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Conserved domains on  [gi|489197160|ref|WP_003106464|]
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MULTISPECIES: pyrroloquinoline quinone biosynthesis protein PqqB [Pseudomonas]

Protein Classification

pyrroloquinoline quinone biosynthesis protein PqqB( domain architecture ID 10012265)

pyrroloquinoline quinone biosynthesis protein PqqB may be involved in the transport of pyrroloquinoline quinone (PQQ) and its precursor to the cytoplasm

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
1-304 0e+00

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


:

Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 574.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTA 80
Cdd:PRK05184   1 MRIIVLGSAAGGGFPQWNCNCPNCRGARAGTIRAKPRTQSSIAVSADGEDWVLLNASPDIRQQIQATPALQPARGLRDTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLSHWnGGLRHRPIALDGePFAIPACPRLRFTAI 160
Cdd:PRK05184  81 IAAVVLTDGQIDHTTGLLTLREGQPFPVYATPAVLEDLSTGFPIFNVLDHY-GGVQRRPIALDG-PFAVPGLPGLRFTAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160 161 PLRSSAPPYSPHRGDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTLWRDDEMLVCEVGDKLG 240
Cdd:PRK05184 159 PVPSKAPPYSPHRSDPEPGDNIGLRIEDRATGKRLFYAPGLAEVTDALRARLAGADCVLFDGTLWTDDEMIRAGVGTKTG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489197160 241 RQMGHLAQSGPGGMLEVLAKVPAARKVLIHINNTNPILDTASAERAELDASGIEVAWDGMHIQL 304
Cdd:PRK05184 239 RRMGHLPQSGPGGMIAALARLPIARKILIHINNTNPILDEDSPERAELEAAGIEVAHDGMEIEL 302
 
Name Accession Description Interval E-value
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
1-304 0e+00

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 574.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTA 80
Cdd:PRK05184   1 MRIIVLGSAAGGGFPQWNCNCPNCRGARAGTIRAKPRTQSSIAVSADGEDWVLLNASPDIRQQIQATPALQPARGLRDTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLSHWnGGLRHRPIALDGePFAIPACPRLRFTAI 160
Cdd:PRK05184  81 IAAVVLTDGQIDHTTGLLTLREGQPFPVYATPAVLEDLSTGFPIFNVLDHY-GGVQRRPIALDG-PFAVPGLPGLRFTAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160 161 PLRSSAPPYSPHRGDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTLWRDDEMLVCEVGDKLG 240
Cdd:PRK05184 159 PVPSKAPPYSPHRSDPEPGDNIGLRIEDRATGKRLFYAPGLAEVTDALRARLAGADCVLFDGTLWTDDEMIRAGVGTKTG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489197160 241 RQMGHLAQSGPGGMLEVLAKVPAARKVLIHINNTNPILDTASAERAELDASGIEVAWDGMHIQL 304
Cdd:PRK05184 239 RRMGHLPQSGPGGMIAALARLPIARKILIHINNTNPILDEDSPERAELEAAGIEVAHDGMEIEL 302
PQQ_syn_pqqB TIGR02108
coenzyme PQQ biosynthesis protein B; This model describes coenzyme PQQ biosynthesis protein B, ...
2-304 0e+00

coenzyme PQQ biosynthesis protein B; This model describes coenzyme PQQ biosynthesis protein B, a gene required for the biosynthesis of pyrrolo-quinoline-quinone (coenzyme PQQ). PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases. Note that this gene appears to be required for PQQ in biosynthesis in Methylobacterium extorquens (under the name pqqG) and in Klebiella pneumoniae but that the equivalent pqqV in Acinetobacter calcoaceticus is not necessary for heterologous expression of PQQ biosynthesis in E. coli. Based on this latter finding, it is suggested (Goosen, et al. 1989) that PqqB might be a transporter or a PQQ-dependent enzyme rather than a PQQ biosynthesis enzyme. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273977 [Multi-domain]  Cd Length: 302  Bit Score: 532.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160    2 HIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTAI 81
Cdd:TIGR02108   1 HIVVLGSAAGGGFPQWNCNCPNCRGARAGTIGAKARTQSSIAVSADGERWVLLNASPDIRQQIQATPALHPQRGLRHTPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   82 GAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEgFPLFPMLSHWNggLRHRPIALDGEP-FAIPACPRLRFTAI 160
Cdd:TIGR02108  81 AGVVLTDGEIDHTTGLLTLREGQPFTLYATEMVLQDLSD-NPIFNVLDHWN--VRRQPIALNEKFeFRIVARPGLEFTPF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  161 PLRSSAPPYSPHR-GDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTLWRDDEMLVCEVGDKL 239
Cdd:TIGR02108 158 AVPGKAPLYSEHRaGDPHPGDTLGLKIEDGTTGKRLFYIPGCAEITDDLKARMAGADLVFFDGTLWRDDEMIRAGVGTKT 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489197160  240 GRQMGHLAQSGPGGMLEVLAKVPAARKVLIHINNTNPILDTASAERAELDASGIEVAWDGMHIQL 304
Cdd:TIGR02108 238 GRRMGHVSMSGEGGSLAVLADLEIARKVLIHINNTNPILDEDSPERAEVEAAGWEVAYDGMEIVL 302
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
1-222 1.39e-129

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. 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: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 367.71  E-value: 1.39e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTA 80
Cdd:cd16274    1 MRIKVLGSAAGGGFPQWNCNCPNCALARAGDGRATARTQSSIAVSADGENWVLINASPDIRQQIEATPELQPRPGLRDTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLsHWNGGLRHRPIALdGEPFAIPACPRLRFTAI 160
Cdd:cd16274   81 IAAVLLTDAEIDHTTGLLSLREGQPLTVYATAPVLEDLTTNFPFFVLL-HAYGGVRRHRILP-GEPFTLAGCPGLTVTPF 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489197160 161 PLRSSAPPYSPHRGDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDG 222
Cdd:cd16274  159 PVPGKAPLYSEHRDAPEPGDTIGLRIEDGRTGGRLFYAPGCAAVTDELRARLAGADCLLFDG 220
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
1-304 2.30e-66

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 208.21  E-value: 2.30e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCrgvrDGSVAAQPRTQSSIALSDDGERwILCNASPDIRAQIAAFPAlqparrpRDTA 80
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC----ASTDPRYGRTRSSILVEADGTR-LLIDAGPDLREQLLRLGL-------DPSK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGC---PHEVWCTQMVHQDLSEGFPLfpMLSHWNGGLRHRPIAlDGEPFAIPAcprLRF 157
Cdd:COG1235   69 IDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFPY--LFAPYPGKLEFHEIE-PGEPFEIGG---LTV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160 158 TAIPLrssappysPHRgdphPGDNIGLFVEdlDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTlwRDDEmlvcevgd 237
Cdd:COG1235  143 TPFPV--------PHD----AGDPVGYRIE--DGGKKLAYATDTGYIPEEVLELLRGADLLILDAT--YDDP-------- 198
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489197160 238 klgrQMGHLAQSgpgGMLEVLAKVPAARKVLIHIN--NTNPILDTASAERAELDAsGIEVAWDGMHIQL 304
Cdd:COG1235  199 ----EPGHLSNE---EALELLARLGPKRLVLTHLSpdNNDHELDYDELEAALLPA-GVEVAYDGMEIEL 259
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
50-271 6.30e-58

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: 184.44  E-value: 6.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   50 RWILCNASPDIRAQiaAFPALQPaRRPRDTAIGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLS 129
Cdd:pfam12706   1 RRILIDPGPDLRQQ--ALPALQP-GRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  130 HWngGLRHRPIALdGEPFAIpACPRLRFTAIPLRSSAPPysphRGDPHPGDNIGLFVEdlDSAGTLFYAPGLGEVDEALL 209
Cdd:pfam12706  78 HY--GVRVHEIDW-GESFTV-GDGGLTVTATPARHGSPR----GLDPNPGDTLGFRIE--GPGKRVYYAGDTGYFPDEIG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489197160  210 EWMRRADCLLVDGTLWRDDEMLvcevgdklgrQMGHLaqsGPGGMLEVLAKVPAARKVLIHI 271
Cdd:pfam12706 148 ERLGGADLLLLDGGAWRDDEMI----------HMGHM---TPEEAVEAAADLGARRKVLIHI 196
 
Name Accession Description Interval E-value
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
1-304 0e+00

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 574.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTA 80
Cdd:PRK05184   1 MRIIVLGSAAGGGFPQWNCNCPNCRGARAGTIRAKPRTQSSIAVSADGEDWVLLNASPDIRQQIQATPALQPARGLRDTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLSHWnGGLRHRPIALDGePFAIPACPRLRFTAI 160
Cdd:PRK05184  81 IAAVVLTDGQIDHTTGLLTLREGQPFPVYATPAVLEDLSTGFPIFNVLDHY-GGVQRRPIALDG-PFAVPGLPGLRFTAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160 161 PLRSSAPPYSPHRGDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTLWRDDEMLVCEVGDKLG 240
Cdd:PRK05184 159 PVPSKAPPYSPHRSDPEPGDNIGLRIEDRATGKRLFYAPGLAEVTDALRARLAGADCVLFDGTLWTDDEMIRAGVGTKTG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489197160 241 RQMGHLAQSGPGGMLEVLAKVPAARKVLIHINNTNPILDTASAERAELDASGIEVAWDGMHIQL 304
Cdd:PRK05184 239 RRMGHLPQSGPGGMIAALARLPIARKILIHINNTNPILDEDSPERAELEAAGIEVAHDGMEIEL 302
PQQ_syn_pqqB TIGR02108
coenzyme PQQ biosynthesis protein B; This model describes coenzyme PQQ biosynthesis protein B, ...
2-304 0e+00

coenzyme PQQ biosynthesis protein B; This model describes coenzyme PQQ biosynthesis protein B, a gene required for the biosynthesis of pyrrolo-quinoline-quinone (coenzyme PQQ). PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases. Note that this gene appears to be required for PQQ in biosynthesis in Methylobacterium extorquens (under the name pqqG) and in Klebiella pneumoniae but that the equivalent pqqV in Acinetobacter calcoaceticus is not necessary for heterologous expression of PQQ biosynthesis in E. coli. Based on this latter finding, it is suggested (Goosen, et al. 1989) that PqqB might be a transporter or a PQQ-dependent enzyme rather than a PQQ biosynthesis enzyme. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273977 [Multi-domain]  Cd Length: 302  Bit Score: 532.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160    2 HIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTAI 81
Cdd:TIGR02108   1 HIVVLGSAAGGGFPQWNCNCPNCRGARAGTIGAKARTQSSIAVSADGERWVLLNASPDIRQQIQATPALHPQRGLRHTPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   82 GAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEgFPLFPMLSHWNggLRHRPIALDGEP-FAIPACPRLRFTAI 160
Cdd:TIGR02108  81 AGVVLTDGEIDHTTGLLTLREGQPFTLYATEMVLQDLSD-NPIFNVLDHWN--VRRQPIALNEKFeFRIVARPGLEFTPF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  161 PLRSSAPPYSPHR-GDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTLWRDDEMLVCEVGDKL 239
Cdd:TIGR02108 158 AVPGKAPLYSEHRaGDPHPGDTLGLKIEDGTTGKRLFYIPGCAEITDDLKARMAGADLVFFDGTLWRDDEMIRAGVGTKT 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489197160  240 GRQMGHLAQSGPGGMLEVLAKVPAARKVLIHINNTNPILDTASAERAELDASGIEVAWDGMHIQL 304
Cdd:TIGR02108 238 GRRMGHVSMSGEGGSLAVLADLEIARKVLIHINNTNPILDEDSPERAEVEAAGWEVAYDGMEIVL 302
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
1-222 1.39e-129

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. 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: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 367.71  E-value: 1.39e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRGVRDGSVAAQPRTQSSIALSDDGERWILCNASPDIRAQIAAFPALQPARRPRDTA 80
Cdd:cd16274    1 MRIKVLGSAAGGGFPQWNCNCPNCALARAGDGRATARTQSSIAVSADGENWVLINASPDIRQQIEATPELQPRPGLRDTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLsHWNGGLRHRPIALdGEPFAIPACPRLRFTAI 160
Cdd:cd16274   81 IAAVLLTDAEIDHTTGLLSLREGQPLTVYATAPVLEDLTTNFPFFVLL-HAYGGVRRHRILP-GEPFTLAGCPGLTVTPF 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489197160 161 PLRSSAPPYSPHRGDPHPGDNIGLFVEDLDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDG 222
Cdd:cd16274  159 PVPGKAPLYSEHRDAPEPGDTIGLRIEDGRTGGRLFYAPGCAAVTDELRARLAGADCLLFDG 220
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
1-304 2.30e-66

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 208.21  E-value: 2.30e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCrgvrDGSVAAQPRTQSSIALSDDGERwILCNASPDIRAQIAAFPAlqparrpRDTA 80
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC----ASTDPRYGRTRSSILVEADGTR-LLIDAGPDLREQLLRLGL-------DPSK 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGC---PHEVWCTQMVHQDLSEGFPLfpMLSHWNGGLRHRPIAlDGEPFAIPAcprLRF 157
Cdd:COG1235   69 IDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFPY--LFAPYPGKLEFHEIE-PGEPFEIGG---LTV 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160 158 TAIPLrssappysPHRgdphPGDNIGLFVEdlDSAGTLFYAPGLGEVDEALLEWMRRADCLLVDGTlwRDDEmlvcevgd 237
Cdd:COG1235  143 TPFPV--------PHD----AGDPVGYRIE--DGGKKLAYATDTGYIPEEVLELLRGADLLILDAT--YDDP-------- 198
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489197160 238 klgrQMGHLAQSgpgGMLEVLAKVPAARKVLIHIN--NTNPILDTASAERAELDAsGIEVAWDGMHIQL 304
Cdd:COG1235  199 ----EPGHLSNE---EALELLARLGPKRLVLTHLSpdNNDHELDYDELEAALLPA-GVEVAYDGMEIEL 259
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
50-271 6.30e-58

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: 184.44  E-value: 6.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   50 RWILCNASPDIRAQiaAFPALQPaRRPRDTAIGAIVLLDSQIDHTTGLLSLREGCPHEVWCTQMVHQDLSEGFPLFPMLS 129
Cdd:pfam12706   1 RRILIDPGPDLRQQ--ALPALQP-GRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  130 HWngGLRHRPIALdGEPFAIpACPRLRFTAIPLRSSAPPysphRGDPHPGDNIGLFVEdlDSAGTLFYAPGLGEVDEALL 209
Cdd:pfam12706  78 HY--GVRVHEIDW-GESFTV-GDGGLTVTATPARHGSPR----GLDPNPGDTLGFRIE--GPGKRVYYAGDTGYFPDEIG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489197160  210 EWMRRADCLLVDGTLWRDDEMLvcevgdklgrQMGHLaqsGPGGMLEVLAKVPAARKVLIHI 271
Cdd:pfam12706 148 ERLGGADLLLLDGGAWRDDEMI----------HMGHM---TPEEAVEAAADLGARRKVLIHI 196
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
1-167 4.09e-10

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 58.02  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRgvRDGSVAAQPRTQSSIALSDDGERWILCNASPDIrAQIaaFPAlqparrprdTA 80
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQ--RARQDPSYRRRPCSALIEVDGERILLDAGLTDL-AER--FPP---------GS 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  81 IGAIVLLDSQIDHTTGLLSLREGCPHE--VWCTqmvhqDLSEGFP-LFpmlSHwNGGLRHRPIALDGEPFAIPAcprLRF 157
Cdd:cd07736   67 IDAILLTHFHMDHVQGLFHLRWGVGDPipVYGP-----PDPQGCAdLF---KH-PGILDFQPLVAPFQSFELGG---LKI 134
                        170
                 ....*....|
gi 489197160 158 TAIPLRSSAP 167
Cdd:cd07736  135 TPLPLNHSKP 144
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
1-162 4.32e-09

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 55.17  E-value: 4.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCR--GVRDgsvaaqPRTQSSIALSDDGERwILCNASPDIRAQiaafpalqpARRPRD 78
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVCDssDPKN------RRLRSSILIETGGKN-ILIDTGPDFRQQ---------ALRAGI 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160  79 TAIGAIVLLDSQIDHTTGLLSLREGCPH-----EVWCTQMVHQDLSEGFPLFPMLSHWNG--GLRHRPIAlDGEPFAIPA 151
Cdd:cd16279   65 RKLDAVLLTHAHADHIHGLDDLRPFNRLqqrpiPVYASEETLDDLKRRFPYFFAATGGGGvpKLDLHIIE-PDEPFTIGG 143
                        170
                 ....*....|.
gi 489197160 152 cprLRFTAIPL 162
Cdd:cd16279  144 ---LEITPLPV 151
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-106 3.15e-07

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 50.55  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489197160   1 MHIRILGSAAGGGFPQWNCNCRNCRGV--RDGsvaaqpRTQSSIALSDDGERwILCNASPDIRAQIAAFPAlqparrprd 78
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKdpRDN------RLRTSALVETEGAR-ILIDCGPDFREQMLRLPF--------- 64
                         90       100
                 ....*....|....*....|....*...
gi 489197160  79 TAIGAIVLLDSQIDHTTGLLSLREGCPH 106
Cdd:PRK02113  65 GKIDAVLITHEHYDHVGGLDDLRPFCRF 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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