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Conserved domains on  [gi|1134132600|ref|WP_076375595|]
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rhodanese-like domain-containing protein [Filimonas lacunae]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869982)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.30|3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|11471246|12177301|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-184 1.55e-76

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: 236.91  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   2 YIEQLYTGCLSEAAYYIESE--GEAAIIDPLRDIA-PYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGP 78
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPetGEAAVIDPVRDSVdRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  79 DAKARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAQNGEDltthsLA 158
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPD----AVFTGDTLFVGDVGRPDLPGEAEG-----LA 151

                         170       180
                  ....*....|....*....|....*.
gi 1134132600 159 GMLYDSLQKRIIPLADDVIVYPAHGA 184
Cdd:cd07724   152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 357-465 5.71e-26

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 101.58  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 357 DMIINIEPDELAMDLPfDDRLIVVDVRKEVEFADGHVKDAVNIPLANLtdPASMSAIQDDDNLYLHCASGYRSVIAASIM 436
Cdd:COG0607     1 ASVKEISPAELAELLE-SEDAVLLDVREPEEFAAGHIPGAINIPLGEL--AERLDELPKDKPIVVYCASGGRSAQAAALL 77

                          90       100
                  ....*....|....*....|....*....
gi 1134132600 437 KKQGIHNLRNVLGGWKAIKEEEKiPTEKS 465
Cdd:COG0607    78 RRAGYTNVYNLAGGIEAWKAAGL-PVEKG 105
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 254-356 8.17e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


:

Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 73.08  E-value: 8.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 254 ALKPLSVAEFKAIAADKDATILDTRPGATFSEAFIPDSIFIGLeGRFAEWAGNlLSFDKPILLVSPEGQ-EKETVIRLTR 332
Cdd:COG0607     2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE-LPKDKPIVVYCASGGrSAQAAALLRR 79

                          90       100
                  ....*....|....*....|....
gi 1134132600 333 VGFSLFeGYLEGGFDSWIKAGEPT 356
Cdd:COG0607    80 AGYTNV-YNLAGGIEAWKAAGLPV 102
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-184 1.55e-76

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: 236.91  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   2 YIEQLYTGCLSEAAYYIESE--GEAAIIDPLRDIA-PYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGP 78
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPetGEAAVIDPVRDSVdRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  79 DAKARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAQNGEDltthsLA 158
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPD----AVFTGDTLFVGDVGRPDLPGEAEG-----LA 151

                         170       180
                  ....*....|....*....|....*.
gi 1134132600 159 GMLYDSLQKRIIPLADDVIVYPAHGA 184
Cdd:cd07724   152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 15-184 1.36e-37

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: 136.74  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  15 AYYIESEGEAAIIDP---LRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAKARFDA----- 86
Cdd:COG0491    17 SYLIVGGDGAVLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEApaaga 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  87 ----------VVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAqnGEDLTThs 156
Cdd:COG0491    97 lfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK----VLFTGDALFSGGVGRPDLP--DGDLAQ-- 168

                         170       180
                  ....*....|....*....|....*...
gi 1134132600 157 lagmLYDSLQkRIIPLADDViVYPAHGA 184
Cdd:COG0491   169 ----WLASLE-RLLALPPDL-VIPGHGP 190
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 357-465 5.71e-26

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 101.58  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 357 DMIINIEPDELAMDLPfDDRLIVVDVRKEVEFADGHVKDAVNIPLANLtdPASMSAIQDDDNLYLHCASGYRSVIAASIM 436
Cdd:COG0607     1 ASVKEISPAELAELLE-SEDAVLLDVREPEEFAAGHIPGAINIPLGEL--AERLDELPKDKPIVVYCASGGRSAQAAALL 77

                          90       100
                  ....*....|....*....|....*....
gi 1134132600 437 KKQGIHNLRNVLGGWKAIKEEEKiPTEKS 465
Cdd:COG0607    78 RRAGYTNVYNLAGGIEAWKAAGL-PVEKG 105
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-182 1.06e-25

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: 103.02  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   15 AYYIESEGEAAIIDPL--RDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPII----------------- 75
Cdd:smart00849   2 SYLVRDDGGAILIDTGpgEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYapegtaellkdllallg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   76 -YGPDAKARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAQNGEDLTt 154
Cdd:smart00849  82 eLGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK----ILFTGDLLFAGGDGRTLVDGGDAAAS- 156

                          170       180
                   ....*....|....*....|....*...
gi 1134132600  155 hslagMLYDSLQKRIIPLADdvIVYPAH 182
Cdd:smart00849 157 -----DALESLLKLLKLLPK--LVVPGH 177
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 368-455 3.80e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 90.44  E-value: 3.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 368 AMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGIHNLRNV 447
Cdd:cd00158     2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNL 81


                  ....*...
gi 1134132600 448 LGGWKAIK 455
Cdd:cd00158    82 EGGMLAWK 89
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 10-207 4.85e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 86.35  E-value: 4.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  10 CLSEA-AYYI--ESEGEAAIIDPLrDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYG---PDAKAR 83
Cdd:PLN02469    8 CLEDNyAYLIidESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgslDNVKGC 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  84 FDAVvaADGQKFTLGK-LQIEVLHTPGHTLESACFLLKDENGKDYAVFTGDTLFVGDVGRpdlaqngedlTTHSLAGMLY 162
Cdd:PLN02469   87 THPV--ENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPAVFTGDTLFIAGCGK----------FFEGTAEQMY 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134132600 163 DSLQKRIIPLADDVIVYPAHG-AGSNC-------------GKKLGAATQ----------STIGEEKQSN 207
Cdd:PLN02469  155 QSLCVTLGSLPKPTQVYCGHEyTVKNLkfaltvepdneklKQKLEWAEKqrqaglptvpSTIEEELETN 223
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 373-457 3.70e-17

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 76.73  E-value: 3.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  373 FDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPAS------------MSAIQDDDNLYLHCASGYRSVIAASIMKKQG 440
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldilefeellkRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....*..
gi 1134132600  441 IHNLRNVLGGWKAIKEE 457
Cdd:smart00450  81 FKNVYLLDGGYKEWSAA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 374-455 4.19e-16

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 73.29  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 374 DDRLIVVDVRKEVEFADGHVKDAVNIPLANLTD--------PASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGIHNLR 445
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLpplpllelLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 1134132600 446 NVLGGWKAIK 455
Cdd:pfam00581  83 VLDGGFEAWK 92
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 254-356 8.17e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 73.08  E-value: 8.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 254 ALKPLSVAEFKAIAADKDATILDTRPGATFSEAFIPDSIFIGLeGRFAEWAGNlLSFDKPILLVSPEGQ-EKETVIRLTR 332
Cdd:COG0607     2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE-LPKDKPIVVYCASGGrSAQAAALLRR 79

                          90       100
                  ....*....|....*....|....
gi 1134132600 333 VGFSLFeGYLEGGFDSWIKAGEPT 356
Cdd:COG0607    80 AGYTNV-YNLAGGIEAWKAAGLPV 102
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-182 5.94e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.17  E-value: 5.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   8 TGCLSEAAYYIESEGEAAIIDPL----RDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAK-- 81
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGgsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAre 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  82 ---------------------ARFDAVVAADGQKFTLGKLQIEVLHTPGHTleSACFLLKDENGKdyAVFTGDTLFVGDV 140
Cdd:pfam00753  81 lldeelglaasrlglpgppvvPLPPDVVLEEGDGILGGGLGLLVTHGPGHG--PGHVVVYYGGGK--VLFTGDLLFAGEI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1134132600 141 GRPDLAQNGEDLTTHSLAGMLYDSLQKRIIPLADdvIVYPAH 182
Cdd:pfam00753 157 GRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAA--VIVPGH 196
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
358-453 4.83e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 58.10  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 358 MIINIEPDELAMDLpfDDRLIVVDVRKEVEFADGHVKDAVNIPLANL-TDPASmSAIQDDDNLYLHCASGYRSVIAASIM 436
Cdd:PRK08762    1 SIREISPAEARARA--AQGAVLIDVREAHERASGQAEGALRIPRGFLeLRIET-HLPDRDREIVLICASGTRSAHAAATL 77

                          90       100
                  ....*....|....*....|
gi 1134132600 437 KKQGIHNLRNVLGG---WKA 453
Cdd:PRK08762   78 RELGYTRVASVAGGfsaWKD 97
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 375-453 3.19e-05

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 45.66  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 375 DRLIVVDVRKEVEFADGHVKDAVNIPLanLTD------------------------------PASMSAIQDD----DNLY 420
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPL--LNDeeraevgtlykqvgpfaaiklglalvspnlAAHVEQWRAFadgpPQPL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1134132600 421 LHCA-SGYRSVIAASIMKKQGIHNLRnVLGGWKA 453
Cdd:TIGR03167  79 LYCWrGGMRSGSLAWLLAQIGFRVPR-LEGGYKA 111
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 258-349 2.06e-04

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 40.32  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 258 LSVAEFKA-IAADKDATILDTRPGATFSEAF--IPDSIFIGLEgRFAEWAGnLLSFDKPILLVSPEGQEKETVI-RLTRV 333
Cdd:cd01444     2 ISVDELAElLAAGEAPVLLDVRDPASYAALPdhIPGAIHLDED-SLDDWLG-DLDRDRPVVVYCYHGNSSAQLAqALREA 79

                          90
                  ....*....|....*.
gi 1134132600 334 GFSLFEgYLEGGFDSW 349
Cdd:cd01444    80 GFTDVR-SLAGGFEAW 94
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 269-355 4.74e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 36.67  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  269 DKDATILDTRPGATFSEAFIPDSIFIGLEgRFAEWAGNLLSFDKPILLVSPE-GQEKETVI------RLTRVGFSLFE-G 340
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLS-ELLDRRGELDILEFEELLKRLGlDKDKPVVVycrsgnRSAKAAWLLRElG 80

                           90       100
                   ....*....|....*....|
gi 1134132600  341 Y-----LEGGFDSWIKAGEP 355
Cdd:smart00450  81 FknvylLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 269-349 6.35e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 35.92  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 269 DKDATILDTRPGATFSEAFIPDSIFI------GLEGRFAEWAGNLLSF--DKPILLVSPEGQE-KETVIRLTRVGFSLFe 339
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVplsslsLPPLPLLELLEKLLELlkDKPIVVYCNSGNRaAAAAALLKALGYKNV- 81

                          90
                  ....*....|
gi 1134132600 340 GYLEGGFDSW 349
Cdd:pfam00581  82 YVLDGGFEAW 91
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-184 1.55e-76

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: 236.91  E-value: 1.55e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   2 YIEQLYTGCLSEAAYYIESE--GEAAIIDPLRDIA-PYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGP 78
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPetGEAAVIDPVRDSVdRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  79 DAKARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAQNGEDltthsLA 158
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPD----AVFTGDTLFVGDVGRPDLPGEAEG-----LA 151

                         170       180
                  ....*....|....*....|....*.
gi 1134132600 159 GMLYDSLQKRIIPLADDVIVYPAHGA 184
Cdd:cd07724   152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 15-182 8.63e-39

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: 138.36  E-value: 8.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  15 AYYIESE--GEAAIIDPLrDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPdAKARFDAV--VAA 90
Cdd:cd07723    11 IYLIVDEatGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGP-AEDRIPGLdhPVK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  91 DGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDlaqNGEdltthslAGMLYDSLQKrII 170
Cdd:cd07723    89 DGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP----ALFTGDTLFSGGCGRFF---EGT-------AEQMYASLQK-LL 153

                         170
                  ....*....|..
gi 1134132600 171 PLADDVIVYPAH 182
Cdd:cd07723   154 ALPDDTLVYCGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 15-184 1.36e-37

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: 136.74  E-value: 1.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  15 AYYIESEGEAAIIDP---LRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAKARFDA----- 86
Cdd:COG0491    17 SYLIVGGDGAVLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEApaaga 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  87 ----------VVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAqnGEDLTThs 156
Cdd:COG0491    97 lfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK----VLFTGDALFSGGVGRPDLP--DGDLAQ-- 168

                         170       180
                  ....*....|....*....|....*...
gi 1134132600 157 lagmLYDSLQkRIIPLADDViVYPAHGA 184
Cdd:COG0491   169 ----WLASLE-RLLALPPDL-VIPGHGP 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-182 5.62e-33

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: 123.55  E-value: 5.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   4 EQLYTGCLSEAAYYIESE-GEAAIIDP-LRDIAPYVELATRRNATIKFIFETHFHADfvsgHI----DLSQSTGAPII-- 75
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEeGEAILIDPgAGALEKILEAIEELGLKIKAILLTHGHFD----HIgglaELKEAPGAPVYih 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  76 -----------------YGPDAKARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVG 138
Cdd:cd06262    77 eadaelledpelnlaffGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG----VLFTGDTLFAG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1134132600 139 DVGRPDLAqnGEDLTThslagmLYDSLQKRIIPLADDVIVYPAH 182
Cdd:cd06262   153 SIGRTDLP--GGDPEQ------LIESIKKLLLLLPDDTVVYPGH 188
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 17-182 5.60e-29

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: 111.86  E-value: 5.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  17 YI---ESEGEAAIIDPLRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPI--------IYGPDAKarfD 85
Cdd:cd16275    15 YIiidKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVymskeeidYYGFRCP---N 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  86 AVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDengkdyAVFTGDTLFVGDVGRPDLaqNGEDltthslAGMLYDSL 165
Cdd:cd16275    92 LIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD------SLFTGDTLFIEGCGRCDL--PGGD------PEEMYESL 157

                         170
                  ....*....|....*....
gi 1134132600 166 Q--KRIIPlaDDVIVYPAH 182
Cdd:cd16275   158 QrlKKLPP--PNTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-207 3.80e-26

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: 105.12  E-value: 3.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   3 IEQLYTGCLSEAAYYIESE--GEAAIIDPLRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDA 80
Cdd:cd16322     1 VRPFTLGPLQENTYLVADEggGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  81 KARFDAVVA-------------------ADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVG 141
Cdd:cd16322    81 LPLYEAADLgakafglgieplpppdrllEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG----LLFSGDLLFQGSIG 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134132600 142 RPDLAqnGEDLTThslagmLYDSLqKRIIPLADDVIVYPAHGAGsncgkklgaatqSTIGEEKQSN 207
Cdd:cd16322   157 RTDLP--GGDPKA------MAASL-RRLLTLPDETRVFPGHGPP------------TTLGEERRTN 201
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 357-465 5.71e-26

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 101.58  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 357 DMIINIEPDELAMDLPfDDRLIVVDVRKEVEFADGHVKDAVNIPLANLtdPASMSAIQDDDNLYLHCASGYRSVIAASIM 436
Cdd:COG0607     1 ASVKEISPAELAELLE-SEDAVLLDVREPEEFAAGHIPGAINIPLGEL--AERLDELPKDKPIVVYCASGGRSAQAAALL 77

                          90       100
                  ....*....|....*....|....*....
gi 1134132600 437 KKQGIHNLRNVLGGWKAIKEEEKiPTEKS 465
Cdd:COG0607    78 RRAGYTNVYNLAGGIEAWKAAGL-PVEKG 105
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-182 1.06e-25

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: 103.02  E-value: 1.06e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   15 AYYIESEGEAAIIDPL--RDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPII----------------- 75
Cdd:smart00849   2 SYLVRDDGGAILIDTGpgEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYapegtaellkdllallg 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   76 -YGPDAKARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRPDLAQNGEDLTt 154
Cdd:smart00849  82 eLGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK----ILFTGDLLFAGGDGRTLVDGGDAAAS- 156

                          170       180
                   ....*....|....*....|....*...
gi 1134132600  155 hslagMLYDSLQKRIIPLADdvIVYPAH 182
Cdd:smart00849 157 -----DALESLLKLLKLLPK--LVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 22-182 1.56e-24

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: 100.32  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  22 GEAAIIDPLRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIyGPD-------------AKARFDAVV 88
Cdd:cd07737    22 KEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPII-GPHkedkfllenlpeqSQMFGFPPA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  89 AA--------DGQKFTLGKLQIEVLHTPGHTLESACFLlkdeNGKDYAVFTGDTLFVGDVGRPDLAQ-NGEDLTthslag 159
Cdd:cd07737   101 EAftpdrwleEGDTVTVGNLTLEVLHCPGHTPGHVVFF----NRESKLAIVGDVLFKGSIGRTDFPGgNHAQLI------ 170

                         170       180
                  ....*....|....*....|...
gi 1134132600 160 mlyDSLQKRIIPLADDVIVYPAH 182
Cdd:cd07737   171 ---ASIKEKLLPLGDDVTFIPGH 190
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 368-455 3.80e-22

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 90.44  E-value: 3.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 368 AMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGIHNLRNV 447
Cdd:cd00158     2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNL 81


                  ....*...
gi 1134132600 448 LGGWKAIK 455
Cdd:cd00158    82 EGGMLAWK 89
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-184 5.60e-21

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: 90.24  E-value: 5.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  16 YYIESEGEAAIIDP-------LRDIapyveLATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPII-YGPDAKARFD-- 85
Cdd:cd16278    21 YLLGAPDGVVVIDPgpddpahLDAL-----LAALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRaFGPHRAGGQDtd 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  86 ---AVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGD---VGRPDlaqnGeDLTTHslag 159
Cdd:cd16278    96 fapDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG----ALFTGDHVMGWSttvIAPPD----G-DLGDY---- 162

                         170       180
                  ....*....|....*....|....*
gi 1134132600 160 mlYDSLQkRIIPLADDVIvYPAHGA 184
Cdd:cd16278   163 --LASLE-RLLALDDRLL-LPGHGP 183
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 10-207 4.85e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 86.35  E-value: 4.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  10 CLSEA-AYYI--ESEGEAAIIDPLrDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYG---PDAKAR 83
Cdd:PLN02469    8 CLEDNyAYLIidESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgslDNVKGC 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  84 FDAVvaADGQKFTLGK-LQIEVLHTPGHTLESACFLLKDENGKDYAVFTGDTLFVGDVGRpdlaqngedlTTHSLAGMLY 162
Cdd:PLN02469   87 THPV--ENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPAVFTGDTLFIAGCGK----------FFEGTAEQMY 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134132600 163 DSLQKRIIPLADDVIVYPAHG-AGSNC-------------GKKLGAATQ----------STIGEEKQSN 207
Cdd:PLN02469  155 QSLCVTLGSLPKPTQVYCGHEyTVKNLkfaltvepdneklKQKLEWAEKqrqaglptvpSTIEEELETN 223
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 7-229 1.81e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 81.77  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   7 YTGCLSEAAYyieSEGEAAIIDPL-----RDIAPYVELATRrnatIKFIFETHFHADFVSGH-IDLSQSTGAPIIYGPDA 80
Cdd:PLN02962   24 YTYLLADVSH---PDKPALLIDPVdktvdRDLSLVKELGLK----LIYAMNTHVHADHVTGTgLLKTKLPGVKSIISKAS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  81 KARFDAVVAAdGQKFTLGKLQIEVLHTPGHTLESACFLLKDENGKDYA--VFTGDTLFVGDVGRPDLaQNGEdltthslA 158
Cdd:PLN02962   97 GSKADLFVEP-GDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPrmAFTGDALLIRGCGRTDF-QGGS-------S 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134132600 159 GMLYDSLQKRIIPLADDVIVYPAHGAGSNcgkklgaaTQSTIGEEKQSNyALLAKTRDEFiAAVTEGLNTP 229
Cdd:PLN02962  168 DQLYKSVHSQIFTLPKDTLIYPAHDYKGF--------TVSTVGEEMLYN-PRLTKDEETF-KTIMENLNLP 228
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 373-457 3.70e-17

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 76.73  E-value: 3.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  373 FDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPAS------------MSAIQDDDNLYLHCASGYRSVIAASIMKKQG 440
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldilefeellkRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....*..
gi 1134132600  441 IHNLRNVLGGWKAIKEE 457
Cdd:smart00450  81 FKNVYLLDGGYKEWSAA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 374-455 4.19e-16

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 73.29  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 374 DDRLIVVDVRKEVEFADGHVKDAVNIPLANLTD--------PASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGIHNLR 445
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLpplpllelLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 1134132600 446 NVLGGWKAIK 455
Cdd:pfam00581  83 VLDGGFEAWK 92
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 254-356 8.17e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 73.08  E-value: 8.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 254 ALKPLSVAEFKAIAADKDATILDTRPGATFSEAFIPDSIFIGLeGRFAEWAGNlLSFDKPILLVSPEGQ-EKETVIRLTR 332
Cdd:COG0607     2 SVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE-LPKDKPIVVYCASGGrSAQAAALLRR 79

                          90       100
                  ....*....|....*....|....
gi 1134132600 333 VGFSLFeGYLEGGFDSWIKAGEPT 356
Cdd:COG0607    80 AGYTNV-YNLAGGIEAWKAAGLPV 102
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 21-184 8.42e-16

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: 75.26  E-value: 8.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  21 EGEAAIIDPLRDIapyveLATRRNATIKFIFETHFHADFVSGHIDLSQ--STGAPIIY--------GPDAKARFDAVVAA 90
Cdd:cd07722    36 EGRPSYIPLLKSV-----LDSEGNATISDILLTHWHHDHVGGLPDVLDllRGPSPRVYkfprpeedEDPDEDGGDIHDLQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  91 DGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLfvgdvgrpdLAQNG---EDLTThslagmlY-DSLq 166
Cdd:cd07722   111 DGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN----ALFTGDCV---------LGHGTavfEDLAA-------YmASL- 169

                         170
                  ....*....|....*...
gi 1134132600 167 KRIIPLADDVIvYPAHGA 184
Cdd:cd07722   170 KKLLSLGPGRI-YPGHGP 186
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 10-182 2.23e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 76.81  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  10 CLSEAAYYI---ESEGEAAIIDPlRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAKARFDA 86
Cdd:PLN02398   83 CLKDNYAYLlhdEDTGTVGVVDP-SEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPG 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  87 --VVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVGRpdLAQNGEDltthslagMLYDS 164
Cdd:PLN02398  162 idIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSG----AIFTGDTLFSLSCGK--LFEGTPE--------QMLSS 227

                         170
                  ....*....|....*...
gi 1134132600 165 LQKrIIPLADDVIVYPAH 182
Cdd:PLN02398  228 LQK-IISLPDDTNIYCGH 244
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 362-452 5.26e-15

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 70.37  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDEL-AMDLpfdDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDpaSMSAIQDDDNLYLHCASGYRSVIAASIMKKQG 440
Cdd:cd01524     1 VQWHELdNYRA---DGVTLIDVRTPQEFEKGHIKGAINIPLDELRD--RLNELPKDKEIIVYCAVGLRGYIAARILTQNG 75

                          90
                  ....*....|..
gi 1134132600 441 IhNLRNVLGGWK 452
Cdd:cd01524    76 F-KVKNLDGGYK 86
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-182 5.94e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.17  E-value: 5.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   8 TGCLSEAAYYIESEGEAAIIDPL----RDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAK-- 81
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGgsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAre 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  82 ---------------------ARFDAVVAADGQKFTLGKLQIEVLHTPGHTleSACFLLKDENGKdyAVFTGDTLFVGDV 140
Cdd:pfam00753  81 lldeelglaasrlglpgppvvPLPPDVVLEEGDGILGGGLGLLVTHGPGHG--PGHVVVYYGGGK--VLFTGDLLFAGEI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1134132600 141 GRPDLAQNGEDLTTHSLAGMLYDSLQKRIIPLADdvIVYPAH 182
Cdd:pfam00753 157 GRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAA--VIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 15-183 3.80e-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: 67.71  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  15 AYYIESEGEAAIID---PLRDIAPYVELATRRN----ATIKFIFETHFHADfvsgHIdlsqsTGAPIIygpdaKARFDAV 87
Cdd:cd07725    17 VYLLRDGDETTLIDtglATEEDAEALWEGLKELglkpSDIDRVLLTHHHPD----HI-----GLAGKL-----QEKSGAT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  88 VA-------ADGQKFTLGKLQIEVLHTPGHTLESACFLlkDENGKDyavftgdtLFVGDVGRPDLAQN--GEDLTTHSLA 158
Cdd:cd07725    83 VYildvtpvKDGDKIDLGGLRLKVIETPGHTPGHIVLY--DEDRRE--------LFVGDAVLPKITPNvsLWAVRVEDPL 152

                         170       180
                  ....*....|....*....|....*
gi 1134132600 159 GMLYDSLQkRIIPLADDvIVYPAHG 183
Cdd:cd07725   153 GAYLESLD-KLEKLDVD-LAYPGHG 175
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 19-182 2.14e-12

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 66.77  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  19 ESEGEAAIIDPlRDIAPYVELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGP-DAKARFDAVVAADGQKFTL 97
Cdd:PRK10241   19 DEAGRCLIVDP-GEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPqETQDKGTTQVVKDGETAFV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  98 GKLQIEVLHTPGHTLESACFLlkdenGKDYaVFTGDTLFVGDVGRpdlaqngedlTTHSLAGMLYDSLQKrIIPLADDVI 177
Cdd:PRK10241   98 LGHEFSVFATPGHTLGHICYF-----SKPY-LFCGDTLFSGGCGR----------LFEGTASQMYQSLKK-INALPDDTL 160


                  ....*
gi 1134132600 178 VYPAH 182
Cdd:PRK10241  161 ICCAH 165
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 365-452 1.12e-11

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 61.13  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 365 DELAMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAiQD------------DDNLYLHCASGYRSVIA 432
Cdd:cd01519     4 EEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSE-EEfekkygfpkpskDKELIFYCKAGVRSKAA 82

                          90       100
                  ....*....|....*....|
gi 1134132600 433 ASIMKKQGIHNLRNVLGGWK 452
Cdd:cd01519    83 AELARSLGYENVGNYPGSWL 102
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 16-182 7.93e-11

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: 60.72  E-value: 7.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  16 YYIESEGEAAIID---PLRDIAPYVELATRRNATIKFifeTHFHADFVSGHID-------------LSQSTGAPIIYGPD 79
Cdd:cd07712    12 YLLRGRDRALLIDtglGIGDLKEYVRTLTDLPLLVVA---THGHFDHIGGLHEfeevyvhpadaeiLAAPDNFETLTWDA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  80 AKARFDAVVA----ADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLFVGDVgrpdlaqngEDLTTH 155
Cdd:cd07712    89 ATYSVPPAGPtlplRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANR----LLFSGDVVYDGPL---------IMDLPH 155

                         170       180
                  ....*....|....*....|....*...
gi 1134132600 156 SLAGMLYDSLQKrIIPLADDV-IVYPAH 182
Cdd:cd07712   156 SDLDDYLASLEK-LSKLPDEFdKVLPGH 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 14-134 4.09e-10

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 59.43  E-value: 4.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  14 AAYYIESEGEAAIIDP-LRDIAPYVELATR----RNATIKFIFETHFHADFVSG---------------H-------ID- 65
Cdd:cd07726    17 ASYLLDGEGRPALIDTgPSSSVPRLLAALEalgiAPEDVDYIILTHIHLDHAGGagllaealpnakvyvHprgarhlIDp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  66 --LSQSTGApiIYGPDAKARFDA---------VVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENGkdyaVFTGDT 134
Cdd:cd07726    97 skLWASARA--VYGDEADRLGGEilpvpeervIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG----LFTGDA 170
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 362-457 6.91e-10

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 56.28  E-value: 6.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDElAMDLPFDDRLIVVDVR--KEVEfADGHVKDAVNIP---LANLTDPAS---MSAIQDDDNLYLHCASGYRSVIAA 433
Cdd:cd01447     1 LSPED-ARALLGSPGVLLVDVRdpRELE-RTGMIPGAFHAPrgmLEFWADPDSpyhKPAFAEDKPFVFYCASGWRSALAG 78

                          90       100
                  ....*....|....*....|....
gi 1134132600 434 SIMKKQGIHNLRNVLGGWKAIKEE 457
Cdd:cd01447    79 KTLQDMGLKPVYNIEGGFKDWKEA 102
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
358-453 4.83e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 58.10  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 358 MIINIEPDELAMDLpfDDRLIVVDVRKEVEFADGHVKDAVNIPLANL-TDPASmSAIQDDDNLYLHCASGYRSVIAASIM 436
Cdd:PRK08762    1 SIREISPAEARARA--AQGAVLIDVREAHERASGQAEGALRIPRGFLeLRIET-HLPDRDREIVLICASGTRSAHAAATL 77

                          90       100
                  ....*....|....*....|
gi 1134132600 437 KKQGIHNLRNVLGG---WKA 453
Cdd:PRK08762   78 RELGYTRVASVAGGfsaWKD 97
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 15-183 7.68e-09

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: 55.69  E-value: 7.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  15 AYYIESEGEAAIID-----PLRDIAPYVELATRRNATIKFIFETHFHADfvsgHI----DLSQSTGAPI---------IY 76
Cdd:cd07721    13 AYLIEDDDGLTLIDtglpgSAKRILKALRELGLSPKDIRRILLTHGHID----HIgslaALKEAPGAPVyahereapyLE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  77 G--------------------PDAKARFDAVVAaDGQKFTLGKlQIEVLHTPGHTLESACFLLKDENgkdyAVFTGDTLF 136
Cdd:cd07721    89 GekpypppvrlgllgllspllPVKPVPVDRTLE-DGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDG----VLIAGDALV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134132600 137 VGD---VGRPDLAqngedltTHSLAgMLYDSLQKriipLAD-DV-IVYPAHG 183
Cdd:cd07721   163 TVGgelVPPPPPF-------TWDME-EALESLRK----LAElDPeVLAPGHG 202
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-184 1.61e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 54.88  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  18 IESEGEAAIIDPL--RDIAP--YVELATRRNATIKFIFETHFHADFVSGhidLS--QSTGAPIIYGPDAKARFDA----- 86
Cdd:cd16282    20 IVGDDGVVVIDTGasPRLARalLAAIRKVTDKPVRYVVNTHYHGDHTLG---NAafADAGAPIIAHENTREELAArgeay 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  87 ---------------------VVAADGQKFTLGKLQIEVLHT-PGHTLESACFLLKDENgkdyAVFTGDTLFvgdVGRPD 144
Cdd:cd16282    97 lelmrrlggdamagtelvlpdRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEG----VLFAGDLVF---NGRIP 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1134132600 145 LAQNGedltthSLAGMLyDSLqKRIIPLADDVIVyPAHGA 184
Cdd:cd16282   170 FLPDG------SLAGWI-AAL-DRLLALDATVVV-PGHGP 200
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 362-457 2.48e-08

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 52.31  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASM--------SAIQDDDNLYLHCASGYRSVIAA 433
Cdd:cd01526    10 VSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAElkslqelpLDNDKDSPIYVVCRRGNDSQTAV 89

                          90       100
                  ....*....|....*....|....*
gi 1134132600 434 SIMKKQGI-HNLRNVLGGWKAIKEE 457
Cdd:cd01526    90 RKLKELGLeRFVRDIIGGLKAWADK 114
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 362-459 5.18e-08

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 51.17  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLPFDDRLIVVDVRKEVEFAD-GHVKDAVNIPLANLTDPAS--------MSAIQDDDNLYLHCASGYRSVIA 432
Cdd:cd01522     1 LTPAEAWALLQADPQAVLVDVRTEAEWKFvGGVPDAVHVAWQVYPDMEInpnflaelEEKVGKDRPVLLLCRSGNRSIAA 80

                          90       100
                  ....*....|....*....|....*..
gi 1134132600 433 ASIMKKQGIHNLRNVLGGWKAIKEEEK 459
Cdd:cd01522    81 AEAAAQAGFTNVYNVLEGFEGDLDAAG 107
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 47-184 5.83e-08

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: 52.59  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVsGHIDLSqsTGAPIIYGPDA-KARFDAVVAADGQKFTLGKlQIEVLHTPGHTLESACFLLKDENGK 125
Cdd:cd07711    61 IDYVVLTHGHPDHI-GNLNLF--PNATVIVGWDIcGDSYDDHSLEEGDGYEIDE-NVEVIPTPGHTPEDVSVLVETEKKG 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134132600 126 DYAVfTGDtLF--VGDVGRPDLAQNGEDLTTHSLAGMlydslqKRIIPLAdDVIVyPAHGA 184
Cdd:cd07711   137 TVAV-AGD-LFerEEDLEDPILWDPLSEDPELQEESR------KRILALA-DWII-PGHGP 187
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 47-148 1.29e-07

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: 52.86  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVSGHIDLSQSTGAPI-IYGPDAKARFD---------------AVVAA-----DGQKFTLGKLQIEVL 105
Cdd:cd16308    61 IKILLTTQAHYDHVGAMAAIKQQTGAKMmVDEKDAKVLADggksdyemggygstfAPVKAdkllhDGDTIKLGGTKLTLL 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134132600 106 HTPGHTLESACFLLK-DENGKDYAVFTG-------DTLFVGDVGRPDLAQN 148
Cdd:cd16308   141 HHPGHTKGSCSFLFDvKDEKRTYRVLIAnmptilpDTKLSGMPGYPGIAKD 191
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 47-115 1.48e-07

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: 52.35  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAK-----------------------ARFDAVVaADGQKFTLGKLQIE 103
Cdd:cd16315    61 VRWLLSSHEHFDHVGGLAALQRATGARVAASAAAApvlesgkpapddpqaglhepfppVRVDRIV-EDGDTVALGSLRLT 139

                          90
                  ....*....|..
gi 1134132600 104 VLHTPGHTLESA 115
Cdd:cd16315   140 AHATPGHTPGAL 151
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 379-450 2.07e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 52.95  E-value: 2.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134132600 379 VVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGIHNLRNVLGG 450
Cdd:PRK05597  277 LIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGG 348
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 14-137 3.20e-07

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: 50.27  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  14 AAYYIESEGEAAIIDPLRdiapYVELATRRNAT---IKFIFETHfhADFVSGHIDLSQSTGAP-IIYGPDAKARFDAV-- 87
Cdd:cd07727    16 ASYLILRPEGNILVDSPR----YSPPLAKRIEAlggIRYIFLTH--RDDVADHAKWAERFGAKrIIHEDDVNAVTRPDev 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134132600  88 -VAADGQKFTLGKlQIEVLHTPGHTLESACFLLKDEngkdYAVFTGDTLFV 137
Cdd:cd07727    90 iVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEK----GVLFTGDHLAW 135
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
 358-453 3.47e-07

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 52.08  E-value: 3.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 358 MIINIEPDELAMDLPFDdrlIVVDVRKEVEFADGHVKDAVNIPLanLTD------------------------------P 407
Cdd:COG2603     1 MSKRITLDDFLELLDDD---PLIDVRSPVEFAEGHIPGAINLPL--LDDeeraevgtcykqqgpfaaiklghalvsgklA 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1134132600 408 ASMSAIQDD----DNLYLHCA-SGYRSVIAASIMKKQGIHNLRnVLGGWKA 453
Cdd:COG2603    76 AHREEAWAFapkhPRPLVYCWrGGLRSGSVAQWLREAGIDVPR-LEGGYKA 125
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 341-451 1.48e-06

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 49.40  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 341 YLEGGFDSWIKAG----------EPTDMIINIEPDELAmDLPF------DDRLIVVDVRK------EVEFAD---GHVKD 395
Cdd:COG2897   103 VLDGGLAAWKAAGlpletgpptpAPGDFTARPDPELLA-DADEvlaalgDPDAVLVDARSperyrgEVEPIDpraGHIPG 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134132600 396 AVNIPLANLTDPASM--SA-----------IQDDDNLYLHCASGYRSVIAASIMKKQGIHNLRNVLGGW 451
Cdd:COG2897   182 AVNLPWTDLLDEDGTfkSAeelralfaalgIDPDKPVITYCGSGVRAAHTWLALELLGYPNVRLYDGSW 250
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 47-147 1.55e-06

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: 49.24  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVSGHIDLSQSTGAPIIYGP-DAKA----------------RFDAV----VAADGQKFTLGKLQIEVL 105
Cdd:cd16288    61 IKILLNSHAHLDHAGGLAALKKLTGAKLMASAeDAALlasggksdfhygddslAFPPVkvdrVLKDGDRVTLGGTTLTAH 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134132600 106 HTPGHTLESACFLLK-DENGKDYAV-------FTGDTLFVGDVGRPDLAQ 147
Cdd:cd16288   141 LTPGHTRGCTTWTMTvKDDGKVYQVvfadsltVNPGYKLVGNPTYPGIAE 190
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-147 1.95e-06

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: 49.12  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  45 ATIKFIFETHFHADFVSGHIDLSQSTGAPIIYG-PDAK------ARFDA----------VVAADGQKFTLGKLQIEVLHT 107
Cdd:cd16280    60 ADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSeADWDmmeeppEEGDNprwgppperdIVIKDGDTLTLGDTTITVYLT 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1134132600 108 PGHTLESACFL--LKDENGKDYAVFTGDTLFVGDVGRPDLAQ 147
Cdd:cd16280   140 PGHTPGTLSLIfpVKDGGKTHRAGLWGGTGLNTGPNLERREQ 181
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 7-111 2.33e-06

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: 48.99  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600   7 YTGCLSEAAYYIESEGEAAIIDP-LRDIAPYVElatrRN--------ATIKFIFETHFHADFVSGHIDLSQSTGAPIIYG 77
Cdd:cd16310    16 YVGTKGIGSYLITSNHGAILLDGgLEENAALIE----QNikalgfklSDIKIIINTHAHYDHAGGLAQLKADTGAKLWAS 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134132600  78 PDAK----------------ARFDAV----VAADGQKFTLGKLQIEVLHTPGHT 111
Cdd:cd16310    92 RGDRpaleagkhigdnitqpAPFPAVkvdrILGDGEKIKLGDITLTATLTPGHT 145
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 47-130 3.17e-06

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: 48.25  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVSGHIDLSQSTGAPII---------------YGPDAKARFDAV----VAADGQKFTLGKLQIEVLHT 107
Cdd:cd16309    61 VKYLLNTHAHFDHAGGLAELKKATGAQLVasaadkpllesgyvgSGDTKNLQFPPVrvdrVIGDGDKVTLGGTTLTAHLT 140

                          90       100
                  ....*....|....*....|....*
gi 1134132600 108 PGHT--LESACFLLKDENGKDYAVF 130
Cdd:cd16309   141 PGHSpgCTSWTTTVKDTAGPPREVL 165
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-136 4.09e-06

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: 47.53  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  16 YYIESEGEAAIIDP-LRDIAPY--VELATRRNATIKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAKA---------- 82
Cdd:cd07743    12 VYVFGDKEALLIDSgLDEDAGRkiRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAfienplleps 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134132600  83 -------------RF--------DAVVAADgqKFTLGKLQIEVLHTPGHTLESACFLLKDEngkdyAVFTGDTLF 136
Cdd:cd07743    92 ylggayppkelrnKFlmakpskvDDIIEEG--ELELGGVGLEIIPLPGHSFGQIGILTPDG-----VLFAGDALF 159
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 17-85 4.10e-06

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: 47.23  E-value: 4.10e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134132600  17 YIESEGEAAIIDplrdiAPYVELATRRNA-TIKFIFETHFHADFVSGHIDLSQSTGAPI-IYGPDAKARFD 85
Cdd:cd07736    41 LIEVDGERILLD-----AGLTDLAERFPPgSIDAILLTHFHMDHVQGLFHLRWGVGDPIpVYGPPDPQGCA 106
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
47-148 2.56e-05

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 45.57  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVSGHIDLSQSTG-----API-IYGP-DAKARFDAVVAA---------------DGQKFTLGKLQIEV 104
Cdd:COG1234    53 IDAIFITHLHGDHIAGLPGLLSTRSlagreKPLtIYGPpGTKEFLEALLKAsgtdldfplefheiePGEVFEIGGFTVTA 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1134132600 105 LHTPgHTLESACFLLkDENGKDYaVFTGDTLFVGDVgrPDLAQN 148
Cdd:COG1234   133 FPLD-HPVPAYGYRF-EEPGRSL-VYSGDTRPCEAL--VELAKG 171
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 45-148 3.12e-05

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: 45.23  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  45 ATIKFIFETHFHADFVSGHIDLSQSTGAPII------------------YGPDAKARFDAV----VAADGQKFTLGKLQI 102
Cdd:cd07708    59 SDTKLILISHAHFDHAGGSAEIKKQTGAKVMagaedvslllsggssdfhYANDSSTYFPQStvdrAVHDGERVTLGGTVL 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134132600 103 EVLHTPGHTLESACFLLKD-ENGKDYAVFTGDTL-------FVGDVGRPDLAQN 148
Cdd:cd07708   139 TAHATPGHTPGCTTWTMTLkDHGKQYQVVFADSLtvnpgyrLVDNPTYPKIVED 192
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 375-453 3.19e-05

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 45.66  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 375 DRLIVVDVRKEVEFADGHVKDAVNIPLanLTD------------------------------PASMSAIQDD----DNLY 420
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPL--LNDeeraevgtlykqvgpfaaiklglalvspnlAAHVEQWRAFadgpPQPL 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1134132600 421 LHCA-SGYRSVIAASIMKKQGIHNLRnVLGGWKA 453
Cdd:TIGR03167  79 LYCWrGGMRSGSLAWLLAQIGFRVPR-LEGGYKA 111
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 362-450 3.23e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 45.85  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGI 441
Cdd:PRK07878  289 ITPRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGF 368


                  ....*....
gi 1134132600 442 HNLRNVLGG 450
Cdd:PRK07878  369 SDAVHLQGG 377
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 ...
 47-111 5.56e-05

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: 44.65  E-value: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADFVSGHIDLSQSTGAPIIYGPDAKA------------------RFDAV----VAADGQKFTLGKLQIEV 104
Cdd:cd16290    61 VKLILNSHAHFDHAGGIAALQRDSGATVAASPAGAAalrsggvdpddpqagaadPFPPVakvrVVADGEVVKLGPLAVTA 140


                  ....*..
gi 1134132600 105 LHTPGHT 111
Cdd:cd16290   141 HATPGHT 147
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 380-454 6.24e-05

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 42.14  E-value: 6.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134132600 380 VDVRKEVEFADGHVKDAVNIPLANLTDPASmSAIQD-DDNLYLHCASGYRSVIAASIMKKQGIHNLRNVlGGWKAI 454
Cdd:PRK10287   24 IDVRVPEQYQQEHVQGAINIPLKEVKERIA-TAVPDkNDTVKLYCNAGRQSGQAKEILSEMGYTHAENA-GGLKDI 97
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 373-455 7.53e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 42.28  E-value: 7.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 373 FDDRLIVVDVRKEVEFADGHVKDAVNIPL---------------------------------ANLTDPASMSAIQDDDNL 419
Cdd:cd01520    10 RKADGPLIDVRSPKEFFEGHLPGAINLPLlddeeralvgtlykqqgreaaielglelvsgklKRILNEAWEARLERDPKL 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1134132600 420 YLHCA-SGYRSVIAASIMKKQGIhNLRNVLGGWKAIK 455
Cdd:cd01520    90 LIYCArGGMRSQSLAWLLESLGI-DVPLLEGGYKAYR 125
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 373-453 9.86e-05

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 44.43  E-value: 9.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 373 FDDRLIVVDVRKEVEFADGHVKDAVNIPLanLTDP---------------------ASM--------------SAIQDDD 417
Cdd:PRK11784   12 FLNDTPLIDVRSPIEFAEGHIPGAINLPL--LNDEeraevgtcykqqgqfaaialgHALvagniaahreeawaDFPRANP 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1134132600 418 NLYLHCA-SGYRSVIAASIMKKQGIhNLRNVLGGWKA 453
Cdd:PRK11784   90 RGLLYCWrGGLRSGSVQQWLKEAGI-DVPRLEGGYKA 125
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 362-451 1.39e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 40.94  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANL------TDPASMSAIQDDDNLYLHCASGYRSVIAASI 435
Cdd:cd01523     1 LDPEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPyfdfleIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                          90
                  ....*....|....*...
gi 1134132600 436 MKKQG--IHNLRNVLGGW 451
Cdd:cd01523    81 LAERGydVDYLAGGMKAW 98
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-182 1.76e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 43.03  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  45 ATIKFIFETHFHADfvsgHI-DLSQSTGAPIIYGPDAKAR------------------FDAVVAADGQKFTLGKLQIE-- 103
Cdd:cd07730    82 EDIDAVILSHLHWD----HIgGLSDFPNARLIVGPGAKEAlrppgypsgflpellpsdFEGRLVRWEEDDFLWVPLGPfp 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 104 ------------VLHTPGHTLESACFLLKDENGKDYavftgdtLFVGD-------VGRPDLAQNGEDLTTHSLAGMLYDS 164
Cdd:cd07730   158 raldlfgdgslyLVDLPGHAPGHLGLLARTTSGTWV-------FLAGDachhrigLLRPSPLLPLPDLDDGADREAARET 230

                         170
                  ....*....|....*....
gi 1134132600 165 LQK-RIIPLADDVIVYPAH 182
Cdd:cd07730   231 LARlRELDAAPDVRVVLAH 249
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 258-349 2.06e-04

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 40.32  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 258 LSVAEFKA-IAADKDATILDTRPGATFSEAF--IPDSIFIGLEgRFAEWAGnLLSFDKPILLVSPEGQEKETVI-RLTRV 333
Cdd:cd01444     2 ISVDELAElLAAGEAPVLLDVRDPASYAALPdhIPGAIHLDED-SLDDWLG-DLDRDRPVVVYCYHGNSSAQLAqALREA 79

                          90
                  ....*....|....*.
gi 1134132600 334 GFSLFEgYLEGGFDSW 349
Cdd:cd01444    80 GFTDVR-SLAGGFEAW 94
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 362-450 2.25e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 40.26  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLpFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTD-PA---SMSAIQDDDNLYLHCASGYRSVIAASIMK 437
Cdd:cd01518     4 LSPAEWNELL-EDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREfPFwldENLDLLKGKKVLMYCTGGIRCEKASAYLK 82

                          90
                  ....*....|...
gi 1134132600 438 KQGIHNLRNVLGG 450
Cdd:cd01518    83 ERGFKNVYQLKGG 95
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
374-457 2.71e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 43.18  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 374 DDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQ---DDDNLYLHCASGYRSVIAASIMKKQGIHNLrNVLGG 450
Cdd:PRK07411  297 ADDFVLIDVRNPNEYEIARIPGSVLVPLPDIENGPGVEKVKellNGHRLIAHCKMGGRSAKALGILKEAGIEGT-NVKGG 375


                  ....*..
gi 1134132600 451 WKAIKEE 457
Cdd:PRK07411  376 ITAWSRE 382
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 14-134 3.01e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.57  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  14 AAYYIESEGEAAIIDPLRDIAPYVELATRRNATIKFIFETHFHADfvsgHI----DLSQS-TGAPI-IYGPDA------- 80
Cdd:COG1235    36 SSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHAD----HIagldDLRPRyGPNPIpVYATPGtlealer 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134132600  81 ---------KARFDAVVAADGQKFTLGKLQIEVLHTPGHTLESACFLLKDENGKdyAVFTGDT 134
Cdd:COG1235   112 rfpylfapyPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKK--LAYATDT 172
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 362-451 4.81e-04

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 39.75  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLPFDDRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGI 441
Cdd:cd01533    12 VSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRTRSIIGAQSLINAGL 91

                          90
                  ....*....|....
gi 1134132600 442 HN----LRNVLGGW 451
Cdd:cd01533    92 PNpvaaLRNGTQGW 105
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 255-356 1.00e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 38.83  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 255 LKP---LSVAEFKAI-AADKDATILDTRPGATFSEAFIPDSIFIGL--------EGRFAEWAGNLLSFDKPILLVSPEGQ 322
Cdd:cd01526     4 LSPeerVSVKDYKNIlQAGKKHVLLDVRPKVHFEICRLPEAINIPLsellskaaELKSLQELPLDNDKDSPIYVVCRRGN 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1134132600 323 EKETVIRLTR-VGFSLFEGYLEGGFDSWIKAGEPT 356
Cdd:cd01526    84 DSQTAVRKLKeLGLERFVRDIIGGLKAWADKVDPT 118
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 21-133 1.60e-03

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: 40.23  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  21 EGEAAIID---------PLRDIAPYveLATRRNATIKFIFETHFHADFVSGHIDLSQS-------TGAPIIYGPDAKARF 84
Cdd:COG2333    20 DGKTILIDtgprpsfdaGERVVLPY--LRALGIRRLDLLVLTHPDADHIGGLAAVLEAfpvgrvlVSGPPDTSETYERLL 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134132600  85 DAV--------VAADGQKFTLGKLQIEVLHTPGHTLE-------SACFLLKDENGKdyAVFTGD 133
Cdd:COG2333    98 EALkekgipvrPCRAGDTWQLGGVRFEVLWPPEDLLEgsdennnSLVLRLTYGGFS--FLLTGD 159
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-134 4.35e-03

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: 38.01  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  14 AAYYIESEGEAAIIDPLRDIAPYVELATRRNATIKFIFETHFHADFVSG------HIDLSQSTGAPIIYGP-DAKARFDA 86
Cdd:cd16272    18 SSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGlptllfARRYGGRKKPLTIYGPkGIKEFLEK 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1134132600  87 VVA------------------ADGQKFTLGKLQIEVLHTPgHTLESACFLLKDENGKdyAVFTGDT 134
Cdd:cd16272    98 LLNfpveilplgfpleieeleEGGEVLELGDLKVEAFPVK-HSVESLGYRIEAEGKS--IVYSGDT 160
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 269-355 4.74e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 36.67  E-value: 4.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  269 DKDATILDTRPGATFSEAFIPDSIFIGLEgRFAEWAGNLLSFDKPILLVSPE-GQEKETVI------RLTRVGFSLFE-G 340
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLS-ELLDRRGELDILEFEELLKRLGlDKDKPVVVycrsgnRSAKAAWLLRElG 80

                           90       100
                   ....*....|....*....|
gi 1134132600  341 Y-----LEGGFDSWIKAGEP 355
Cdd:smart00450  81 FknvylLDGGYKEWSAAGPP 100
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 362-404 5.06e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 37.26  E-value: 5.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1134132600 362 IEPDELAMDL-PFDDRLIVVDVRKEVEFADGHVKDAVNIPLANL 404
Cdd:cd01446     2 IDCAWLAALLrEGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTI 45
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 379-453 5.99e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 36.11  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 379 VVDVRKEVEFADGHVKDAVNIPLANLT----DPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQGIHN---LRNVLGGW 451
Cdd:cd01529    15 LLDVRAEDEYAAGHLPGKRSIPGAALVlrsqELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPvalLDGGTSAW 94


                  ..
gi 1134132600 452 KA 453
Cdd:cd01529    95 VA 96
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 269-349 6.35e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 35.92  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 269 DKDATILDTRPGATFSEAFIPDSIFI------GLEGRFAEWAGNLLSF--DKPILLVSPEGQE-KETVIRLTRVGFSLFe 339
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVplsslsLPPLPLLELLEKLLELlkDKPIVVYCNSGNRaAAAAALLKALGYKNV- 81

                          90
                  ....*....|
gi 1134132600 340 GYLEGGFDSW 349
Cdd:pfam00581  82 YVLDGGFEAW 91
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 47-182 6.76e-03

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: 37.96  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600  47 IKFIFETHFHADfvsgHID-LSQSTGAPII---------YGPDAKAR-FDAVVAADGQKFTLGKLQ-----------IEV 104
Cdd:cd07729    89 IDYVILSHLHFD----HAGgLDLFPNATIIvqraeleyaTGPDPLAAgYYEDVLALDDDLPGGRVRlvdgdydlfpgVTL 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 105 LHTPGHTLESACFLLKDENGkdYAVFTGDTLFVgdvgRPDLAQNGEDLTTHSLAGML--YDSLQKriipLAD--DVIVYP 180
Cdd:cd07729   165 IPTPGHTPGHQSVLVRLPEG--TVLLAGDAAYT----YENLEEGRPPGINYDPEAALasLERLKA----LAEreGARVIP 234


                  ..
gi 1134132600 181 AH 182
Cdd:cd07729   235 GH 236
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 362-400 6.79e-03

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 36.43  E-value: 6.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1134132600 362 IEPDELA--MDLPFDDR---LIVVDVRKEVEFADGHVKDAVNIP 400
Cdd:cd01530     4 ISPETLArlLQGKYDNFfdkYIIIDCRFPYEYNGGHIKGAVNLS 47
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 374-451 8.35e-03

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 36.07  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 374 DDRLIVVDVR------KEVEFAD-----GHVKDAVNIPLANLTDPASMSAIQD-------------DDNLYLHCASGYRS 429
Cdd:cd01449    12 SGDVQLVDARsperfrGEVPEPRpglrsGHIPGAVNIPWTSLLDEDGTFKSPEelralfaalgitpDKPVIVYCGSGVTA 91

                          90       100
                  ....*....|....*....|..
gi 1134132600 430 VIAASIMKKQGIHNLRNVLGGW 451
Cdd:cd01449    92 CVLLLALELLGYKNVRLYDGSW 113
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 362-450 8.72e-03

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 35.83  E-value: 8.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 362 IEPDELAMDLPFDDRLIV-VDVRKEVEFADGHVKDAVNIPLANL-TDPASMSAIQDDDNLYLHCASGYRSVIAASIMKKQ 439
Cdd:cd01528     2 ISVAELAEWLADEREEPVlIDVREPEELEIAFLPGFLHLPMSEIpERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                          90
                  ....*....|.
gi 1134132600 440 GIHNLRNVLGG 450
Cdd:cd01528    82 GFENVYNLQGG 92
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 375-453 9.93e-03

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 35.54  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132600 375 DRLIVVDVRKEVEFADGHVKDAVNIPLANLTDPASMSAIQDDDNLYLHCASGYRSV--IAASIMKKQG---IHNLRNVLG 449
Cdd:cd01532     9 EEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEDLapRAARRLSELGytdVALLEGGLQ 88


                  ....
gi 1134132600 450 GWKA 453
Cdd:cd01532    89 GWRA 92
 
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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