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Conserved domains on  [gi|727169128|ref|WP_033637743|]
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MULTISPECIES: N-acetylneuraminate synthase family protein [Serratia]

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 ...
 128-458 1.51e-162

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


:

Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 472.66  E-value: 1.51e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 128 SPTYIIAEIGNNHNGDIKLAKHLVDLAVDAGADCVKFQMRDLSSLY---KGGNDKDKSADLGAQYTLDLLRKFQLSNEEL 204
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTsdsAPKAFYQSGSLWGGESLYELYKRLELPWEWH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 205 IEVFDYCKEKGLTPLCTPWDLKSLEVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDFLKSK 284
Cdd:COG2089   81 KELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 285 GA-EFVILHCNSTYPTPFKDVNLAYIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGNDHKVSLL 363
Cdd:COG2089  161 GNdQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 364 PPEFKEMVVRIREVEESMGNaGERTITQGEMINRETLAKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQLVGKKA 443
Cdd:COG2089  241 PDELKAMVEAIRNAEKALGS-GIKGPTPSEKKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKA 319

                        330
                 ....*....|....*
gi 727169128 444 NRDHEKGGYFYESDL 458
Cdd:COG2089  320 KRDIKAGTPLTWDDL 334
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 2-118 4.06e-45

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).


The actual alignment was detected with superfamily member cd17773:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 118  Bit Score: 157.03  E-value: 4.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   2 LIQKKISDFLVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWIT-NGDFDLSREMSEVMNQNVRYKKVD 80
Cdd:cd17773    1 IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLeNPNADLSQPVSHVANTNFVSAPEG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727169128  81 APRNEIESLFSNGVDVLPLVDDYRRLVAVALQSEKGLT 118
Cdd:cd17773   81 ESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR 118
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
 515-745 9.35e-21

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: 92.05  E-value: 9.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  515 AENIGFAVHSPELFANdhildLATDDPVYLAHSIKQLQRVCDVTRALKQyfpkterPVIVVNAGgfNTTGFLPKESRQAM 594
Cdd:pfam01261  38 EHGLEIVVHAPYLGDN-----LASPDEEEREKAIDRLKRAIELAAALGA-------KLVVFHPG--SDLGDDPEEALARL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  595 YERIGAALGEINQEGVEIIIQTMPPFPWHFGGqsyhnlfvDPDEIKAFCEKYGY---RICYDTSHSmmacnYYQWDLHEF 671
Cdd:pfam01261 104 AESLRELADLAEREGVRLALEPLAGKGTNVGN--------TFEEALEIIDEVDSpnvGVCLDTGHL-----FAAGDGDLF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  672 TQKVG-PYTAHMHIVDALGVDGEG----VQIGKGDVNFDELADDLRRHA-PGAqFIPEVWqGHKNQGEGFWHALNFLEKY 745
Cdd:pfam01261 171 ELRLGdRYIGHVHLKDSKNPLGSGpdrhVPIGEGVIDFEALFRALKEIGyDGP-LSLETF-NDGPPEEGAREGLEWLREL 248
 
Name Accession Description Interval E-value
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
 128-458 1.51e-162

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


Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 472.66  E-value: 1.51e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 128 SPTYIIAEIGNNHNGDIKLAKHLVDLAVDAGADCVKFQMRDLSSLY---KGGNDKDKSADLGAQYTLDLLRKFQLSNEEL 204
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTsdsAPKAFYQSGSLWGGESLYELYKRLELPWEWH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 205 IEVFDYCKEKGLTPLCTPWDLKSLEVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDFLKSK 284
Cdd:COG2089   81 KELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 285 GA-EFVILHCNSTYPTPFKDVNLAYIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGNDHKVSLL 363
Cdd:COG2089  161 GNdQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 364 PPEFKEMVVRIREVEESMGNaGERTITQGEMINRETLAKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQLVGKKA 443
Cdd:COG2089  241 PDELKAMVEAIRNAEKALGS-GIKGPTPSEKKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKA 319

                        330
                 ....*....|....*
gi 727169128 444 NRDHEKGGYFYESDL 458
Cdd:COG2089  320 KRDIKAGTPLTWDDL 334
NeuB_NnaB TIGR03569
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to ...
 130-450 3.12e-116

N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to include only authentic NeuB N-acetylneuraminate (sialic acid) synthase enzymes. The majority of the genes identified by this model are observed adjacent to both the NeuA and NeuC genes which together effect the biosynthesis of CMP-N-acetylneuraminate from UDP-N-acetylglucosamine.


Pssm-ID: 274655 [Multi-domain]  Cd Length: 329  Bit Score: 353.43  E-value: 3.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  130 TYIIAEIGNNHNGDIKLAKHLVDLAVDAGADCVKFQ---MRDLSSlykggnDKDKSAD-----LGAQYT-LDLLRKFQLS 200
Cdd:TIGR03569   1 TFIIAEAGVNHNGDLELAKKLVDAAAEAGADAVKFQtfkAEDLVS------KNAPKAEyqkinTGAEESqLEMLKKLELS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  201 NEELIEVFDYCKEKGLTPLCTPWDLKSLEVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDF 280
Cdd:TIGR03569  75 EEDHRELKEYCESKGIEFLSTPFDLESADFLEDLGVPRFKIPSGEITNAPLLKKIARFGKPVILSTGMATLEEIEAALGV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  281 LKSKGAE---FVILHCNSTYPTPFKDVNLAYIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGND 357
Cdd:TIGR03569 155 LRDAGTPdsnITLLHCTTEYPAPFEDVNLNAMDTLKEAFDLPVGYSDHTLGIEAPIAAVALGATVIEKHFTLDKNLPGPD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  358 HKVSLLPPEFKEMVVRIREVEESMGNaGERTITQGEMINRETLAKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQ 437
Cdd:TIGR03569 235 HKASLEPDELKEMVQGIRNVEKALGD-GVKRPTPSEQKNRDVARKSLVAAKDIKKGEIFTEDNLTVKRPGNGISPMEYWE 313

                         330
                  ....*....|...
gi 727169128  438 LVGKKANRDHEKG 450
Cdd:TIGR03569 314 VIGKKASRDYEED 326
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
 151-383 8.37e-112

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: 338.33  E-value: 8.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  151 VDLAVDAGADCVKFQMRDLSSLY--KGGNDKDKSADLGAQYTLDLLRKFQLSNEELIEVFDYCKEKGLTPLCTPWDLKSL 228
Cdd:pfam03102   1 IDAAAEAGADAVKFQTFTAETLVskEAPKADYQITTWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFDLESV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  229 EVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDFLKSKGAE-FVILHCNSTYPTPFKDVNLA 307
Cdd:pfam03102  81 DFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEdLTLLHCTSEYPAPFEDVNLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169128  308 YIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGNDHKVSLLPPEFKEMVVRIREVEESMGN 383
Cdd:pfam03102 161 AIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALGD 236
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 2-118 4.06e-45

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: 157.03  E-value: 4.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   2 LIQKKISDFLVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWIT-NGDFDLSREMSEVMNQNVRYKKVD 80
Cdd:cd17773    1 IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLeNPNADLSQPVSHVANTNFVSAPEG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727169128  81 APRNEIESLFSNGVDVLPLVDDYRRLVAVALQSEKGLT 118
Cdd:cd17773   81 ESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR 118
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
 515-745 9.35e-21

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: 92.05  E-value: 9.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  515 AENIGFAVHSPELFANdhildLATDDPVYLAHSIKQLQRVCDVTRALKQyfpkterPVIVVNAGgfNTTGFLPKESRQAM 594
Cdd:pfam01261  38 EHGLEIVVHAPYLGDN-----LASPDEEEREKAIDRLKRAIELAAALGA-------KLVVFHPG--SDLGDDPEEALARL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  595 YERIGAALGEINQEGVEIIIQTMPPFPWHFGGqsyhnlfvDPDEIKAFCEKYGY---RICYDTSHSmmacnYYQWDLHEF 671
Cdd:pfam01261 104 AESLRELADLAEREGVRLALEPLAGKGTNVGN--------TFEEALEIIDEVDSpnvGVCLDTGHL-----FAAGDGDLF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  672 TQKVG-PYTAHMHIVDALGVDGEG----VQIGKGDVNFDELADDLRRHA-PGAqFIPEVWqGHKNQGEGFWHALNFLEKY 745
Cdd:pfam01261 171 ELRLGdRYIGHVHLKDSKNPLGSGpdrhVPIGEGVIDFEALFRALKEIGyDGP-LSLETF-NDGPPEEGAREGLEWLREL 248
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
 401-458 1.82e-19

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: 82.39  E-value: 1.82e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 727169128 401 AKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQLVGKKANRDHEKGGYFYESDL 458
Cdd:cd11615    1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
492-746 2.29e-18

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 85.45  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 492 LDFVEFHLSYQDmELDLTEFFSGAENIGFAVHSPELFANDhildlATDDPVYLAHSIKQLQRVCDVTRALKQyfpkterP 571
Cdd:COG1082   27 YDGVELAGGDLD-EADLAELRAALADHGLEISSLHAPGLN-----LAPDPEVREAALERLKRAIDLAAELGA-------K 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 572 VIVVNAGGFNTTGFLPKESRQAMYERIGAALGEINQEGVEIIIQTmppfpwHFGgqsyhNLFVDPDEIKAFCEKYGY--- 648
Cdd:COG1082   94 VVVVHPGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALEN------HEG-----TFVNTPEEALRLLEAVDSpnv 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 649 RICYDTSHSMMAcnyyQWDLHEFTQKVGPYTAHMHIVDALGvdGEGVQIGKGDVNFDELADDLRRHAPGAQFIPEVWQGH 728
Cdd:COG1082  163 GLLLDTGHALLA----GEDPVELLRKLGDRIKHVHLKDADG--DQHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDP 236

                        250
                 ....*....|....*...
gi 727169128 729 KNQGEGFWHALNFLEKYL 746
Cdd:COG1082  237 DDPEEAARESLEYLRKLL 254
CBS COG0517
CBS domain [Signal transduction mechanisms];
12-107 1.52e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.66  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWI-TNGDFDLSREMSEVMNQNVRYKKVDAPRNEIESLF 90
Cdd:COG0517   14 VSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALaAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELM 93

                         90
                 ....*....|....*...
gi 727169128  91 -SNGVDVLPLVDDYRRLV 107
Cdd:COG0517   94 eEHKIRRLPVVDDDGRLV 111
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
 401-458 2.77e-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: 45.25  E-value: 2.77e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727169128   401 AKSLIINRDLKKGEIITREMVEVKS------PGQGLQPlyLEQLVGKKANRDHEKGGYFYESDL 458
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTP--YGQVIGRVARRDIAAGEPITASNL 62
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 12-55 1.24e-04

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 40.27  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 727169128   12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWI 55
Cdd:pfam00571  12 VSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRAL 55
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
12-112 2.68e-03

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 40.52  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDfDLSREMSEVMNQ-----NVRYKKVDAprneI 86
Cdd:PRK11543 212 VALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGG-ALTTPVNEAMTRggttlQAQSRAIDA----K 286

                         90       100
                 ....*....|....*....|....*..
gi 727169128  87 ESLFSNGVDVLPLVDDYRRLV-AVALQ 112
Cdd:PRK11543 287 EILMKRKITAAPVVDENGKLTgAINLQ 313
AP2Ec smart00518
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
 517-708 4.68e-03

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites


Pssm-ID: 214707  Cd Length: 273  Bit Score: 39.59  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   517 NIGFAVHSPelfandHILDLATDDPVYLAHSIKQLQRVCDVTRALKQYFpkterpvIVVNAGgfnTTGflpKESRQAMYE 596
Cdd:smart00518  58 NIDVSVHAP------YLINLASPDKEKVEKSIERLIDEIKRCEELGIKA-------LVFHPG---SYL---KQSKEEALN 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   597 RIGAALGEI--NQEGVEIIIQTMPPFPWHFGGQsyhnlFVDPDE-IKAFCEKYGYRICYDTSH---SMMACN----YYQW 666
Cdd:smart00518 119 RIIESLNEVidETKGVVILLETTAGKGSQIGST-----FEDLKEiIDLIKELDRIGVCIDTCHifaAGYDINtvegFEKV 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 727169128   667 dLHEFTQKVG-PYTAHMHIVDALGVDGEGVQ----IGKGDVNFDELA 708
Cdd:smart00518 194 -LEEFENVLGlEYLKAIHLNDSKIELGSGKDrhenLGEGYIGFEPFR 239
kpsF TIGR00393
KpsF/GutQ family protein; This model describes a number of closely related proteins with the ...
 11-109 5.51e-03

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: 39.40  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   11 LVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDfDLSREMSEVMNQNVRYKKVDAPRNE-IESL 89
Cdd:TIGR00393 168 LIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGG-SLKSEVRDFMTLGPKTFKLDALLLEaLEFL 246

                          90       100
                  ....*....|....*....|
gi 727169128   90 FSNGVDVLPLVDDYRRLVAV 109
Cdd:TIGR00393 247 ERRKITSLVVVDDHNKVLGV 266
 
Name Accession Description Interval E-value
SpsE COG2089
Sialic acid synthase SpsE, contains C-terminal SAF domain [Cell wall/membrane/envelope ...
 128-458 1.51e-162

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


Pssm-ID: 441692 [Multi-domain]  Cd Length: 335  Bit Score: 472.66  E-value: 1.51e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 128 SPTYIIAEIGNNHNGDIKLAKHLVDLAVDAGADCVKFQMRDLSSLY---KGGNDKDKSADLGAQYTLDLLRKFQLSNEEL 204
Cdd:COG2089    1 HPPFIIAEIGVNHNGDLELAKELIDAAAEAGADAVKFQTYTADTLTsdsAPKAFYQSGSLWGGESLYELYKRLELPWEWH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 205 IEVFDYCKEKGLTPLCTPWDLKSLEVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDFLKSK 284
Cdd:COG2089   81 KELKEYCKELGIIFFSTPFDEESVDFLEELGVPAYKIASGEITNLPLLRYIAKTGKPIILSTGMATLEEIEEAVEALREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 285 GA-EFVILHCNSTYPTPFKDVNLAYIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGNDHKVSLL 363
Cdd:COG2089  161 GNdQIALLHCTSAYPAPPEDVNLRAIPTLKEAFGVPVGLSDHTLGIEVPIAAVALGASVIEKHFTLDRSLPGPDHAFSLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 364 PPEFKEMVVRIREVEESMGNaGERTITQGEMINRETLAKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQLVGKKA 443
Cdd:COG2089  241 PDELKAMVEAIRNAEKALGS-GIKGPTPSEKKNRRVARRSLVAARDIKAGEVITEENLRVKRPGTGLSPKYLDEVLGKKA 319

                        330
                 ....*....|....*
gi 727169128 444 NRDHEKGGYFYESDL 458
Cdd:COG2089  320 KRDIKAGTPLTWDDL 334
NeuB_NnaB TIGR03569
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to ...
 130-450 3.12e-116

N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to include only authentic NeuB N-acetylneuraminate (sialic acid) synthase enzymes. The majority of the genes identified by this model are observed adjacent to both the NeuA and NeuC genes which together effect the biosynthesis of CMP-N-acetylneuraminate from UDP-N-acetylglucosamine.


Pssm-ID: 274655 [Multi-domain]  Cd Length: 329  Bit Score: 353.43  E-value: 3.12e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  130 TYIIAEIGNNHNGDIKLAKHLVDLAVDAGADCVKFQ---MRDLSSlykggnDKDKSAD-----LGAQYT-LDLLRKFQLS 200
Cdd:TIGR03569   1 TFIIAEAGVNHNGDLELAKKLVDAAAEAGADAVKFQtfkAEDLVS------KNAPKAEyqkinTGAEESqLEMLKKLELS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  201 NEELIEVFDYCKEKGLTPLCTPWDLKSLEVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDF 280
Cdd:TIGR03569  75 EEDHRELKEYCESKGIEFLSTPFDLESADFLEDLGVPRFKIPSGEITNAPLLKKIARFGKPVILSTGMATLEEIEAALGV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  281 LKSKGAE---FVILHCNSTYPTPFKDVNLAYIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGND 357
Cdd:TIGR03569 155 LRDAGTPdsnITLLHCTTEYPAPFEDVNLNAMDTLKEAFDLPVGYSDHTLGIEAPIAAVALGATVIEKHFTLDKNLPGPD 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  358 HKVSLLPPEFKEMVVRIREVEESMGNaGERTITQGEMINRETLAKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQ 437
Cdd:TIGR03569 235 HKASLEPDELKEMVQGIRNVEKALGD-GVKRPTPSEQKNRDVARKSLVAAKDIKKGEIFTEDNLTVKRPGNGISPMEYWE 313

                         330
                  ....*....|...
gi 727169128  438 LVGKKANRDHEKG 450
Cdd:TIGR03569 314 VIGKKASRDYEED 326
NeuB pfam03102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
 151-383 8.37e-112

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: 338.33  E-value: 8.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  151 VDLAVDAGADCVKFQMRDLSSLY--KGGNDKDKSADLGAQYTLDLLRKFQLSNEELIEVFDYCKEKGLTPLCTPWDLKSL 228
Cdd:pfam03102   1 IDAAAEAGADAVKFQTFTAETLVskEAPKADYQITTWGGESQYELLKKLELSEEWHKELFEYCREKGIIFLSTPFDLESV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  229 EVLENYGMEGYKVASADFTNHEMLAALAATGKPLICSTGMCSEAEIKSSVDFLKSKGAE-FVILHCNSTYPTPFKDVNLA 307
Cdd:pfam03102  81 DFLESLGVPAYKIASGEITNLPLLRYIAKTGKPVILSTGMATLGEIEEAVEVLRRAGNEdLTLLHCTSEYPAPFEDVNLR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727169128  308 YIKRLQQVTGCLVGYSGHERGISVPIAVTALGARVIEKHFTIDKSMEGNDHKVSLLPPEFKEMVVRIREVEESMGN 383
Cdd:pfam03102 161 AIPTLKEAFGVPVGYSDHTLGIAAPIAAVALGAKVIEKHFTLDRNLPGPDHAASLEPDELKEMVRAIRNVEKALGD 236
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 2-118 4.06e-45

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: 157.03  E-value: 4.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   2 LIQKKISDFLVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWIT-NGDFDLSREMSEVMNQNVRYKKVD 80
Cdd:cd17773    1 IIERNITPYVVFAEDSILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLeNPNADLSQPVSHVANTNFVSAPEG 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 727169128  81 APRNEIESLFSNGVDVLPLVDDYRRLVAVALQSEKGLT 118
Cdd:cd17773   81 ESPEKIEALFSSRISYIPLVDERGRLVAVARKRAAEIR 118
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
 515-745 9.35e-21

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: 92.05  E-value: 9.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  515 AENIGFAVHSPELFANdhildLATDDPVYLAHSIKQLQRVCDVTRALKQyfpkterPVIVVNAGgfNTTGFLPKESRQAM 594
Cdd:pfam01261  38 EHGLEIVVHAPYLGDN-----LASPDEEEREKAIDRLKRAIELAAALGA-------KLVVFHPG--SDLGDDPEEALARL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  595 YERIGAALGEINQEGVEIIIQTMPPFPWHFGGqsyhnlfvDPDEIKAFCEKYGY---RICYDTSHSmmacnYYQWDLHEF 671
Cdd:pfam01261 104 AESLRELADLAEREGVRLALEPLAGKGTNVGN--------TFEEALEIIDEVDSpnvGVCLDTGHL-----FAAGDGDLF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  672 TQKVG-PYTAHMHIVDALGVDGEG----VQIGKGDVNFDELADDLRRHA-PGAqFIPEVWqGHKNQGEGFWHALNFLEKY 745
Cdd:pfam01261 171 ELRLGdRYIGHVHLKDSKNPLGSGpdrhVPIGEGVIDFEALFRALKEIGyDGP-LSLETF-NDGPPEEGAREGLEWLREL 248
SAF_NeuB_like cd11615
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
 401-458 1.82e-19

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: 82.39  E-value: 1.82e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 727169128 401 AKSLIINRDLKKGEIITREMVEVKSPGQGLQPLYLEQLVGKKANRDHEKGGYFYESDL 458
Cdd:cd11615    1 RRSLVAARDIKAGEVLTEENLRVKRPGGGLSPKYLDEVLGKKAKRDIKAGEPLTWDDL 58
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 6-107 1.32e-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: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   6 KISDFLVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGdFDLSREMSEVMNQNVRYKKVDAPRNE 85
Cdd:cd04607    1 NWKKVLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKG-LSLDAPVEEVMNKNPITASPSTSREE 79

                         90       100
                 ....*....|....*....|...
gi 727169128  86 IESLF-SNGVDVLPLVDDYRRLV 107
Cdd:cd04607   80 LLALMrAKKILQLPIVDEQGRVV 102
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
492-746 2.29e-18

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 85.45  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 492 LDFVEFHLSYQDmELDLTEFFSGAENIGFAVHSPELFANDhildlATDDPVYLAHSIKQLQRVCDVTRALKQyfpkterP 571
Cdd:COG1082   27 YDGVELAGGDLD-EADLAELRAALADHGLEISSLHAPGLN-----LAPDPEVREAALERLKRAIDLAAELGA-------K 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 572 VIVVNAGGFNTTGFLPKESRQAMYERIGAALGEINQEGVEIIIQTmppfpwHFGgqsyhNLFVDPDEIKAFCEKYGY--- 648
Cdd:COG1082   94 VVVVHPGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALEN------HEG-----TFVNTPEEALRLLEAVDSpnv 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128 649 RICYDTSHSMMAcnyyQWDLHEFTQKVGPYTAHMHIVDALGvdGEGVQIGKGDVNFDELADDLRRHAPGAQFIPEVWQGH 728
Cdd:COG1082  163 GLLLDTGHALLA----GEDPVELLRKLGDRIKHVHLKDADG--DQHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDP 236

                        250
                 ....*....|....*...
gi 727169128 729 KNQGEGFWHALNFLEKYL 746
Cdd:COG1082  237 DDPEEAARESLEYLRKLL 254
CBS COG0517
CBS domain [Signal transduction mechanisms];
12-107 1.52e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.66  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWI-TNGDFDLSREMSEVMNQNVRYKKVDAPRNEIESLF 90
Cdd:COG0517   14 VSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALaAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELM 93

                         90
                 ....*....|....*...
gi 727169128  91 -SNGVDVLPLVDDYRRLV 107
Cdd:COG0517   94 eEHKIRRLPVVDDDGRLV 111
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 12-109 1.99e-13

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: 67.27  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDFDLSREMSEVMNQNVRYKKVDAPRNEIESLFS 91
Cdd:cd02205    7 VDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEALELML 86

                         90
                 ....*....|....*....
gi 727169128  92 -NGVDVLPLVDDYRRLVAV 109
Cdd:cd02205   87 eHGIRRLPVVDDDGKLVGI 105
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 12-109 4.61e-10

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 57.92  E-value: 4.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFR-RWITNGDFDLSREMSEVMNQNVRYKKVDAPRNEIESLF 90
Cdd:COG2905   12 VSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRrRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEALELM 91

                         90       100
                 ....*....|....*....|
gi 727169128  91 -SNGVDVLPLVDDyRRLVAV 109
Cdd:COG2905   92 eEHRIRHLPVVDD-GKLVGI 110
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
12-107 1.40e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 56.80  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDF-DLSREM-----SEVMNQNVRYKKVDAPRNE 85
Cdd:COG3448   15 VSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLdELEERLldlpvEDVMTRPVVTVTPDTPLEE 94

                         90       100
                 ....*....|....*....|...
gi 727169128  86 IESLFS-NGVDVLPLVDDYRRLV 107
Cdd:COG3448   95 AAELMLeHGIHRLPVVDDDGRLV 117
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 11-109 4.76e-09

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: 55.08  E-value: 4.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  11 LVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDFDLSREMSEVMNQNVRYKKVDAPRNEIESLF 90
Cdd:cd04604   17 LVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELM 96

                         90       100
                 ....*....|....*....|
gi 727169128  91 -SNGVDVLPLVDDYRRLVAV 109
Cdd:cd04604   97 eEHKITVLPVVDEDGKPVGI 116
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-107 8.57e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.43  E-value: 8.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   1 MLIQKKISDFL------VFETESIIKALEKINSNKKRIIFVVtEDGKLCGSFSDGDFRRWITNGDFDLSREMSEVMNQNV 74
Cdd:COG2524   82 LVLKMKVKDIMtkdvitVSPDTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDV 160

                         90       100       110
                 ....*....|....*....|....*....|....
gi 727169128  75 RYKKVDAPRNEIESLF-SNGVDVLPLVDDYRRLV 107
Cdd:COG2524  161 VTVSEDDSLEEALRLMlEHGIGRLPVVDDDGKLV 194
SAF pfam08666
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
 403-458 2.87e-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: 47.94  E-value: 2.87e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  403 SLIINRDLKKGEIITREMVEVKSPGQ----GLQPLYLEQLVGKKANRDHEKGGYFYESDL 458
Cdd:pfam08666   3 VVVAARDLPAGEVITADDLTLVRPPLalppGLFPIAYGEVIGKVARRDIAAGEPLTASDL 62
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
6-107 2.24e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 47.60  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   6 KISDFL-------VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRrwitngDFDLSREMSEVMNQNVRYKK 78
Cdd:COG4109   17 LVEDIMtledvatLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVT 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 727169128  79 VDAPRNEI-ESLFSNGVDVLPLVDDYRRLV 107
Cdd:COG4109   91 PDTSLASAaHKMIWEGIELLPVVDDDGRLL 120
SAF smart00858
This domain family includes a range of different proteins. Such as antifreeze proteins and ...
 401-458 2.77e-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: 45.25  E-value: 2.77e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 727169128   401 AKSLIINRDLKKGEIITREMVEVKS------PGQGLQPlyLEQLVGKKANRDHEKGGYFYESDL 458
Cdd:smart00858   1 DNVVVAARDLPAGEVITAEDLRLGHvalrdlPGGGLTP--YGQVIGRVARRDIAAGEPITASNL 62
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 8-107 6.36e-06

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: 45.79  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   8 SDFL-VFETESIIKALEKINSNKKRI-----IFVVTEDGKLCGSFSdgdFRRWITNgdfDLSREMSEVMNQNVRYKKVDA 81
Cdd:cd04606    9 TEFVaVRPDWTVEEALEYLRRLAPDPetiyyIYVVDEDRRLLGVVS---LRDLLLA---DPDTKVSDIMDTDVISVSADD 82

                         90       100
                 ....*....|....*....|....*..
gi 727169128  82 PRNEIESLFS-NGVDVLPLVDDYRRLV 107
Cdd:cd04606   83 DQEEVARLFAkYDLLALPVVDEEGRLV 109
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 12-55 1.24e-04

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 40.27  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 727169128   12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWI 55
Cdd:pfam00571  12 VSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRAL 55
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
8-107 2.39e-04

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 44.29  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   8 SDFL-VFETESIIKALEKINSNKKRI-----IFVVTEDGKLCGSFSdgdFRRWITNgdfDLSREMSEVMNQNVRYKKVDA 81
Cdd:COG2239  137 TEFVaVREDWTVGEALRYLRRQAEDPetiyyIYVVDDDGRLVGVVS---LRDLLLA---DPDTKVSDIMDTDVISVPADD 210

                         90       100
                 ....*....|....*....|....*..
gi 727169128  82 PRNEIESLFS-NGVDVLPLVDDYRRLV 107
Cdd:COG2239  211 DQEEVARLFErYDLLALPVVDEEGRLV 237
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 17-117 3.34e-04

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 40.77  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  17 SIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDFDLSREMSEVMNQNVRYKKVDAPRNE-IESLFSNGVD 95
Cdd:cd17771   14 PLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLDAPISEVMTPDPVRLPPSASAFEaALLMAEHGFR 93

                         90       100
                 ....*....|....*....|..
gi 727169128  96 VLPLVDDyRRLVAVAlqSEKGL 117
Cdd:cd17771   94 HVCVVDN-GRLVGVV--SERDL 112
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 12-55 1.78e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; 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: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 38.94  E-value: 1.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 727169128  12 VFETESIIKALEKINSN--KKRII--FVVTEDGKLCGSFSDGDFRRWI 55
Cdd:cd17784   72 VHPDETLLEAIKKMDSNapDEEIInqLPVVDDGKLVGIISDGDIIRAI 119
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
12-112 2.68e-03

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 40.52  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  12 VFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDfDLSREMSEVMNQ-----NVRYKKVDAprneI 86
Cdd:PRK11543 212 VALTASVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGG-ALTTPVNEAMTRggttlQAQSRAIDA----K 286

                         90       100
                 ....*....|....*....|....*..
gi 727169128  87 ESLFSNGVDVLPLVDDYRRLV-AVALQ 112
Cdd:PRK11543 287 EILMKRKITAAPVVDENGKLTgAINLQ 313
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 16-107 3.03e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. 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: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 37.88  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  16 ESIIKALEKINSNKKRIIFVVTEDGKLCGsfsdgdfrrWITNGDFDLSRE----MSEVMNQNVRYKKVDAP-RNEIESLF 90
Cdd:cd04583   11 RTLAQAIEIMREKRVDSLLVVDKDNVLLG---------IVDIEDINRNYRkakkVGEIMERDVFTVKEDSLlRDTVDRIL 81

                         90
                 ....*....|....*..
gi 727169128  91 SNGVDVLPLVDDYRRLV 107
Cdd:cd04583   82 KRGLKYVPVVDEQGRLV 98
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 15-109 3.32e-03

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. 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.


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 38.48  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128  15 TESIIKALEKINSNKKRIIFVVTEDgKLCGSFSDGDFRRWITNGDFD--------------LSRE-MSEVMNQNVRYKKV 79
Cdd:cd17777   18 SAPILSAFEKMNRRGIRRLVVVDEN-KLEGILSARDLVSYLGGGCLFkivesrhqgdlysaLNREvVETIMTPNPVYVYE 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 727169128  80 DAP-RNEIESLFSNGVDVLPLVDDYRRLVAV 109
Cdd:cd17777   97 DSDlIEALTIMVTRGIGSLPVVDRDGRPVGI 127
AP2Ec smart00518
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
 517-708 4.68e-03

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites


Pssm-ID: 214707  Cd Length: 273  Bit Score: 39.59  E-value: 4.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   517 NIGFAVHSPelfandHILDLATDDPVYLAHSIKQLQRVCDVTRALKQYFpkterpvIVVNAGgfnTTGflpKESRQAMYE 596
Cdd:smart00518  58 NIDVSVHAP------YLINLASPDKEKVEKSIERLIDEIKRCEELGIKA-------LVFHPG---SYL---KQSKEEALN 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   597 RIGAALGEI--NQEGVEIIIQTMPPFPWHFGGQsyhnlFVDPDE-IKAFCEKYGYRICYDTSH---SMMACN----YYQW 666
Cdd:smart00518 119 RIIESLNEVidETKGVVILLETTAGKGSQIGST-----FEDLKEiIDLIKELDRIGVCIDTCHifaAGYDINtvegFEKV 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 727169128   667 dLHEFTQKVG-PYTAHMHIVDALGVDGEGVQ----IGKGDVNFDELA 708
Cdd:smart00518 194 -LEEFENVLGlEYLKAIHLNDSKIELGSGKDrhenLGEGYIGFEPFR 239
CpaB COG3745
Flp pilus assembly protein CpaB [Intracellular trafficking, secretion, and vesicular transport, ...
 404-458 5.15e-03

Flp pilus assembly protein CpaB [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442959 [Multi-domain]  Cd Length: 259  Bit Score: 39.59  E-value: 5.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727169128 404 LIINRDLKKGEIITREMVEVKS-PGQGLQPLYL---EQLVGKKANRDHEKGGYFYESDL 458
Cdd:COG3745   44 VVAARDIPAGTPLTADDLAVVEwPADAVPEGAFtdpEELVGRVARVPIEAGEPILASKL 102
kpsF TIGR00393
KpsF/GutQ family protein; This model describes a number of closely related proteins with the ...
 11-109 5.51e-03

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: 39.40  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727169128   11 LVFETESIIKALEKINSNKKRIIFVVTEDGKLCGSFSDGDFRRWITNGDfDLSREMSEVMNQNVRYKKVDAPRNE-IESL 89
Cdd:TIGR00393 168 LIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGG-SLKSEVRDFMTLGPKTFKLDALLLEaLEFL 246

                          90       100
                  ....*....|....*....|
gi 727169128   90 FSNGVDVLPLVDDYRRLVAV 109
Cdd:TIGR00393 247 ERRKITSLVVVDDHNKVLGV 266
 
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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