NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|672184200|ref|XP_008812405|]
View 

probable pectate lyase 8 [Phoenix dactylifera]

Protein Classification

polysaccharide lyase family 1 protein( domain architecture ID 10652760)

polysaccharide lyase family 1 protein such as pectate lyase that catalyzes the eliminative cleavage of pectate to yield oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at the non-reducing ends, and pectin lyase that catalyzes the eliminative cleavage of the methyl ester pectin

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
177-371 1.10e-88

Amb_all domain;


:

Pssm-ID: 214765  Cd Length: 190  Bit Score: 267.99  E-value: 1.10e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200   177 DMVITLKQ--ELIMNSFKTIDGRGANVHIANGaCITIQFVTNIIIHGLHIHDCKPtgnamvrsspsHYGWrtmaDGDAVS 254
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPKP-----------VYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200   255 IFGSSHIWVDHCSLSKCA---------DGLVDAVMGSTAITISNNYFTHHNEVMLLGHSDSYERDKAMQVTIAFNHFGeG 325
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 672184200   326 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGNRYLAP 371
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
177-371 1.10e-88

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 267.99  E-value: 1.10e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200   177 DMVITLKQ--ELIMNSFKTIDGRGANVHIANGaCITIQFVTNIIIHGLHIHDCKPtgnamvrsspsHYGWrtmaDGDAVS 254
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPKP-----------VYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200   255 IFGSSHIWVDHCSLSKCA---------DGLVDAVMGSTAITISNNYFTHHNEVMLLGHSDSYERDKAMQVTIAFNHFGeG 325
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 672184200   326 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGNRYLAP 371
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
127-411 6.91e-52

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 177.49  E-value: 6.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200 127 IGFGR---SAIGGRDGRYYAVTDPRDddpvnprpgtLRHAVIQEEPLWIVFkrDMVITL-KQELIMNSFKTIDGRGANVH 202
Cdd:COG3866   36 EGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGAT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200 203 IANGAcITIQFVTNIIIHGLHIHDCKPTGNAmvrsspshygwrtmaDGDAVSIFGSSHIWVDHCSLSKCADGLVDAVMGS 282
Cdd:COG3866  104 ITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200 283 TAITISNNYF----THHNEVMLLGHSDSYERDKAmQVTIAFNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGGSA 357
Cdd:COG3866  168 DNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGKL-RVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672184200 358 GPTINSQGNRYLAPANPFAKEVTKRVETDGSVWKRWNW---RSEGDLLLNGAYFTPS 411
Cdd:COG3866  246 GAQVLVENNYFENVKGPLATSDGSSLLDPGYLYARGNVfdnSTGTAPAGSGTVFTPP 302
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 186-366 5.05e-20

Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.


Pssm-ID: 366158  Cd Length: 211  Bit Score: 88.03  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200  186 LIMNSFKTIDGRGANVHIANGACITI--QFVTNIIIHGLHIHDCKPTGNAMVRSSPSHYGWRTMADGDAVSIFGSSHIWV 263
Cdd:pfam00544  13 SGGAAYANFCDQKARSQIGVPSNTTIigIIGTNGKFTNFGSLIIKGSSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200  264 DHCSLS----KCA---------DGLVDAVMGSTAITISNNYFTHHNEVMLLGHSDSYE-RDKA-MQVTIAFNHFgEGLIQ 328
Cdd:pfam00544  93 DHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNNsQDTGkLRVTYHHNVY-NRVTE 171

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 672184200  329 RMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGN 366
Cdd:pfam00544 172 RAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209
 
Name Accession Description Interval E-value
Amb_all smart00656
Amb_all domain;
177-371 1.10e-88

Amb_all domain;


Pssm-ID: 214765  Cd Length: 190  Bit Score: 267.99  E-value: 1.10e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200   177 DMVITLKQ--ELIMNSFKTIDGRGANVHIANGaCITIQFVTNIIIHGLHIHDCKPtgnamvrsspsHYGWrtmaDGDAVS 254
Cdd:smart00656   1 DVTITLDNagTIIINSNKTIDGRGSKVEIKGG-GLTIKSVSNVIIRNLTIHDPKP-----------VYGS----DGDAIS 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200   255 IFGSSHIWVDHCSLSKCA---------DGLVDAVMGSTAITISNNYFTHHNEVMLLGHSDSYERDKAMQVTIAFNHFGeG 325
Cdd:smart00656  65 IDGSSNVWIDHVSLSGCTvtgfgddtyDGLIDIKNGSTYVTISNNYFHNHWKVMLLGHSDSDTDDGKMRVTIAHNYFG-N 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 672184200   326 LIQRMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGNRYLAP 371
Cdd:smart00656 144 LRQRAPRVRFGYVHVYNNYYTGWTSYAIGGRMGATILSEGNYFEAP 189
PelB COG3866
Pectate lyase [Carbohydrate transport and metabolism];
127-411 6.91e-52

Pectate lyase [Carbohydrate transport and metabolism];


Pssm-ID: 443075 [Multi-domain]  Cd Length: 326  Bit Score: 177.49  E-value: 6.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200 127 IGFGR---SAIGGRDGRYYAVTDPRDddpvnprpgtLRHAVIQEEPLWIVFkrDMVITL-KQELIMNSFKTIDGRGANVH 202
Cdd:COG3866   36 EGFASvngGTTGGAGGTVVTVTTLAD----------LRAALEASGPRIIVV--SGTIDLsKSPLKVNSNKTIAGQGDGAT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200 203 IANGAcITIQFVTNIIIHGLHIHDCKPTGNAmvrsspshygwrtmaDGDAVSIFGSSHIWVDHCSLSKCADGLVDAVMGS 282
Cdd:COG3866  104 ITGGG-LNIKGASNVIIRNLRFRNGDDGGGS---------------GGDAIGIEGAHNVWIDHCTFSWGYDGLLDIKRGS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200 283 TAITISNNYF----THHNEVMLLGHSDSYERDKAmQVTIAFNHFgEGLIQRMPRCRHGYFHVVNNDYTHW-EMYAIGGSA 357
Cdd:COG3866  168 DNVTVSWNIFaegkGDHGKGMLIGSSDSDTTGKL-RVTFHHNLF-ANNDSRNPRVRFGQVHVYNNYFYNWgNNYGIGSGG 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 672184200 358 GPTINSQGNRYLAPANPFAKEVTKRVETDGSVWKRWNW---RSEGDLLLNGAYFTPS 411
Cdd:COG3866  246 GAQVLVENNYFENVKGPLATSDGSSLLDPGYLYARGNVfdnSTGTAPAGSGTVFTPP 302
Pectate_lyase_4 pfam00544
Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an ...
 186-366 5.05e-20

Pectate lyase; This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.


Pssm-ID: 366158  Cd Length: 211  Bit Score: 88.03  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200  186 LIMNSFKTIDGRGANVHIANGACITI--QFVTNIIIHGLHIHDCKPTGNAMVRSSPSHYGWRTMADGDAVSIFGSSHIWV 263
Cdd:pfam00544  13 SGGAAYANFCDQKARSQIGVPSNTTIigIIGTNGKFTNFGSLIIKGSSNVIVRNLYIGTPDGWNKDWDAIRIDNSPNVWV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672184200  264 DHCSLS----KCA---------DGLVDAVMGSTAITISNNYFTHHNEVMLLGHSDSYE-RDKA-MQVTIAFNHFgEGLIQ 328
Cdd:pfam00544  93 DHVTISdgsfTDDgyttkyvqhDGALDIKKGSDYVTISYSLFHGHKKTGLIGHSDDNNsQDTGkLRVTYHHNVY-NRVTE 171

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 672184200  329 RMPRCRHGYFHVVNNDYTHWEMYAIGGSAGPTINSQGN 366
Cdd:pfam00544 172 RAPLVRYGSIHAYNNVYVNIYLYSFGVGQNGSVLSESN 209
 
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