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Conserved domains on  [gi|1261331627|ref|WP_097855901.1|]
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lytic polysaccharide monooxygenase

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 13400040)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain; similar to Homo sapiens interleukin-5 receptor subunit alpha and interferon gamma receptor 2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3397 COG3397
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function ...
 14-283 4.87e-87

Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function prediction only];


:

Pssm-ID: 442624 [Multi-domain]  Cd Length: 294  Bit Score: 268.11  E-value: 4.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  14 KSKKGIGACVLAAGVTAITMIPQSAYAHGFVEKPSSRAALCSQNYGA----LNLNCG-------NIMYEPQSL--EAPKG 80
Cdd:COG3397     2 MRRRRLLLAAALAALLALLLAAGPASAHGYVESPASRAYLCYLDGGEdaapQNPACWaavaagpQAQYEWQSVlrEGPKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  81 FPDGGPIDGKIASAGGLFGGILDQQTsNRWFKNTIKGGAN-TFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRAELE--P 157
Cdd:COG3397    82 FPQAGIPDGQLCSAGRARFSGLDLQR-GDWPKTPVTAGANfTFTWTATAPHATTYWRYYITKQGWDPTQPLTWSDLElvP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 158 IGTVKHDGSAASNNLTHTINVPTDRNGYHVILAVWDVADTSNAFYNVIDVNLVNNETP------DTVAPSQPTELNASKV 231
Cdd:COG3397   161 FCTVTDPGARPGGTYTHTVNLPAGRSGRHVIYAVWQRSDTAEAFYNCSDVNFGGGGGTppwtaaGTSVEITTPPTPPPPS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1261331627 232 SANSVEITWKAST-DNIGVKEYQVLRNGEVIDTVPGTTFIDKKLKADTEYTYT 283
Cdd:COG3397   241 TPATTPTPSTTTTgSGGATTVATSTTAGGAVTTTTTVVNTGAGATGGEAATTT 293
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
214-404 1.42e-34

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 136.29  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 214 TPDTVAPSQPTELNASKVSANSVEITWKASTDNiGVKEYQVLRNG------EVIDTVPGTTFIDKKLKADTEYTYTIKAL 287
Cdd:COG3401   227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAV 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 288 DSAGNISKESEKLKVKTthaipDIEAPGQPKGLHSMGTTATTVDLMWSPSEDNvGVDHYIVYR--ESAGVMNKIGTAAN- 364
Cdd:COG3401   306 DAAGNESAPSNVVSVTT-----DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRstSGGGTYTKIAETVTt 379

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1261331627 365 TSFMDKDLKANTSYKYVVTAVDLAGNESSRSDVLTVTTKS 404
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTAS 419
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 412-433 3.98e-05

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


:

Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 40.63  E-value: 3.98e-05
                          10        20
                  ....*....|....*....|..
gi 1261331627 412 WDARKAYTKGDRVVHEGKVYEA 433
Cdd:cd12215     3 WDASTVYTGGDQVTYNGKVYEA 24
 
Name Accession Description Interval E-value
COG3397 COG3397
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function ...
 14-283 4.87e-87

Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function prediction only];


Pssm-ID: 442624 [Multi-domain]  Cd Length: 294  Bit Score: 268.11  E-value: 4.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  14 KSKKGIGACVLAAGVTAITMIPQSAYAHGFVEKPSSRAALCSQNYGA----LNLNCG-------NIMYEPQSL--EAPKG 80
Cdd:COG3397     2 MRRRRLLLAAALAALLALLLAAGPASAHGYVESPASRAYLCYLDGGEdaapQNPACWaavaagpQAQYEWQSVlrEGPKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  81 FPDGGPIDGKIASAGGLFGGILDQQTsNRWFKNTIKGGAN-TFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRAELE--P 157
Cdd:COG3397    82 FPQAGIPDGQLCSAGRARFSGLDLQR-GDWPKTPVTAGANfTFTWTATAPHATTYWRYYITKQGWDPTQPLTWSDLElvP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 158 IGTVKHDGSAASNNLTHTINVPTDRNGYHVILAVWDVADTSNAFYNVIDVNLVNNETP------DTVAPSQPTELNASKV 231
Cdd:COG3397   161 FCTVTDPGARPGGTYTHTVNLPAGRSGRHVIYAVWQRSDTAEAFYNCSDVNFGGGGGTppwtaaGTSVEITTPPTPPPPS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1261331627 232 SANSVEITWKAST-DNIGVKEYQVLRNGEVIDTVPGTTFIDKKLKADTEYTYT 283
Cdd:COG3397   241 TPATTPTPSTTTTgSGGATTVATSTTAGGAVTTTTTVVNTGAGATGGEAATTT 293
PRK13211 PRK13211
N-acetylglucosamine-binding protein GbpA;
15-215 4.60e-82

N-acetylglucosamine-binding protein GbpA;


Pssm-ID: 237309 [Multi-domain]  Cd Length: 478  Bit Score: 261.10  E-value: 4.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  15 SKKGIGACVLAAgvtAITMIPQSAYAHGFVEKPSSRAALCSQNYGALNLNCGNIMYEPQSLEAPKGFPDGGPIDGKIASA 94
Cdd:PRK13211    1 MKMKLNKLALAA---ALLLVSGSALAHGYVSSPESRAYLCKLGAGEKNTNCGAVQYEPQSVEGPSGFPESGPPDGKIASA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  95 GGLFGGILDQQTSNRWFKNTIKGGANTFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRA--ELEPIGTVKHDGSAASNNL 172
Cdd:PRK13211   78 GNAQFSPLDEQTADRWVKRPIKAGPNTFEWTFTANHVTRNWRYYITKQDWNPNQPLTRDsfDLTPFCVVDGGMVQPPKRV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1261331627 173 THTINVPTdRNGYHVILAVWDVADTSNAFYNVIDVNLVNNETP 215
Cdd:PRK13211  158 SHECNVPE-RTGYQVILAVWEVGDTANSFYNVIDVNFDGGGGV 199
LPMO_AA10 cd21177
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins ...
 41-208 1.85e-68

lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs), which may act on chitin or cellulose. The family used to be called CBM33. Activities in this family include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54), lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56), lytic chitin monooxygenase (EC 1.14.99.53), and lytic xylan monooxygenase/xylan oxidase (glycosidic bond-cleaving) (EC 1.14.99.-). Also included are viral chitin-binding glycoproteins such as fusolin and spheroidin-like proteins.


Pssm-ID: 410624 [Multi-domain]  Cd Length: 180  Bit Score: 216.02  E-value: 1.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  41 HGFVEKPSSRAALCSQN--YGALNLNCGNIMYEPQSLEAP---------KGFPDGGPIDGKIASAGGLFGGILDQQtSNR 109
Cdd:cd21177     1 HGYVSSPPSRAYLCALGggEGPPNPACGAAQYEPQSVEGPdwngvdyndDGFPVAGPPDGKLCSAGNGRFAGLDEQ-SGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 110 WFKNTIK-GGANTFTWKYTAAHPTSKWHYYITKKGWDPNK-PLTRAELEPIGTVKHDGSAASNN-LTHTINVPtDRNGYH 186
Cdd:cd21177    80 WPKTPVKpGGTFTFTWTATAPHKTSYWRYYITKPGWDPNQlTLAWFDLEPFCTVDGPGGQLPGGtYTHTVTLP-ARSGYH 158

                         170       180
                  ....*....|....*....|..
gi 1261331627 187 VILAVWDVADTSNAFYNVIDVN 208
Cdd:cd21177   159 VIYAVWQRADTGEAFYNCSDVD 180
LPMO_10 pfam03067
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
 41-207 2.15e-58

Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.


Pssm-ID: 460793 [Multi-domain]  Cd Length: 184  Bit Score: 190.29  E-value: 2.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  41 HGFVEKPSSRAALCSQNYG------------ALNLNCGNIMYEPQSLEAPK-GFPDGGPIDGKIASAG-GLFGGiLDQQT 106
Cdd:pfam03067   1 HGYVTSPPSRQYLCREGPEggeapnnpacraAVAAGGTQAQYEWNSVEGPKgGRHQAGIPDGGLCSAGdPNFSG-LDLPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 107 SNrWFKNTIKGGAN-TFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRAELE--PIGTVKHDGSAASNNLTH--TINVPTD 181
Cdd:pfam03067  80 TD-WPKTTYTAGQTiTFTWTLTAPHKTGYFEFYITKPGWDPTKPLTWSDLElgPFATVTDPGQQPPAGGAYyiTVTLPSG 158

                         170       180
                  ....*....|....*....|....*.
gi 1261331627 182 RNGYHVILAVWDVADTSNAFYNVIDV 207
Cdd:pfam03067 159 RSGRHVILQVWQRSDTGEAFYNCSDV 184
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
214-404 1.42e-34

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 136.29  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 214 TPDTVAPSQPTELNASKVSANSVEITWKASTDNiGVKEYQVLRNG------EVIDTVPGTTFIDKKLKADTEYTYTIKAL 287
Cdd:COG3401   227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAV 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 288 DSAGNISKESEKLKVKTthaipDIEAPGQPKGLHSMGTTATTVDLMWSPSEDNvGVDHYIVYR--ESAGVMNKIGTAAN- 364
Cdd:COG3401   306 DAAGNESAPSNVVSVTT-----DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRstSGGGTYTKIAETVTt 379

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1261331627 365 TSFMDKDLKANTSYKYVVTAVDLAGNESSRSDVLTVTTKS 404
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTAS 419
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 314-402 4.83e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 314 PGQPKGLHSMGTTATTVDLMWSPSEDNVG-VDHYIVYRESAGVMN----KIGTAANTSFMDKDLKANTSYKYVVTAVDLA 388
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1261331627 389 GnESSRSDVLTVTT 402
Cdd:cd00063    81 G-ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 220-291 4.50e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  220 PSQPTELNASKVSANSVEITWKASTDNIGVK---EYQVLRNG------EVIDTVPGTTFIDKKLKADTEYTYTIKALDSA 290
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyivGYRVEYREegsewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1261331627  291 G 291
Cdd:smart00060  81 G 81
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 314-389 3.57e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  314 PGQPKGLHSMGTTATTVDLMWSPSEDNVGVDHYIVYR-----ESAGVMNKIGTAANTSFMDKDLKANTSYKYVVTAVDLA 388
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1261331627  389 G 389
Cdd:smart00060  81 G 81
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 412-433 3.98e-05

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 40.63  E-value: 3.98e-05
                          10        20
                  ....*....|....*....|..
gi 1261331627 412 WDARKAYTKGDRVVHEGKVYEA 433
Cdd:cd12215     3 WDASTVYTGGDQVTYNGKVYEA 24
fn3 pfam00041
Fibronectin type III domain;
315-385 8.50e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 8.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261331627 315 GQPKGLHSMGTTATTVDLMWSPSEDNVG-VDHYIVYRESAG---VMNKIGTAANTSFMD-KDLKANTSYKYVVTAV 385
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYRPKNsgePWNEITVPGTTTSVTlTGLKPGTEYEVRVQAV 76
Ig_like_BLP2 NF040520
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ...
 211-397 3.48e-04

Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.


Pssm-ID: 468522 [Multi-domain]  Cd Length: 729  Bit Score: 43.10  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 211 NNETPDTVAPSQPTelnaSKVSANSVEITWKASTdniGVKEYQVLRNGEVIDTVpgttfidkklKADTEYTYTIK----- 285
Cdd:NF040520  160 SNGPVDITPPATPT----ATLADDTQTITGKAEA---NAKIYIKDATGKVIATG----------QADASGNYTIKldqpl 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 286 ---------ALDSAGNISKESEKLKVKtthaipDIEAPGQPKG-LHSMGTTATtvdlmwSPSEDNVGVDHYivyrESAGv 355
Cdd:NF040520  223 vngnkvnvtAIDAAGNASKATVVTGTK------DTIAPDAPQAqLNADGTIVT------GKTEANAKVSVY----DADG- 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1261331627 356 mNKIGTA-ANTS--FMDKDLKANTSYKY-VVTAVDLAGNESSRSDV 397
Cdd:NF040520  286 -KLLGTVtANKEglYSIKVSPPLTSDKGgTVIAEDAAGNKSEPSKI 330
ChtBD3 smart00495
Chitin-binding domain type 3;
409-433 7.74e-03

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 34.16  E-value: 7.74e-03
                           10        20
                   ....*....|....*....|....*
gi 1261331627  409 YEKWDARKAYTKGDRVVHEGKVYEA 433
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKA 25
 
Name Accession Description Interval E-value
COG3397 COG3397
Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function ...
 14-283 4.87e-87

Predicted carbohydrate-binding protein, contains CBM5 and CBM33 domains [General function prediction only];


Pssm-ID: 442624 [Multi-domain]  Cd Length: 294  Bit Score: 268.11  E-value: 4.87e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  14 KSKKGIGACVLAAGVTAITMIPQSAYAHGFVEKPSSRAALCSQNYGA----LNLNCG-------NIMYEPQSL--EAPKG 80
Cdd:COG3397     2 MRRRRLLLAAALAALLALLLAAGPASAHGYVESPASRAYLCYLDGGEdaapQNPACWaavaagpQAQYEWQSVlrEGPKG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  81 FPDGGPIDGKIASAGGLFGGILDQQTsNRWFKNTIKGGAN-TFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRAELE--P 157
Cdd:COG3397    82 FPQAGIPDGQLCSAGRARFSGLDLQR-GDWPKTPVTAGANfTFTWTATAPHATTYWRYYITKQGWDPTQPLTWSDLElvP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 158 IGTVKHDGSAASNNLTHTINVPTDRNGYHVILAVWDVADTSNAFYNVIDVNLVNNETP------DTVAPSQPTELNASKV 231
Cdd:COG3397   161 FCTVTDPGARPGGTYTHTVNLPAGRSGRHVIYAVWQRSDTAEAFYNCSDVNFGGGGGTppwtaaGTSVEITTPPTPPPPS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1261331627 232 SANSVEITWKAST-DNIGVKEYQVLRNGEVIDTVPGTTFIDKKLKADTEYTYT 283
Cdd:COG3397   241 TPATTPTPSTTTTgSGGATTVATSTTAGGAVTTTTTVVNTGAGATGGEAATTT 293
PRK13211 PRK13211
N-acetylglucosamine-binding protein GbpA;
15-215 4.60e-82

N-acetylglucosamine-binding protein GbpA;


Pssm-ID: 237309 [Multi-domain]  Cd Length: 478  Bit Score: 261.10  E-value: 4.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  15 SKKGIGACVLAAgvtAITMIPQSAYAHGFVEKPSSRAALCSQNYGALNLNCGNIMYEPQSLEAPKGFPDGGPIDGKIASA 94
Cdd:PRK13211    1 MKMKLNKLALAA---ALLLVSGSALAHGYVSSPESRAYLCKLGAGEKNTNCGAVQYEPQSVEGPSGFPESGPPDGKIASA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  95 GGLFGGILDQQTSNRWFKNTIKGGANTFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRA--ELEPIGTVKHDGSAASNNL 172
Cdd:PRK13211   78 GNAQFSPLDEQTADRWVKRPIKAGPNTFEWTFTANHVTRNWRYYITKQDWNPNQPLTRDsfDLTPFCVVDGGMVQPPKRV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1261331627 173 THTINVPTdRNGYHVILAVWDVADTSNAFYNVIDVNLVNNETP 215
Cdd:PRK13211  158 SHECNVPE-RTGYQVILAVWEVGDTANSFYNVIDVNFDGGGGV 199
LPMO_AA10 cd21177
lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins ...
 41-208 1.85e-68

lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 10 (AA10); AA10 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs), which may act on chitin or cellulose. The family used to be called CBM33. Activities in this family include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54), lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56), lytic chitin monooxygenase (EC 1.14.99.53), and lytic xylan monooxygenase/xylan oxidase (glycosidic bond-cleaving) (EC 1.14.99.-). Also included are viral chitin-binding glycoproteins such as fusolin and spheroidin-like proteins.


Pssm-ID: 410624 [Multi-domain]  Cd Length: 180  Bit Score: 216.02  E-value: 1.85e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  41 HGFVEKPSSRAALCSQN--YGALNLNCGNIMYEPQSLEAP---------KGFPDGGPIDGKIASAGGLFGGILDQQtSNR 109
Cdd:cd21177     1 HGYVSSPPSRAYLCALGggEGPPNPACGAAQYEPQSVEGPdwngvdyndDGFPVAGPPDGKLCSAGNGRFAGLDEQ-SGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 110 WFKNTIK-GGANTFTWKYTAAHPTSKWHYYITKKGWDPNK-PLTRAELEPIGTVKHDGSAASNN-LTHTINVPtDRNGYH 186
Cdd:cd21177    80 WPKTPVKpGGTFTFTWTATAPHKTSYWRYYITKPGWDPNQlTLAWFDLEPFCTVDGPGGQLPGGtYTHTVTLP-ARSGYH 158

                         170       180
                  ....*....|....*....|..
gi 1261331627 187 VILAVWDVADTSNAFYNVIDVN 208
Cdd:cd21177   159 VIYAVWQRADTGEAFYNCSDVD 180
LPMO_10 pfam03067
Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with ...
 41-207 2.15e-58

Lytic polysaccharide mono-oxygenase, cellulose-degrading; This domain is found associated with a wide variety of cellulose binding domains. This is a family of two very closely related proteins that together act as both a C1- and a C4-oxidising lytic polysaccharide mono-oxygenase, degrading cellulose. This domain is also found in baculoviral spheroidins and spindolins, protein of unknown function.


Pssm-ID: 460793 [Multi-domain]  Cd Length: 184  Bit Score: 190.29  E-value: 2.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  41 HGFVEKPSSRAALCSQNYG------------ALNLNCGNIMYEPQSLEAPK-GFPDGGPIDGKIASAG-GLFGGiLDQQT 106
Cdd:pfam03067   1 HGYVTSPPSRQYLCREGPEggeapnnpacraAVAAGGTQAQYEWNSVEGPKgGRHQAGIPDGGLCSAGdPNFSG-LDLPR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 107 SNrWFKNTIKGGAN-TFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRAELE--PIGTVKHDGSAASNNLTH--TINVPTD 181
Cdd:pfam03067  80 TD-WPKTTYTAGQTiTFTWTLTAPHKTGYFEFYITKPGWDPTKPLTWSDLElgPFATVTDPGQQPPAGGAYyiTVTLPSG 158

                         170       180
                  ....*....|....*....|....*.
gi 1261331627 182 RNGYHVILAVWDVADTSNAFYNVIDV 207
Cdd:pfam03067 159 RSGRHVILQVWQRSDTGEAFYNCSDV 184
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
214-404 1.42e-34

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 136.29  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 214 TPDTVAPSQPTELNASKVSANSVEITWKASTDNiGVKEYQVLRNG------EVIDTVPGTTFIDKKLKADTEYTYTIKAL 287
Cdd:COG3401   227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTES-DATGYRVYRSNsgdgpfTKVATVTTTSYTDTGLTNGTTYYYRVTAV 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 288 DSAGNISKESEKLKVKTthaipDIEAPGQPKGLHSMGTTATTVDLMWSPSEDNvGVDHYIVYR--ESAGVMNKIGTAAN- 364
Cdd:COG3401   306 DAAGNESAPSNVVSVTT-----DLTPPAAPSGLTATAVGSSSITLSWTASSDA-DVTGYNVYRstSGGGTYTKIAETVTt 379

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1261331627 365 TSFMDKDLKANTSYKYVVTAVDLAGNESSRSDVLTVTTKS 404
Cdd:COG3401   380 TSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTAS 419
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
177-402 4.13e-21

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 96.22  E-value: 4.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 177 NVPTDRNGYHVILAVWDVADTSNAFYNVIDVNLVNNETPDTVAPSQPTELNASKVSANSVEITWKASTDNIGVKEYQVLR 256
Cdd:COG3401   104 GGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATT 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 257 NGEVIDTVPGTTFIDkkLKADTEYTYTIKALDSAGNiSKESEKLKVKTthaipDIEAPGQPKGLHSMGTTATTVDLMWSP 336
Cdd:COG3401   184 SLTVTSTTLVDGGGD--IEPGTTYYYRVAATDTGGE-SAPSNEVSVTT-----PTTPPSAPTGLTATADTPGSVTLSWDP 255

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261331627 337 SEDNvGVDHYIVYR--ESAGVMNKIGTAANTSFMDKDLKANTSYKYVVTAVDLAGNESSRSDVLTVTT 402
Cdd:COG3401   256 VTES-DATGYRVYRsnSGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTT 322
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
219-297 1.00e-12

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 69.42  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 219 APSQPTELNASKVSANSVEITWKASTDNIGVKEYQVLRNGEVIDTVPG-TTFIDKKLKADTEYTYTIKALDSAGNISKES 297
Cdd:COG3979     2 APTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVATVTGlTAWTVTGLTPGTEYTFTVGACDAAGNVSAAS 81
COG3979 COG3979
Chitodextrinase [Carbohydrate transport and metabolism];
312-402 1.19e-12

Chitodextrinase [Carbohydrate transport and metabolism];


Pssm-ID: 443178 [Multi-domain]  Cd Length: 369  Bit Score: 69.03  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 312 EAPGQPKGLHSMGTTATTVDLMWSPSEDNVGVDHYIVYRESAGVMNkigTAANTSFMDKDLKANTSYKYVVTAVDLAGNE 391
Cdd:COG3979     1 QAPTAPTGLTASNVTSSSVSLSWDASTDNVGVTGYDVYRGGDQVAT---VTGLTAWTVTGLTPGTEYTFTVGACDAAGNV 77

                          90
                  ....*....|.
gi 1261331627 392 SSRSDVLTVTT 402
Cdd:COG3979    78 SAASGTSTAMF 88
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 314-402 4.83e-10

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 314 PGQPKGLHSMGTTATTVDLMWSPSEDNVG-VDHYIVYRESAGVMN----KIGTAANTSFMDKDLKANTSYKYVVTAVDLA 388
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYREKGSGDwkevEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1261331627 389 GnESSRSDVLTVTT 402
Cdd:cd00063    81 G-ESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 220-304 2.99e-09

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 54.04  E-value: 2.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 220 PSQPTELNASKVSANSVEITWKASTDNIG-VKEYQVLR------NGEVIDTVPG--TTFIDKKLKADTEYTYTIKALDSA 290
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGpITGYVVEYrekgsgDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....
gi 1261331627 291 GnISKESEKLKVKT 304
Cdd:cd00063    81 G-ESPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 220-291 4.50e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  220 PSQPTELNASKVSANSVEITWKASTDNIGVK---EYQVLRNG------EVIDTVPGTTFIDKKLKADTEYTYTIKALDSA 290
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGyivGYRVEYREegsewkEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1261331627  291 G 291
Cdd:smart00060  81 G 81
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
214-406 3.38e-08

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 56.11  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 214 TPDTVAPSQPTELNASKVSANSVEITWKASTDNIGVkEYQVLRNGEVIDTVPGT--TFIDKKLKADTEYTYTIKALDSAG 291
Cdd:COG4733   532 PPVNVTTSESLSVVAQGTAVTTLTVSWDAPAGAVAY-EVEWRRDDGNWVSVPRTsgTSFEVPGIYAGDYEVRVRAINALG 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 292 NISKESEKLKVKTTHaipDIEAPGQPKGLHSMGTTaTTVDLMWSPSEDnVGVDHYIVYR------ESAGVMNKIGTAanT 365
Cdd:COG4733   611 VSSAWAASSETTVTG---KTAPPPAPTGLTATGGL-GGITLSWSFPVD-ADTLRTEIRYsttgdwASATVAQALYPG--N 683

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1261331627 366 SFMDKDLKANTSYKYVVTAVDLAGNESSRSDVLTVTTKSED 406
Cdd:COG4733   684 TYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAG 724
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 314-389 3.57e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 50.69  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  314 PGQPKGLHSMGTTATTVDLMWSPSEDNVGVDHYIVYR-----ESAGVMNKIGTAANTSFMDKDLKANTSYKYVVTAVDLA 388
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRveyreEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                   .
gi 1261331627  389 G 389
Cdd:smart00060  81 G 81
LPMO_auxiliary cd21174
lytic polysaccharide monooxygenase auxiliary activity protein; Many proteins in this ...
 78-206 8.15e-08

lytic polysaccharide monooxygenase auxiliary activity protein; Many proteins in this superfamily are copper-dependent lytic polysaccharide monooxygenases (LPMOs) and include lytic polysaccharide monooxygenase auxiliary activity families 9 (AA9) and 10 (AA10). The substrate-binding surface of this family is a flat beta-sandwich fold.


Pssm-ID: 410621  Cd Length: 136  Bit Score: 51.09  E-value: 8.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627  78 PKGFPDGGPIDGKIASAgglfggildqQTSNRWFKNTIK-GGANTFTWKYTAAH-PTSKWHYYITKKGWDPNKPLTRAEL 155
Cdd:cd21174    18 SDGFVLNASLPILICSG----------QSAGAWRKNDIPlGGTATVSTKQAAGHdLGGRVGVYISICSGDFSSGNSSADL 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1261331627 156 EPIGTVKHDGSAASNNLTHTINVPtDRNGYHVILAVWDvADTSNAFYNVID 206
Cdd:cd21174    88 PFFDVTEFPSVGVTGRVSASSGLP-LDGGNATIQVVKN-GGNDQFLYNCAD 136
gp37 PHA03387
spherodin-like protein; Provisional
 107-207 3.12e-06

spherodin-like protein; Provisional


Pssm-ID: 177623  Cd Length: 267  Bit Score: 48.47  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 107 SNRWFKNTI------KGGANTFTWKYTAAHPTSKWHYYITKKGWDPNKPLTRAELEPIGT-----VKHDGS--AASNNLT 173
Cdd:PHA03387  133 FPNWRPDTLyknkyqSGHQTNLHFCPTAVHEPSYFEVFVTKPEYDYRNELTWNDLELIGGngsqlVPNDGSdeLCASSQV 212

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1261331627 174 HTINV--PTdRNGYHVILAVW---DVAdtSNAFYNVIDV 207
Cdd:PHA03387  213 YSIPVrvPF-RSGKFVLYVRWqriDVV--GEGFYNCADV 248
Fusolin-like cd21178
fusolin and similar proteins; Fusolin is a protein found in spindles of insect poxviruses that ...
 107-208 4.57e-06

fusolin and similar proteins; Fusolin is a protein found in spindles of insect poxviruses that resembles the lytic polysaccharide monooxygenases of chitinovorous bacteria and may function to disrupt the chitin-rich peritrophic matrix that protects insects against oral infections. Thus, it is a component of the virus occlusion bodies (which are large proteinaceous polyhedra) that protect the virus from the outside environment for extended periods until they are ingested by insect larvae.


Pssm-ID: 410625  Cd Length: 227  Bit Score: 47.71  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 107 SNRWFKNTI-KGGANTFTWKYTAAHPTSKWHYYITKKGWDPNK-PLTRAELEPIGTV-------KHDGSAASNNLTHTIN 177
Cdd:cd21178   114 SGSWRPTTIpLRVPIELYFCPTAIHEPSYFEVYITKPEFDVGKdKVTWSDLELIYSNtsnlvpnNPDDECCDNSLVYRIP 193

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1261331627 178 VPTD-RNGYHVILAVW---DVAdtSNAFYNVIDVN 208
Cdd:cd21178   194 VPIPyRSNQFVLYVRWqreDPV--GEGFYNCADVV 226
fn3 pfam00041
Fibronectin type III domain;
221-292 8.29e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 43.94  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 221 SQPTELNASKVSANSVEITWKASTDNIGVK-----EYQVLRNGEVI--DTVPGTT--FIDKKLKADTEYTYTIKALDSAG 291
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPItgyevEYRPKNSGEPWneITVPGTTtsVTLTGLKPGTEYEVRVQAVNGGG 80


                  .
gi 1261331627 292 N 292
Cdd:pfam00041  81 E 81
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 412-433 3.98e-05

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 40.63  E-value: 3.98e-05
                          10        20
                  ....*....|....*....|..
gi 1261331627 412 WDARKAYTKGDRVVHEGKVYEA 433
Cdd:cd12215     3 WDASTVYTGGDQVTYNGKVYEA 24
fn3 pfam00041
Fibronectin type III domain;
315-385 8.50e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 8.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261331627 315 GQPKGLHSMGTTATTVDLMWSPSEDNVG-VDHYIVYRESAG---VMNKIGTAANTSFMD-KDLKANTSYKYVVTAV 385
Cdd:pfam00041   1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGpITGYEVEYRPKNsgePWNEITVPGTTTSVTlTGLKPGTEYEVRVQAV 76
ChiA1_BD cd12214
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ...
 412-455 2.02e-04

chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).


Pssm-ID: 213177 [Multi-domain]  Cd Length: 45  Bit Score: 38.86  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1261331627 412 WDARKAYTKGDRVVHEGKVYEAVQDHQGNGDSNWIFALSLWKPV 455
Cdd:cd12214     2 WAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALWQPA 45
Ig_like_BLP2 NF040520
Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus ...
 211-397 3.48e-04

Ig-like repeat protein Blp2; Blp2 (BAP-like protein 2), found broadly in the genus Acinetobacter, resembles the much larger biofilm-associated proteins Bap and Blp1 in N-terminal sequence and the presence of tandem Ig-like repeats.


Pssm-ID: 468522 [Multi-domain]  Cd Length: 729  Bit Score: 43.10  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 211 NNETPDTVAPSQPTelnaSKVSANSVEITWKASTdniGVKEYQVLRNGEVIDTVpgttfidkklKADTEYTYTIK----- 285
Cdd:NF040520  160 SNGPVDITPPATPT----ATLADDTQTITGKAEA---NAKIYIKDATGKVIATG----------QADASGNYTIKldqpl 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261331627 286 ---------ALDSAGNISKESEKLKVKtthaipDIEAPGQPKG-LHSMGTTATtvdlmwSPSEDNVGVDHYivyrESAGv 355
Cdd:NF040520  223 vngnkvnvtAIDAAGNASKATVVTGTK------DTIAPDAPQAqLNADGTIVT------GKTEANAKVSVY----DADG- 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1261331627 356 mNKIGTA-ANTS--FMDKDLKANTSYKY-VVTAVDLAGNESSRSDV 397
Cdd:NF040520  286 -KLLGTVtANKEglYSIKVSPPLTSDKGgTVIAEDAAGNKSEPSKI 330
ChtBD3 smart00495
Chitin-binding domain type 3;
409-433 7.74e-03

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 34.16  E-value: 7.74e-03
                           10        20
                   ....*....|....*....|....*
gi 1261331627  409 YEKWDARKAYTKGDRVVHEGKVYEA 433
Cdd:smart00495   1 APAWQAGTVYTAGDVVSYNGKVYKA 25
 
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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