFTYPQDKDRFEYHYPRGFDDCFTIEPDLPFKSFL 355
|
|
| UlaG-like_MBL-fold |
cd16284 |
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase ... |
41-252 |
4.91e-86 |
|
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain; UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. 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.
Pssm-ID: 293842 Cd Length: 178 Bit Score: 257.39 E-value: 4.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 41 FRMWWLANNGIWLKTHEDTNILVDLWNgtgkqthgsglmkqghqmmrmsgvqkmqpnlrlqpFVIDPYAVKNVDALLVTH 120
Cdd:cd16284 2 FAMWWLGCTGIWLKSEGNTNICIDFWC-----------------------------------FVLDPFAIKQIDAVLATH 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 121 IHSDHLDINTAAAVLQNSGPETKFIGPQAVVDIWKGWGVPEERTIVVHPGDEVTVKSVTIKALEAFDRTVLLTVDNDVTI 200
Cdd:cd16284 47 DHNDHIDVNVAAAVLQNCAPDVPFIGPQACVDLWIGWGVPKERCIVVKPGDVVKIKDIEIHVLDSFDRTALVTLPADQKL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1905566313 201 KDSLPQDMDEIAVNYLFKTSGGNLYHAADSHMSNMFAKHGNENHVDVEIINY 252
Cdd:cd16284 127 AGKMPDDMDERAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNDHKIDVALGSY 178
|
|
| UlaG |
COG2220 |
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
40-297 |
5.66e-40 |
|
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];
Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 140.82 E-value: 5.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 40 NFRMWWLANNGIWLKThEDTNILVDLWNGtgkqthgsglmkqghqmmrmsgvqkmQPNLRLQPFVIDPYAVKNVDALLVT 119
Cdd:COG2220 3 GMKITWLGHATFLIET-GGKRILIDPVFS--------------------------GRASPVNPLPLDPEDLPKIDAVLVT 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 120 HIHSDHLDINTAAAVLQNSgpeTKFIGPQAVVDIWKGWGVPeeRTIVVHPGDEVTVKSVTIKALEAFDRTvlltvdndvt 199
Cdd:COG2220 56 HDHYDHLDDATLRALKRTG---ATVVAPLGVAAWLRAWGFP--RVTELDWGESVELGGLTVTAVPARHSS---------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 200 ikdSLPQDMDEIAVNYLFKTSGGNLYHAADSHMSNMFAKHGNENHVDVEIINYGenprGITDKVTSIDVLRSAEDLKAKV 279
Cdd:COG2220 121 ---GRPDRNGGLWVGFVIETDGKTIYHAGDTGYFPEMKEIGERFPIDVALLPIG----AYPFTMGPEEAAEAARDLKPKV 193
|
250
....*....|....*...
gi 1905566313 280 VIPVHYDIWSNFDADPQE 297
Cdd:COG2220 194 VIPIHYGTFPLLDEDPLE 211
|
|
| PRK00685 |
PRK00685 |
metal-dependent hydrolase; Provisional |
104-301 |
3.02e-10 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 234811 [Multi-domain] Cd Length: 228 Bit Score: 59.44 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 104 VIDPY-------AVK----NVDALLVTHIHSDHL-DintAAAVLQNSGpeTKFIGPQAVVDIWKGWGVpeERTIVVHPGD 171
Cdd:PRK00685 21 LIDPFitgnplaDLKpedvKVDYILLTHGHGDHLgD---TVEIAKRTG--ATVIANAELANYLSEKGV--EKTHPMNIGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 172 EVTVKSVTIKALEAFDRTVLLTVDNDVTIKDslpqdmdeiAVNYLFKTSGGNLYHAADSHM-SNMfAKHGNENHVDVEII 250
Cdd:PRK00685 94 TVEFDGGKVKLTPALHSSSFIDEDGITYLGN---------PTGFVITFEGKTIYHAGDTGLfSDM-KLIGELHKPDVALL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1905566313 251 NYGEN----PRgitdkvtsiDVLRSAEDLKAKVVIPVHYDIWSNFDADPQEIVKL 301
Cdd:PRK00685 164 PIGDNftmgPE---------DAALAVELIKPKIVIPMHYNTFPLIEQDPEKFKAL 209
|
|
| ElaC |
COG1234 |
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; |
47-185 |
7.11e-07 |
|
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440847 [Multi-domain] Cd Length: 250 Bit Score: 49.81 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 47 ANNGIWLKtHEDTNILVDLwngtgkqthGSGLMkqgHQMMRMSgvqkmqpnlrlqpfvIDPyavKNVDALLVTHIHSDH- 125
Cdd:COG1234 18 ATSSYLLE-AGGERLLIDC---------GEGTQ---RQLLRAG---------------LDP---RDIDAIFITHLHGDHi 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1905566313 126 LDINTAAAVLQNSGPETKF--IGPQAVVDIWK------GWGVPEE-RTIVVHPGDEVTVKSVTIKALEA 185
Cdd:COG1234 67 AGLPGLLSTRSLAGREKPLtiYGPPGTKEFLEallkasGTDLDFPlEFHEIEPGEVFEIGGFTVTAFPL 135
|
|
| Lactamase_B_2 |
pfam12706 |
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
113-285 |
5.95e-06 |
|
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.
Pssm-ID: 432732 [Multi-domain] Cd Length: 196 Bit Score: 46.53 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 113 VDALLVTHIHSDHL-DINTAAAvlqnsGPETKFIGPQAVVDIWKGWGVPE-------ERTIVVHPGDEVTVKSVTIKaLE 184
Cdd:pfam12706 29 IDAVLLTHDHYDHLaGLLDLRE-----GRPRPLYAPLGVLAHLRRNFPYLfllehygVRVHEIDWGESFTVGDGGLT-VT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 185 AFdrTVLLTVDNDVTIKDSLpqdmdeiAVNYLFKTSGGNLYHAADSHM--SNMFAKHGNenhVDVEIIN---YGENPRGI 259
Cdd:pfam12706 103 AT--PARHGSPRGLDPNPGD-------TLGFRIEGPGKRVYYAGDTGYfpDEIGERLGG---ADLLLLDggaWRDDEMIH 170
|
170 180
....*....|....*....|....*.
gi 1905566313 260 TDKVTSIDVLRSAEDLKAKVVIPVHY 285
Cdd:pfam12706 171 MGHMTPEEAVEAAADLGARRKVLIHI 196
|
|
| Lactamase_B |
smart00849 |
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
110-185 |
1.41e-05 |
|
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: 44.85 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 110 VKNVDALLVTHIHSDHldINTAAAVLQNsgPETKFIGPQAVVDIWKG----------WGVPEERTIVVHPGDEVTVKSVT 179
Cdd:smart00849 33 PKKIDAIILTHGHPDH--IGGLPELLEA--PGAPVYAPEGTAELLKDllallgelgaEAEPAPPDRTLKDGDELDLGGGE 108
|
....*.
gi 1905566313 180 IKALEA 185
Cdd:smart00849 109 LEVIHT 114
|
|
| ComEC |
COG2333 |
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ... |
104-197 |
6.32e-05 |
|
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441904 [Multi-domain] Cd Length: 253 Bit Score: 44.08 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 104 VIDPY----AVKNVDALLVTHIHSDHldINTAAAVLQN--------SGPETKFIGPQAVVDIWKGWGVPeerTIVVHPGD 171
Cdd:COG2333 40 VVLPYlralGIRRLDLLVLTHPDADH--IGGLAAVLEAfpvgrvlvSGPPDTSETYERLLEALKEKGIP---VRPCRAGD 114
|
90 100
....*....|....*....|....*.
gi 1905566313 172 EVTVKSVTIKALEAFDRTVLLTVDND 197
Cdd:COG2333 115 TWQLGGVRFEVLWPPEDLLEGSDENN 140
|
|
| metallo-hydrolase-like_MBL-fold |
cd07741 |
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
105-284 |
1.26e-04 |
|
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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) 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: 293827 [Multi-domain] Cd Length: 212 Bit Score: 42.56 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 105 IDPyavKNVDALLVTHIHSDHL-DINTAAAVLQNSGPETK--FIGPQAVVDiwkgwGVPE----------ERTIVVHPGD 171
Cdd:cd07741 49 LDP---TKLDAIILSHRHLDHSnDANVLIEAMTEGGFKKRgtLLAPEDALN-----GEPVvllyyhrrklEEIEILEEGD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 172 EVTVKSVTIKALEAFDRtvlltvdndvtikdslpqdmDEIAVNYLFKTSGGNLYHAADSHMSN-MFAKHGNenhVDVEII 250
Cdd:cd07741 121 EYELGGIKIEATRHKHS--------------------DPTTYGFIFRTSDKKIGYISDTRYFEeLIEYYSN---CDVLII 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1905566313 251 NYG-ENPRGITDKVTSIDVLRSAEDLKAKVVIPVH 284
Cdd:cd07741 178 NVTrPRPRKGVDHLSVEDVEKILKEIKPKLAILTH 212
|
|
| hydroxyacylglutathione_hydrolase_MBL-fold |
cd07723 |
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ... |
103-184 |
3.77e-04 |
|
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: 40.52 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 103 FVIDP--------YAVKN---VDALLVTHIHSDHLDINTAaavLQNSGPETKFIGPQAvvdiwkgwGVPEERTIVVHPGD 171
Cdd:cd07723 23 AVVDPgeaepvlaALEKNgltLTAILTTHHHWDHTGGNAE---LKALFPDAPVYGPAE--------DRIPGLDHPVKDGD 91
|
90
....*....|...
gi 1905566313 172 EVTVKSVTIKALE 184
Cdd:cd07723 92 EIKLGGLEVKVLH 104
|
|
| ComA-like_MBL-fold |
cd07731 |
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ... |
110-183 |
2.40e-03 |
|
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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.
Pssm-ID: 293817 [Multi-domain] Cd Length: 179 Bit Score: 38.27 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 110 VKNVDALLVTHIHSDHldINTAAAVLQN--------SGPETKFIGPQAVVDIWKGWGVPeerTIVVHPGDEVTVKSVTIK 181
Cdd:cd07731 46 IKKLDYLILTHPDADH--IGGLDAVLKNfpvkevymPGVTHTTKTYEDLLDAIKEKGIP---VTPCKAGDRWQLGGVSFE 120
|
..
gi 1905566313 182 AL 183
Cdd:cd07731 121 VL 122
|
|
| RNaseZ_short-form-like_MBL-fold |
cd07716 |
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ... |
55-185 |
4.68e-03 |
|
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293802 [Multi-domain] Cd Length: 175 Bit Score: 37.42 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 55 THEDTNILVDLWNGTgkqthgsglmkqghqmmrMSGVQKmqpnlrlqpfVIDPyavKNVDALLVTHIHSDH-LDINT--- 130
Cdd:cd07716 24 EADGFRILLDCGSGV------------------LSRLQR----------YIDP---EDLDAVVLSHLHPDHcADLGVlqy 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1905566313 131 AAAVLQNSGPETK--FIGPQAVVDIWKGWGVPEERT--IVVHPGDEVTVKSVTIKALEA 185
Cdd:cd07716 73 ARRYHPRGARKPPlpLYGPAGPAERLAALYGLEDVFdfHPIEPGEPLEIGPFTITFFRT 131
|
|
| arylsulfatase_AtsA-like_MBL-fold |
cd07719 |
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ... |
112-200 |
8.76e-03 |
|
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.
Pssm-ID: 293805 [Multi-domain] Cd Length: 193 Bit Score: 36.73 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905566313 112 NVDALLVTHIHSDH----LDINTAAAVLQNSGPeTKFIGP---QAVVD-IWKGWGVPEE-RTIVVHPGDevTVKSVTIKA 182
Cdd:cd07719 51 DLDAVFLTHLHSDHvadlPALLLTAWLAGRKTP-LPVYGPpgtRALVDgLLAAYALDIDyRARIGDEGR--PDPGALVEV 127
|
90
....*....|....*...
gi 1905566313 183 LEaFDRTVLLTVDNDVTI 200
Cdd:cd07719 128 HE-IAAGGVVYEDDGVKV 144
|
|
| |
