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Conserved domains on  [gi|896406034|ref|WP_049343032|]
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MULTISPECIES: N-acetylneuraminate synthase family protein [Rothia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
 129-460 4.14e-153

Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 448.39  E-value: 4.14e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 129 SPAFIIAEIGNNHQGSVDFAKELVDLAVESGADAVKFQLRDMDALYRQRGAA---TAGEDLGVQYTLDLLSRFSLSVDQM 205
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKafyQSGSLWGGESLYELYKRLELPWEWH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 206 YEVFDHVKQHNMDIMCTPWDAPSVQALVDYGIQGMKIASADLTNHELLRDVASRGLPMLVSTGMSREEEIRESVALLRNA 285
Cdd:COG2089   81 KELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 286 GAS-YALLQCQSAYPAPFKDVNLAYMDRLAEIGQCLVGYSGHERGYHVPIAAVARGAKIIEKHFTTDKTLEGNDHTVSLL 364
Cdd:COG2089  161 GNDqIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 365 PEEFKAMVQQIREVEAAIGSAApREVSTGELMNRVNLAKSLVATRHIAKGEVVTEADVAVKSPGRGLQPNHLPQLVGRTM 444
Cdd:COG2089  241 PDELKAMVEAIRNAEKALGSGI-KGPTPSEKKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKA 319

                        330
                 ....*....|....*.
gi 896406034 445 QRDVEEGSFFFEGDLK 460
Cdd:COG2089  320 KRDIKAGTPLTWDDLE 335
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 2-119 8.23e-62

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase; This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). 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: 341409 [Multi-domain]  Cd Length: 118  Bit Score: 202.86  E-value: 8.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   2 IIERNIAPYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSALDAANTNPQTAPAD 81
Cdd:cd17773    1 IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLENPNADLSQPVSHVANTNFVSAPEG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 896406034  82 ADPETLRAYFAKGINHVPLTDERGHLVALAMDEQDVLR 119
Cdd:cd17773   81 ESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR 118
AP2Ec super family cl23721
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
 516-746 6.54e-17

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


The actual alignment was detected with superfamily member pfam01261:

Pssm-ID: 474032 [Multi-domain]  Cd Length: 248  Bit Score: 80.88  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  516 KLDMGFTTHLPDLFAGdflvdLASKDPEVWERSIAEVQRTIDITRDL-TRYftvdedpimVVTMGGFTKDKHIPVSeRAE 594
Cdd:pfam01261  38 EHGLEIVVHAPYLGDN-----LASPDEEEREKAIDRLKRAIELAAALgAKL---------VVFHPGSDLGDDPEEA-LAR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  595 KYERIGEALKHLDASGVRLAAQTLPPYPWLMGGqqyhnlflDPKDTAEFSRAYDTA---LCLDISHTMLASNFlniplSE 671
Cdd:pfam01261 103 LAESLRELADLAEREGVRLALEPLAGKGTNVGN--------TFEEALEIIDEVDSPnvgVCLDTGHLFAAGDG-----DL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  672 AVEQLAPLSI-HLHLVDGVGVDGEG----VQVGEGDVDWAALGKQLRELAPKASFIPEIWqGHINNGEGFFTALDRLEKW 746
Cdd:pfam01261 170 FELRLGDRYIgHVHLKDSKNPLGSGpdrhVPIGEGVIDFEALFRALKEIGYDGPLSLETF-NDGPPEEGAREGLEWLREL 248
 
Name Accession Description Interval E-value
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
 129-460 4.14e-153

Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 448.39  E-value: 4.14e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 129 SPAFIIAEIGNNHQGSVDFAKELVDLAVESGADAVKFQLRDMDALYRQRGAA---TAGEDLGVQYTLDLLSRFSLSVDQM 205
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKafyQSGSLWGGESLYELYKRLELPWEWH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 206 YEVFDHVKQHNMDIMCTPWDAPSVQALVDYGIQGMKIASADLTNHELLRDVASRGLPMLVSTGMSREEEIRESVALLRNA 285
Cdd:COG2089   81 KELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 286 GAS-YALLQCQSAYPAPFKDVNLAYMDRLAEIGQCLVGYSGHERGYHVPIAAVARGAKIIEKHFTTDKTLEGNDHTVSLL 364
Cdd:COG2089  161 GNDqIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 365 PEEFKAMVQQIREVEAAIGSAApREVSTGELMNRVNLAKSLVATRHIAKGEVVTEADVAVKSPGRGLQPNHLPQLVGRTM 444
Cdd:COG2089  241 PDELKAMVEAIRNAEKALGSGI-KGPTPSEKKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKA 319

                        330
                 ....*....|....*.
gi 896406034 445 QRDVEEGSFFFEGDLK 460
Cdd:COG2089  320 KRDIKAGTPLTWDDLE 335
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
 152-384 6.39e-100

NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.


Pssm-ID: 427137  Cd Length: 239  Bit Score: 307.52  E-value: 6.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  152 VDLAVESGADAVKFQLRDMDALY--RQRGAATAGEDLGVQYTLDLLSRFSLSVDQMYEVFDHVKQHNMDIMCTPWDAPSV 229
Cdd:pfam03102   1 IDAAAEAGADAVKFQTFTAETLVskEAPKADYQITTWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFDLESV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  230 QALVDYGIQGMKIASADLTNHELLRDVASRGLPMLVSTGMSREEEIRESVALLRNAGAS-YALLQCQSAYPAPFKDVNLA 308
Cdd:pfam03102  81 DFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEdLTLLHCTSEYPAPFEDVNLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896406034  309 YMDRLAEIGQCLVGYSGHERGYHVPIAAVARGAKIIEKHFTTDKTLEGNDHTVSLLPEEFKAMVQQIREVEAAIGS 384
Cdd:pfam03102 161 AIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALGD 236
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 2-119 8.23e-62

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase; This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). 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: 341409 [Multi-domain]  Cd Length: 118  Bit Score: 202.86  E-value: 8.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   2 IIERNIAPYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSALDAANTNPQTAPAD 81
Cdd:cd17773    1 IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLENPNADLSQPVSHVANTNFVSAPEG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 896406034  82 ADPETLRAYFAKGINHVPLTDERGHLVALAMDEQDVLR 119
Cdd:cd17773   81 ESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR 118
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
 402-459 1.60e-18

C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).


Pssm-ID: 212160 [Multi-domain]  Cd Length: 58  Bit Score: 79.69  E-value: 1.60e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896406034 402 AKSLVATRHIAKGEVVTEADVAVKSPGRGLQPNHLPQLVGRTMQRDVEEGSFFFEGDL 459
Cdd:cd11615    1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
 516-746 6.54e-17

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 80.88  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  516 KLDMGFTTHLPDLFAGdflvdLASKDPEVWERSIAEVQRTIDITRDL-TRYftvdedpimVVTMGGFTKDKHIPVSeRAE 594
Cdd:pfam01261  38 EHGLEIVVHAPYLGDN-----LASPDEEEREKAIDRLKRAIELAAALgAKL---------VVFHPGSDLGDDPEEA-LAR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  595 KYERIGEALKHLDASGVRLAAQTLPPYPWLMGGqqyhnlflDPKDTAEFSRAYDTA---LCLDISHTMLASNFlniplSE 671
Cdd:pfam01261 103 LAESLRELADLAEREGVRLALEPLAGKGTNVGN--------TFEEALEIIDEVDSPnvgVCLDTGHLFAAGDG-----DL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  672 AVEQLAPLSI-HLHLVDGVGVDGEG----VQVGEGDVDWAALGKQLRELAPKASFIPEIWqGHINNGEGFFTALDRLEKW 746
Cdd:pfam01261 170 FELRLGDRYIgHVHLKDSKNPLGSGpdrhVPIGEGVIDFEALFRALKEIGYDGPLSLETF-NDGPPEEGAREGLEWLREL 248
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
541-747 7.39e-15

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 75.05  E-value: 7.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 541 DPEVWERSIAEVQRTIDITRDLtryftvdEDPIMVVTMGGFTKDKHIPVSERAEKYERIGEALKHLDASGVRLAaqtlpp 620
Cdd:COG1082   69 DPEVREAALERLKRAIDLAAEL-------GAKVVVVHPGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLA------ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 621 ypwlmggqqYHN----LFLDPKDTAEFSRAYDTA---LCLDISHTMLAsnflNIPLSEAVEQLAPLSIHLHLVDGVGvdG 693
Cdd:COG1082  136 ---------LENhegtFVNTPEEALRLLEAVDSPnvgLLLDTGHALLA----GEDPVELLRKLGDRIKHVHLKDADG--D 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896406034 694 EGVQVGEGDVDWAALGKQLRELAPKASFIPEIWQGHINNGEGFFTALDRLEKWL 747
Cdd:COG1082  201 QHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDPDDPEEAARESLEYLRKLL 254
CBS COG0517
CBS domain [Signal transduction mechanisms];
9-108 1.58e-13

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 67.97  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   9 PYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSALDAANTNPQTAPADADPETLR 88
Cdd:COG0517   11 VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAA 90

                         90       100
                 ....*....|....*....|.
gi 896406034  89 AYFAK-GINHVPLTDERGHLV 108
Cdd:COG0517   91 ELMEEhKIRRLPVVDDDGRLV 111
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
 402-460 3.19e-06

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins;


Pssm-ID: 214862 [Multi-domain]  Cd Length: 63  Bit Score: 44.86  E-value: 3.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896406034   402 AKSLVATRHIAKGEVVTEADVAVKS------PGRGLQPNHlpQLVGRTMQRDVEEGSFFFEGDLK 460
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTPYG--QVIGRVARRDIAAGEPITASNLE 63
kpsF TIGR00393
KpsF/GutQ family protein; This model describes a number of closely related proteins with the ...
 21-110 2.35e-04

KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars]


Pssm-ID: 129488 [Multi-domain]  Cd Length: 268  Bit Score: 43.64  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   21 ALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLiaNPTASLETSALDAANTNPQTAPADA-DPETLRAYFAKGINHVP 99
Cdd:TIGR00393 178 ALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRAL--LGGGSLKSEVRDFMTLGPKTFKLDAlLLEALEFLERRKITSLV 255

                          90
                  ....*....|.
gi 896406034  100 LTDERGHLVAL 110
Cdd:TIGR00393 256 VVDDHNKVLGV 266
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
11-121 5.71e-04

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 42.83  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  11 VVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANptASLETSALDAANTNPQTAPADADP-ETLRA 89
Cdd:PRK11543 211 QVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGG--GALTTPVNEAMTRGGTTLQAQSRAiDAKEI 288

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896406034  90 YFAKGINHVPLTDERGHLVAlAMDEQDVLRIG 121
Cdd:PRK11543 289 LMKRKITAAPVVDENGKLTG-AINLQDFYQAG 319
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
 533-746 2.46e-03

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 40.38  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 533 FLVDLASKDPEVWERSIAEVQRTIDITRDLTRYFtvdedpimVVTMGGFTKDKhipvsERAEKYERIGEALKHLDAS--- 609
Cdd:cd00019   68 YLINLASPDKEKREKSIERLKDEIERCEELGIRL--------LVFHPGSYLGQ-----SKEEGLKRVIEALNELIDKaet 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 610 -GVRLAAQTlppypwlMGGqQYHNLfldPKDTAEFSRAYDTA-------LCLDISHTMLASNFLNIPLS-----EAVEQL 676
Cdd:cd00019  135 kGVVIALET-------MAG-QGNEI---GSSFEELKEIIDLIkekprvgVCIDTCHIFAAGYDISTVEGfekvlEEFDKV 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896406034 677 APLS--IHLHLVDGVGVDGEG----VQVGEGDVDWAALGKQLREL-APKASFIPEIWqGHINNGEGFFTALDRLEKW 746
Cdd:cd00019  204 IGLEylKAIHLNDSKGELGSGkdrhEPIGEGDIDGEELFKELKKDpYQNIPLILETP-SENRDAAKIKKEIKLLRKL 279
 
Name Accession Description Interval E-value
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
 129-460 4.14e-153

Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 448.39  E-value: 4.14e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 129 SPAFIIAEIGNNHQGSVDFAKELVDLAVESGADAVKFQLRDMDALYRQRGAA---TAGEDLGVQYTLDLLSRFSLSVDQM 205
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTSDSAPKafyQSGSLWGGESLYELYKRLELPWEWH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 206 YEVFDHVKQHNMDIMCTPWDAPSVQALVDYGIQGMKIASADLTNHELLRDVASRGLPMLVSTGMSREEEIRESVALLRNA 285
Cdd:COG2089   81 KELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 286 GAS-YALLQCQSAYPAPFKDVNLAYMDRLAEIGQCLVGYSGHERGYHVPIAAVARGAKIIEKHFTTDKTLEGNDHTVSLL 364
Cdd:COG2089  161 GNDqIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 365 PEEFKAMVQQIREVEAAIGSAApREVSTGELMNRVNLAKSLVATRHIAKGEVVTEADVAVKSPGRGLQPNHLPQLVGRTM 444
Cdd:COG2089  241 PDELKAMVEAIRNAEKALGSGI-KGPTPSEKKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKA 319

                        330
                 ....*....|....*.
gi 896406034 445 QRDVEEGSFFFEGDLK 460
Cdd:COG2089  320 KRDIKAGTPLTWDDLE 335
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
 152-384 6.39e-100

NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.


Pssm-ID: 427137  Cd Length: 239  Bit Score: 307.52  E-value: 6.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  152 VDLAVESGADAVKFQLRDMDALY--RQRGAATAGEDLGVQYTLDLLSRFSLSVDQMYEVFDHVKQHNMDIMCTPWDAPSV 229
Cdd:pfam03102   1 IDAAAEAGADAVKFQTFTAETLVskEAPKADYQITTWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFDLESV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  230 QALVDYGIQGMKIASADLTNHELLRDVASRGLPMLVSTGMSREEEIRESVALLRNAGAS-YALLQCQSAYPAPFKDVNLA 308
Cdd:pfam03102  81 DFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEdLTLLHCTSEYPAPFEDVNLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896406034  309 YMDRLAEIGQCLVGYSGHERGYHVPIAAVARGAKIIEKHFTTDKTLEGNDHTVSLLPEEFKAMVQQIREVEAAIGS 384
Cdd:pfam03102 161 AIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALGD 236
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 2-119 8.23e-62

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase; This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). 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: 341409 [Multi-domain]  Cd Length: 118  Bit Score: 202.86  E-value: 8.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   2 IIERNIAPYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSALDAANTNPQTAPAD 81
Cdd:cd17773    1 IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLENPNADLSQPVSHVANTNFVSAPEG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 896406034  82 ADPETLRAYFAKGINHVPLTDERGHLVALAMDEQDVLR 119
Cdd:cd17773   81 ESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR 118
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 11-110 1.44e-18

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. 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: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 81.72  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  11 VVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANptASLETSALDAANTNPQTAPADADPETLRAY 90
Cdd:cd04607    6 LVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKG--LSLDAPVEEVMNKNPITASPSTSREELLAL 83

                         90       100
                 ....*....|....*....|.
gi 896406034  91 F-AKGINHVPLTDERGHLVAL 110
Cdd:cd04607   84 MrAKKILQLPIVDEQGRVVGL 104
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
 402-459 1.60e-18

C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).


Pssm-ID: 212160 [Multi-domain]  Cd Length: 58  Bit Score: 79.69  E-value: 1.60e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896406034 402 AKSLVATRHIAKGEVVTEADVAVKSPGRGLQPNHLPQLVGRTMQRDVEEGSFFFEGDL 459
Cdd:cd11615    1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
 516-746 6.54e-17

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 80.88  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  516 KLDMGFTTHLPDLFAGdflvdLASKDPEVWERSIAEVQRTIDITRDL-TRYftvdedpimVVTMGGFTKDKHIPVSeRAE 594
Cdd:pfam01261  38 EHGLEIVVHAPYLGDN-----LASPDEEEREKAIDRLKRAIELAAALgAKL---------VVFHPGSDLGDDPEEA-LAR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  595 KYERIGEALKHLDASGVRLAAQTLPPYPWLMGGqqyhnlflDPKDTAEFSRAYDTA---LCLDISHTMLASNFlniplSE 671
Cdd:pfam01261 103 LAESLRELADLAEREGVRLALEPLAGKGTNVGN--------TFEEALEIIDEVDSPnvgVCLDTGHLFAAGDG-----DL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  672 AVEQLAPLSI-HLHLVDGVGVDGEG----VQVGEGDVDWAALGKQLRELAPKASFIPEIWqGHINNGEGFFTALDRLEKW 746
Cdd:pfam01261 170 FELRLGDRYIgHVHLKDSKNPLGSGpdrhVPIGEGVIDFEALFRALKEIGYDGPLSLETF-NDGPPEEGAREGLEWLREL 248
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
541-747 7.39e-15

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 75.05  E-value: 7.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 541 DPEVWERSIAEVQRTIDITRDLtryftvdEDPIMVVTMGGFTKDKHIPVSERAEKYERIGEALKHLDASGVRLAaqtlpp 620
Cdd:COG1082   69 DPEVREAALERLKRAIDLAAEL-------GAKVVVVHPGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLA------ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 621 ypwlmggqqYHN----LFLDPKDTAEFSRAYDTA---LCLDISHTMLAsnflNIPLSEAVEQLAPLSIHLHLVDGVGvdG 693
Cdd:COG1082  136 ---------LENhegtFVNTPEEALRLLEAVDSPnvgLLLDTGHALLA----GEDPVELLRKLGDRIKHVHLKDADG--D 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 896406034 694 EGVQVGEGDVDWAALGKQLRELAPKASFIPEIWQGHINNGEGFFTALDRLEKWL 747
Cdd:COG1082  201 QHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDPDDPEEAARESLEYLRKLL 254
CBS COG0517
CBS domain [Signal transduction mechanisms];
9-108 1.58e-13

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 67.97  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   9 PYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSALDAANTNPQTAPADADPETLR 88
Cdd:COG0517   11 VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAA 90

                         90       100
                 ....*....|....*....|.
gi 896406034  89 AYFAK-GINHVPLTDERGHLV 108
Cdd:COG0517   91 ELMEEhKIRRLPVVDDDGRLV 111
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 2-119 5.70e-11

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 60.61  E-value: 5.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   2 IIERNiaPYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSALDAANTNPQTAPAD 81
Cdd:COG2905    4 IMSRD--VVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPD 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896406034  82 ADP-ETLRAYFAKGINHVPLTDErGHLVALaMDEQDVLR 119
Cdd:COG2905   82 DSLaEALELMEEHRIRHLPVVDD-GKLVGI-VSITDLLR 118
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 9-119 2.03e-10

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; 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: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 58.41  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   9 PYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTAsLETSALDAANTNPQTAPADADPETLR 88
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLA-LDTPVAEVMTPDVITVSPDTDLEEAL 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896406034  89 AYFAK-GINHVPLTDERGHLVALAmDEQDVLR 119
Cdd:cd02205   83 ELMLEhGIRRLPVVDDDGKLVGIV-TRRDILR 113
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
9-108 9.02e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 54.49  E-value: 9.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   9 PYVVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTASLETSAL-----DAANTNPQTAPADAD 83
Cdd:COG3448   12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLdlpveDVMTRPVVTVTPDTP 91

                         90       100
                 ....*....|....*....|....*.
gi 896406034  84 PETLRAYFA-KGINHVPLTDERGHLV 108
Cdd:COG3448   92 LEEAAELMLeHGIHRLPVVDDDGRLV 117
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
9-119 2.73e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 51.81  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   9 PYVVFAEDPILTALQKISANGQRIiFLVNESGILRGSLSDGDFRRWLiANPTASLETSALDAANTNPQTAPADADPETLR 88
Cdd:COG2524   96 VITVSPDTTLEEALELMLEKGISG-LPVVDDGKLVGIITERDLLKAL-AEGRDLLDAPVSDIMTRDVVTVSEDDSLEEAL 173

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896406034  89 AYFAK-GINHVPLTDERGHLVALaMDEQDVLR 119
Cdd:COG2524  174 RLMLEhGIGRLPVVDDDGKLVGI-ITRTDILR 204
SAF pfam08666
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
 404-460 7.02e-07

SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.


Pssm-ID: 430140 [Multi-domain]  Cd Length: 63  Bit Score: 46.78  E-value: 7.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896406034  404 SLVATRHIAKGEVVTEADVAVKSPGR----GLQPNHLPQLVGRTMQRDVEEGSFFFEGDLK 460
Cdd:pfam08666   3 VVVAARDLPAGEVITADDLTLVRPPLalppGLFPIAYGEVIGKVARRDIAAGEPLTASDLE 63
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 11-108 1.80e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 47.38  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  11 VVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANPTaSLETSALDAANTNPQTAPADAdpetlRAY 90
Cdd:cd04604   17 LVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLD-ILNLPAKDVMTRNPKTISPDA-----LAA 90

                         90       100
                 ....*....|....*....|....
gi 896406034  91 FA------KGINHVPLTDERGHLV 108
Cdd:cd04604   91 EAlelmeeHKITVLPVVDEDGKPV 114
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
 402-460 3.19e-06

This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins;


Pssm-ID: 214862 [Multi-domain]  Cd Length: 63  Bit Score: 44.86  E-value: 3.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896406034   402 AKSLVATRHIAKGEVVTEADVAVKS------PGRGLQPNHlpQLVGRTMQRDVEEGSFFFEGDLK 460
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTPYG--QVIGRVARRDIAAGEPITASNLE 63
SAF_CpaB_FlgA_like cd11614
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus ...
 405-459 5.15e-05

SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB; FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure.


Pssm-ID: 212159 [Multi-domain]  Cd Length: 61  Bit Score: 41.69  E-value: 5.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 896406034 405 LVATRHIAKGEVVTEADVAVKS-PGRGLQPNHLP---QLVGRTMQRDVEEGSFFFEGDL 459
Cdd:cd11614    3 VVAARDLPAGTVITADDLTLVEvPLSLLPPGALTdpdDVVGRVARRPLRAGEPITASML 61
kpsF TIGR00393
KpsF/GutQ family protein; This model describes a number of closely related proteins with the ...
 21-110 2.35e-04

KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars]


Pssm-ID: 129488 [Multi-domain]  Cd Length: 268  Bit Score: 43.64  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034   21 ALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLiaNPTASLETSALDAANTNPQTAPADA-DPETLRAYFAKGINHVP 99
Cdd:TIGR00393 178 ALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRAL--LGGGSLKSEVRDFMTLGPKTFKLDAlLLEALEFLERRKITSLV 255

                          90
                  ....*....|.
gi 896406034  100 LTDERGHLVAL 110
Cdd:TIGR00393 256 VVDDHNKVLGV 266
ChapFlgA pfam13144
Chaperone for flagella basal body P-ring formation; ChapFlgA is a family similar to the SAF ...
 405-468 4.81e-04

Chaperone for flagella basal body P-ring formation; ChapFlgA is a family similar to the SAF family, and includes chaperones for flagellar basal-body proteins and pilus-assembly proteins, FlgA, RcpB and CpaB. ChapFlgA is necessary for the formation of the P-ring of the flagellum, FlgI, which sits in the peptidoglycan layer of the outer membrane of the bacterium. FlgA plays an auxiliary role in P-ring assembly.


Pssm-ID: 432991 [Multi-domain]  Cd Length: 122  Bit Score: 40.60  E-value: 4.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896406034  405 LVATRHIAKGEVVTEADVAVKS-PGRGLQPNHLP-QLVGRTMQRDVEEGSFFFEGDLKD-DLVTRRD 468
Cdd:pfam13144   4 VVAARPLARGEVITASDLALKKrDLARLPGGYLTdQAIGKRVKRSIRAGQPIRQNMLEApPLVKKGQ 70
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
11-121 5.71e-04

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 42.83  E-value: 5.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  11 VVFAEDPILTALQKISANGQRIIFLVNESGILRGSLSDGDFRRWLIANptASLETSALDAANTNPQTAPADADP-ETLRA 89
Cdd:PRK11543 211 QVALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGG--GALTTPVNEAMTRGGTTLQAQSRAiDAKEI 288

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896406034  90 YFAKGINHVPLTDERGHLVAlAMDEQDVLRIG 121
Cdd:PRK11543 289 LMKRKITAAPVVDENGKLTG-AINLQDFYQAG 319
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
 533-746 2.46e-03

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 40.38  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 533 FLVDLASKDPEVWERSIAEVQRTIDITRDLTRYFtvdedpimVVTMGGFTKDKhipvsERAEKYERIGEALKHLDAS--- 609
Cdd:cd00019   68 YLINLASPDKEKREKSIERLKDEIERCEELGIRL--------LVFHPGSYLGQ-----SKEEGLKRVIEALNELIDKaet 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034 610 -GVRLAAQTlppypwlMGGqQYHNLfldPKDTAEFSRAYDTA-------LCLDISHTMLASNFLNIPLS-----EAVEQL 676
Cdd:cd00019  135 kGVVIALET-------MAG-QGNEI---GSSFEELKEIIDLIkekprvgVCIDTCHIFAAGYDISTVEGfekvlEEFDKV 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896406034 677 APLS--IHLHLVDGVGVDGEG----VQVGEGDVDWAALGKQLREL-APKASFIPEIWqGHINNGEGFFTALDRLEKW 746
Cdd:cd00019  204 IGLEylKAIHLNDSKGELGSGkdrhEPIGEGDIDGEELFKELKKDpYQNIPLILETP-SENRDAAKIKKEIKLLRKL 279
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 11-163 2.61e-03

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 41.19  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  11 VVFAEDPILTALQKISANGQRIIFLVNESGILRGSL------SDGDFrrwlIANPTASLE---TSALDAAntnpqTAPAD 81
Cdd:PLN02274 111 VVKSPSSTISSLDELKASRGFSSVCVTETGTMGSKLlgyvtkRDWDF----VNDRETKLSevmTSDDDLV-----TAPAG 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  82 ADPETLRAYFAK-GINHVPLTDERGHLVALaMDEQDVLRI------GKHTISEDSPAFIIAEIGNNhqgsvDFAKELVDL 154
Cdd:PLN02274 182 IDLEEAEAVLKDsKKGKLPLVNEDGELVDL-VTRTDVKRVkgypklGKPSVGKDGKLLVGAAIGTR-----ESDKERLEH 255


                 ....*....
gi 896406034 155 AVESGADAV 163
Cdd:PLN02274 256 LVKAGVDVV 264
FlgA COG1261
Flagellar basal body P-ring formation protein FlgA [Cell motility];
405-468 3.38e-03

Flagellar basal body P-ring formation protein FlgA [Cell motility];


Pssm-ID: 440873 [Multi-domain]  Cd Length: 158  Bit Score: 38.72  E-value: 3.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896406034 405 LVATRHIAKGEVVTEADVAVKS-PGRGLQPNHLP---QLVGRTMQRDVEEGSFFFEGDLKD-DLVTRRD 468
Cdd:COG1261   36 VVAARPLARGEVITADDLRLEEgDLARLPGGALTdpdELVGKVARRSLRAGQPLRASDLRApPLVKRGQ 104
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 21-108 5.60e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 37.31  E-value: 5.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896406034  21 ALQKISANGQRI-----IFLVNESGILRGSLSdgdFRRWLIANPTASLEtsalDAANTNPQTAPADADPETLRAYFAK-G 94
Cdd:cd04606   23 ALEYLRRLAPDPetiyyIYVVDEDRRLLGVVS---LRDLLLADPDTKVS----DIMDTDVISVSADDDQEEVARLFAKyD 95

                         90
                 ....*....|....
gi 896406034  95 INHVPLTDERGHLV 108
Cdd:cd04606   96 LLALPVVDEEGRLV 109
 
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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