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Conserved domains on  [gi|18043760|gb|AAH19817|]
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Hydroxyacyl glutathione hydrolase [Mus musculus]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 1004484)

hydroxyacylglutathione hydrolase catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid

CATH:  3.60.15.10
EC:  3.1.2.6
Gene Ontology:  GO:0004416|GO:0019243|GO:0046872
SCOP:  4002292

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 1-256 1.45e-132

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 374.87  E-value: 1.45e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    1 MKVELLPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGD- 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   80 DRIGALTHKVTHLSTLQVGS-LSVKCLSTPCHTSGHICYFV-SKPGssEPSAVFTGDTLFVAGCGKFYEGTADEMYKALL 157
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVtGKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  158 EVLGRLPPDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAG 237
Cdd:PLN02469 159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250
                 ....*....|....*....
gi 18043760  238 ETDPVTTMRAIRREKDQFK 256
Cdd:PLN02469 239 CESPVEALREVRKMKDNWK 257
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-256 1.45e-132

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 374.87  E-value: 1.45e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    1 MKVELLPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGD- 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   80 DRIGALTHKVTHLSTLQVGS-LSVKCLSTPCHTSGHICYFV-SKPGssEPSAVFTGDTLFVAGCGKFYEGTADEMYKALL 157
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVtGKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  158 EVLGRLPPDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAG 237
Cdd:PLN02469 159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250
                 ....*....|....*....
gi 18043760  238 ETDPVTTMRAIRREKDQFK 256
Cdd:PLN02469 239 CESPVEALREVRKMKDNWK 257
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-255 2.97e-105

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 305.23  E-value: 2.97e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760     6 LPALTDNYMYLIIDEDTQeAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYGG-DDRIGA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    85 LTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFvskpgSSEPSAVFTGDTLFVAGCGKFYEGTADEMYKALLEvLGRLP 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   165 PDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGET--DPV 242
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQgaDPV 235

                         250
                  ....*....|...
gi 18043760   243 TTMRAIRREKDQF 255
Cdd:TIGR03413 236 EVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-173 6.42e-95

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: 275.88  E-value: 6.42e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   6 LPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGG-DDRIGA 84
Cdd:cd07723   3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  85 LTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCGKFYEGTADEMYKALLEVLGrLP 164
Cdd:cd07723  83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LP 156


                ....*....
gi 18043760 165 PDTKVYCGH 173
Cdd:cd07723 157 DDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-255 1.34e-43

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 142.58  E-value: 1.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   174 EYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGETDPVTTMRAIRREKD 253
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 18043760   254 QF 255
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-196 4.93e-34

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: 122.11  E-value: 4.93e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   3 VELLPALTDNYMYLIIDEDtqEAAIVDP----VQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYGG 78
Cdd:COG0491   6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  79 DDRIGALTHK----------------VTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCG 142
Cdd:COG0491  83 AAEAEALEAPaagalfgrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK-----VLFTGDALFSGGVG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18043760 143 K--FYEGTADEMYKAlLEVLGRLPPDTkVYCGHEYTVNNLKFARHVEpGNAAIQEK 196
Cdd:COG0491 158 RpdLPDGDLAQWLAS-LERLLALPPDL-VIPGHGPPTTAEAIDYLEE-LLAALGER 210
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-173 2.64e-27

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: 103.79  E-value: 2.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760     13 YMYLIIDEDtqEAAIVDPV--QPQKVIEAAKKHHV-KLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYG------------ 77
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760     78 -------GDDRIGALTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVskpgsSEPSAVFTGDTLFVAGCG-KFYEGTA 149
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 18043760    150 DEMYKALLEVLGRL-PPDTKVYCGH 173
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-256 1.45e-132

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 374.87  E-value: 1.45e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    1 MKVELLPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGD- 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   80 DRIGALTHKVTHLSTLQVGS-LSVKCLSTPCHTSGHICYFV-SKPGssEPSAVFTGDTLFVAGCGKFYEGTADEMYKALL 157
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVtGKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  158 EVLGRLPPDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAG 237
Cdd:PLN02469 159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250
                 ....*....|....*....
gi 18043760  238 ETDPVTTMRAIRREKDQFK 256
Cdd:PLN02469 239 CESPVEALREVRKMKDNWK 257
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-255 2.97e-105

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 305.23  E-value: 2.97e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760     6 LPALTDNYMYLIIDEDTQeAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYGG-DDRIGA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    85 LTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFvskpgSSEPSAVFTGDTLFVAGCGKFYEGTADEMYKALLEvLGRLP 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   165 PDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGET--DPV 242
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQgaDPV 235

                         250
                  ....*....|...
gi 18043760   243 TTMRAIRREKDQF 255
Cdd:TIGR03413 236 EVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-173 6.42e-95

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: 275.88  E-value: 6.42e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   6 LPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGG-DDRIGA 84
Cdd:cd07723   3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  85 LTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCGKFYEGTADEMYKALLEVLGrLP 164
Cdd:cd07723  83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LP 156


                ....*....
gi 18043760 165 PDTKVYCGH 173
Cdd:cd07723 157 DDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-255 6.04e-72

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 223.18  E-value: 6.04e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    1 MKVELLPALTDNYMYLIIDEDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLvKLEPGLKVYGGD- 79
Cdd:PLN02398  76 LQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLEL-KARYGAKVIGSAv 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   80 --DRIGALTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVskPGSSepsAVFTGDTLFVAGCGKFYEGTADEMYKALL 157
Cdd:PLN02398 155 dkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF--PGSG---AIFTGDTLFSLSCGKLFEGTPEQMLSSLQ 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  158 EVLGrLPPDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAG 237
Cdd:PLN02398 230 KIIS-LPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLS 308

                        250       260
                 ....*....|....*....|.
gi 18043760  238 ETDPVT---TMRAIRREKDQF 255
Cdd:PLN02398 309 IPDTADeaeALGIIRRAKDNF 329
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-255 6.93e-50

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 164.23  E-value: 6.93e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    1 MKVELLPALTDNYMYLIIDeDTQEAAIVDPVQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYG-GD 79
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLND-EAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGpQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   80 DRIGALTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFvSKPgssepsAVFTGDTLFVAGCGKFYEGTADEMYKALLEV 159
Cdd:PRK10241  80 TQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-SKP------YLFCGDTLFSGGCGRLFEGTASQMYQSLKKI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  160 lGRLPPDTKVYCGHEYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRV----------KE 229
Cdd:PRK10241 153 -NALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTedidlinvinEE 231

                        250       260
                 ....*....|....*....|....*.
gi 18043760  230 KTVQQhagetdPVTTMRAIRREKDQF 255
Cdd:PRK10241 232 TLLQQ------PEERFAWLRSKKDRF 251
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-255 1.34e-43

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 142.58  E-value: 1.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   174 EYTVNNLKFARHVEPGNAAIQEKLAWAKEKYAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGETDPVTTMRAIRREKD 253
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 18043760   254 QF 255
Cdd:pfam16123  81 NF 82
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-173 2.65e-43

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: 144.99  E-value: 2.65e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  11 DNYMYLIIDEDTQEAAIVDPV-QPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVY-------GGDDRI 82
Cdd:cd16275  11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLA-KYDAPVYmskeeidYYGFRC 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  83 GALtHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSkpgssepSAVFTGDTLFVAGCG--KFYEGTADEMYKAlLEVL 160
Cdd:cd16275  90 PNL-IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLG-------DSLFTGDTLFIEGCGrcDLPGGDPEEMYES-LQRL 160

                       170
                ....*....|....
gi 18043760 161 GRL-PPDTKVYCGH 173
Cdd:cd16275 161 KKLpPPNTRVYPGH 174
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-175 2.03e-36

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: 127.13  E-value: 2.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  15 YLIIDEDTQEAAIVDPV--QPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLvKLEPGLKVYGGDDRIGALTHK-VTH 91
Cdd:cd07724  15 YLVGDPETGEAAVIDPVrdSVDRYLDLAAELGLKITYVLETHVHADHVSGAREL-AERTGAPIVIGEGAPASFFDRlLKD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  92 LSTLQVGSLSVKCLSTPCHTSGHICYFVskpgsSEPSAVFTGDTLFVAGCG-----KFYEGTADEMYKALLEVLGRLPPD 166
Cdd:cd07724  94 GDVLELGNLTLEVLHTPGHTPESVSYLV-----GDPDAVFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQRKLLLLPDE 168


                ....*....
gi 18043760 167 TKVYCGHEY 175
Cdd:cd07724 169 TLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-173 1.15e-35

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: 125.48  E-value: 1.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  15 YLIIDEDtQEAAIVDPVQP--QKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYGGDDRIGALTHKVTHL 92
Cdd:cd06262  13 YLVSDEE-GEAILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKE-APGAPVYIHEADAELLEDPELNL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  93 S--------------------TLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCGK--FYEGTAD 150
Cdd:cd06262  91 AffgggplpppepdilledgdTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFAGSIGRtdLPGGDPE 165

                       170       180
                ....*....|....*....|...
gi 18043760 151 EMYKALLEVLGRLPPDTKVYCGH 173
Cdd:cd06262 166 QLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-196 4.93e-34

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: 122.11  E-value: 4.93e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   3 VELLPALTDNYMYLIIDEDtqEAAIVDP----VQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYGG 78
Cdd:COG0491   6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  79 DDRIGALTHK----------------VTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCG 142
Cdd:COG0491  83 AAEAEALEAPaagalfgrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK-----VLFTGDALFSGGVG 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18043760 143 K--FYEGTADEMYKAlLEVLGRLPPDTkVYCGHEYTVNNLKFARHVEpGNAAIQEK 196
Cdd:COG0491 158 RpdLPDGDLAQWLAS-LERLLALPPDL-VIPGHGPPTTAEAIDYLEE-LLAALGER 210
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-173 2.64e-27

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: 103.79  E-value: 2.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760     13 YMYLIIDEDtqEAAIVDPV--QPQKVIEAAKKHHV-KLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYG------------ 77
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760     78 -------GDDRIGALTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVskpgsSEPSAVFTGDTLFVAGCG-KFYEGTA 149
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 18043760    150 DEMYKALLEVLGRL-PPDTKVYCGH 173
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 15-173 6.45e-25

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: 98.19  E-value: 6.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  15 YLIIDEDTQEAAIVDP-VQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLvKLEPGLKVY----------------- 76
Cdd:cd16322  14 YLVADEGGGEAVLVDPgDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYlhpddlplyeaadlgak 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  77 ----GGDDRIGAlTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCGKFYEGTADE- 151
Cdd:cd16322  93 afglGIEPLPPP-DRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG-----LLFSGDLLFQGSIGRTDLPGGDPk 166

                       170       180
                ....*....|....*....|...
gi 18043760 152 -MYKALLEVLgRLPPDTKVYCGH 173
Cdd:cd16322 167 aMAASLRRLL-TLPDETRVFPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 15-173 1.93e-22

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: 91.08  E-value: 1.93e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  15 YLIIDEDTQEAAIVDP-VQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEpGLKVYGG--DDR--IGAL---- 85
Cdd:cd07737  14 SLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHY-GVPIIGPhkEDKflLENLpeqs 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  86 -------------THKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFvskpgSSEPSAVFTGDTLFVAGCGK--FYEGTAD 150
Cdd:cd07737  93 qmfgfppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-----NRESKLAIVGDVLFKGSIGRtdFPGGNHA 167

                       170       180
                ....*....|....*....|...
gi 18043760 151 EMYKALLEVLGRLPPDTKVYCGH 173
Cdd:cd07737 168 QLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-175 1.98e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 79.07  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   13 YMYLIIDEDTQE--AAIVDPVQP--QKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGDDRIGALTHK 88
Cdd:PLN02962  24 YTYLLADVSHPDkpALLIDPVDKtvDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKASGSKADLF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   89 VTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSK-PGSSEPSAVFTGDTLFVAGCGK--FYEGTADEMYKALLEVLGRLPP 165
Cdd:PLN02962 104 VEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVHSQIFTLPK 183

                        170
                 ....*....|
gi 18043760  166 DTKVYCGHEY 175
Cdd:PLN02962 184 DTLIYPAHDY 193
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-173 9.71e-14

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: 68.02  E-value: 9.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   2 KVELLPALTDNYMYLIIDEDtqEAAIVD---PVQPQKVIEAAKKHHVK---LTTVLTTHHHWDHAGGNEKLVKlEPGLKV 75
Cdd:cd07721   1 GVYQLPLLPPVNAYLIEDDD--GLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKE-APGAPV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  76 YGGDDRIGALTHKVTHLSTLQVGSL----------------------------SVKCLSTPCHTSGHICYFVSKPGssep 127
Cdd:cd07721  78 YAHEREAPYLEGEKPYPPPVRLGLLgllspllpvkpvpvdrtledgdtldlagGLRVIHTPGHTPGHISLYLEEDG---- 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18043760 128 sAVFTGDTLFVAG---CGKFYEGTAD-EMYKALLEVLGRLPPDTkVYCGH 173
Cdd:cd07721 154 -VLIAGDALVTVGgelVPPPPPFTWDmEEALESLRKLAELDPEV-LAPGH 201
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-135 1.46e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 64.43  E-value: 1.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  15 YLIidEDTQEAAIVDPvQP------QKVIEAAKKHHVKLttVLTTHHHWDHAGGNEKLVKLePGLKVYGGDDRIGAL--- 85
Cdd:cd16278  21 YLL--GAPDGVVVIDP-GPddpahlDALLAALGGGRVSA--ILVTHTHRDHSPGAARLAER-TGAPVRAFGPHRAGGqdt 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18043760  86 ----THKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDT 135
Cdd:cd16278  95 dfapDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDH 143
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-173 6.41e-12

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: 62.55  E-value: 6.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  34 QKVIEAAKKHHVklTTVLTTHHHWDHAGGNEKLVKL--EPGLKVY-----GGDDRIGALTHKVTHLS---TLQVGSLSVK 103
Cdd:cd07722  46 KSVLDSEGNATI--SDILLTHWHHDHVGGLPDVLDLlrGPSPRVYkfprpEEDEDPDEDGGDIHDLQdgqVFKVEGATLR 123

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18043760 104 CLSTPCHTSGHICYFVskpgsSEPSAVFTGDTlfVAGcgkfyEGTAD-EMYKAL---LEVLGRLPPdTKVYCGH 173
Cdd:cd07722 124 VIHTPGHTTDHVCFLL-----EEENALFTGDC--VLG-----HGTAVfEDLAAYmasLKKLLSLGP-GRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-173 1.26e-11

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: 62.12  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  15 YLIIDEDtqEAAIVDP------VQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVY------------ 76
Cdd:cd07726  19 YLLDGEG--RPALIDTgpsssvPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYvhprgarhlidp 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  77 ------------------GGD------DRIGALTHKvthlSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGSsepsaVFT 132
Cdd:cd07726  97 sklwasaravygdeadrlGGEilpvpeERVIVLEDG----ETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG-----LFT 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18043760 133 GDTLFVAGCGKFYEGTAD--------EMYKALLEVLGRLPPDtKVYCGH 173
Cdd:cd07726 168 GDAAGVRYPELDVVGPPStpppdfdpEAWLESLDRLLSLKPE-RIYLTH 215
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 9-173 2.60e-11

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: 60.78  E-value: 2.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   9 LTDNYMYLIIDE--DTQEAAIvdpvQPQKVIEAAKKHHVKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVYGGDDRIgalt 86
Cdd:cd07725  20 LRDGDETTLIDTglATEEDAE----ALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQE-KSGATVYILDVTP---- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  87 hkVTHLSTLQVGSLSVKCLSTPCHTSGHICYFvskpgSSEPSAVFTGDTL--FVAGCGKFYEGTADEMYKALLEVLGRLP 164
Cdd:cd07725  91 --VKDGDKIDLGGLRLKVIETPGHTPGHIVLY-----DEDRRELFVGDAVlpKITPNVSLWAVRVEDPLGAYLESLDKLE 163

                       170
                ....*....|.
gi 18043760 165 --PDTKVYCGH 173
Cdd:cd07725 164 klDVDLAYPGH 174
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-173 9.24e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.61  E-value: 9.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    15 YLIIDEDtqEAAIVDPV--QPQKVIEAAKKHHVK---LTTVLTTHHHWDHAGGNEKLVK-------LEPGLKVYGGDD-- 80
Cdd:pfam00753   9 YLIEGGG--GAVLIDTGgsAEAALLLLLAALGLGpkdIDAVILTHGHFDHIGGLGELAEatdvpviVVAEEARELLDEel 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760    81 -----RIGALTHKVTHLST------LQVGSLSVKCLS-TPCHTSGHICYFVSKPGSsepSAVFTGDTLFVAGCGKFYEGT 148
Cdd:pfam00753  87 glaasRLGLPGPPVVPLPPdvvleeGDGILGGGLGLLvTHGPGHGPGHVVVYYGGG---KVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 18043760   149 AD---------EMYKALLEVLGRLPPDtKVYCGH 173
Cdd:pfam00753 164 GGllvlhpssaESSLESLLKLAKLKAA-VIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-173 8.63e-07

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: 48.33  E-value: 8.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  16 LIIDEDtqEAAIVD----PVQPQKVIEAAKKH-HVKLTTVLTTHHHWDHAGGN-------------------------EK 65
Cdd:cd16282  19 FIVGDD--GVVVIDtgasPRLARALLAAIRKVtDKPVRYVVNTHYHGDHTLGNaafadagapiiahentreelaargeAY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  66 LVKLEPGLKVYGGDDRIGALTHKVTHLSTLQVGSLSVKCLST-PCHTSGHICYFVskpgssePSA--VFTGDTLFVAGCG 142
Cdd:cd16282  97 LELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWL-------PEEgvLFAGDLVFNGRIP 169

                       170       180       190
                ....*....|....*....|....*....|.
gi 18043760 143 KFYEGTADEMYKAlLEVLGRLPPDTKVyCGH 173
Cdd:cd16282 170 FLPDGSLAGWIAA-LDRLLALDATVVV-PGH 198
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 16-115 4.28e-06

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: 46.04  E-value: 4.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  16 LIIDEDTQeaAIVDPVQP---QKVIEAAKKHHVKL---TTVLTTHHHWDHAGGNEklvkLEPGLKVYGGDDRIGALTHKV 89
Cdd:cd07711  26 LIKDGGKN--ILVDTGTPwdrDLLLKALAEHGLSPediDYVVLTHGHPDHIGNLN----LFPNATVIVGWDICGDSYDDH 99

                        90       100
                ....*....|....*....|....*...
gi 18043760  90 ThLSTLQVGSLS--VKCLSTPCHTSGHI 115
Cdd:cd07711 100 S-LEEGDGYEIDenVEVIPTPGHTPEDV 126
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 13-173 8.46e-06

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: 44.93  E-value: 8.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  13 YMYLIIDEDtqEAAIVDPVQPqkvIEAAKKHHVKLT----TVLTTHHHWDHAGGN-------------------EKLVKL 69
Cdd:cd07712  10 NIYLLRGRD--RALLIDTGLG---IGDLKEYVRTLTdlplLVVATHGHFDHIGGLhefeevyvhpadaeilaapDNFETL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  70 EPGLKVYGGDDriGALTHKVTHLSTLQVGSLSVKCLSTPCHTSGHICYFVSKPGssepsAVFTGDTLFVAGCGKFYEGTA 149
Cdd:cd07712  85 TWDAATYSVPP--AGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANR-----LLFSGDVVYDGPLIMDLPHSD 157

                       170       180
                ....*....|....*....|....*
gi 18043760 150 DEMYKALLEVLGRLPPD-TKVYCGH 173
Cdd:cd07712 158 LDDYLASLEKLSKLPDEfDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 11-76 1.09e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 44.83  E-value: 1.09e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18043760  11 DNYMYLI---IDEDTQEAAivdpvqpQKVIEAAKKhhvKLTTVLTTHHHWDHAGGNEKLVKlEPGLKVY 76
Cdd:cd07743  17 DKEALLIdsgLDEDAGRKI-------RKILEELGW---KLKAIINTHSHADHIGGNAYLQK-KTGCKVY 74
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 9-140 4.21e-05

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: 43.59  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760   9 LTDNYMYLIIDEDTQEAAivdpvqpqKVIEA-AKKHHVKLTTV---LTTHHHWDHAGGNEKLvKLEPGLKVYGGDDRIGA 84
Cdd:cd16310  27 ITSNHGAILLDGGLEENA--------ALIEQnIKALGFKLSDIkiiINTHAHYDHAGGLAQL-KADTGAKLWASRGDRPA 97

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18043760  85 LTH-----------------KVTHL----STLQVGSLSVKCLSTPCHTSGHICYFVSKPGSSEPSAVFTGDTLFVAG 140
Cdd:cd16310  98 LEAgkhigdnitqpapfpavKVDRIlgdgEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGRPLRVVFPCSLSVAG 174
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 50-192 6.14e-05

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: 43.31  E-value: 6.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  50 VLTTHHHWDHAGGNEKLVKLEpGLKVYGGDDRIGAL-----------------------THKVTHLSTLQVGSLSVKCLS 106
Cdd:cd16313  64 ILSSHDHWDHAGGIAALQKLT-GAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760 107 TPCHTSGHICY-FVSKPGSSEPSAVFtGDTLFVAGCGKF-YEG--TADEMYKALLEVLGRLPPDTKVYCGHEYTVNNLKF 182
Cdd:cd16313 143 TPGHTTGGTSWtWQSCEQGRCANMVF-ADSLTAVSADGYrFSAhpAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRV 221

                       170
                ....*....|
gi 18043760 183 ARHVEPGNAA 192
Cdd:cd16313 222 KRGAAEGNAA 231
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
46-150 8.73e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 39.79  E-value: 8.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18043760  46 KLTTVLTTHHHWDHAGG------NEKLVKLEPGLKVYG---GDDRIGALT-------------HKVTHLSTLQVGSLSVK 103
Cdd:COG1234  52 DIDAIFITHLHGDHIAGlpgllsTRSLAGREKPLTIYGppgTKEFLEALLkasgtdldfplefHEIEPGEVFEIGGFTVT 131

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18043760 104 CLSTpCHTSGHICYFVSKPGSsepSAVFTGDTLFVAGCGKFYEGtAD 150
Cdd:COG1234 132 AFPL-DHPVPAYGYRFEEPGR---SLVYSGDTRPCEALVELAKG-AD 173
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
40-80 2.21e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 38.71  E-value: 2.21e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18043760  40 AKKHHVKLTT----VLTtHHHWDHAGGNEKLVKLEPGLKVYGGDD 80
Cdd:COG1237  48 AEKLGIDLSDidavVLS-HGHYDHTGGLPALLELNPKAPVYAHPD 91
 
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.
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