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Conserved domains on  [gi|1948761234|ref|WP_198411226|]
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SpoIIE family protein phosphatase [Marinimicrobium alkaliphilum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
prot_phos_SiaA super family cl45717
biofilm regulation protein phosphatase SiaA;
149-410 7.36e-59

biofilm regulation protein phosphatase SiaA;


The actual alignment was detected with superfamily member NF038263:

Pssm-ID: 439563 [Multi-domain]  Cd Length: 658  Bit Score: 202.97  E-value: 7.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 149 AEKNRQIMHSIDYASVIQRAMLrtSDQALSESLPTAH-LEWQPRDTVGGDFYHFVNRAEGWFAAIADCTGHGVPGAFMTL 227
Cdd:NF038263  405 AAAHKKIQDSIDYASLIQRAIL--PDRQLTRALGEHHfVLWKPRDVVGGDFYLFREDEGGYLIGVVDCAGHGVPGALMTM 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 228 IASSCLGQALEKLGPEDPAALLAEVNQSIKSQLGQC------STNgitpesddgFDATFMWFDRRSQALTVAGAKAALFs 301
Cdd:NF038263  483 LARAAIDHAIQELGLDDPAAILRRTDQALRAMLRDAelpralATN---------MDAGLVYVDLRRGRLRFAGAKISLY- 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 302 lSPDSEEVLHFKGDRMGVGHVDTPDnfkWHNQRLFLPPETLVLVTTDGLIDQIGDRKNIAFGKRPIRTLLQNQRQATPAA 381
Cdd:NF038263  553 -ASDGEEVEELKGGRRALGDRRRGE---YENIELPLEPGWTYYLTTDGFLDQAGGEHGFGFGNRRFAELLRRHARLPLAE 628

                         250       260
                  ....*....|....*....|....*....
gi 1948761234 382 LSKSLLDQLSLWQGEELRRDDLTFFCFRI 410
Cdd:NF038263  629 QAEAFEQALAEYQGEHPQRDDITVLSFRF 657
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 30-141 1.95e-51

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


:

Pssm-ID: 341373 [Multi-domain]  Cd Length: 121  Bit Score: 168.38  E-value: 1.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  30 VSPDLTNQDVQALFDQHAKVTSLPVVDNGLPVGLINRDRFLTQVAKPFHKEVYGRKNCTLFMDAEPLIVDQGLSIEALTF 109
Cdd:cd04598     8 VSPDTTNDEVYELFEENPDLHALPVVDNGRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMDKDPLVVDADTPIEELSQ 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1948761234 110 QAVASGEKALSDGFIITDDNTYLGLGSGMDLM 141
Cdd:cd04598    88 LATSRDQRYLYDGFIITENGRYLGVGTGRDLL 119
 
Name Accession Description Interval E-value
prot_phos_SiaA NF038263
biofilm regulation protein phosphatase SiaA;
149-410 7.36e-59

biofilm regulation protein phosphatase SiaA;


Pssm-ID: 439563 [Multi-domain]  Cd Length: 658  Bit Score: 202.97  E-value: 7.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 149 AEKNRQIMHSIDYASVIQRAMLrtSDQALSESLPTAH-LEWQPRDTVGGDFYHFVNRAEGWFAAIADCTGHGVPGAFMTL 227
Cdd:NF038263  405 AAAHKKIQDSIDYASLIQRAIL--PDRQLTRALGEHHfVLWKPRDVVGGDFYLFREDEGGYLIGVVDCAGHGVPGALMTM 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 228 IASSCLGQALEKLGPEDPAALLAEVNQSIKSQLGQC------STNgitpesddgFDATFMWFDRRSQALTVAGAKAALFs 301
Cdd:NF038263  483 LARAAIDHAIQELGLDDPAAILRRTDQALRAMLRDAelpralATN---------MDAGLVYVDLRRGRLRFAGAKISLY- 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 302 lSPDSEEVLHFKGDRMGVGHVDTPDnfkWHNQRLFLPPETLVLVTTDGLIDQIGDRKNIAFGKRPIRTLLQNQRQATPAA 381
Cdd:NF038263  553 -ASDGEEVEELKGGRRALGDRRRGE---YENIELPLEPGWTYYLTTDGFLDQAGGEHGFGFGNRRFAELLRRHARLPLAE 628

                         250       260
                  ....*....|....*....|....*....
gi 1948761234 382 LSKSLLDQLSLWQGEELRRDDLTFFCFRI 410
Cdd:NF038263  629 QAEAFEQALAEYQGEHPQRDDITVLSFRF 657
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 30-141 1.95e-51

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341373 [Multi-domain]  Cd Length: 121  Bit Score: 168.38  E-value: 1.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  30 VSPDLTNQDVQALFDQHAKVTSLPVVDNGLPVGLINRDRFLTQVAKPFHKEVYGRKNCTLFMDAEPLIVDQGLSIEALTF 109
Cdd:cd04598     8 VSPDTTNDEVYELFEENPDLHALPVVDNGRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMDKDPLVVDADTPIEELSQ 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1948761234 110 QAVASGEKALSDGFIITDDNTYLGLGSGMDLM 141
Cdd:cd04598    88 LATSRDQRYLYDGFIITENGRYLGVGTGRDLL 119
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
 148-411 2.45e-47

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 167.55  E-value: 2.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 148 QAEKNRQIMHSIDYASVIQRAMLRTSDQALsESLPTAHLeWQPRDTVGGDFYHFVNRAEG-WFAAIADCTGHGVPGAFMT 226
Cdd:COG2208   189 EEEKNRRLERELELARRIQRSLLPPRLPEV-PGLDIAAR-YRPADEVGGDFYDVFPLDDGrLAVVIGDVSGHGVPAALLM 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 227 LIASSCLGQALEKLGpeDPAALLAEVNQSIKSQLGQCSTngitpesddgFDATFMWFDRRSQALTVAGAK--AALFsLSP 304
Cdd:COG2208   267 AMLRSALRALAREGL--DPAEVLERLNRALYEDLGGGRF----------VTAFLGVLDPETGRLTYANAGhpPPLL-LRA 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 305 DsEEVLHFKGDRMGVGhvdTPDNFKWHNQRLFLPPETLVLVTTDGLIDQIgDRKNIAFGKRPIRTLLQNQRQATPAALSK 384
Cdd:COG2208   334 D-GEVEELDGGGLPLG---LLPDAEYEEHEIPLEPGDRLLLYTDGLTEAR-NGDGELFGEERLLELLAENADLPAEELLD 408

                         250       260
                  ....*....|....*....|....*..
gi 1948761234 385 SLLDQLSLWQGEELRRDDLTFFCFRIH 411
Cdd:COG2208   409 ALLEALEEFRGGGPQEDDITLLALRRR 435
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
 207-411 1.33e-16

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 77.69  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 207 GWFAAIADCTGHGVPGAFMTLIASSCLgQALEKLGPeDPAALLAEVNQSIKSQLgqcstngitpESDDGFDATFMWFDRR 286
Cdd:pfam07228   4 RLALVIGDVMGHGLPAALLMGLLRTAL-RALAAEGL-DPAEVLKRLNRLLQRNL----------EEDMFATAVLAVYDPE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 287 SQALTVAGA---KAALFSLSPDSEEVLHFKGDRMGVghvdtPDNFKWHNQRLFLPPETLVLVTTDGLIDQIGDRKNIaFG 363
Cdd:pfam07228  72 TGTLEYANAghpPPLLLRPDGGVVELLESPGLPLGI-----LPDAPYEVVELELEPGDTLLLYTDGLTEARDPDGEL-FG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1948761234 364 KRPIRTLLQNQRQATPAALSKSLLDQLSLWQGEELrRDDLTFFCFRIH 411
Cdd:pfam07228 146 LERLLALLAERHGLPPEELLDALLEALLRLGGGEL-EDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
193-390 4.41e-07

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 50.04  E-value: 4.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  193 TVGGDFYHFVNRAEG-WFAAIADCTGHGVPGAFMTLIASSCLGQALEKLgpEDPAALLAEVNQSIKSQLgqcstngitpE 271
Cdd:smart00331  15 QVGGDFYDVVKLPEGrLLIAIADVMGKGLAAALAMSMARSALRTLLSEG--ISLSQILERLNRAIYENG----------E 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  272 SDDGFDATFMWFDRRSQALTVAGAKAALFSL-SPDSEEVLHFKGDRMGVGHVDTPDNFKwhnQRLFLPPETLVLVTTDGL 350
Cdd:smart00331  83 DGMFATLFLALYDFAGGTLSYANAGHSPPYLlRADGGLVEDLDDLGAPLGLEPDVEVDV---RELTLEPGDLLLLYTDGL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1948761234  351 IdqigDRKNIAFGKRPIRTLLQNqrqaTPAALSKSLLDQL 390
Cdd:smart00331 160 T----EARNPERLEELLEELLGS----PPAEIAQRILEEL 191
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
30-151 1.78e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 41.39  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  30 VSPDLTNQDVQALFDQHaKVTSLPVVD-NGLPVGLINRDRFLTQVAKPFHKEVYGRKNCTL---FMDAEPLIVDQGLSIE 105
Cdd:COG3448    15 VSPDTTLREALELMREH-GIRGLPVVDeDGRLVGIVTERDLLRALLPDRLDELEERLLDLPvedVMTRPVVTVTPDTPLE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1948761234 106 ALTFQAVASGEKALsdgFIITDDNTYLGLGSGMDLMNLVAELQAEK 151
Cdd:COG3448    94 EAAELMLEHGIHRL---PVVDDDGRLVGIVTRTDLLRALARLLEEE 136
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 30-105 4.98e-04

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 41.99  E-value: 4.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948761234  30 VSPDLTNQDVQALFDQHaKVTSLPVVDNGLPVGLI-NRD-RFLTQVAKPFhKEVygrknctlfMDAEPLI-VDQGLSIE 105
Cdd:pfam00478  93 LSPDATVADALALMERY-GISGVPVVDDGKLVGIVtNRDlRFETDLSQPV-SEV---------MTKENLVtAPEGTTLE 160
 
Name Accession Description Interval E-value
prot_phos_SiaA NF038263
biofilm regulation protein phosphatase SiaA;
149-410 7.36e-59

biofilm regulation protein phosphatase SiaA;


Pssm-ID: 439563 [Multi-domain]  Cd Length: 658  Bit Score: 202.97  E-value: 7.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 149 AEKNRQIMHSIDYASVIQRAMLrtSDQALSESLPTAH-LEWQPRDTVGGDFYHFVNRAEGWFAAIADCTGHGVPGAFMTL 227
Cdd:NF038263  405 AAAHKKIQDSIDYASLIQRAIL--PDRQLTRALGEHHfVLWKPRDVVGGDFYLFREDEGGYLIGVVDCAGHGVPGALMTM 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 228 IASSCLGQALEKLGPEDPAALLAEVNQSIKSQLGQC------STNgitpesddgFDATFMWFDRRSQALTVAGAKAALFs 301
Cdd:NF038263  483 LARAAIDHAIQELGLDDPAAILRRTDQALRAMLRDAelpralATN---------MDAGLVYVDLRRGRLRFAGAKISLY- 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 302 lSPDSEEVLHFKGDRMGVGHVDTPDnfkWHNQRLFLPPETLVLVTTDGLIDQIGDRKNIAFGKRPIRTLLQNQRQATPAA 381
Cdd:NF038263  553 -ASDGEEVEELKGGRRALGDRRRGE---YENIELPLEPGWTYYLTTDGFLDQAGGEHGFGFGNRRFAELLRRHARLPLAE 628

                         250       260
                  ....*....|....*....|....*....
gi 1948761234 382 LSKSLLDQLSLWQGEELRRDDLTFFCFRI 410
Cdd:NF038263  629 QAEAFEQALAEYQGEHPQRDDITVLSFRF 657
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 30-141 1.95e-51

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341373 [Multi-domain]  Cd Length: 121  Bit Score: 168.38  E-value: 1.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  30 VSPDLTNQDVQALFDQHAKVTSLPVVDNGLPVGLINRDRFLTQVAKPFHKEVYGRKNCTLFMDAEPLIVDQGLSIEALTF 109
Cdd:cd04598     8 VSPDTTNDEVYELFEENPDLHALPVVDNGRPVGLINRHQFLDRLATPYGRELYGKRPCSLFMDKDPLVVDADTPIEELSQ 87

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1948761234 110 QAVASGEKALSDGFIITDDNTYLGLGSGMDLM 141
Cdd:cd04598    88 LATSRDQRYLYDGFIITENGRYLGVGTGRDLL 119
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
 148-411 2.45e-47

Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 167.55  E-value: 2.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 148 QAEKNRQIMHSIDYASVIQRAMLRTSDQALsESLPTAHLeWQPRDTVGGDFYHFVNRAEG-WFAAIADCTGHGVPGAFMT 226
Cdd:COG2208   189 EEEKNRRLERELELARRIQRSLLPPRLPEV-PGLDIAAR-YRPADEVGGDFYDVFPLDDGrLAVVIGDVSGHGVPAALLM 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 227 LIASSCLGQALEKLGpeDPAALLAEVNQSIKSQLGQCSTngitpesddgFDATFMWFDRRSQALTVAGAK--AALFsLSP 304
Cdd:COG2208   267 AMLRSALRALAREGL--DPAEVLERLNRALYEDLGGGRF----------VTAFLGVLDPETGRLTYANAGhpPPLL-LRA 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 305 DsEEVLHFKGDRMGVGhvdTPDNFKWHNQRLFLPPETLVLVTTDGLIDQIgDRKNIAFGKRPIRTLLQNQRQATPAALSK 384
Cdd:COG2208   334 D-GEVEELDGGGLPLG---LLPDAEYEEHEIPLEPGDRLLLYTDGLTEAR-NGDGELFGEERLLELLAENADLPAEELLD 408

                         250       260
                  ....*....|....*....|....*..
gi 1948761234 385 SLLDQLSLWQGEELRRDDLTFFCFRIH 411
Cdd:COG2208   409 ALLEALEEFRGGGPQEDDITLLALRRR 435
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
 207-411 1.33e-16

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 77.69  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 207 GWFAAIADCTGHGVPGAFMTLIASSCLgQALEKLGPeDPAALLAEVNQSIKSQLgqcstngitpESDDGFDATFMWFDRR 286
Cdd:pfam07228   4 RLALVIGDVMGHGLPAALLMGLLRTAL-RALAAEGL-DPAEVLKRLNRLLQRNL----------EEDMFATAVLAVYDPE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234 287 SQALTVAGA---KAALFSLSPDSEEVLHFKGDRMGVghvdtPDNFKWHNQRLFLPPETLVLVTTDGLIDQIGDRKNIaFG 363
Cdd:pfam07228  72 TGTLEYANAghpPPLLLRPDGGVVELLESPGLPLGI-----LPDAPYEVVELELEPGDTLLLYTDGLTEARDPDGEL-FG 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1948761234 364 KRPIRTLLQNQRQATPAALSKSLLDQLSLWQGEELrRDDLTFFCFRIH 411
Cdd:pfam07228 146 LERLLALLAERHGLPPEELLDALLEALLRLGGGEL-EDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
193-390 4.41e-07

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 50.04  E-value: 4.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  193 TVGGDFYHFVNRAEG-WFAAIADCTGHGVPGAFMTLIASSCLGQALEKLgpEDPAALLAEVNQSIKSQLgqcstngitpE 271
Cdd:smart00331  15 QVGGDFYDVVKLPEGrLLIAIADVMGKGLAAALAMSMARSALRTLLSEG--ISLSQILERLNRAIYENG----------E 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  272 SDDGFDATFMWFDRRSQALTVAGAKAALFSL-SPDSEEVLHFKGDRMGVGHVDTPDNFKwhnQRLFLPPETLVLVTTDGL 350
Cdd:smart00331  83 DGMFATLFLALYDFAGGTLSYANAGHSPPYLlRADGGLVEDLDDLGAPLGLEPDVEVDV---RELTLEPGDLLLLYTDGL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1948761234  351 IdqigDRKNIAFGKRPIRTLLQNqrqaTPAALSKSLLDQL 390
Cdd:smart00331 160 T----EARNPERLEELLEELLGS----PPAEIAQRILEEL 191
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
30-151 1.78e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 41.39  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234  30 VSPDLTNQDVQALFDQHaKVTSLPVVD-NGLPVGLINRDRFLTQVAKPFHKEVYGRKNCTL---FMDAEPLIVDQGLSIE 105
Cdd:COG3448    15 VSPDTTLREALELMREH-GIRGLPVVDeDGRLVGIVTERDLLRALLPDRLDELEERLLDLPvedVMTRPVVTVTPDTPLE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1948761234 106 ALTFQAVASGEKALsdgFIITDDNTYLGLGSGMDLMNLVAELQAEK 151
Cdd:COG3448    94 EAAELMLEHGIHRL---PVVDDDGRLVGIVTRTDLLRALARLLEEE 136
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 30-105 4.98e-04

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 41.99  E-value: 4.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1948761234  30 VSPDLTNQDVQALFDQHaKVTSLPVVDNGLPVGLI-NRD-RFLTQVAKPFhKEVygrknctlfMDAEPLI-VDQGLSIE 105
Cdd:pfam00478  93 LSPDATVADALALMERY-GISGVPVVDDGKLVGIVtNRDlRFETDLSQPV-SEV---------MTKENLVtAPEGTTLE 160
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
9-107 6.32e-04

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 40.64  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948761234   9 RTTMPRPTQVSARDLCAHQLQ-VSPDLTNQDVQALFDQHaKVTSLPVVDNGLPVGLINRDRFLTQVAkpfhkEVYGRKNC 87
Cdd:COG2524    77 EKELGLVLKMKVKDIMTKDVItVSPDTTLEEALELMLEK-GISGLPVVDDGKLVGIITERDLLKALA-----EGRDLLDA 150

                          90       100
                  ....*....|....*....|...
gi 1948761234  88 TL--FMDAEPLIVDQGLSI-EAL 107
Cdd:COG2524   151 PVsdIMTRDVVTVSEDDSLeEAL 173
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 30-89 7.06e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 38.93  E-value: 7.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1948761234  30 VSPDLTNQDVQALFDQHaKVTSLPVVDNG--LpVGLI-NRD-RFLT-------QVAKPFHKEVYGRKNCTL 89
Cdd:cd04601     7 LSPDATVADVLELKAEY-GISGVPVTEDGgkL-VGIVtSRDiRFETdlstpvsEVMTPDERLVTAPEGITL 75
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 14-70 7.51e-04

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.04  E-value: 7.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1948761234  14 RPTQVSARDLCAHQLQ-VSPDLTNQDVQALFDQHaKVTSLPVVDNGLPVGLINRDRFL 70
Cdd:COG2905    61 DPLDTPVSEVMTRPPItVSPDDSLAEALELMEEH-RIRHLPVVDDGKLVGIVSITDLL 117
 
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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