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Conserved domains on  [gi|1176154624|gb|OQX71796|]
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hypothetical protein B6D52_00120 [Candidatus Parcubacteria bacterium 4484_255]

Protein Classification

ComEC/Rec2 family competence protein( domain architecture ID 11457082)

ComEC/Rec2 family competence protein similar to Bacillus subtilis ComE operon protein 3, which is required for DNA internalization; the comE operon is required for the binding and uptake of transforming DNA

Gene Ontology:  GO:0016020|GO:0030420
PubMed:  7968523|8901420

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 51-302 1.09e-96

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: 285.60  E-value: 1.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  51 LRVVFLDVGQGDAILIQTPQ-QNIIIDGGPDKSIV---RKLDQYIP---IteRRIDLMILTHPDGDHLTGLVEILRRWPV 123
Cdd:COG2333     1 LRVTFLDVGQGDAILIRTPDgKTILIDTGPRPSFDageRVVLPYLRalgI--RRLDLLVLTHPDADHIGGLAAVLEAFPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 124 ITVAESGLKSNSPAYIEFNSLIKSKNIKRHIINVPQRITFeDNLFFDFLWPCSKESIENNEgdcNFLSLVFMLNYGDNNF 203
Cdd:COG2333    79 GRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQL-GGVRFEVLWPPEDLLEGSDE---NNNSLVLRLTYGGFSF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 204 LFTGDATKETEEELMSQGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLDNFRKINANVLR 283
Cdd:COG2333   155 LLTGDAEAEAEAALLARGPDLKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGRDNRYGHPHPEVLERLRAAGIRVYR 234

                         250
                  ....*....|....*....
gi 1176154624 284 TDEKGDIIFESNGQTLTLK 302
Cdd:COG2333   235 TDRDGAITVTSDGDGLRVE 253
 
Name Accession Description Interval E-value
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 51-302 1.09e-96

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: 285.60  E-value: 1.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  51 LRVVFLDVGQGDAILIQTPQ-QNIIIDGGPDKSIV---RKLDQYIP---IteRRIDLMILTHPDGDHLTGLVEILRRWPV 123
Cdd:COG2333     1 LRVTFLDVGQGDAILIRTPDgKTILIDTGPRPSFDageRVVLPYLRalgI--RRLDLLVLTHPDADHIGGLAAVLEAFPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 124 ITVAESGLKSNSPAYIEFNSLIKSKNIKRHIINVPQRITFeDNLFFDFLWPCSKESIENNEgdcNFLSLVFMLNYGDNNF 203
Cdd:COG2333    79 GRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQL-GGVRFEVLWPPEDLLEGSDE---NNNSLVLRLTYGGFSF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 204 LFTGDATKETEEELMSQGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLDNFRKINANVLR 283
Cdd:COG2333   155 LLTGDAEAEAEAALLARGPDLKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGRDNRYGHPHPEVLERLRAAGIRVYR 234

                         250
                  ....*....|....*....
gi 1176154624 284 TDEKGDIIFESNGQTLTLK 302
Cdd:COG2333   235 TDRDGAITVTSDGDGLRVE 253
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 52-234 7.29e-64

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 199.28  E-value: 7.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  52 RVVFLDVGQGDAILIQTPQQNIIIDGGP-----DKSIVRKLDQY-IpiteRRIDLMILTHPDGDHLTGLVEILRRWPVIT 125
Cdd:cd07731     1 RVHFLDVGQGDAILIQTPGKTILIDTGPrdsfgEDVVVPYLKARgI----KKLDYLILTHPDADHIGGLDAVLKNFPVKE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 126 VAESGLKSNSPAYIEFNSLIKSKNIKRHIINVPQRITFeDNLFFDFLWPCSKESIENNEGdcnflSLVFMLNYGDNNFLF 205
Cdd:cd07731    77 VYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQL-GGVSFEVLSPPKDDYDDLNNN-----SCVLRLTYGGTSFLL 150

                         170       180
                  ....*....|....*....|....*....
gi 1176154624 206 TGDATKETEEELMSQGLNLRADVLKAGHH 234
Cdd:cd07731   151 TGDAEKEAEEELLASGPDLLADVLKVGHH 179
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 40-288 1.59e-36

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 138.11  E-value: 1.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  40 FLFFVSPVSADLRVVFLDVGQGDAILIQTPQQNIIIDGG---PDKSIVRKLdqYIPITERR---IDLMILTHPDGDHLTG 113
Cdd:TIGR00361 429 FLLFIYPCLSSWQVDMLDVGQGLAMFIGANGKGILYDTGepwREGSLGEKV--IIPFLTAKgikLEALILSHADQDHIGG 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 114 LVEILRRWPVITVAESGLKSNSPAYIEFNSLIKSKNIKrhiinvpqritfedNLFFDFLWPcskESIENNEGdcNFLSLV 193
Cdd:TIGR00361 507 AEIILKHHPVKRLVIPKGFVEEGVAIEECKRGDVWQWQ--------------GLQFHVLSP---EAPDPASK--NNHSCV 567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 194 FMLNYGDNNFLFTGDATKETEEELMSQGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLDN 273
Cdd:TIGR00361 568 LWVDDGGNSWLLTGDLEAEGEQEVMRVFPNIKADVLQVGHHGSKTSTSEELIQQVQPKVAIISAGRNNRWHHPHQKVLQR 647

                         250
                  ....*....|....*
gi 1176154624 274 FRKINANVLRTDEKG 288
Cdd:TIGR00361 648 LQRHSIRVLRTDQNG 662
PRK11539 PRK11539
ComEC family competence protein; Provisional
 52-290 6.42e-23

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 98.91  E-value: 6.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  52 RVVFLDVGQGDAILIQTPQQNIIIDGGP--------DKSIvrkldqyIP-ITERRIDL--MILTHPDGDHLTGLVEILRR 120
Cdd:PRK11539  502 RVDMLDVGHGLAVVIERNGKAILYDTGNawptgdsaQQVI-------IPwLRWHGLTPegIILSHEHLDHRGGLASLLHA 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 121 WPVITVaesglksNSPayiefnsliksknikrhIINVPQRITFEDN------LFFDFLWPCSKESI-ENNEgdcnflSLV 193
Cdd:PRK11539  575 WPMAWI-------RSP-----------------LNWANHLPCVRGEqwqwqgLTFSVHWPLEQSNDaGNND------SCV 624

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 194 FMLNYGDNNFLFTGDATKETEEELMS-QGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLD 272
Cdd:PRK11539  625 IRVDDGKHSILLTGDLEAQAEQKLLSrYWQQLAATLLQVPHHGSNTSSSLPFIRAVNGKVALASASRYNAWRLPSVKVKQ 704

                         250
                  ....*....|....*...
gi 1176154624 273 NFRKINANVLRTDEKGDI 290
Cdd:PRK11539  705 RYQQQGYQWRDTPHSGQL 722
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
56-258 5.11e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.49  E-value: 5.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  56 LDVGQGDAILIQTPQQNIIIDGGPDKSIVRKLD-QYIPITERRIDLMILTHPDGDHLTGLVEILRRWPVITVAESGLKSN 134
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLlAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 135 SPAYIEFNSLIKSKNIKRHIINVPQRITFEDNLFFDFLWPCSKESIENNEGdcnflSLVFMLNYGDNNFLFTGDATKETE 214
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHG-----PGHVVVYYGGGKVLFTGDLLFAGE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1176154624 215 EELMSqglnLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVG 258
Cdd:pfam00753 156 IGRLD----LPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPG 195
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 63-258 2.58e-09

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: 55.64  E-value: 2.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624   63 AILIQTPQQNIIIDGGPDKS--IVRKLDQYIPiteRRIDLMILTHPDGDHLTGLVEILRRW--PVI-TVAESGLKSNSPA 137
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAedLLAELKKLGP---KKIDAIILTHGHPDHIGGLPELLEAPgaPVYaPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  138 YIEFNSLIKSKNIKRHIINVPQRITFEDnLFFDFLW-PC-SKESIennegdcnflSLVFmlnyGDNNFLFTGDATKETEE 215
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGG-GELEVIHtPGhTPGSI----------VLYL----PEGKILFTGDLLFAGGD 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1176154624  216 elmsqglnlrADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVG 258
Cdd:smart00849 144 ----------GRTLVDGGDAAASDALESLLKLLKLLPKLVVPG 176
 
Name Accession Description Interval E-value
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 51-302 1.09e-96

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: 285.60  E-value: 1.09e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  51 LRVVFLDVGQGDAILIQTPQ-QNIIIDGGPDKSIV---RKLDQYIP---IteRRIDLMILTHPDGDHLTGLVEILRRWPV 123
Cdd:COG2333     1 LRVTFLDVGQGDAILIRTPDgKTILIDTGPRPSFDageRVVLPYLRalgI--RRLDLLVLTHPDADHIGGLAAVLEAFPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 124 ITVAESGLKSNSPAYIEFNSLIKSKNIKRHIINVPQRITFeDNLFFDFLWPCSKESIENNEgdcNFLSLVFMLNYGDNNF 203
Cdd:COG2333    79 GRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQL-GGVRFEVLWPPEDLLEGSDE---NNNSLVLRLTYGGFSF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 204 LFTGDATKETEEELMSQGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLDNFRKINANVLR 283
Cdd:COG2333   155 LLTGDAEAEAEAALLARGPDLKADVLKVPHHGSKTSSSPAFLEAVRPRVAVISVGRDNRYGHPHPEVLERLRAAGIRVYR 234

                         250
                  ....*....|....*....
gi 1176154624 284 TDEKGDIIFESNGQTLTLK 302
Cdd:COG2333   235 TDRDGAITVTSDGDGLRVE 253
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 52-234 7.29e-64

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 199.28  E-value: 7.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  52 RVVFLDVGQGDAILIQTPQQNIIIDGGP-----DKSIVRKLDQY-IpiteRRIDLMILTHPDGDHLTGLVEILRRWPVIT 125
Cdd:cd07731     1 RVHFLDVGQGDAILIQTPGKTILIDTGPrdsfgEDVVVPYLKARgI----KKLDYLILTHPDADHIGGLDAVLKNFPVKE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 126 VAESGLKSNSPAYIEFNSLIKSKNIKRHIINVPQRITFeDNLFFDFLWPCSKESIENNEGdcnflSLVFMLNYGDNNFLF 205
Cdd:cd07731    77 VYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQL-GGVSFEVLSPPKDDYDDLNNN-----SCVLRLTYGGTSFLL 150

                         170       180
                  ....*....|....*....|....*....
gi 1176154624 206 TGDATKETEEELMSQGLNLRADVLKAGHH 234
Cdd:cd07731   151 TGDAEKEAEEELLASGPDLLADVLKVGHH 179
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 40-288 1.59e-36

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 138.11  E-value: 1.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  40 FLFFVSPVSADLRVVFLDVGQGDAILIQTPQQNIIIDGG---PDKSIVRKLdqYIPITERR---IDLMILTHPDGDHLTG 113
Cdd:TIGR00361 429 FLLFIYPCLSSWQVDMLDVGQGLAMFIGANGKGILYDTGepwREGSLGEKV--IIPFLTAKgikLEALILSHADQDHIGG 506

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 114 LVEILRRWPVITVAESGLKSNSPAYIEFNSLIKSKNIKrhiinvpqritfedNLFFDFLWPcskESIENNEGdcNFLSLV 193
Cdd:TIGR00361 507 AEIILKHHPVKRLVIPKGFVEEGVAIEECKRGDVWQWQ--------------GLQFHVLSP---EAPDPASK--NNHSCV 567

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 194 FMLNYGDNNFLFTGDATKETEEELMSQGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLDN 273
Cdd:TIGR00361 568 LWVDDGGNSWLLTGDLEAEGEQEVMRVFPNIKADVLQVGHHGSKTSTSEELIQQVQPKVAIISAGRNNRWHHPHQKVLQR 647

                         250
                  ....*....|....*
gi 1176154624 274 FRKINANVLRTDEKG 288
Cdd:TIGR00361 648 LQRHSIRVLRTDQNG 662
PRK11539 PRK11539
ComEC family competence protein; Provisional
 52-290 6.42e-23

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 98.91  E-value: 6.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  52 RVVFLDVGQGDAILIQTPQQNIIIDGGP--------DKSIvrkldqyIP-ITERRIDL--MILTHPDGDHLTGLVEILRR 120
Cdd:PRK11539  502 RVDMLDVGHGLAVVIERNGKAILYDTGNawptgdsaQQVI-------IPwLRWHGLTPegIILSHEHLDHRGGLASLLHA 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 121 WPVITVaesglksNSPayiefnsliksknikrhIINVPQRITFEDN------LFFDFLWPCSKESI-ENNEgdcnflSLV 193
Cdd:PRK11539  575 WPMAWI-------RSP-----------------LNWANHLPCVRGEqwqwqgLTFSVHWPLEQSNDaGNND------SCV 624

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 194 FMLNYGDNNFLFTGDATKETEEELMS-QGLNLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVGKDNNFGHPSLRVLD 272
Cdd:PRK11539  625 IRVDDGKHSILLTGDLEAQAEQKLLSrYWQQLAATLLQVPHHGSNTSSSLPFIRAVNGKVALASASRYNAWRLPSVKVKQ 704

                         250
                  ....*....|....*...
gi 1176154624 273 NFRKINANVLRTDEKGDI 290
Cdd:PRK11539  705 RYQQQGYQWRDTPHSGQL 722
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
56-258 5.11e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.49  E-value: 5.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  56 LDVGQGDAILIQTPQQNIIIDGGPDKSIVRKLD-QYIPITERRIDLMILTHPDGDHLTGLVEILRRWPVITVAESGLKSN 134
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLlAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 135 SPAYIEFNSLIKSKNIKRHIINVPQRITFEDNLFFDFLWPCSKESIENNEGdcnflSLVFMLNYGDNNFLFTGDATKETE 214
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHG-----PGHVVVYYGGGKVLFTGDLLFAGE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1176154624 215 EELMSqglnLRADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVG 258
Cdd:pfam00753 156 IGRLD----LPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPG 195
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 63-258 2.58e-09

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: 55.64  E-value: 2.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624   63 AILIQTPQQNIIIDGGPDKS--IVRKLDQYIPiteRRIDLMILTHPDGDHLTGLVEILRRW--PVI-TVAESGLKSNSPA 137
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAedLLAELKKLGP---KKIDAIILTHGHPDHIGGLPELLEAPgaPVYaPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  138 YIEFNSLIKSKNIKRHIINVPQRITFEDnLFFDFLW-PC-SKESIennegdcnflSLVFmlnyGDNNFLFTGDATKETEE 215
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGG-GELEVIHtPGhTPGSI----------VLYL----PEGKILFTGDLLFAGGD 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1176154624  216 elmsqglnlrADVLKAGHHGSKHSSGLNFLKAVNPEYAIISVG 258
Cdd:smart00849 144 ----------GRTLVDGGDAAASDALESLLKLLKLLPKLVVPG 176
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 63-255 1.95e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 51.05  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  63 AILIQTPQQNIIIDGGPDksiVRKLDQYIPITERRIDLMILTHPDGDHLTGLVEILRRW-----PVITVAE--SGLKSNs 135
Cdd:COG1235    37 SILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYgpnpiPVYATPGtlEALERR- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624 136 payIEFNSLIKSKNIKRHIINVPQRITFEDnlfFDFlwpcskESIENNEGDCNflSLVFMLNYGDNNFLFTGDaTKETEE 215
Cdd:COG1235   113 ---FPYLFAPYPGKLEFHEIEPGEPFEIGG---LTV------TPFPVPHDAGD--PVGYRIEDGGKKLAYATD-TGYIPE 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1176154624 216 ELMSQglnLR-ADVL------KAGHHGskHSS---GLNFLKAVNPEYAII 255
Cdd:COG1235   178 EVLEL---LRgADLLildatyDDPEPG--HLSneeALELLARLGPKRLVL 222
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 65-127 3.07e-06

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: 47.38  E-value: 3.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176154624  65 LIQTPQQNIIIDGGPDKSIVRKLDQYIPITERRIDLMILTHPDGDHLTGLVEILRRWPVITVA 127
Cdd:COG0491    19 LIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 72-165 3.42e-06

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 46.92  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  72 NIIIDGGPD-KSIVRKLDQYIPITERRIDLMILTHPDGDHLTGLVEILRRWPVITVAESG----LKSNSPayieFNSLIK 146
Cdd:pfam12706   2 RILIDPGPDlRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGvlahLRRNFP----YLFLLE 77

                          90
                  ....*....|....*....
gi 1176154624 147 SKNIKRHIINVPQRITFED 165
Cdd:pfam12706  78 HYGVRVHEIDWGESFTVGD 96
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 63-168 9.65e-06

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 45.33  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176154624  63 AILIQTPQQNIIIDGGPdkSIVRKLDQYIpITERRIDLMILTHPDGDHLTGLVEILRRW-------PVITVAESGLKSNS 135
Cdd:cd16272    19 SYLLETGGTRILLDCGE--GTVYRLLKAG-VDPDKLDAIFLSHFHLDHIGGLPTLLFARryggrkkPLTIYGPKGIKEFL 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1176154624 136 PAYIEFNSLIKSKNIK-RHIINVPQRITFEDNLF 168
Cdd:cd16272    96 EKLLNFPVEILPLGFPlEIEELEEGGEVLELGDL 129
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 62-117 1.85e-04

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


Pssm-ID: 293814  Cd Length: 249  Bit Score: 42.25  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176154624  62 DAILIQTPQQNIIIDGG------PDK-----------SIVRKLDQyIPITERRIDLMILTHPDGDHLTGLVEI 117
Cdd:cd07728    44 DPILIQYQGKNYLIDAGigngklTEKqkrnfgvteesSIEESLAE-LGLTPEDIDYVLMTHLHFDHASGLTKV 115
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 63-121 2.27e-04

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 41.31  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176154624  63 AILIQTPQQNIIIDGGPDksiVRK--LDQYIpiteRRIDLMILTHPDGDHLTGLVEiLRRW 121
Cdd:cd16279    37 SILIETGGKNILIDTGPD---FRQqaLRAGI----RKLDAVLLTHAHADHIHGLDD-LRPF 89
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 58-120 4.98e-04

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: 40.99  E-value: 4.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176154624  58 VGQGD--AILIQTPQQNIIIDGGPDKSI------VRKLDqyipITERRIDLMILTHPDGDHLTGLVEILRR 120
Cdd:cd07708    17 VGTDDlaAYLIVTPQGNILIDGDMEQNApmikanIKKLG----FKFSDTKLILISHAHFDHAGGSAEIKKQ 83
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 71-126 2.96e-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: 38.24  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1176154624  71 QNIIIDGGPDK---SIVRKLDQYIPIteRRIDLMILTHPDGDHLTGLVEILRRWPVITV 126
Cdd:cd07709    41 KTALIDTVKEPffdEFLENLEEVIDP--RKIDYIVVNHQEPDHSGSLPELLELAPNAKI 97
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
63-121 6.49e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 37.48  E-value: 6.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1176154624  63 AILIQTPQQNIIIDGGPdkSIVRKLDQYiPITERRIDLMILTHPDGDHLTGLVEILRRW 121
Cdd:COG1234    21 SYLLEAGGERLLIDCGE--GTQRQLLRA-GLDPRDIDAIFITHLHGDHIAGLPGLLSTR 76
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 65-123 7.83e-03

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: 36.82  E-value: 7.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176154624  65 LIQTPQQNIIIDGG-PD--KSIVRKLDQyIPITERRIDLMILTHPDGDHLTGLVEILRRWPV 123
Cdd:cd07721    15 LIEDDDGLTLIDTGlPGsaKRILKALRE-LGLSPKDIRRILLTHGHIDHIGSLAALKEAPGA 75
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 63-126 8.06e-03

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 37.22  E-value: 8.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1176154624  63 AILIQTPQQNIIIDGGPDKSIV---RKLDqyIPITErrIDLMILTHPDGDHLTGLVEILRRWPVITV 126
Cdd:cd07713    22 SLLIETEGKKILFDTGQSGVLLhnaKKLG--IDLSD--IDAVVLSHGHYDHTGGLKALLELNPKAPV 84
 
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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