NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|823631031|pdb|4P62|A]
View 

Chain A, Metallo-beta-lactamase AIM-1

Protein Classification

subclass B3 metallo-beta-lactamase( domain architecture ID 10888870)

subclass B3 metallo-beta-lactamase hydrolyzes the beta-lactam ring of beta-lactam antibiotics such as penicillin, cephalosporin and carbapenem, resulting in antibiotic resistance

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-294 1.36e-162

Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup AIM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


:

Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 452.04  E-value: 1.36e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16314   1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16314  81 QRATGAPVVAREPAATTLERGRSDRSDPQFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDdaaHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAAAPLMDTTACRR 276
Cdd:cd16314 161 AVCRDMVYADSVTAISDDIYRYSD---HPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWERLGPAAGIPLADTGACRA 237

                       250
                ....*....|....*...
4P62_A      277 YAQGARQRLEKRLAEEAA 294
Cdd:cd16314 238 YAQTGRARLDARLADEAA 255
 
Name Accession Description Interval E-value
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-294 1.36e-162

Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup AIM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 452.04  E-value: 1.36e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16314   1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16314  81 QRATGAPVVAREPAATTLERGRSDRSDPQFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDdaaHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAAAPLMDTTACRR 276
Cdd:cd16314 161 AVCRDMVYADSVTAISDDIYRYSD---HPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWERLGPAAGIPLADTGACRA 237

                       250
                ....*....|....*...
4P62_A      277 YAQGARQRLEKRLAEEAA 294
Cdd:cd16314 238 YAQTGRARLDARLADEAA 255
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 59-250 3.42e-29

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: 109.57  E-value: 3.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A          59 SALLVTSDAGHILVDAATPQAGPqILANIRALGfrPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLKRGL 138
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAED-LLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A         139 PDRTDPqfevAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRScegddcRQMVYA-DsltAISDDVYR 217
Cdd:smart00849  78 ALLGEL----GAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE------GKILFTgD---LLFAGGDG 144

                          170       180       190
                   ....*....|....*....|....*....|...
4P62_A         218 YSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:smart00849 145 RTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 57-250 4.42e-26

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: 102.46  E-value: 4.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISALLVTSDAGHILVDA-ATPQAGPQILANIRALGfrpEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLK 135
Cdd:COG0491  14 GVNSYLIVGGDGAVLIDTgLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      136 rglpDRTDPQFEVAEPVAPVaniVTLADDGVVSVGPLALTAVASPGHTPGGTSWtwrscegddcrqmVYADSLTAISDDV 215
Cdd:COG0491  91 ----APAAGALFGREPVPPD---RTLEDGDTLELGGPGLEVIHTPGHTPGHVSF-------------YVPDEKVLFTGDA 150

                       170       180       190
                ....*....|....*....|....*....|....*...
4P62_A      216 ---YRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:COG0491 151 lfsGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
53-250 3.07e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 94.36  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A         53 VGTCGISALLVTSDAGHILVDAATPQAGPQILAnIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAID 132
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A        133 TLKRGLPDRTDPQFEVAEPVAPVANIVTLADDG-VVSVGPLALTAVASPGHTPGGTSWTWRSCE----GDdcrqMVYADS 207
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGdGILGGGLGLLVTHGPGHGPGHVVVYYGGGKvlftGD----LLFAGE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
4P62_A        208 LtaISDDVYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:pfam00753 156 I--GRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PRK02113 PRK02113
MBL fold metallo-hydrolase;
59-139 1.13e-05

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 45.93  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A        59 SALLVTSDAGHILVDAatpqaGPQILANIRALGFRPEDvrAIVLSHEHFDHAGSLAELQ---KATGAPVYARAPAIDTLK 135
Cdd:PRK02113  36 TSALVETEGARILIDC-----GPDFREQMLRLPFGKID--AVLITHEHYDHVGGLDDLRpfcRFGEVPIYAEQYVAERLR 108


                 ....
4P62_A       136 RGLP 139
Cdd:PRK02113 109 SRMP 112
 
Name Accession Description Interval E-value
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-294 1.36e-162

Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup AIM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 452.04  E-value: 1.36e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16314   1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16314  81 QRATGAPVVAREPAATTLERGRSDRSDPQFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDdaaHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAAAPLMDTTACRR 276
Cdd:cd16314 161 AVCRDMVYADSVTAISDDIYRYSD---HPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWERLGPAAGIPLADTGACRA 237

                       250
                ....*....|....*...
4P62_A      277 YAQGARQRLEKRLAEEAA 294
Cdd:cd16314 238 YAQTGRARLDARLADEAA 255
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-289 1.37e-143

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 404.04  E-value: 1.37e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16290   1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16290  81 QRDSGATVAASPAGAAALRSGGVDPDDPQAGAADPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDDaAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAA----APLMDTT 272
Cdd:cd16290 161 GRCLDIVYADSLTAVSADGFRFSDD-AHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRARepgpNPFIDPN 239

                       250
                ....*....|....*..
4P62_A      273 ACRRYAQGARQRLEKRL 289
Cdd:cd16290 240 ACRAYAAAAEARLEARL 256
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-289 7.19e-123

Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 351.27  E-value: 7.19e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16315   1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16315  81 QRATGARVAASAAAAPVLESGKPAPDDPQAGLHEPFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCEG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDdaaHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGprAAAPLMDTTACRR 276
Cdd:cd16315 161 ADCRTIVYADSLSPVSADGYRFSD---HPDYVAAYRAGLAKVAALPCDILLTPHPSASDMFERLS--GGAPLADPDACAA 235

                       250
                ....*....|...
4P62_A      277 YAQGARQRLEKRL 289
Cdd:cd16315 236 YAAGAEKRLDERL 248
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 37-290 1.19e-106

SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 310.26  E-value: 1.19e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16313   1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16313  81 QKLTGAQVLASPATVAVLRSGSMGKDDPQFGGLTPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDdaaHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAA---APLMDTTA 273
Cdd:cd16313 161 GRCANMVFADSLTAVSADGYRFSA---HPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAegnAAFIDGGG 237

                       250
                ....*....|....*..
4P62_A      274 CRRYAQGARQRLEKRLA 290
Cdd:cd16313 238 CRAYAAKAREKLNKRLA 254
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-290 7.89e-95

Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 280.72  E-value: 7.89e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16312   1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEvAEPVAPVANI--VTLADDG-VVSVGPLALTAVASPGHTPGGTSWTWRS 193
Cdd:cd16312  81 QKASGATVAASAHGAQVLQSGTNGKDDPQYQ-AKPVVHVAKVakVKEVGEGdTLKVGPLRLTAHMTPGHTPGGTTWTWTS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      194 CEGDDCRQMVYADSLTAISDDVYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAAA--PLMDT 271
Cdd:cd16312 160 CEGQRCLDVVYADSLNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKRRSGDtnPFIDA 239

                       250
                ....*....|....*....
4P62_A      272 TACRRYAQGARQRLEKRLA 290
Cdd:cd16312 240 EACRAYAAGAAKSLEKRLA 258
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-290 1.30e-93

Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B2-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293869  Cd Length: 257  Bit Score: 277.64  E-value: 1.30e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16311   1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16311  81 QRRSGALVAASPSAALDLASGEVGPDDPQYHALPKYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSCDG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDVYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRI--GPRAAAP-LMDTTA 273
Cdd:cd16311 161 PRCLNMVYADSQNAVSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLeaSDRSARPaLVDREA 240

                       250
                ....*....|....*..
4P62_A      274 CRRYAQGARQRLEKRLA 290
Cdd:cd16311 241 CRRYASRAREALEKRIA 257
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 37-283 3.48e-81

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 245.53  E-value: 3.48e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd07708   1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDrTDPQFEVAEPVAPVANIVTLADDG-VVSVGPLALTAVASPGHTPGGTSWTWRSCE 195
Cdd:cd07708  81 KKQTGAKVMAGAEDVSLLLSGGSS-DFHYANDSSTYFPQSTVDRAVHDGeRVTLGGTVLTAHATPGHTPGCTTWTMTLKD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      196 GDDCRQMVYADSLTAISDdvYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAAA---PLMDTT 272
Cdd:cd07708 160 HGKQYQVVFADSLTVNPG--YRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGqnnPFVDPG 237

                       250
                ....*....|.
4P62_A      273 ACRRYAQGARQ 283
Cdd:cd07708 238 GCKAYAEAKAN 248
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-290 7.02e-69

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 214.11  E-value: 7.02e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16288   1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGlpDRTDPQFEVAEPV-APVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCE 195
Cdd:cd16288  81 KKLTGAKLMASAEDAALLASG--GKSDFHYGDDSLAfPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      196 GDDCRQMVYADSLTAISDdvYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGL---WNRIGPRAAAPLMDTT 272
Cdd:cd16288 159 DGKVYQVVFADSLTVNPG--YKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLkekRARLAAGQPNAFIDPE 236

                       250
                ....*....|....*...
4P62_A      273 ACRRYAQGARQRLEKRLA 290
Cdd:cd16288 237 GYRNFIEKAKADFEKQLA 254
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 37-283 3.31e-60

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 191.57  E-value: 3.31e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16289   1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDrtDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16289  81 KRATGARVAANAESAVLLARGGSD--DIHFGDGITFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISddvYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGlWNRIGPRAAAPlmDTTACRR 276
Cdd:cd16289 159 GKPVRIAYADSLSAPG---YQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASG-WDYAAGAAPHA--KPMTCKA 232


                ....*..
4P62_A      277 YAQGARQ 283
Cdd:cd16289 233 YADAAEQ 239
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-290 1.27e-54

Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of BJP-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 177.68  E-value: 1.27e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16309   1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDrTDPQFEVAEPVAPVANIVTLADDgvVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16309  81 KKATGAQLVASAADKPLLESGYVG-SGDTKNLQFPPVRVDRVIGDGDK--VTLGGTTLTAHLTPGHSPGCTSWTTTVKDT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTAISDDvyRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWN---RIGPRAAAPLMDTTA 273
Cdd:cd16309 158 AGPPREVLFFCSATVAGN--QLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAkraRQSAGEPDAFVDAGE 235

                       250
                ....*....|....*..
4P62_A      274 CRRYAQGARQRLEKRLA 290
Cdd:cd16309 236 LQRFNTKMEDDFEKALA 252
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-290 1.82e-54

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 177.26  E-value: 1.82e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16310   1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGLPDRTDPQFEVAEPVAPVANIvtLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCEG 196
Cdd:cd16310  81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRI--LGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKEN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      197 DDCRQMVYADSLTaISDDVyrYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAAA---PLMDTTA 273
Cdd:cd16310 159 GRPLRVVFPCSLS-VAGNV--LVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGqanAFVDPGE 235

                       250
                ....*....|....*..
4P62_A      274 CRRYAQGARQRLEKRLA 290
Cdd:cd16310 236 LARIVDQSEAAFNKELA 252
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-290 3.43e-38

Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of FEZ-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293865  Cd Length: 255  Bit Score: 135.27  E-value: 3.43e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16307   1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGlpDRTDPQF----EVAEPVAPVANIvtLADDGVVSVGPLALTAVASPGHTPGGTSWTWR 192
Cdd:cd16307  81 KRETHAKYMVMDGDVDVVESG--GKSDFFYgndpSTYFPPAHVDKV--LHDGEQVELGGTVLTAHLTAGHTKGCTTWTMK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      193 SCEGDDCRQMVYADSLTAISDdvYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGL---WNRIGPRAAAPLM 269
Cdd:cd16307 157 VKDHGKTYDVVIVGSPNVNPG--AKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLknkYVRLQKGGANPFI 234

                       250       260
                ....*....|....*....|.
4P62_A      270 DTTACRRYAQGARQRLEKRLA 290
Cdd:cd16307 235 DPEGYKAYVAEKEQAFRTELE 255
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 37-290 1.24e-37

Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of GOB-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 133.75  E-value: 1.24e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd16308   1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      117 QKATGAPVYARAPAIDTLKRGlpDRTDPQFEVAEPV-APVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCE 195
Cdd:cd16308  81 KQQTGAKMMVDEKDAKVLADG--GKSDYEMGGYGSTfAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVKD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      196 GDDCRQMVYADSLTAISDDvyRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPHPSASGLWNRIGPRAA---APLMDTT 272
Cdd:cd16308 159 EKRTYRVLIANMPTILPDT--KLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPynpAAFADRA 236

                       250
                ....*....|....*...
4P62_A      273 ACRRYAQGARQRLEKRLA 290
Cdd:cd16308 237 GYDKALAGLEKSYDKKIK 254
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 37-290 3.10e-37

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) 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, 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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 132.71  E-value: 3.10e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       37 WNDPAMPQKVYGNTWYVGTCGISALLVTSDAGHILVDAA-TPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAE 115
Cdd:cd16280   1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILIDALnNNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      116 LQKATGAPVYARAPAIDTLKRGLPDRTDPqfevAEPVAPVANIVtLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCE 195
Cdd:cd16280  81 LKDLYGAKVVMSEADWDMMEEPPEEGDNP----RWGPPPERDIV-IKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      196 GDDcRQMVyadSL--------TAISDDVYRYSDDAAHpgylaaFRNtlaRVAALDCDILVTPHPSASGLWNRI------G 261
Cdd:cd16280 156 GGK-THRA---GLwggtglntGPNLERREQYIASLER------FKK---IAEEAGVDVFLSNHPFQDGSLEKRealrnrK 222

                       250       260
                ....*....|....*....|....*....
4P62_A      262 PRAAAPLMDTTACRRYAQGARQRLEKRLA 290
Cdd:cd16280 223 PGEPNPFVDGQAWVDFYDEVLALCARVLA 251
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 57-250 1.14e-34

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: 124.64  E-value: 1.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYAR---APAIDT 133
Cdd:cd07721  10 PVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHereAPYLEG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      134 LKRGLPDRTDPQ---FEVAEPVAPVANIVTLADDGVVSVGPlALTAVASPGHTPGGTSwtwrscegddcrqMVYADSLTA 210
Cdd:cd07721  90 EKPYPPPVRLGLlglLSPLLPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHIS-------------LYLEEDGVL 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
4P62_A      211 ISDDVYRYSDDAAHPGY------LAAFRNTLARVAALDCDILVTPH 250
Cdd:cd07721 156 IAGDALVTVGGELVPPPppftwdMEEALESLRKLAELDPEVLAPGH 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 59-250 3.42e-29

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: 109.57  E-value: 3.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A          59 SALLVTSDAGHILVDAATPQAGPqILANIRALGfrPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLKRGL 138
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAED-LLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A         139 PDRTDPqfevAEPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTWRScegddcRQMVYA-DsltAISDDVYR 217
Cdd:smart00849  78 ALLGEL----GAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE------GKILFTgD---LLFAGGDG 144

                          170       180       190
                   ....*....|....*....|....*....|...
4P62_A         218 YSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:smart00849 145 RTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 57-250 4.42e-26

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: 102.46  E-value: 4.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISALLVTSDAGHILVDA-ATPQAGPQILANIRALGfrpEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLK 135
Cdd:COG0491  14 GVNSYLIVGGDGAVLIDTgLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      136 rglpDRTDPQFEVAEPVAPVaniVTLADDGVVSVGPLALTAVASPGHTPGGTSWtwrscegddcrqmVYADSLTAISDDV 215
Cdd:COG0491  91 ----APAAGALFGREPVPPD---RTLEDGDTLELGGPGLEVIHTPGHTPGHVSF-------------YVPDEKVLFTGDA 150

                       170       180       190
                ....*....|....*....|....*....|....*...
4P62_A      216 ---YRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:COG0491 151 lfsGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGH 188
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 62-188 2.08e-25

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: 99.67  E-value: 2.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       62 LVTSDAGH-ILVDAATPqAGPQILANIRALGfrpEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLKRGLPD 140
Cdd:cd06262  14 LVSDEEGEaILIDPGAG-ALEKILEAIEELG---LKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPELN 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
4P62_A      141 RTDPQFEVAEPVAPvanIVTLADDGVVSVGPLALTAVASPGHTPGGTS 188
Cdd:cd06262  90 LAFFGGGPLPPPEP---DILLEDGDTIELGGLELEVIHTPGHTPGSVC 134
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
53-250 3.07e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 94.36  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A         53 VGTCGISALLVTSDAGHILVDAATPQAGPQILAnIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAID 132
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A        133 TLKRGLPDRTDPQFEVAEPVAPVANIVTLADDG-VVSVGPLALTAVASPGHTPGGTSWTWRSCE----GDdcrqMVYADS 207
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGdGILGGGLGLLVTHGPGHGPGHVVVYYGGGKvlftGD----LLFAGE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
4P62_A        208 LtaISDDVYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:pfam00753 156 I--GRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 58-250 1.11e-17

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: 79.46  E-value: 1.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       58 ISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL-QKATGAPVYA--RA------ 128
Cdd:cd07726  16 IASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYVhpRGarhlid 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      129 PA--IDTLKRGLPDRTDPQFEVAEPVaPVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTwrscegDDCRQMVYA- 205
Cdd:cd07726  96 PSklWASARAVYGDEADRLGGEILPV-PEERVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFL------DEESDGLFTg 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
4P62_A      206 DSL-TAISDDVYRYSDDAAHPGY-LAAFRNTLARVAALDCDILVTPH 250
Cdd:cd07726 169 DAAgVRYPELDVVGPPSTPPPDFdPEAWLESLDRLLSLKPERIYLTH 215
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 59-187 7.47e-16

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 75.32  E-value: 7.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       59 SALLVTSDAGHILVDAatpqaGPQILANIRALGFRPEDVRAIVLSHEHFDH---AGSLAELQKATGAPVYARAPAIDTLK 135
Cdd:COG1235  36 SSILVEADGTRLLIDA-----GPDLREQLLRLGLDPSKIDAILLTHEHADHiagLDDLRPRYGPNPIPVYATPGTLEALE 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
4P62_A      136 RGLpdrtdPQFEVaePVAPVANIVTLADDGVVSVGPLALTAVASPgHTPGGT 187
Cdd:COG1235 111 RRF-----PYLFA--PYPGKLEFHEIEPGEPFEIGGLTVTPFPVP-HDAGDP 154
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 58-185 4.52e-15

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 72.97  E-value: 4.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       58 ISALLVTSDAGHILVDA-ATPQAGP---QILANIRALGFRPEDVRAIVLSHEHFDHAGSLAelqKATGAPVYARA----P 129
Cdd:cd07720  49 VNAFLVRTGGRLILVDTgAGGLFGPtagKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLV---DAGGKPVFPNAevhvS 125

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4P62_A      130 AID-------TLKRGLPDRTDPQFEVAEP-VAPVANIVTLADDGVVSVGplaLTAVASPGHTPG 185
Cdd:cd07720 126 EAEwdfwlddANAAKAPEGAKRFFDAARDrLRPYAAAGRFEDGDEVLPG---ITAVPAPGHTPG 186
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-246 2.36e-14

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) 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, 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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 69.83  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       49 NTWyvgtcgisalLVTSDAGHILVDaatPqaGPQILANIRAL--GFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYA 126
Cdd:cd16278  19 NTY----------LLGAPDGVVVID---P--GPDDPAHLDALlaALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      127 RAPAidtlkrgLPDRTDPQFEVAEPvapvanivtLADDGVVSVGPLALTAVASPGHTPGGTSWTWRSCE----GDdcrqM 202
Cdd:cd16278  84 FGPH-------RAGGQDTDFAPDRP---------LADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGalftGD----H 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
4P62_A      203 VYADSLTAISddvyrysddaaHP-GYLAAFRNTLARVAALDCDIL 246
Cdd:cd16278 144 VMGWSTTVIA-----------PPdGDLGDYLASLERLLALDDRLL 177
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 58-188 4.70e-14

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. 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.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 69.94  E-value: 4.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       58 ISALLVTSDAGHILVD------AATPQAGPQ------------ILANIRALGFRPEDVRAIVLSHEHFDHAGSL------ 113
Cdd:cd07729  32 VYAYLIEHPEGTILVDtgfhpdAADDPGGLElafppgvteeqtLEEQLARLGLDPEDIDYVILSHLHFDHAGGLdlfpna 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      114 ------AELQKATGAPVYARAPAIDTLKRgLPDRTDPQFEVAEPVAPVAnivtladDGVvsvgplalTAVASPGHTPGGT 187
Cdd:cd07729 112 tiivqrAELEYATGPDPLAAGYYEDVLAL-DDDLPGGRVRLVDGDYDLF-------PGV--------TLIPTPGHTPGHQ 175


                .
4P62_A      188 S 188
Cdd:cd07729 176 S 176
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 57-172 6.05e-14

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 70.34  E-value: 6.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISaLLVTSDAGHILVDAAtpqAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAE-LQKATGAPVYARAPAIDTLK 135
Cdd:cd07713  20 GLS-LLIETEGKKILFDTG---QSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVYAHPDAFEPRY 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
4P62_A      136 RGLPDRTDPQ-FEVAEPVAPVANIV-----TLADDGVVSVGPL 172
Cdd:cd07713  96 SKRGGGKKGIgIGREELEKAGARLVlveepTEIAPGVYLTGEI 138
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-247 1.54e-13

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) 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, 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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 67.98  E-value: 1.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       51 WYVGTCGisalLVTSDAGHILVDA-ATPQAGPQILANIRALGFRPedVRAIVLSHEHFDHAGSLAELqKATGAPVYARAP 129
Cdd:cd16282  12 GFISNIG----FIVGDDGVVVIDTgASPRLARALLAAIRKVTDKP--VRYVVNTHYHGDHTLGNAAF-ADAGAPIIAHEN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      130 AIDTLKRG-------LPDRTDPQFEVAEPVAPVaniVTLADDGVVSVGPLALTAVA-SPGHTPG---------GTSWTwr 192
Cdd:cd16282  85 TREELAARgeaylelMRRLGGDAMAGTELVLPD---RTFDDGLTLDLGGRTVELIHlGPAHTPGdlvvwlpeeGVLFA-- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
4P62_A      193 sceGDdcrqMVYADSLTAISDdvyrysddaahpGYLAAFRNTLARVAALDCDILV 247
Cdd:cd16282 160 ---GD----LVFNGRIPFLPD------------GSLAGWIAALDRLLALDATVVV 195
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 58-250 8.30e-13

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 65.40  E-value: 8.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       58 ISALLVTSDAGHILVDA--ATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYarapaidtlk 135
Cdd:cd07725  15 VNVYLLRDGDETTLIDTglATEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVY---------- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      136 rglpdrtdpqfevaepvapVANIVTLADDGVVSVGPLALTAVASPGHTPGGTSWtwrSCEGDdcRQMVYADSLTA----- 210
Cdd:cd07725  85 -------------------ILDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVL---YDEDR--RELFVGDAVLPkitpn 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
4P62_A      211 ISDDVYRYSDDaahpgyLAAFRNTLARVAALDCDILVTPH 250
Cdd:cd07725 141 VSLWAVRVEDP------LGAYLESLDKLEKLDVDLAYPGH 174
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 69-188 1.17e-12

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 64.87  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       69 HILVDAATPQAG--------PQILANIRALGFRpedVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLkrGLPD 140
Cdd:cd16275  15 YIIIDKATREAAvvdpawdiEKILAKLNELGLT---LTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYY--GFRC 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
4P62_A      141 RtdpqfevaepvapvaNIVTLADDGVVSVGPLALTAVASPGHTPGGTS 188
Cdd:cd16275  90 P---------------NLIPLEDGDTIKIGDTEITCLLTPGHTPGSMC 122
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
57-130 2.25e-12

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 65.67  E-value: 2.25e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
4P62_A       57 GISALlVTSDAGHILVDAATPQAgpqILANIRALGFRPEDVRAIVLSHEHFDHAGSLAE-LQKATGAPVYARAPA 130
Cdd:COG1237  22 GLSAL-IETEGKRILFDTGQSDV---LLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPAlLELNPKAPVYAHPDA 92
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-264 3.22e-12

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) 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, 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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 63.76  E-value: 3.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       49 NTWYVGTCGISALLVTSDAGHILVDAAtPQAGPQILANIRALGFRPedVRAIVLSHEHFDHAGSlAELQKATGAPVYARA 128
Cdd:cd16276   1 GVYWVTDGGYQSMFLVTDKGVIVVDAP-PSLGENLLAAIRKVTDKP--VTHVVYSHNHADHIGG-ASIFKDEGATIIAHE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      129 PAIDTLKRGL-PDRtdpqfevaepvaPVANiVTLADDGVVSVG--PLALTAVAsPGHTPGGTSWTWRscegdDCRQMVYA 205
Cdd:cd16276  77 ATAELLKRNPdPKR------------PVPT-VTFDDEYTLEVGgqTLELSYFG-PNHGPGNIVIYLP-----KQKVLMAV 137

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
4P62_A      206 DSLTAISDDVYRYSDDAAHPGYLAAfrntLARVAALDCDILVTPHPsasglwNRIGPRA 264
Cdd:cd16276 138 DLINPGWVPFFNFAGSEDIPGYIEA----LDELLEYDFDTFVGGHG------NRLGTRE 186
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 53-185 9.19e-12

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 63.14  E-value: 9.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       53 VGTCGISALLVTSDAGH--ILVDAATPQagPQILANIRALGFrpeDVRAIVLSHEHFDHAGSLAELQKATGAPVYarAPA 130
Cdd:cd16322   6 LGPLQENTYLVADEGGGeaVLVDPGDES--EKLLARFGTTGL---TLLYILLTHAHFDHVGGVADLRRHPGAPVY--LHP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
4P62_A      131 IDTLKRGLPDRTDPQFEVAEPVAPVANiVTLADDGVVSVGPLALTAVASPGHTPG 185
Cdd:cd16322  79 DDLPLYEAADLGAKAFGLGIEPLPPPD-RLLEDGQTLTLGGLEFKVLHTPGHSPG 132
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 61-185 1.31e-11

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: 61.71  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       61 LLVTSDAGH-ILVDAATPQagpQILANIRALGFRPEdvrAIVLSHEHFDHAGSLAELQKATG-APVYA----RAPAIDtl 134
Cdd:cd07723  13 LIVDEATGEaAVVDPGEAE---PVLAALEKNGLTLT---AILTTHHHWDHTGGNAELKALFPdAPVYGpaedRIPGLD-- 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
4P62_A      135 krglpdrtdpqfevaepvapvaniVTLADDGVVSVGPLALTAVASPGHTPG 185
Cdd:cd07723  85 ------------------------HPVKDGDEIKLGGLEVKVLHTPGHTLG 111
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 52-188 1.68e-11

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 61.83  E-value: 1.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       52 YVGTCGISalLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAelqkatgapVYARAPAI 131
Cdd:cd07711  18 FRASSTVT--LIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLN---------LFPNATVI 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
4P62_A      132 DTLKRGLPDRTDPQFEVAEPVAPvanivtlaDDGVvsvgplalTAVASPGHTPGGTS 188
Cdd:cd07711  87 VGWDICGDSYDDHSLEEGDGYEI--------DENV--------EVIPTPGHTPEDVS 127
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 61-185 1.07e-10

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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 60.72  E-value: 1.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       61 LLVTSDAGHILVDA-------ATPQ----------AGPQI------LANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQ 117
Cdd:cd07742  22 LLVETDDGLVLVDTgfgladvADPKrrlggpfrrlLRPRLdedetaVRQIEALGFDPSDVRHIVLTHLDLDHAGGLADFP 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4P62_A      118 KATgapVYARAPAIDTLKRGlPDRTDPQFEVAEPVAPVANIVTLADDGVV-----SVGPLA-----LTAVASPGHTPG 185
Cdd:cd07742 102 HAT---VHVHAAELDAATSP-RTRYERRRYRPQQLAHGPWWVTYAAGGERwfgfeAVRPLDglppeILLVPLPGHTRG 175
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-250 1.68e-10

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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 59.08  E-value: 1.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       50 TWYVgTCGISALLVTSDAGH-ILVDAATP-QAGPQILANIRALGFRPedvRAIVLSHEHFDHAGSLAELQKATGAPVYar 127
Cdd:cd07743   1 TYYI-PGPTNIGVYVFGDKEaLLIDSGLDeDAGRKIRKILEELGWKL---KAIINTHSHADHIGGNAYLQKKTGCKVY-- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      128 APAID------------TLKRGLPDRTD-PQFEVAEPVaPVANIVtlaDDGVVSVGPLALTAVASPGHTPG----GTswt 190
Cdd:cd07743  75 APKIEkafienpllepsYLGGAYPPKELrNKFLMAKPS-KVDDII---EEGELELGGVGLEIIPLPGHSFGqigiLT--- 147

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
4P62_A      191 wrsceGDDcrqmVY--ADSLtaISDDV---YR--YSDDAahpgylAAFRNTLARVAALDCDILVTPH 250
Cdd:cd07743 148 -----PDG----VLfaGDAL--FGEEVlekYGipFLYDV------EEQLETLEKLEELDADYYVPGH 197
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
59-177 3.89e-10

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 59.05  E-value: 3.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       59 SALLVTSDAGHILVDAatpqaGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGA-------PVYARAPAI 131
Cdd:COG1234  20 SSYLLEAGGERLLIDC-----GEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLagrekplTIYGPPGTK 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
4P62_A      132 DTLKRGL-PDRTDPQFEVaepvapvaNIVTLADDGVVSVGPLALTAV 177
Cdd:COG1234  95 EFLEALLkASGTDLDFPL--------EFHEIEPGEVFEIGGFTVTAF 133
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 59-178 1.03e-09

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: 56.68  E-value: 1.03e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       59 SALLVTSDAGHILVDAatpqaGPQILANIRALGfRPEDVRAIVLSHEHFDHAGSLAELQKA-TGAPVYARAPAIDTLkrg 137
Cdd:cd07716  19 SGYLLEADGFRILLDC-----GSGVLSRLQRYI-DPEDLDAVVLSHLHPDHCADLGVLQYArRYHPRGARKPPLPLY--- 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
4P62_A      138 LPDRTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAVA 178
Cdd:cd07716  90 GPAGPAERLAALYGLEDVFDFHPIEPGEPLEIGPFTITFFR 130
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 54-185 2.92e-09

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 57.12  E-value: 2.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       54 GTCGISALLVTSDAGHILVDAATPQAGPqiLANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATG-APVYARAPAID 132
Cdd:COG1236  10 GEVTGSCYLLETGGTRILIDCGLFQGGK--ERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFrGPIYATPATAD 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
4P62_A      133 TLKRGLPD---------RTDPQFEVAEPVAPVANIVTLADDGVVSVGPLALT---AvaspGHTPG 185
Cdd:COG1236  88 LARILLGDsakiqeeeaEAEPLYTEEDAERALELFQTVDYGEPFEIGGVRVTfhpA----GHILG 148
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 70-182 3.56e-09

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: 55.39  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A         70 ILVDAatpqaGPQILANIRALGF----RPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLKRGLPdrtdpq 145
Cdd:pfam12706   3 ILIDP-----GPDLRQQALPALQpgrlRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFP------ 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
4P62_A        146 FEVAEPVAPVaNIVTLADDGVVSVGPLALTAVASPGH 182
Cdd:pfam12706  72 YLFLLEHYGV-RVHEIDWGESFTVGDGGLTVTATPAR 107
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 59-177 6.95e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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, 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. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 54.40  E-value: 6.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       59 SALLVTSDAGHILVDAatpqaGP----QIL-ANIRalgfrpeDVRAIVLSHEHFDHAGSLAEL------QKATGaPVYAR 127
Cdd:cd16279  36 SSILIETGGKNILIDT-----GPdfrqQALrAGIR-------KLDAVLLTHAHADHIHGLDDLrpfnrlQQRPI-PVYAS 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
4P62_A      128 APAIDTLKRGLPdrtDPQFEVAEPVAPVANIVTLADDGVVSVGPLALTAV 177
Cdd:cd16279 103 EETLDDLKRRFP---YFFAATGGGGVPKLDLHIIEPDEPFTIGGLEITPL 149
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 64-191 9.20e-09

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. 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.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 53.94  E-value: 9.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       64 TSDAGHILVDAATPQA---------GPQILANIRALGFRpedVRAIVLSHEHFDHAGSLAELQKATGAPVYarapaidtl 134
Cdd:cd07724  10 LGTLSYLVGDPETGEAavidpvrdsVDRYLDLAAELGLK---ITYVLETHVHADHVSGARELAERTGAPIV--------- 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
4P62_A      135 krgLPDRTDPQFEVaepvapvanivTLADDG-VVSVGPLALTAVASPGHTPGGTSWTW 191
Cdd:cd07724  78 ---IGEGAPASFFD-----------RLLKDGdVLELGNLTLEVLHTPGHTPESVSYLV 121
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 57-188 2.12e-08

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) 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, 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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 53.68  E-value: 2.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISALLVTSDaGH-ILVDAAT------------PQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAP 123
Cdd:cd16277  12 LIHSWLVRTP-GRtILVDTGIgndkprpgppafHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWNTRLVDGRWVP 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
4P62_A      124 VYARA----PAID-TLKRGLPDRTDPQFEVAE-PVAPV-----ANIVTlaDDGVVSVGplaLTAVASPGHTPGGTS 188
Cdd:cd16277  91 TFPNArylfSRAEyDHWSSPDAGGPPNRGVFEdSVLPVieaglADLVD--DDHEILDG---IRLEPTPGHTPGHVS 161
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-244 2.30e-08

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) 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, 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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 53.81  E-value: 2.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       69 HILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELqkaTGAPVYARAPAIDTLKR-GLPDRTDPQFe 147
Cdd:cd07730  56 RLYRTPVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDF---PNARLIVGPGAKEALRPpGYPSGFLPEL- 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      148 VAEPVAPVANIVTLADDGVVSVGPLA----------LTAVASPGHTPG-------GTSWTWrscegddcrqmVY--ADS- 207
Cdd:cd07730 132 LPSDFEGRLVRWEEDDFLWVPLGPFPraldlfgdgsLYLVDLPGHAPGhlgllarTTSGTW-----------VFlaGDAc 200

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
4P62_A      208 ---LTAISDDVYRYSDDAAHPGYLAAFRNTLARVAALDCD 244
Cdd:cd07730 201 hhrIGLLRPSPLLPLPDLDDGADREAARETLARLRELDAA 240
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 59-140 2.80e-08

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 52.85  E-value: 2.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       59 SALLVTSDAGHILVDAATPQAGPQI-LANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATG-APVYARAPAIDTLKR 136
Cdd:cd16295  13 SCYLLETGGKRILLDCGLFQGGKELeELNNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFrGPIYATPATKDLAEL 92


                ....
4P62_A      137 GLPD 140
Cdd:cd16295  93 LLLD 96
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 49-219 3.01e-08

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 52.58  E-value: 3.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       49 NTWYVGT-----CGISALLVTSDAGHILVDAATPQagPQILANIRALGfrpeDVRAIVLSHEhfDHAGSLAELQKATGAP 123
Cdd:cd07727   1 GVYYCGFhseksFGAASYLILRPEGNILVDSPRYS--PPLAKRIEALG----GIRYIFLTHR--DDVADHAKWAERFGAK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      124 VYarapaidtLKRGlpDRTDPQFEVAEPVAPVANIVTLADDgvvsvgplaLTAVASPGHTPGGTSWTWRS----CEGDDC 199
Cdd:cd07727  73 RI--------IHED--DVNAVTRPDEVIVLWGGDPWELDPD---------LTLIPVPGHTRGSVVLLYKEkgvlFTGDHL 133

                       170       180
                ....*....|....*....|
4P62_A      200 RQMVYADSLTAiSDDVYRYS 219
Cdd:cd07727 134 AWSRRRGWLSA-FRYVCWYS 152
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 54-151 4.09e-08

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 51.49  E-value: 4.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       54 GTCGISALLVTSDaGHILVDAATPqaGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDT 133
Cdd:cd07733   6 GSKGNCTYLETED-GKLLIDAGLS--GRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRA 82

                        90
                ....*....|....*...
4P62_A      134 LKRGLPDRTDPQFEVAEP 151
Cdd:cd07733  83 MERKVGLIDVDQKQIFEP 100
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-128 6.33e-08

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) 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, 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: 293839  Cd Length: 252  Bit Score: 52.50  E-value: 6.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       60 ALLVTSDAGHILVDAAT-------------PQAGPQILANIRALGFRPEDVRAIVLSHEHFDHA-GSLAELQKATGAPVY 125
Cdd:cd16281  45 CLLIETGGRNILIDTGIgdkqdpkfrsiyvQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCgGATRADDDGLVELLF 124


                ...
4P62_A      126 ARA 128
Cdd:cd16281 125 PNA 127
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 70-250 7.54e-08

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: 52.10  E-value: 7.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       70 ILVDAATPQAGPQILANIRALgFRPEDVRAIVLSHEHFDHAGSLAE-LQKATGAPVYARAPAIDTLKRGLPDRTDpqfev 148
Cdd:cd07709  43 ALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLKHFYPGIDE----- 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      149 aepvapvaNIVTLADDGVVSVGPLALTAVASPG-HTPGGTsWTWRSCEG----DD------CRQMVYADSLTAISDDVYR 217
Cdd:cd07709 117 --------RFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTM-VTYDPEDKilfsGDafgahgASGELFDDEVEDYLEEARR 187

                       170       180       190
                ....*....|....*....|....*....|....*..
4P62_A      218 YsddaaHPGYLAAF----RNTLARVAALDCDILVTPH 250
Cdd:cd07709 188 Y-----YANIMGPFskqvRKALEKLEALDIKMIAPSH 219
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 57-189 8.16e-08

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 51.56  E-value: 8.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISALLVTSDAGHILVDAATPQAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATG--APVYARAPAIDTL 134
Cdd:cd07734  10 GRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIfrGPIYATHPTVALG 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
4P62_A      135 KRGLPDrtdpQFEVAEPVAPVANIVTLAD-----DGVVSVGP---------LALTAVASpGHTPGGTSW 189
Cdd:cd07734  90 RLLLED----YVKSAERIGQDQSLYTPEDieealKHIVPLGYgqsidlfpaLSLTAYNA-GHVLGAAMW 153
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 81-186 8.87e-08

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 51.40  E-value: 8.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       81 PQILANIRALGFRPEdvrAIVLSHEHFDHAGSLAELQKATGAPVY----ARAPAIDTL-----KRGLPDrtdpqfevAEP 151
Cdd:cd07737  34 DKILQAIEDLGLTLK---KILLTHGHLDHVGGAAELAEHYGVPIIgphkEDKFLLENLpeqsqMFGFPP--------AEA 102

                        90       100       110
                ....*....|....*....|....*....|....*
4P62_A      152 VAPVAnivTLADDGVVSVGPLALTAVASPGHTPGG 186
Cdd:cd07737 103 FTPDR---WLEEGDTVTVGNLTLEVLHCPGHTPGH 134
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 49-183 4.82e-07

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 49.07  E-value: 4.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       49 NTWYVGTcGISALLVtsDAGhilvdaatpQAGPQILANIRAL--GFRPEDVRAIVLSHEHFDHAGSLAELQKAtgapvyA 126
Cdd:cd07722  19 NTYLVGT-GKRRILI--DTG---------EGRPSYIPLLKSVldSEGNATISDILLTHWHHDHVGGLPDVLDL------L 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
4P62_A      127 RAPAIDTLKRGLPDRTDPQFEVAEPVAPvanivtLADDGVVSVGPLALTAVASPGHT 183
Cdd:cd07722  81 RGPSPRVYKFPRPEEDEDPDEDGGDIHD------LQDGQVFKVEGATLRVIHTPGHT 131
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 70-186 6.54e-07

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. 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: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 48.78  E-value: 6.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       70 ILVDAATPQAgpQILANIRALGFRPEDVraiVLSHEHFDHAGSLAELQKatgapVYARAPAIDTLKRGLPDRTDPQFEVA 149
Cdd:cd07712  21 LLIDTGLGIG--DLKEYVRTLTDLPLLV---VATHGHFDHIGGLHEFEE-----VYVHPADAEILAAPDNFETLTWDAAT 90

                        90       100       110
                ....*....|....*....|....*....|....*..
4P62_A      150 EPVAPVANIVTLADDGVVSVGPLALTAVASPGHTPGG 186
Cdd:cd07712  91 YSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGS 127
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 51-189 3.12e-06

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.22  E-value: 3.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       51 WYVGTcgiSALLVTSDAGHILVDaatP-QAGPQILANirALGFRPEDVR---AIVLSHEHFDHAG--SLAELqKATGAPV 124
Cdd:COG2220   7 TWLGH---ATFLIETGGKRILID---PvFSGRASPVN--PLPLDPEDLPkidAVLVTHDHYDHLDdaTLRAL-KRTGATV 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4P62_A      125 YArapaidtlkrglpdrtdpQFEVAEPVAP--VANIVTLADDGVVSVGPLALTAV----ASPGHTPGGTSW 189
Cdd:COG2220  78 VA------------------PLGVAAWLRAwgFPRVTELDWGESVELGGLTVTAVparhSSGRPDRNGGLW 130
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 57-116 7.31e-06

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: 45.58  E-value: 7.31e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       57 GISALLVTSDAgHILVDAatpqaGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL 116
Cdd:cd07719  18 GPSTLVVVGGR-VYLVDA-----GSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPAL 71
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 59-121 7.72e-06

Ribonuclease Z; 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. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 45.33  E-value: 7.72e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
4P62_A       59 SALLVTSDAGHILVDAatpqaGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATG 121
Cdd:cd16272  18 SSYLLETGGTRILLDC-----GEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARR 75
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
61-136 8.83e-06

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 46.49  E-value: 8.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       61 LLVTSDAGHILVDAATPQAG----PQILANIRALGFRPEDVRAIVLSHEHFDH-AGSLAELQKATGAPVYARAPAIDTLK 135
Cdd:COG5212  33 LRPLGSDDYVLLDAGTVVSGlelaEQKGAFKGRQGYVLEHIKGYLISHAHLDHiAGLPILSPDDSPKTIYALPETIDALR 112


                .
4P62_A      136 R 136
Cdd:COG5212 113 N 113
PRK02113 PRK02113
MBL fold metallo-hydrolase;
59-139 1.13e-05

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 45.93  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A        59 SALLVTSDAGHILVDAatpqaGPQILANIRALGFRPEDvrAIVLSHEHFDHAGSLAELQ---KATGAPVYARAPAIDTLK 135
Cdd:PRK02113  36 TSALVETEGARILIDC-----GPDFREQMLRLPFGKID--AVLITHEHYDHVGGLDDLRpfcRFGEVPIYAEQYVAERLR 108


                 ....
4P62_A       136 RGLP 139
Cdd:PRK02113 109 SRMP 112
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 50-126 1.21e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 45.57  E-value: 1.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
4P62_A        50 TWYvgtcGISALLVTSDAGHILVDaatpqagPQILANIRAlGFRPEDVRA--IVLSHEHFDHAGSLAELQKATGAPVYA 126
Cdd:PRK00685   4 TWL----GHSAFLIETGGKKILID-------PFITGNPLA-DLKPEDVKVdyILLTHGHGDHLGDTVEIAKRTGATVIA 70
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 83-187 1.57e-05

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 45.09  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       83 ILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLKRGLPDrtdpqfevaEPVAPVANIVTLA 162
Cdd:cd07714  42 IIPDFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELNVPIYATPLTLALIKKKLEE---------FKLIKKVKLNEIK 112

                        90       100       110
                ....*....|....*....|....*....|....*
4P62_A      163 DDGVVSVGPLALTAVA----SPG------HTPGGT 187
Cdd:cd07714 113 PGERIKLGDFEVEFFRvthsIPDsvglaiKTPEGT 147
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-188 1.59e-05

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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 44.56  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       55 TCgisaLLVTSDAGHILVDAatpqaGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLA----ELQKATG----APVYA 126
Cdd:cd07740  17 TC----FHVASEAGRFLIDC-----GASSLIALKRAGIDPNAIDAIFITHLHGDHFGGLPffllDAQFVAKrtrpLTIAG 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
4P62_A      127 RAPAIDTLKRGLP------DRTDPQFEVaepvapvaNIVTLADDGVVSVGPLALTAVASPgHTPGGTS 188
Cdd:cd07740  88 PPGLRERLRRAMEalfpgsSKVPRRFDL--------EVIELEPGEPTTLGGVTVTAFPVV-HPSGALP 146
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 53-119 1.59e-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: 45.23  E-value: 1.59e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4P62_A       53 VGtCGISALLVTSDAGHILVDA----ATPQAGPQILANIRALGFRpeDVRAIVLSHEHFDHAGSLAELQKA 119
Cdd:COG2333   8 VG-QGDAILIRTPDGKTILIDTgprpSFDAGERVVLPYLRALGIR--RLDLLVLTHPDADHIGGLAAVLEA 75
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 60-119 2.62e-05

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: 44.05  E-value: 2.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
4P62_A       60 ALLVTSDAGHILVDA--ATPQAGPQILANIRALGfrpedVR---AIVLSHEHFDHAGSLAELQKA 119
Cdd:cd07731  12 AILIQTPGKTILIDTgpRDSFGEDVVVPYLKARG-----IKkldYLILTHPDADHIGGLDAVLKN 71
NorV COG0426
Flavorubredoxin [Energy production and conversion];
70-135 3.05e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 44.82  E-value: 3.05e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
4P62_A       70 ILVDAATPQAGPQILANIRALgFRPEDVRAIVLSHEHFDHAGSLAE-LQKATGAPVYARAPAIDTLK 135
Cdd:COG0426  45 ALIDTVGESFFEEFLENLSKV-IDPKKIDYIIVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLP 110
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
95-187 8.16e-05

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 43.90  E-value: 8.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       95 EDVRAIVLSHEHFDHAGSLAELQKATGAPVYARAPAIDTLKRGLPDrtdpqfevaEPVAPVANIVTLADDGVVSVGPLAL 174
Cdd:COG0595  62 DKIKGIVLTHGHEDHIGALPYLLKELNVPVYGTPLTLALLEAKLKE---------HGLLKKVKLHVVKPGDRIKFGPFKV 132

                        90       100
                ....*....|....*....|...
4P62_A      175 TAVA---S-PG------HTPGGT 187
Cdd:COG0595 133 EFFRvthSiPDslglaiRTPAGT 155
PRK11539 PRK11539
ComEC family competence protein; Provisional
 83-169 1.15e-04

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 43.44  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A        83 ILANIRALGFRPEDvraIVLSHEHFDHAGSLAELQKA-TGAPVYARAPAIDTL--KRGLPDR-TDPQFEVAEPVAPVANI 158
Cdd:PRK11539 541 IIPWLRWHGLTPEG---IILSHEHLDHRGGLASLLHAwPMAWIRSPLNWANHLpcVRGEQWQwQGLTFSVHWPLEQSNDA 617

                         90
                 ....*....|....*..
4P62_A       159 ------VTLADDGVVSV 169
Cdd:PRK11539 618 gnndscVIRVDDGKHSI 634
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 83-128 1.64e-04

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 42.25  E-value: 1.64e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
4P62_A       83 ILANIRALGFRPEDVRAIVLSHEHFDHAGSLAELQKATGAPVYARA 128
Cdd:cd07728  82 IEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQLVSVFPNA 127
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-250 1.10e-03

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.41  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       58 ISALLVTSDAGHILVDA-ATPQAGPQILANIRALGfrpEDVRAIVLSHEHFDHAGSLAELQKA-TGAPVYARAPAIDTLK 135
Cdd:cd07739  16 VTSTLIYGETEAVLVDAqFTRADAERLADWIKASG---KTLTTIYITHGHPDHYFGLEVLLEAfPDAKVVATPAVVAHIK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A      136 RGLPD---RTDPQFEVAEPVAPVanIVTLADDGVVSVGPLALTAVASPGHTPGGTSWTW-RSCE----GDdcrqMVYads 207
Cdd:cd07739  93 AQLEPklaFWGPLLGGNAPARLV--VPEPLDGDTLTLEGHPLEIVGVGGGDTDDTTYLWiPSLKtvvaGD----VVY--- 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
4P62_A      208 ltaisDDVYRYSDDAAHPGYLAAFRNTLARVAALDCDILVTPH 250
Cdd:cd07739 164 -----NGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH 201
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-111 1.26e-03

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: 39.10  E-value: 1.26e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
4P62_A       69 HILVDaatPqaGPQILANIRALGFRPEDVRAIVLSHEHFDHAG 111
Cdd:cd07741  31 NIHID---P--GPGALVRMCRPKLDPTKLDAIILSHRHLDHSN 68
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 62-136 1.83e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 39.02  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       62 LVTSDAGHILVDA-ATPQAGPQILANIRA-LGFRPedVRAIVLSHEHFDH---AGSLAELQKATGAPVYARAPAIDTLKR 136
Cdd:cd07710  22 FIEGDTGLIIIDTlESAEAAKAALELFRKhTGDKP--VKAIIYTHSHPDHfggAGGFVEEEDSGKVPIIAPEGFMEEAVS 99
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 61-126 1.90e-03

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 38.37  E-value: 1.90e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
4P62_A       61 LLVTSDAGHILVDAATPQagpqiLANIralgFRPEDVRAIVLSHEHFDHAGSLAELQKATGA--PVYA 126
Cdd:cd07736  40 ALIEVDGERILLDAGLTD-----LAER----FPPGSIDAILLTHFHMDHVQGLFHLRWGVGDpiPVYG 98
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 56-136 3.33e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 38.35  E-value: 3.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       56 CGISALLV--TSDAGHILVDAATP--------QAGPQILANIRALGFRPEDVRAIVLSHEHFDHAGSLAEL------QKA 119
Cdd:cd07735  15 GNTSSFLLdpAGSDGDILLDAGTGvgalsleeMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPLLspndggQRG 94

                        90
                ....*....|....*..
4P62_A      120 TGAPVYARAPAIDTLKR 136
Cdd:cd07735  95 SPKTIYGLPETIDALKK 111
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-177 3.58e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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, 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 37.98  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4P62_A       54 GTCgisaLLVTSDAGHILVDAATPQAGPQ-------------ILANIRALGFRPE-----------DVRAIVLSHEHFDH 109
Cdd:cd07732  13 GNC----IEVETGGTRILLDFGLPLDPESkyfdevldflelgLLPDIVGLYRDPLllgglrseedpSVDAVLLSHAHLDH 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
4P62_A      110 AGSLAELqkATGAPVYARAPAIDTLKRGLpdrtdPQFEVAEPVAPvaNIVTLADDGVVSVGPLALTAV 177
Cdd:cd07732  89 YGLLNYL--RPDIPVYMGEATKRILKALL-----PFFGEGDPVPR--NIRVFESGKSFTIGDFTVTPY 147
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 100-135 6.54e-03

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 37.82  E-value: 6.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
4P62_A       100 IVLSHEHFDHAGSLAEL-QKATGAPVYARAPAIDTLK 135
Cdd:PRK05452  75 IVINHAEEDHAGALTELmAQIPDTPIYCTANAIDSIN 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH