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Conserved domains on  [gi|610629982|gb|EZH76006|]
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metallo-beta-lactamase [Aquimarina atlantica]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870238)

uncharacterized member of the MBL fold metallo-hydrolase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-243 3.95e-114

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


:

Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 327.66  E-value: 3.95e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   5 HHLNCVQIESPMG--SAIGHCLLLEGINRFVLIDSGIGLSETKDPEKKLGKELIEVTGFKFDEKRTAIAQIQKLGFRPEK 82
Cdd:cd07742    1 HHLNCGTMRPPGGdlRLVCHCLLVETDDGLVLVDTGFGLADVADPKRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  83 IKDCIVSHLDPDHIGGLADFPDMRIHIAKEEYESFKSGN-----ERYLPQQLAHNPEIKLYEKSNSKWFGLPARKvDLD- 156
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATSPRtryerRRYRPQQLAHGPWWVTYAAGGERWFGFEAVR-PLDg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 157 FETEIYLIPLFGHTLGHCGVTFKENEKWIFYVGDAYYLRDEISDLNHPVDELA---RIRAVDNEMRKESLQKIREIVKKH 233
Cdd:cd07742  160 LPPEILLVPLPGHTRGHCGVAVRTGDRWLLHAGDAYFHHGELDPLPPPPPPLRlfqRLLAVDRSARLANLARLRELARDH 239

                        250
                 ....*....|
gi 610629982 234 GKEIEYFGYH 243
Cdd:cd07742  240 GDEVEVFCAH 249
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-243 3.95e-114

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 327.66  E-value: 3.95e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   5 HHLNCVQIESPMG--SAIGHCLLLEGINRFVLIDSGIGLSETKDPEKKLGKELIEVTGFKFDEKRTAIAQIQKLGFRPEK 82
Cdd:cd07742    1 HHLNCGTMRPPGGdlRLVCHCLLVETDDGLVLVDTGFGLADVADPKRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  83 IKDCIVSHLDPDHIGGLADFPDMRIHIAKEEYESFKSGN-----ERYLPQQLAHNPEIKLYEKSNSKWFGLPARKvDLD- 156
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATSPRtryerRRYRPQQLAHGPWWVTYAAGGERWFGFEAVR-PLDg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 157 FETEIYLIPLFGHTLGHCGVTFKENEKWIFYVGDAYYLRDEISDLNHPVDELA---RIRAVDNEMRKESLQKIREIVKKH 233
Cdd:cd07742  160 LPPEILLVPLPGHTRGHCGVAVRTGDRWLLHAGDAYFHHGELDPLPPPPPPLRlfqRLLAVDRSARLANLARLRELARDH 239

                        250
                 ....*....|
gi 610629982 234 GKEIEYFGYH 243
Cdd:cd07742  240 GDEVEVFCAH 249
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-228 1.34e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 62.00  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   20 IGHCLLLEGINRFVLIDSGIGLSetkdpekklgkelievtgfkfdekRTAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGL 99
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAE------------------------AALLLLLAALGLGPKDIDAVILTHGHFDHIGGL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  100 ADFPDMRIHIAKEEYESFKSGNERYLPQQLAHNPEIKLYEKSNSKWFGLPARKVDLDFETEIYLIPLFGHTLGHCGVTFk 179
Cdd:pfam00753  61 GELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYY- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 610629982  180 ENEKWIFyVGDAYYLRDEIsDLNHPVDELARIRAVDNEMRKESLQKIRE 228
Cdd:pfam00753 140 GGGKVLF-TGDLLFAGEIG-RLDLPLGGLLVLHPSSAESSLESLLKLAK 186
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 4-240 3.79e-11

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: 60.86  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   4 IHHLNCVQIESPMGSaigHCLLLEGINRFVLIDSGIGLSETKDpekklgkelievtgfkfdekrtAIAQIQKLGfrpEKI 83
Cdd:COG0491    1 VYVLPGGTPGAGLGV---NSYLIVGGDGAVLIDTGLGPADAEA----------------------LLAALAALG---LDI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  84 KDCIVSHLDPDHIGGLADFPDM---RIHIAKEEYESFKSGNERYLPQQLAHNPEIKLYEKSnskwfglparKVDLDfETE 160
Cdd:COG0491   53 KAVLLTHLHPDHVGGLAALAEAfgaPVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGD----------TLELG-GPG 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 161 IYLIPLFGHTLGHCGVTFKEnEKWIFyVGDAYY----LRDEISDLNHP--VDELARIRAVDNE---------MRKESLQK 225
Cdd:COG0491  122 LEVIHTPGHTPGHVSFYVPD-EKVLF-TGDALFsggvGRPDLPDGDLAqwLASLERLLALPPDlvipghgppTTAEAIDY 199

                        250
                 ....*....|....*
gi 610629982 226 IREIVKKHGKEIEYF 240
Cdd:COG0491  200 LEELLAALGERANPF 214
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-233 1.26e-10

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: 58.72  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982    22 HCLLLEGINRFVLIDSGiglsetkdpekklgkelievtgfkFDEKRTAIAQIQKLGfrPEKIKDCIVSHLDPDHIGGLAD 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTG------------------------PGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPE 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   102 F---PDMRIHIAKEEYESFKSGNERYLPQQLAHNPEIKLYEKSNSKWFGLPARKVDldfeteiyLIPLFGHTLGHCGVTF 178
Cdd:smart00849  55 LleaPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELE--------VIHTPGHTPGSIVLYL 126

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 610629982   179 KenEKWIFYVGDAYYLRDEISDLNHPVDELARIRAvdNEMRKESLQKIREIVKKH 233
Cdd:smart00849 127 P--EGKILFTGDLLFAGGDGRTLVDGGDAAASDAL--ESLLKLLKLLPKLVVPGH 177
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 5-243 3.95e-114

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 327.66  E-value: 3.95e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   5 HHLNCVQIESPMG--SAIGHCLLLEGINRFVLIDSGIGLSETKDPEKKLGKELIEVTGFKFDEKRTAIAQIQKLGFRPEK 82
Cdd:cd07742    1 HHLNCGTMRPPGGdlRLVCHCLLVETDDGLVLVDTGFGLADVADPKRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  83 IKDCIVSHLDPDHIGGLADFPDMRIHIAKEEYESFKSGN-----ERYLPQQLAHNPEIKLYEKSNSKWFGLPARKvDLD- 156
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATSPRtryerRRYRPQQLAHGPWWVTYAAGGERWFGFEAVR-PLDg 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 157 FETEIYLIPLFGHTLGHCGVTFKENEKWIFYVGDAYYLRDEISDLNHPVDELA---RIRAVDNEMRKESLQKIREIVKKH 233
Cdd:cd07742  160 LPPEILLVPLPGHTRGHCGVAVRTGDRWLLHAGDAYFHHGELDPLPPPPPPLRlfqRLLAVDRSARLANLARLRELARDH 239

                        250
                 ....*....|
gi 610629982 234 GKEIEYFGYH 243
Cdd:cd07742  240 GDEVEVFCAH 249
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 23-245 3.24e-35

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: 126.18  E-value: 3.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  23 CLLLEGINRFVLIDSGIGlsetkDPEKKLGKELIEVTGFKFDEKRTAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGLADF 102
Cdd:cd07729   34 AYLIEHPEGTILVDTGFH-----PDAADDPGGLELAFPPGVTEEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 103 PDMRIHIAKEEYESFKSgnerylpqqlAHNPEIKLYEKSNSKWFGLPARKVDL-DFETE----IYLIPLFGHTLGHCGVT 177
Cdd:cd07729  109 PNATIIVQRAELEYATG----------PDPLAAGYYEDVLALDDDLPGGRVRLvDGDYDlfpgVTLIPTPGHTPGHQSVL 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 610629982 178 FKENEKWIFYVGDAYYLRDEIsdlnhpVDELARIRAVDNEMRKESLQKIREIVKKHGKEIeYFGyHDP 245
Cdd:cd07729  179 VRLPEGTVLLAGDAAYTYENL------EEGRPPGINYDPEAALASLERLKALAEREGARV-IPG-HDP 238
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-234 9.48e-28

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: 106.58  E-value: 9.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  30 NRFVLIDSGIGlsetKDPEK--KLGKELIEVTGFKFDEKRTAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGLADFPDMRI 107
Cdd:cd07730   33 GGKILFDLGYR----KDFEEytPRVPERLYRTPVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDFPNARL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 108 HIAKEEYESFKSGNER------YLPQQLAHNPEIKLYEKSNSKWFGLPARKVDLdFET-EIYLIPLFGHTLGHCGVTFK- 179
Cdd:cd07730  109 IVGPGAKEALRPPGYPsgflpeLLPSDFEGRLVRWEEDDFLWVPLGPFPRALDL-FGDgSLYLVDLPGHAPGHLGLLARt 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 610629982 180 ENEKWIFYVGDAYYLRDeisDLNHPVDELARIRAVDNEMR---KESLQKIREIVKKHG 234
Cdd:cd07730  188 TSGTWVFLAGDACHHRI---GLLRPSPLLPLPDLDDGADReaaRETLARLRELDAAPD 242
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 23-191 1.61e-16

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 76.43  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  23 CLLLEGINRFVLIDSGIGlsETKDPekKLGKelievtgfkfdekrtAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGLAD- 101
Cdd:cd07720   51 AFLVRTGGRLILVDTGAG--GLFGP--TAGK---------------LLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDa 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 102 -----FPDMRIHIAKEEYESFKS-GNERYLPQQLAHNPE-----IKLYEKsnskwfglparKVDLDFETEIY----LIPL 166
Cdd:cd07720  112 ggkpvFPNAEVHVSEAEWDFWLDdANAAKAPEGAKRFFDaardrLRPYAA-----------AGRFEDGDEVLpgitAVPA 180

                        170       180
                 ....*....|....*....|....*
gi 610629982 167 FGHTLGHCGVTFKENEKWIFYVGDA 191
Cdd:cd07720  181 PGHTPGHTGYRIESGGERLLIWGDI 205
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-190 3.81e-13

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 67.13  E-value: 3.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  23 CLLLEGINRFVLIDSGIGlseTKDPEKKLGKelievtgFKFDEKRTAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGL--- 99
Cdd:cd16281   45 CLLIETGGRNILIDTGIG---DKQDPKFRSI-------YVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGAtra 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 100 -AD------FPDMRIHIAKEEYESFKSGNER----YLPQ---QLAHNPEIKLYEKSNSKWFGlparkvdldfetEIYLIP 165
Cdd:cd16281  115 dDDglvellFPNATYWVQKRHWEWALNPNPRerasFLPEniePLEESGRLKLIDGSDAELGP------------GIRFHL 182

                        170       180
                 ....*....|....*....|....*
gi 610629982 166 LFGHTLGHCGVTFKENEKWIFYVGD 190
Cdd:cd16281  183 SDGHTPGQMLPEISTPGGTVVFAAD 207
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-228 1.34e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 62.00  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   20 IGHCLLLEGINRFVLIDSGIGLSetkdpekklgkelievtgfkfdekRTAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGL 99
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAE------------------------AALLLLLAALGLGPKDIDAVILTHGHFDHIGGL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  100 ADFPDMRIHIAKEEYESFKSGNERYLPQQLAHNPEIKLYEKSNSKWFGLPARKVDLDFETEIYLIPLFGHTLGHCGVTFk 179
Cdd:pfam00753  61 GELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYY- 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 610629982  180 ENEKWIFyVGDAYYLRDEIsDLNHPVDELARIRAVDNEMRKESLQKIRE 228
Cdd:pfam00753 140 GGGKVLF-TGDLLFAGEIG-RLDLPLGGLLVLHPSSAESSLESLLKLAK 186
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 11-229 2.16e-11

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: 61.47  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  11 QIESPMGSaigHCLLLEGINRFVLIDsgiglsetkdpekklgkelievTGFKFDEKRtAIAQIQKLGFRPEKIKDCIVSH 90
Cdd:cd07721    4 QLPLLPPV---NAYLIEDDDGLTLID----------------------TGLPGSAKR-ILKALRELGLSPKDIRRILLTH 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  91 LDPDHIGGLADF---PDMRIHIAKEEyESFKSGNERYLPQQLAHNpeIKLYEKSNSKWFGLPARKVD----LDFETEIYL 163
Cdd:cd07721   58 GHIDHIGSLAALkeaPGAPVYAHERE-APYLEGEKPYPPPVRLGL--LGLLSPLLPVKPVPVDRTLEdgdtLDLAGGLRV 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 610629982 164 IPLFGHTLGHCGVtFKENEKWIFyVGDAYYLRDeisDLNHPVDELArirAVDNEMRKESLQKIREI 229
Cdd:cd07721  135 IHTPGHTPGHISL-YLEEDGVLI-AGDALVTVG---GELVPPPPPF---TWDMEEALESLRKLAEL 192
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 4-240 3.79e-11

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: 60.86  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   4 IHHLNCVQIESPMGSaigHCLLLEGINRFVLIDSGIGLSETKDpekklgkelievtgfkfdekrtAIAQIQKLGfrpEKI 83
Cdd:COG0491    1 VYVLPGGTPGAGLGV---NSYLIVGGDGAVLIDTGLGPADAEA----------------------LLAALAALG---LDI 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  84 KDCIVSHLDPDHIGGLADFPDM---RIHIAKEEYESFKSGNERYLPQQLAHNPEIKLYEKSnskwfglparKVDLDfETE 160
Cdd:COG0491   53 KAVLLTHLHPDHVGGLAALAEAfgaPVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGD----------TLELG-GPG 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 161 IYLIPLFGHTLGHCGVTFKEnEKWIFyVGDAYY----LRDEISDLNHP--VDELARIRAVDNE---------MRKESLQK 225
Cdd:COG0491  122 LEVIHTPGHTPGHVSFYVPD-EKVLF-TGDALFsggvGRPDLPDGDLAqwLASLERLLALPPDlvipghgppTTAEAIDY 199

                        250
                 ....*....|....*
gi 610629982 226 IREIVKKHGKEIEYF 240
Cdd:COG0491  200 LEELLAALGERANPF 214
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-233 1.26e-10

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: 58.72  E-value: 1.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982    22 HCLLLEGINRFVLIDSGiglsetkdpekklgkelievtgfkFDEKRTAIAQIQKLGfrPEKIKDCIVSHLDPDHIGGLAD 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTG------------------------PGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPE 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   102 F---PDMRIHIAKEEYESFKSGNERYLPQQLAHNPEIKLYEKSNSKWFGLPARKVDldfeteiyLIPLFGHTLGHCGVTF 178
Cdd:smart00849  55 LleaPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELE--------VIHTPGHTPGSIVLYL 126

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 610629982   179 KenEKWIFYVGDAYYLRDEISDLNHPVDELARIRAvdNEMRKESLQKIREIVKKH 233
Cdd:smart00849 127 P--EGKILFTGDLLFAGGDGRTLVDGGDAAASDAL--ESLLKLLKLLPKLVVPGH 177
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 11-190 2.32e-10

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 59.19  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  11 QIESPMgsaigHCLLLEGINRFVLIDSGIGLSETKDPEKKlgkelievtGFKFDEKRTAIAQIQKLGFRPEKIKDCIVSH 90
Cdd:cd07728   38 QIELRT-----DPILIQYQGKNYLIDAGIGNGKLTEKQKR---------NFGVTEESSIEESLAELGLTPEDIDYVLMTH 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  91 LDPDHIGGLAD---------FPDMRIHIAKEEYESFKSGNER----YLP---QQLAHnpEIKLYEKSnskwfglparkvd 154
Cdd:cd07728  104 LHFDHASGLTKvkgeqlvsvFPNATIYVSEIEWEEMRNPNIRskntYWKenwEPIED--QVKTFSDE------------- 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 610629982 155 LDFETEIYLIPLFGHTLGHCGVTFKENEKWIFYVGD 190
Cdd:cd07728  169 IEIVPGITMIHTGGHSDGHSIIEIEQGGETAIHMAD 204
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 8-235 2.70e-10

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: 57.98  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982   8 NCVQIESPMGSAIGHCLLLEGINRFVLIDSGIGLSetkdpekklgKELIevtgfkfdekrtaIAQIQKLGFRPEKIKDCI 87
Cdd:cd07711    9 YARRDSDGGFRASSTVTLIKDGGKNILVDTGTPWD----------RDLL-------------LKALAEHGLSPEDIDYVV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  88 VSHLDPDHIGGLADFPDMRIHIAKEEYEsfksgnERYLPQQLAHNPEIKLyeksnskwfglparkvdldfETEIYLIPLF 167
Cdd:cd07711   66 LTHGHPDHIGNLNLFPNATVIVGWDICG------DSYDDHSLEEGDGYEI--------------------DENVEVIPTP 119

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 610629982 168 GHTLGHCGVTFK-ENEKWIFYVGDAYYLRDEISDlnhpvDELARIRAVDNEMRKESLQKIRE----IVKKHGK 235
Cdd:cd07711  120 GHTPEDVSVLVEtEKKGTVAVAGDLFEREEDLED-----PILWDPLSEDPELQEESRKRILAladwIIPGHGP 187
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 22-220 1.45e-09

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: 56.10  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  22 HCLLLEGINRFVLIDSGIGLSETKDpekklgkelievtgfkfdekrtaiaQIQKLGFRPEKikdCIVSHLDPDHIGGLAD 101
Cdd:cd07712   10 NIYLLRGRDRALLIDTGLGIGDLKE-------------------------YVRTLTDLPLL---VVATHGHFDHIGGLHE 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 102 FPDMRIHiaKEEYESFKSGNERYLPQQLAHNPEIKLYEKSNSKWFGlpaRKVDL-DFETEIYLIPlfGHTLGHcgVTFKE 180
Cdd:cd07712   62 FEEVYVH--PADAEILAAPDNFETLTWDAATYSVPPAGPTLPLRDG---DVIDLgDRQLEVIHTP--GHTPGS--IALLD 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 610629982 181 NEKWIFYVGDAYYLRDEISDLNH-PVDE----LARIRAVDNEMRK 220
Cdd:cd07712  133 RANRLLFSGDVVYDGPLIMDLPHsDLDDylasLEKLSKLPDEFDK 177
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-205 2.71e-09

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 55.61  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  22 HCLLLEGINRFVLIDSGIGlsETKDPekklgkelieVTGFKFDEKRTA-IAQIQKLGFRPEKIKDCIVSHLDPDHIGG-- 98
Cdd:cd16277   14 HSWLVRTPGRTILVDTGIG--NDKPR----------PGPPAFHNLNTPyLERLAAAGVRPEDVDYVLCTHLHVDHVGWnt 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  99 -LAD------FPDMRIHIAKEEYESFKSGNERYLPQQLAhnpeiklYEKSNskwfgLP------ARKVDLDFE--TEIYL 163
Cdd:cd16277   82 rLVDgrwvptFPNARYLFSRAEYDHWSSPDAGGPPNRGV-------FEDSV-----LPvieaglADLVDDDHEilDGIRL 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 610629982 164 IPLFGHTLGHCGVTFKENEKWIFYVGDAyylrdeisdLNHPV 205
Cdd:cd16277  150 EPTPGHTPGHVSVELESGGERALFTGDV---------MHHPI 182
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 70-190 7.92e-07

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: 48.05  E-value: 7.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  70 IAQIQKLGFRPEKIkdcIVSHLDPDHIGGLADF---PDMRIHIAKEEYESFKSGNERYlpqqlahnpeiklyekSNSKWF 146
Cdd:cd06262   36 LEAIEELGLKIKAI---LLTHGHFDHIGGLAELkeaPGAPVYIHEADAELLEDPELNL----------------AFFGGG 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 610629982 147 GLPARKVDLDFE---------TEIYLIPLFGHTLGHCGVTFKEnEKWIFyVGD 190
Cdd:cd06262   97 PLPPPEPDILLEdgdtielggLELEVIHTPGHTPGSVCFYIEE-EGVLF-TGD 147
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 70-172 1.42e-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: 47.96  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  70 IAQIQKLGFRPEKIKDCIVSHLDPDHIGG---LADFPDMRIHIAKEEYESFKSGNERYlpqqlahnpeiklyekSNSKWF 146
Cdd:cd16280   49 VDGLEKLGLDPADIKYILITHGHGDHYGGaayLKDLYGAKVVMSEADWDMMEEPPEEG----------------DNPRWG 112

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 610629982 147 GLPARKVDL---------DFETEIYLIPlfGHTLG 172
Cdd:cd16280  113 PPPERDIVIkdgdtltlgDTTITVYLTP--GHTPG 145
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 55-206 3.54e-06

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 46.10  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  55 LIEVTGFK--FDEKRTAIAQIQKLGFRPEKIKDCIVSHLDPDHIGGLADFPDMRihiakeeyesFKSGNER----YLPQQ 128
Cdd:cd16272   21 LLETGGTRilLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFAR----------RYGGRKKpltiYGPKG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 129 LAHNPEIKLYEKSNSKWFGLPARKVDLDFETEIYLIPLF-------GHTLGHCGVTFKENEKWIFYVGDAYYLrDEISDL 201
Cdd:cd16272   91 IKEFLEKLLNFPVEILPLGFPLEIEELEEGGEVLELGDLkveafpvKHSVESLGYRIEAEGKSIVYSGDTGPC-ENLVEL 169


                 ....*
gi 610629982 202 NHPVD 206
Cdd:cd16272  170 AKGAD 174
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 23-215 3.71e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 46.81  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  23 CLLLEGINRFVLIDSGIGLSEtkdpekklgkelievtgfkfdekrtaiaQIQKLGFRPEKIKDCIVSHLDPDHIGGLADF 102
Cdd:COG1235   37 SILVEADGTRLLIDAGPDLRE----------------------------QLLRLGLDPSKIDAILLTHEHADHIAGLDDL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982 103 ------PDMRIHIAKEEYESFKsgnERYLPQQLAHNPEIKLYEKSNSKWFGLParkvDLDFETeiylIPLFGHTLGHCGV 176
Cdd:COG1235   89 rprygpNPIPVYATPGTLEALE---RRFPYLFAPYPGKLEFHEIEPGEPFEIG----GLTVTP----FPVPHDAGDPVGY 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 610629982 177 TFKENEKWIFYVGDAYYLRDEIsdlnhpvdeLARIRAVD 215
Cdd:COG1235  158 RIEDGGKKLAYATDTGYIPEEV---------LELLRGAD 187
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 20-101 4.76e-05

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: 43.49  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  20 IGHC----LLLEGINRFVLIDSGIglsetkdPEkklGKELIevtgfkfdekrtaIAQIQKLGFRPEKIKDCIVSHLDPDH 95
Cdd:cd16315   17 VGTCgisaILITGDDGHVLIDSGT-------EE---AAPLV-------------LANIRKLGFDPKDVRWLLSSHEHFDH 73


                 ....*.
gi 610629982  96 IGGLAD 101
Cdd:cd16315   74 VGGLAA 79
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-229 3.34e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 40.59  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  17 GSAIGhcLLLEGINRFVLIDSGIGlsetKDPEKKLGKELIEVTgfkfdekrtaiaqiqklgfrpEKIKDCIVSHLDPDHI 96
Cdd:cd07743    7 PTNIG--VYVFGDKEALLIDSGLD----EDAGRKIRKILEELG---------------------WKLKAIINTHSHADHI 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  97 GGLADFpdmrihiaKEEY--ESFKSGNERYLPQqlahNPEI--------KLYEKSNSKWFGLPARKVD--------LDFE 158
Cdd:cd07743   60 GGNAYL--------QKKTgcKVYAPKIEKAFIE----NPLLepsylggaYPPKELRNKFLMAKPSKVDdiieegelELGG 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 610629982 159 TEIYLIPLFGHTLGHCGVTFKENekwIFYVGDAYYLRDEISdlNHPVDELariraVDNEMRKESLQKIREI 229
Cdd:cd07743  128 VGLEIIPLPGHSFGQIGILTPDG---VLFAGDALFGEEVLE--KYGIPFL-----YDVEEQLETLEKLEEL 188
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
14-201 4.38e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 40.56  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  14 SPMGSAIGH--CLLLEGINRFVLIDSGIGlsetkdpekklgkelievtgfkfdekrtAIAQIQKLGFRPEKIKDCIVSHL 91
Cdd:COG1234   10 GAVPTPGRAtsSYLLEAGGERLLIDCGEG----------------------------TQRQLLRAGLDPRDIDAIFITHL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  92 DPDHIGGLADFPDMRIHiakeeyesfkSGNER----YLPQQLAHnpEIKLYEKSNSKWFGLPARKVDLDFET-------E 160
Cdd:COG1234   62 HGDHIAGLPGLLSTRSL----------AGREKpltiYGPPGTKE--FLEALLKASGTDLDFPLEFHEIEPGEvfeiggfT 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 610629982 161 IYLIPLFgHTLGHCGVTFKENEKWIFYVGDAYYlRDEISDL 201
Cdd:COG1234  130 VTAFPLD-HPVPAYGYRFEEPGRSLVYSGDTRP-CEALVEL 168
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 10-191 7.54e-04

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: 39.59  E-value: 7.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  10 VQIESPMGSAIGH--CLLLEGINRFVLIDSGIGLSETKdpekklgkelievtgfkfdekRTAIAQIQKLGFRPEKIKDCI 87
Cdd:cd07725    2 YRLSLPLPGPLGHvnVYLLRDGDETTLIDTGLATEEDA---------------------EALWEGLKELGLKPSDIDRVL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  88 VSHLDPDHIGGLADF-PDMRIHIAKEEYESFKSGNerylpqqlahnpeiklyeksnskwfglparKVDLDfETEIYLIPL 166
Cdd:cd07725   61 LTHHHPDHIGLAGKLqEKSGATVYILDVTPVKDGD------------------------------KIDLG-GLRLKVIET 109

                        170       180
                 ....*....|....*....|....*
gi 610629982 167 FGHTLGHCGVTFKENEkwIFYVGDA 191
Cdd:cd07725  110 PGHTPGHIVLYDEDRR--ELFVGDA 132
NorV COG0426
Flavorubredoxin [Energy production and conversion];
70-111 1.09e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.81  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 610629982  70 IAQIQKLgFRPEKIKDCIVSHLDPDHIGGLAD----FPDMRIHIAK 111
Cdd:COG0426   59 LENLSKV-IDPKKIDYIIVNHQEPDHSGSLPEllelAPNAKIVCSK 103
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 71-100 1.29e-03

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: 39.23  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 610629982  71 AQIQKLGFRPEKIKDCIVSHLDPDHIGGLA 100
Cdd:cd16288   49 ANIRKLGFKPSDIKILLNSHAHLDHAGGLA 78
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 64-190 1.55e-03

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: 38.87  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  64 DEKRTAIAQIQKLGFRPEKIkdcIVSHLDPDHIGGLADFpdmRIHIAKEEYesfksgnerylpqqlAHNPEIKLYEKSN- 142
Cdd:cd16322   31 DESEKLLARFGTTGLTLLYI---LLTHAHFDHVGGVADL---RRHPGAPVY---------------LHPDDLPLYEAADl 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 610629982 143 -SKWFGLparKVDLDFETEIYL-----IPLFG------HTLGHC--GVTFKENEKWIFYVGD 190
Cdd:cd16322   90 gAKAFGL---GIEPLPPPDRLLedgqtLTLGGlefkvlHTPGHSpgHVCFYVEEEGLLFSGD 148
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 71-105 3.66e-03

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 37.92  E-value: 3.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 610629982  71 AQIQKLGFRPEKIKDCIVSHLDPDHIGGLADFPDM 105
Cdd:cd16313   49 ASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKL 83
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 71-100 3.87e-03

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 37.95  E-value: 3.87e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 610629982  71 AQIQKLGFRPEKIKDCIVSHLDPDHIGGLA 100
Cdd:cd16314   49 ANIRALGFRPEDVRYIVSSHEHFDHAGGIA 78
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 ...
 70-100 6.11e-03

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: 37.33  E-value: 6.11e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 610629982  70 IAQIQKLGFRPEKIKDCIVSHLDPDHIGGLA 100
Cdd:cd16290   48 EANIRALGFRLEDVKLILNSHAHFDHAGGIA 78
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 70-109 6.38e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 37.08  E-value: 6.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 610629982  70 IAQIQKLgFRPEKIKDCIVSHLDPDHIGGLADF----PDMRIHI 109
Cdd:cd07709   57 LENLEEV-IDPRKIDYIVVNHQEPDHSGSLPELlelaPNAKIVC 99
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 70-102 6.77e-03

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: 37.08  E-value: 6.77e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 610629982  70 IAQIQKLGFRPEKIKDCIVSHLDPDHIGGLADF 102
Cdd:cd16309   48 KDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 30-108 8.75e-03

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: 36.36  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610629982  30 NRFVLIDSGiglsETKDPEKKLGKELIEVTGfkfdekrtaiaqiqklgfrPEKIKDCIVSHLDPDHIGGLAD------FP 103
Cdd:cd07722   27 KRRILIDTG----EGRPSYIPLLKSVLDSEG-------------------NATISDILLTHWHHDHVGGLPDvldllrGP 83


                 ....*
gi 610629982 104 DMRIH 108
Cdd:cd07722   84 SPRVY 88
 
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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