NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|896093477|ref|WP_049128942|]
View 

MULTISPECIES: right-handed parallel beta-helix repeat-containing protein [Klebsiella]

Protein Classification

right-handed parallel beta-helix repeat-containing protein( domain architecture ID 12131601)

right-handed parallel beta-helix repeat-containing protein that may share some similarity with pectate lyases, similar to Bacteroides thetaiotaomicron alpha-1,3-galactosidase B that removes both branched alpha-1,3-linked galactose residues of blood group B antigens and linear alpha-1,3-linked galactose structures

PubMed:  38767844

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
450-611 1.35e-06

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


:

Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 48.56  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  450 HGLLLDASYWH-INGVEITDKS---LRIQGSHN-LIENVTAYRNDDTGIQISSpadvgrplwASYNRVVNSeSFSNEdpg 524
Cdd:pfam13229   1 SGILLNGSSNAtIKNNTISNNGgygIYLRGSSNaTIENNTITNNGGDGIEISG---------SSNNTISNN-TISNN--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  525 kinaDGFAVKMRVGEGNRLEGCYSHDNIDDGFDLFNkiedgaNGVVVIENSIARNNTSNGFKLGGEGQPVahEVRNSIAI 604
Cdd:pfam13229  68 ----GGGGIALRGSSNNLIENNTISNNGGAGIYLSD------SSNNTIENNIIHNNGGSGIVIEDSSNNV--TISNNTVT 135

                  ....*..
gi 896093477  605 GNHLDGF 611
Cdd:pfam13229 136 NNKGAGI 142
 
Name Accession Description Interval E-value
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
450-611 1.35e-06

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 48.56  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  450 HGLLLDASYWH-INGVEITDKS---LRIQGSHN-LIENVTAYRNDDTGIQISSpadvgrplwASYNRVVNSeSFSNEdpg 524
Cdd:pfam13229   1 SGILLNGSSNAtIKNNTISNNGgygIYLRGSSNaTIENNTITNNGGDGIEISG---------SSNNTISNN-TISNN--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  525 kinaDGFAVKMRVGEGNRLEGCYSHDNIDDGFDLFNkiedgaNGVVVIENSIARNNTSNGFKLGGEGQPVahEVRNSIAI 604
Cdd:pfam13229  68 ----GGGGIALRGSSNNLIENNTISNNGGAGIYLSD------SSNNTIENNIIHNNGGSGIVIEDSSNNV--TISNNTVT 135

                  ....*..
gi 896093477  605 GNHLDGF 611
Cdd:pfam13229 136 NNKGAGI 142
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
401-610 8.50e-06

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 48.37  E-value: 8.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 401 DLASAVELVPAGGEIILAAGDYPQTVIplsasglKDKTKTLKATGKAVIHG------LLLDASYWHINGVEIT------- 467
Cdd:COG3420   23 SLQAAIDAAPPGDTIEVPPGTYEGNIV-------IDKPLTLIGEGGAVIDGggkgtvITITADNVTVRGLTITgsgdslt 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 468 --DKSLRIQGSHN-LIENVTaYRNDDTGIQISSPADV--------GRP-----------LWAS-YNRVVNSESFSNEDpg 524
Cdd:COG3420   96 ddDAGIYVRGADNaVIENNR-IENNLFGIYLEGSDNNvirnntisGNRdlradrgngihLWNSpGNVIEGNTISGGRD-- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 525 KINADgFAVKMRVgEGNRLEGC-------YSHDN-IDDgfdlfNKIEDGANGV-------VVIENSIARNNTSNGFKLGg 589
Cdd:COG3420  173 GIYLE-FSDNNVI-RNNTIRNLrygihymYSNDNlVEG-----NTFRDNGAGIalmyskgNTVRGNTILGNSGYGILLK- 244
                        250       260
                 ....*....|....*....|.
gi 896093477 590 egqpvahEVRNSIAIGNHLDG 610
Cdd:COG3420  245 -------ESSDSVIEGNTISG 258
PL-6 cd14251
Polysaccharide Lyase Family 6; Polysaccharide Lyase Family 6 is a family of beta-helical ...
398-525 1.86e-03

Polysaccharide Lyase Family 6; Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate.


Pssm-ID: 271210 [Multi-domain]  Cd Length: 369  Bit Score: 41.06  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 398 SPLDLASAVELVPAGGEIILAAGDYPQTVIPLSASGLKDKTKTLKA--TGKAVIHGllldasywhingveitDKSLRIQG 475
Cdd:cd14251    3 NSEELQAAIANAKPGDTIVLANGTYTDVELIFIGKGTTEAPITLKAetPGKVVITG----------------ASSLRIGG 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896093477 476 SHNLIENVTAYRNDDTGIQISSPADVGRPlwASYNRVVNS--ESFSNEDPGK 525
Cdd:cd14251   67 EYLVVEGLVFKDGYTPKGAISFRANSLEL--ANHCRLTNCviDDFNTPDRGD 116
 
Name Accession Description Interval E-value
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
450-611 1.35e-06

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 48.56  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  450 HGLLLDASYWH-INGVEITDKS---LRIQGSHN-LIENVTAYRNDDTGIQISSpadvgrplwASYNRVVNSeSFSNEdpg 524
Cdd:pfam13229   1 SGILLNGSSNAtIKNNTISNNGgygIYLRGSSNaTIENNTITNNGGDGIEISG---------SSNNTISNN-TISNN--- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  525 kinaDGFAVKMRVGEGNRLEGCYSHDNIDDGFDLFNkiedgaNGVVVIENSIARNNTSNGFKLGGEGQPVahEVRNSIAI 604
Cdd:pfam13229  68 ----GGGGIALRGSSNNLIENNTISNNGGAGIYLSD------SSNNTIENNIIHNNGGSGIVIEDSSNNV--TISNNTVT 135

                  ....*..
gi 896093477  605 GNHLDGF 611
Cdd:pfam13229 136 NNKGAGI 142
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
401-610 8.50e-06

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 48.37  E-value: 8.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 401 DLASAVELVPAGGEIILAAGDYPQTVIplsasglKDKTKTLKATGKAVIHG------LLLDASYWHINGVEIT------- 467
Cdd:COG3420   23 SLQAAIDAAPPGDTIEVPPGTYEGNIV-------IDKPLTLIGEGGAVIDGggkgtvITITADNVTVRGLTITgsgdslt 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 468 --DKSLRIQGSHN-LIENVTaYRNDDTGIQISSPADV--------GRP-----------LWAS-YNRVVNSESFSNEDpg 524
Cdd:COG3420   96 ddDAGIYVRGADNaVIENNR-IENNLFGIYLEGSDNNvirnntisGNRdlradrgngihLWNSpGNVIEGNTISGGRD-- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 525 KINADgFAVKMRVgEGNRLEGC-------YSHDN-IDDgfdlfNKIEDGANGV-------VVIENSIARNNTSNGFKLGg 589
Cdd:COG3420  173 GIYLE-FSDNNVI-RNNTIRNLrygihymYSNDNlVEG-----NTFRDNGAGIalmyskgNTVRGNTILGNSGYGILLK- 244
                        250       260
                 ....*....|....*....|.
gi 896093477 590 egqpvahEVRNSIAIGNHLDG 610
Cdd:COG3420  245 -------ESSDSVIEGNTISG 258
Chondroitinas_B pfam14592
Chondroitinase B; This family includes chondroitinases. These enzymes cleave the ...
398-555 1.50e-04

Chondroitinase B; This family includes chondroitinases. These enzymes cleave the glycosaminoglycan dermatan sulfate.


Pssm-ID: 434056  Cd Length: 426  Bit Score: 44.79  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  398 SPLDLASAVELVPAGGEIILAAGDYPQTVIPLSASGLKDKTKTLKA--TGKAVIHG---LLLDASYWHINGVEITDkslr 472
Cdd:pfam14592   3 SNKELYQAIKQAKPGDEIVLKNGVWKDVQIKFKGEGTEGKPITLKAetPGKVFIEGdskLELGGEYLVVEGLYFKN---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477  473 iqgSHNLIENVTAYRNDDTGIqisspadvgrplwASYNRVVNS--ESFSNEDPGKINAdgfAVKMRvGEGNRLEGCYSHD 550
Cdd:pfam14592  79 ---GHTPNRAVIAFKIHGEGV-------------ANHSRVTNCviLDFTEADRDYIDT---WVTFW-GKHNRLDHCYITG 138

                  ....*
gi 896093477  551 NIDDG 555
Cdd:pfam14592 139 KSNFG 143
PL-6 cd14251
Polysaccharide Lyase Family 6; Polysaccharide Lyase Family 6 is a family of beta-helical ...
398-525 1.86e-03

Polysaccharide Lyase Family 6; Polysaccharide Lyase Family 6 is a family of beta-helical polysaccharide lyases. Members include alginate lyase (EC 4.2.2.3) and chondroitinase B (EC 4.2.2.19). Chondroitinase B is an enzyme that only cleaves the beta-(1,4)-linkage of dermatan sulfate (DS), leading to 4,5-unsaturated dermatan sulfate disaccharides as the product. DS is a highly sulfated, unbranched polysaccharide belonging to a family of glycosaminoglycans (GAGs) composed of alternating hexosamine (gluco- or galactosamine) and uronic acid (D-glucuronic or L-iduronic acid) moieties. DS contains alternating 1,4-beta-D-galactosamine (GalNac) and 1,3-alpha-L-iduronic acid units. The related chondroitin sulfate (CS) contains alternating GalNac and 1,3-beta-D-glucuronic acid units. Alginate lyases (known as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11) catalyze the degradation of alginate, a copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate.


Pssm-ID: 271210 [Multi-domain]  Cd Length: 369  Bit Score: 41.06  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896093477 398 SPLDLASAVELVPAGGEIILAAGDYPQTVIPLSASGLKDKTKTLKA--TGKAVIHGllldasywhingveitDKSLRIQG 475
Cdd:cd14251    3 NSEELQAAIANAKPGDTIVLANGTYTDVELIFIGKGTTEAPITLKAetPGKVVITG----------------ASSLRIGG 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896093477 476 SHNLIENVTAYRNDDTGIQISSPADVGRPlwASYNRVVNS--ESFSNEDPGK 525
Cdd:cd14251   67 EYLVVEGLVFKDGYTPKGAISFRANSLEL--ANHCRLTNCviDDFNTPDRGD 116
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH