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Conserved domains on  [gi|1140110194|gb|APZ94751|]
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Xanthan lyase precursor [Fuerstiella marisgermanici]

Protein Classification

PSCyt2 and PSD1 domain-containing protein( domain architecture ID 10541425)

protein containing domains PSCyt1, PSCyt2, CBM6-CBM35-CBM36_like, and PSD1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PSCyt2 pfam07583
Protein of unknown function (DUF1549); A family of paralogues in the planctomyces.
165-377 1.65e-95

Protein of unknown function (DUF1549); A family of paralogues in the planctomyces.


:

Pssm-ID: 429550  Cd Length: 208  Bit Score: 299.44  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 165 IDRFVVAKHREAGLKPNSDATPYEILRRLHFGLVGLPPSRHDIAAFIDDYETDpdgAIANVVDQLLASRHFGERWGRHWL 244
Cdd:pfam07583   1 IDRFVLAKLEEEGLKPSPEADRRTLLRRVSLDLTGLPPTPEEVEAFLADPSPD---AYEKLVDRLLASPHYGERWARHWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 245 DVTRFAESSGGGRSLMFPEAWRFRDYVIQSFNDDKPFDQLAREHIAGDLLPfetdQQRDDQVTGVGYLTLGPTNYE-QQD 323
Cdd:pfam07583  78 DLARYADTHGYERDNPRPNAWPYRDWVIRAFNENKPYDQFVREQLAGDLLP----NTDAEQLVATGFLRNGPWNEEgGND 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1140110194 324 KELLRMEVVDEQIDTLGRTFLGLTLGCARCHDHKFDPLPTADYYGMAGIFRSTQ 377
Cdd:pfam07583 154 PEEFRQDYVDDRVDTTGQVFLGLTVGCARCHDHKFDPISQKDYYALAAFFNNTR 207
PSD1 pfam07587
Protein of unknown function (DUF1553); A family of proteins found in Rhodopirellula baltica.
671-921 5.82e-88

Protein of unknown function (DUF1553); A family of proteins found in Rhodopirellula baltica.


:

Pssm-ID: 429553  Cd Length: 213  Bit Score: 279.76  E-value: 5.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 671 GRLELADWVVSPENPLTARVFVNRVWLHLFGEGLVRTPDNFGKMGRPPTHPELLDYLAYTFVhEDHWSVKKLIRRIATSR 750
Cdd:pfam07587   1 RRLGLARWLTSPENPLTARVIVNRVWQHLFGRGLVETVDDFGSQGEPPTHPELLDWLAVEFV-ESGWSLKRLHRLIVLSA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 751 VYRLASSPR---QAGDPDNRLLTQGFRRRLDAESLRDFVLQISgqldldttggrtieriaqydnaydhrkfsrtmRSVYV 827
Cdd:pfam07587  80 TYRQSSRASpelLEKDPENRLLARGPRRRLDAEQIRDSALAVS--------------------------------RSLYT 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 828 PFFRNSMLEIFSVFDVANPNLVTGRRASSTLPSQALYLLNSPFVLEQSELAAKHFLATESsdpatidiLIQKAYLATLSR 907
Cdd:pfam07587 128 FWKRTVPPPFLETFDAPSREVCTVRRDRTNTPLQALVLLNDPFVLEAARALAERLLDEGA--------RIRRAFRRVLGR 199
                         250
                  ....*....|....
gi 1140110194 908 PPSDAELRTLTSFV 921
Cdd:pfam07587 200 PPTAEELAILLAFL 213
CBM6-CBM35-CBM36_like super family cl14880
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ...
439-571 3.93e-32

Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.


The actual alignment was detected with superfamily member cd14488:

Pssm-ID: 449372  Cd Length: 132  Bit Score: 121.64  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 439 PGIVVDDVDARL--AGDWTPSASVQAYVGKGYQHDANMKVDRRAAFETMLPQSGRYRVRYAYSSSSNRCDRVPIDVHHAG 516
Cdd:cd14488     1 NGVVVDNSDAGFsaSGNWTTSTSIAGYYGTDYRYAEPVKGSDPATFTFKIPATGSYEVYVWYPANPNRNSAAPYVVETAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1140110194 517 GMSTVTIDQRTrpgVDGLFADLGEFEFTADQPAVVSVNPEEAGNGVLIIDAVQFV 571
Cdd:cd14488    81 GTSTVRVDQTT---GGGTWVSLGTFEFKAGDQNKVTVSNWTTGGGYVIADAVRVV 132
PSCyt1 pfam07635
Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that ...
43-100 4.69e-15

Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that contains the C-{CPWHF}-{CPWR}-C-H-{CFYW} motif typical of cytochromes C, or CxxCH.


:

Pssm-ID: 429568  Cd Length: 59  Bit Score: 70.11  E-value: 4.69e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194  43 CYECHSADAKnvRGGLLLDSKAGTRDGGESGAAVVPGNPADSLLLSALKH--ESFEMPPD 100
Cdd:pfam07635   1 CFDCHGPDDQ--EGGLRLDSRDAALKGGDSGPAIVPGDPENSELWERIRSddPDMEMPPP 58
 
Name Accession Description Interval E-value
PSCyt2 pfam07583
Protein of unknown function (DUF1549); A family of paralogues in the planctomyces.
165-377 1.65e-95

Protein of unknown function (DUF1549); A family of paralogues in the planctomyces.


Pssm-ID: 429550  Cd Length: 208  Bit Score: 299.44  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 165 IDRFVVAKHREAGLKPNSDATPYEILRRLHFGLVGLPPSRHDIAAFIDDYETDpdgAIANVVDQLLASRHFGERWGRHWL 244
Cdd:pfam07583   1 IDRFVLAKLEEEGLKPSPEADRRTLLRRVSLDLTGLPPTPEEVEAFLADPSPD---AYEKLVDRLLASPHYGERWARHWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 245 DVTRFAESSGGGRSLMFPEAWRFRDYVIQSFNDDKPFDQLAREHIAGDLLPfetdQQRDDQVTGVGYLTLGPTNYE-QQD 323
Cdd:pfam07583  78 DLARYADTHGYERDNPRPNAWPYRDWVIRAFNENKPYDQFVREQLAGDLLP----NTDAEQLVATGFLRNGPWNEEgGND 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1140110194 324 KELLRMEVVDEQIDTLGRTFLGLTLGCARCHDHKFDPLPTADYYGMAGIFRSTQ 377
Cdd:pfam07583 154 PEEFRQDYVDDRVDTTGQVFLGLTVGCARCHDHKFDPISQKDYYALAAFFNNTR 207
PSD1 pfam07587
Protein of unknown function (DUF1553); A family of proteins found in Rhodopirellula baltica.
671-921 5.82e-88

Protein of unknown function (DUF1553); A family of proteins found in Rhodopirellula baltica.


Pssm-ID: 429553  Cd Length: 213  Bit Score: 279.76  E-value: 5.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 671 GRLELADWVVSPENPLTARVFVNRVWLHLFGEGLVRTPDNFGKMGRPPTHPELLDYLAYTFVhEDHWSVKKLIRRIATSR 750
Cdd:pfam07587   1 RRLGLARWLTSPENPLTARVIVNRVWQHLFGRGLVETVDDFGSQGEPPTHPELLDWLAVEFV-ESGWSLKRLHRLIVLSA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 751 VYRLASSPR---QAGDPDNRLLTQGFRRRLDAESLRDFVLQISgqldldttggrtieriaqydnaydhrkfsrtmRSVYV 827
Cdd:pfam07587  80 TYRQSSRASpelLEKDPENRLLARGPRRRLDAEQIRDSALAVS--------------------------------RSLYT 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 828 PFFRNSMLEIFSVFDVANPNLVTGRRASSTLPSQALYLLNSPFVLEQSELAAKHFLATESsdpatidiLIQKAYLATLSR 907
Cdd:pfam07587 128 FWKRTVPPPFLETFDAPSREVCTVRRDRTNTPLQALVLLNDPFVLEAARALAERLLDEGA--------RIRRAFRRVLGR 199
                         250
                  ....*....|....
gi 1140110194 908 PPSDAELRTLTSFV 921
Cdd:pfam07587 200 PPTAEELAILLAFL 213
CBM6-CBM35-CBM36_like_2 cd14488
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; ...
439-571 3.93e-32

uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.


Pssm-ID: 271154  Cd Length: 132  Bit Score: 121.64  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 439 PGIVVDDVDARL--AGDWTPSASVQAYVGKGYQHDANMKVDRRAAFETMLPQSGRYRVRYAYSSSSNRCDRVPIDVHHAG 516
Cdd:cd14488     1 NGVVVDNSDAGFsaSGNWTTSTSIAGYYGTDYRYAEPVKGSDPATFTFKIPATGSYEVYVWYPANPNRNSAAPYVVETAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1140110194 517 GMSTVTIDQRTrpgVDGLFADLGEFEFTADQPAVVSVNPEEAGNGVLIIDAVQFV 571
Cdd:cd14488    81 GTSTVRVDQTT---GGGTWVSLGTFEFKAGDQNKVTVSNWTTGGGYVIADAVRVV 132
PSCyt1 pfam07635
Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that ...
43-100 4.69e-15

Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that contains the C-{CPWHF}-{CPWR}-C-H-{CFYW} motif typical of cytochromes C, or CxxCH.


Pssm-ID: 429568  Cd Length: 59  Bit Score: 70.11  E-value: 4.69e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194  43 CYECHSADAKnvRGGLLLDSKAGTRDGGESGAAVVPGNPADSLLLSALKH--ESFEMPPD 100
Cdd:pfam07635   1 CFDCHGPDDQ--EGGLRLDSRDAALKGGDSGPAIVPGDPENSELWERIRSddPDMEMPPP 58
 
Name Accession Description Interval E-value
PSCyt2 pfam07583
Protein of unknown function (DUF1549); A family of paralogues in the planctomyces.
165-377 1.65e-95

Protein of unknown function (DUF1549); A family of paralogues in the planctomyces.


Pssm-ID: 429550  Cd Length: 208  Bit Score: 299.44  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 165 IDRFVVAKHREAGLKPNSDATPYEILRRLHFGLVGLPPSRHDIAAFIDDYETDpdgAIANVVDQLLASRHFGERWGRHWL 244
Cdd:pfam07583   1 IDRFVLAKLEEEGLKPSPEADRRTLLRRVSLDLTGLPPTPEEVEAFLADPSPD---AYEKLVDRLLASPHYGERWARHWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 245 DVTRFAESSGGGRSLMFPEAWRFRDYVIQSFNDDKPFDQLAREHIAGDLLPfetdQQRDDQVTGVGYLTLGPTNYE-QQD 323
Cdd:pfam07583  78 DLARYADTHGYERDNPRPNAWPYRDWVIRAFNENKPYDQFVREQLAGDLLP----NTDAEQLVATGFLRNGPWNEEgGND 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1140110194 324 KELLRMEVVDEQIDTLGRTFLGLTLGCARCHDHKFDPLPTADYYGMAGIFRSTQ 377
Cdd:pfam07583 154 PEEFRQDYVDDRVDTTGQVFLGLTVGCARCHDHKFDPISQKDYYALAAFFNNTR 207
PSD1 pfam07587
Protein of unknown function (DUF1553); A family of proteins found in Rhodopirellula baltica.
671-921 5.82e-88

Protein of unknown function (DUF1553); A family of proteins found in Rhodopirellula baltica.


Pssm-ID: 429553  Cd Length: 213  Bit Score: 279.76  E-value: 5.82e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 671 GRLELADWVVSPENPLTARVFVNRVWLHLFGEGLVRTPDNFGKMGRPPTHPELLDYLAYTFVhEDHWSVKKLIRRIATSR 750
Cdd:pfam07587   1 RRLGLARWLTSPENPLTARVIVNRVWQHLFGRGLVETVDDFGSQGEPPTHPELLDWLAVEFV-ESGWSLKRLHRLIVLSA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 751 VYRLASSPR---QAGDPDNRLLTQGFRRRLDAESLRDFVLQISgqldldttggrtieriaqydnaydhrkfsrtmRSVYV 827
Cdd:pfam07587  80 TYRQSSRASpelLEKDPENRLLARGPRRRLDAEQIRDSALAVS--------------------------------RSLYT 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 828 PFFRNSMLEIFSVFDVANPNLVTGRRASSTLPSQALYLLNSPFVLEQSELAAKHFLATESsdpatidiLIQKAYLATLSR 907
Cdd:pfam07587 128 FWKRTVPPPFLETFDAPSREVCTVRRDRTNTPLQALVLLNDPFVLEAARALAERLLDEGA--------RIRRAFRRVLGR 199
                         250
                  ....*....|....
gi 1140110194 908 PPSDAELRTLTSFV 921
Cdd:pfam07587 200 PPTAEELAILLAFL 213
CBM6-CBM35-CBM36_like_2 cd14488
uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; ...
439-571 3.93e-32

uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.


Pssm-ID: 271154  Cd Length: 132  Bit Score: 121.64  E-value: 3.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194 439 PGIVVDDVDARL--AGDWTPSASVQAYVGKGYQHDANMKVDRRAAFETMLPQSGRYRVRYAYSSSSNRCDRVPIDVHHAG 516
Cdd:cd14488     1 NGVVVDNSDAGFsaSGNWTTSTSIAGYYGTDYRYAEPVKGSDPATFTFKIPATGSYEVYVWYPANPNRNSAAPYVVETAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1140110194 517 GMSTVTIDQRTrpgVDGLFADLGEFEFTADQPAVVSVNPEEAGNGVLIIDAVQFV 571
Cdd:cd14488    81 GTSTVRVDQTT---GGGTWVSLGTFEFKAGDQNKVTVSNWTTGGGYVIADAVRVV 132
PSCyt1 pfam07635
Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that ...
43-100 4.69e-15

Planctomycete cytochrome C; These proteins share a region of homology at their N-terminus that contains the C-{CPWHF}-{CPWR}-C-H-{CFYW} motif typical of cytochromes C, or CxxCH.


Pssm-ID: 429568  Cd Length: 59  Bit Score: 70.11  E-value: 4.69e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140110194  43 CYECHSADAKnvRGGLLLDSKAGTRDGGESGAAVVPGNPADSLLLSALKH--ESFEMPPD 100
Cdd:pfam07635   1 CFDCHGPDDQ--EGGLRLDSRDAALKGGDSGPAIVPGDPENSELWERIRSddPDMEMPPP 58
 
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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