|
Name |
Accession |
Description |
Interval |
E-value |
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1-268 |
4.42e-76 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
:
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 238.01 E-value: 4.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 1 MKLTKSLLALAVLPMFASaddLSQTQNHTIQPQIVGGVTADPRDWKFYTQIVSRYGNRS-YCGASYIGNGYVLTAAHCVE 79
Cdd:COG5640 1 MRRRRLLAALAAAALALA---LAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqFCGGTLIAPRWVLTAAHCVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 80 GDSPSQIAVKIGGVVYNGSDGVRANVSEIHMHPAYRRATLSHDLAVLKLDSVPQGVSSVEIANGSLTqyASIGDWLSVAG 159
Cdd:COG5640 78 GDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLATSADA--AAPGTPATVAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 160 LGRTSEG-GSSPSRLQEVDVPLVSDMTCRQAGGNYttvGEVSFCAGIPQGGIDSCQGDSGGPIVINRSGVITQLGVVSWG 238
Cdd:COG5640 156 WGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGFD---GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWG 232
|
250 260 270
....*....|....*....|....*....|
gi 516229815 239 IGCARPGMYGVYSDIAAMRNFVDGVIGTAT 268
Cdd:COG5640 233 GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
392-434 |
1.46e-16 |
|
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: 72.99 E-value: 1.46e-16
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 516229815 392 VWQASLVYLKGDTVTWNGKVWQAQWWTQGDNPADSgpWGVWQK 434
Cdd:cd12215 2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| choice_anch_D |
NF012200 |
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long ... |
263-368 |
3.07e-04 |
|
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM.
:
Pssm-ID: 467954 [Multi-domain] Cd Length: 107 Bit Score: 39.91 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 263 VIGTATPPKENVSVGYTTEQTLASFNVGELQQHSFVIQNSGSTTFTVENVRAFASGVTDAAVIANdqcSQATLAMNASCR 342
Cdd:NF012200 5 LTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTIEGLTISGTNAGDFTVSGN---SPTTLAAGGSCT 81
|
90 100
....*....|....*....|....*.
gi 516229815 343 VDVEFGATQSGEARVALNFNVDKTST 368
Cdd:NF012200 82 LTVTFDPTAAGARSGTLTIASNDAGE 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1-268 |
4.42e-76 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 238.01 E-value: 4.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 1 MKLTKSLLALAVLPMFASaddLSQTQNHTIQPQIVGGVTADPRDWKFYTQIVSRYGNRS-YCGASYIGNGYVLTAAHCVE 79
Cdd:COG5640 1 MRRRRLLAALAAAALALA---LAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqFCGGTLIAPRWVLTAAHCVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 80 GDSPSQIAVKIGGVVYNGSDGVRANVSEIHMHPAYRRATLSHDLAVLKLDSVPQGVSSVEIANGSLTqyASIGDWLSVAG 159
Cdd:COG5640 78 GDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLATSADA--AAPGTPATVAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 160 LGRTSEG-GSSPSRLQEVDVPLVSDMTCRQAGGNYttvGEVSFCAGIPQGGIDSCQGDSGGPIVINRSGVITQLGVVSWG 238
Cdd:COG5640 156 WGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGFD---GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWG 232
|
250 260 270
....*....|....*....|....*....|
gi 516229815 239 IGCARPGMYGVYSDIAAMRNFVDGVIGTAT 268
Cdd:COG5640 233 GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
34-261 |
4.22e-67 |
|
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 214.06 E-value: 4.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 34 IVGGVTADPRDWKFytqIVS--RYGNRSYCGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGVVYNGSD--GVRANVSEIH 109
Cdd:cd00190 1 IVGGSEAKIGSFPW---QVSlqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEggGQVIKVKKVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 110 MHPAYRRATLSHDLAVLKLD-SVPQG--VSSVEIANGSLTQYAsiGDWLSVAGLGRTSEGGSSPSRLQEVDVPLVSDMTC 186
Cdd:cd00190 78 VHPNYNPSTYDNDIALLKLKrPVTLSdnVRPICLPSSGYNLPA--GTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516229815 187 RQAGGNYTTVGEVSFCAGIPQGGIDSCQGDSGGPIVINRSGVITQLGVVSWGIGCARPGMYGVYSDIAAMRNFVD 261
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
34-260 |
1.42e-66 |
|
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 212.54 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 34 IVGGVTADPRDWKFytqIVS--RYGNRSYCGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGV-VYNGSDGVRANVSEIHM 110
Cdd:smart00020 2 IVGGSEANIGSFPW---QVSlqYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHdLSSGEEGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 111 HPAYRRATLSHDLAVLKLD-SVPQG--VSSVEIANGSLTQYAsiGDWLSVAGLGRTSEG-GSSPSRLQEVDVPLVSDMTC 186
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKePVTLSdnVRPICLPSSNYNVPA--GTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516229815 187 RQAGGNYTTVGEVSFCAGIPQGGIDSCQGDSGGPIVINrSGVITQLGVVSWGIGCARPGMYGVYSDIAAMRNFV 260
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
34-260 |
4.10e-43 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 151.06 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 34 IVGGVTADPRDWKFytqIVSRYGNRSY--CGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGVVYNGSDGVRANVSEIHMH 111
Cdd:pfam00089 1 IVGGDEAQPGSFPW---QVSLQLSSGKhfCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 112 PAYRRATLSHDLAVLKLDSVPQGVSSVE-IANGSLTQYASIGDWLSVAGLGRTSEGGsSPSRLQEVDVPLVSDMTCRQAG 190
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRpICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 191 GNYTTvgEVSFCAGIpqGGIDSCQGDSGGPIVINRSGVItqlGVVSWGIGCARPGMYGVYSDIAAMRNFV 260
Cdd:pfam00089 157 GGTVT--DTMICAGA--GGKDACQGDSGGPLVCSDGELI---GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
392-434 |
1.46e-16 |
|
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: 72.99 E-value: 1.46e-16
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 516229815 392 VWQASLVYLKGDTVTWNGKVWQAQWWTQGDNPADSgpWGVWQK 434
Cdd:cd12215 2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
391-432 |
4.26e-10 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 54.57 E-value: 4.26e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 516229815 391 TVWQASLVYLKGDTVTWNGKVWQAQWWTQGDNPADSgpWGVW 432
Cdd:smart00495 2 PAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
407-432 |
6.51e-06 |
|
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding.
Pssm-ID: 427014 Cd Length: 25 Bit Score: 42.59 E-value: 6.51e-06
10 20
....*....|....*....|....*.
gi 516229815 407 WNGKVWQAQWWTQGDNPADSGpWGVW 432
Cdd:pfam02839 1 HNGKAYQAKWWTQGGDPPTSS-GGPW 25
|
|
| choice_anch_D |
NF012200 |
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long ... |
263-368 |
3.07e-04 |
|
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM.
Pssm-ID: 467954 [Multi-domain] Cd Length: 107 Bit Score: 39.91 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 263 VIGTATPPKENVSVGYTTEQTLASFNVGELQQHSFVIQNSGSTTFTVENVRAFASGVTDAAVIANdqcSQATLAMNASCR 342
Cdd:NF012200 5 LTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTIEGLTISGTNAGDFTVSGN---SPTTLAAGGSCT 81
|
90 100
....*....|....*....|....*.
gi 516229815 343 VDVEFGATQSGEARVALNFNVDKTST 368
Cdd:NF012200 82 LTVTFDPTAAGARSGTLTIASNDAGE 107
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5640 |
COG5640 |
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
1-268 |
4.42e-76 |
|
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 238.01 E-value: 4.42e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 1 MKLTKSLLALAVLPMFASaddLSQTQNHTIQPQIVGGVTADPRDWKFYTQIVSRYGNRS-YCGASYIGNGYVLTAAHCVE 79
Cdd:COG5640 1 MRRRRLLAALAAAALALA---LAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqFCGGTLIAPRWVLTAAHCVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 80 GDSPSQIAVKIGGVVYNGSDGVRANVSEIHMHPAYRRATLSHDLAVLKLDSVPQGVSSVEIANGSLTqyASIGDWLSVAG 159
Cdd:COG5640 78 GDGPSDLRVVIGSTDLSTSGGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAPLATSADA--AAPGTPATVAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 160 LGRTSEG-GSSPSRLQEVDVPLVSDMTCRQAGGNYttvGEVSFCAGIPQGGIDSCQGDSGGPIVINRSGVITQLGVVSWG 238
Cdd:COG5640 156 WGRTSEGpGSQSGTLRKADVPVVSDATCAAYGGFD---GGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWG 232
|
250 260 270
....*....|....*....|....*....|
gi 516229815 239 IGCARPGMYGVYSDIAAMRNFVDGVIGTAT 268
Cdd:COG5640 233 GGPCAAGYPGVYTRVSAYRDWIKSTAGGLG 262
|
|
| Tryp_SPc |
cd00190 |
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
34-261 |
4.22e-67 |
|
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 214.06 E-value: 4.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 34 IVGGVTADPRDWKFytqIVS--RYGNRSYCGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGVVYNGSD--GVRANVSEIH 109
Cdd:cd00190 1 IVGGSEAKIGSFPW---QVSlqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEggGQVIKVKKVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 110 MHPAYRRATLSHDLAVLKLD-SVPQG--VSSVEIANGSLTQYAsiGDWLSVAGLGRTSEGGSSPSRLQEVDVPLVSDMTC 186
Cdd:cd00190 78 VHPNYNPSTYDNDIALLKLKrPVTLSdnVRPICLPSSGYNLPA--GTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516229815 187 RQAGGNYTTVGEVSFCAGIPQGGIDSCQGDSGGPIVINRSGVITQLGVVSWGIGCARPGMYGVYSDIAAMRNFVD 261
Cdd:cd00190 156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
|
|
| Tryp_SPc |
smart00020 |
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
34-260 |
1.42e-66 |
|
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 212.54 E-value: 1.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 34 IVGGVTADPRDWKFytqIVS--RYGNRSYCGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGV-VYNGSDGVRANVSEIHM 110
Cdd:smart00020 2 IVGGSEANIGSFPW---QVSlqYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHdLSSGEEGQVIKVSKVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 111 HPAYRRATLSHDLAVLKLD-SVPQG--VSSVEIANGSLTQYAsiGDWLSVAGLGRTSEG-GSSPSRLQEVDVPLVSDMTC 186
Cdd:smart00020 79 HPNYNPSTYDNDIALLKLKePVTLSdnVRPICLPSSNYNVPA--GTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516229815 187 RQAGGNYTTVGEVSFCAGIPQGGIDSCQGDSGGPIVINrSGVITQLGVVSWGIGCARPGMYGVYSDIAAMRNFV 260
Cdd:smart00020 157 RRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
|
|
| Trypsin |
pfam00089 |
Trypsin; |
34-260 |
4.10e-43 |
|
Trypsin;
Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 151.06 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 34 IVGGVTADPRDWKFytqIVSRYGNRSY--CGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGVVYNGSDGVRANVSEIHMH 111
Cdd:pfam00089 1 IVGGDEAQPGSFPW---QVSLQLSSGKhfCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 112 PAYRRATLSHDLAVLKLDSVPQGVSSVE-IANGSLTQYASIGDWLSVAGLGRTSEGGsSPSRLQEVDVPLVSDMTCRQAG 190
Cdd:pfam00089 78 PNYNPDTLDNDIALLKLESPVTLGDTVRpICLPDASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETCRSAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 191 GNYTTvgEVSFCAGIpqGGIDSCQGDSGGPIVINRSGVItqlGVVSWGIGCARPGMYGVYSDIAAMRNFV 260
Cdd:pfam00089 157 GGTVT--DTMICAGA--GGKDACQGDSGGPLVCSDGELI---GIVSWGYGCASGNYPGVYTPVSSYLDWI 219
|
|
| ChiC_BD |
cd12215 |
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ... |
392-434 |
1.46e-16 |
|
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: 72.99 E-value: 1.46e-16
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 516229815 392 VWQASLVYLKGDTVTWNGKVWQAQWWTQGDNPADSgpWGVWQK 434
Cdd:cd12215 2 AWDASTVYTGGDQVTYNGKVYEAKWWTQGEEPGTS--WGVWKL 42
|
|
| eMpr |
COG3591 |
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
52-260 |
1.70e-10 |
|
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 60.08 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 52 VSRYGNRSYCGASYIGNGYVLTAAHCVEGDSPSQIAVKIGGVV-YNGSDGVRANVSEIHMHPAYRRATLS-HDLAVLKLD 129
Cdd:COG3591 5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPgYNGGPYGTATATRFRVPPGWVASGDAgYDYALLRLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 130 -SVPQGVSSVEIANGSLTQYasiGDWLSVAGLGRtseggsspsrlqevDVPLVSDMTCrqaGGNYTTVGEvsfcaGIPQG 208
Cdd:COG3591 85 ePLGDTTGWLGLAFNDAPLA---GEPVTIIGYPG--------------DRPKDLSLDC---SGRVTGVQG-----NRLSY 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 516229815 209 GIDSCQGDSGGPIVINRSGVITQLGVVSWG-IGCARPGMYGVYSDIAAMRNFV 260
Cdd:COG3591 140 DCDTTGGSSGSPVLDDSDGGGRVVGVHSAGgADRANTGVRLTSAIVAALRAWA 192
|
|
| ChtBD3 |
smart00495 |
Chitin-binding domain type 3; |
391-432 |
4.26e-10 |
|
Chitin-binding domain type 3;
Pssm-ID: 197760 [Multi-domain] Cd Length: 41 Bit Score: 54.57 E-value: 4.26e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 516229815 391 TVWQASLVYLKGDTVTWNGKVWQAQWWTQGDNPADSgpWGVW 432
Cdd:smart00495 2 PAWQAGTVYTAGDVVSYNGKVYKAKWWTQGEEPGSS--SGPW 41
|
|
| CBM_5_12 |
pfam02839 |
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase ... |
407-432 |
6.51e-06 |
|
Carbohydrate binding domain; This short domain is found in many different glycosyl hydrolase enzymes and is presumed to have a carbohydrate binding function. The domain has six aromatic groups that may be important for binding.
Pssm-ID: 427014 Cd Length: 25 Bit Score: 42.59 E-value: 6.51e-06
10 20
....*....|....*....|....*.
gi 516229815 407 WNGKVWQAQWWTQGDNPADSGpWGVW 432
Cdd:pfam02839 1 HNGKAYQAKWWTQGGDPPTSS-GGPW 25
|
|
| ChtBD3 |
cd00036 |
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ... |
392-429 |
7.69e-06 |
|
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 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)). Streptomyces griseus 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. ChiC contains the characteristic chitin-binding aromatic residues. 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.
Pssm-ID: 213175 Cd Length: 40 Bit Score: 42.75 E-value: 7.69e-06
10 20 30
....*....|....*....|....*....|....*...
gi 516229815 392 VWQASLVYLKGDTVTWNGKVWQAQWWTQGDNPADSGPW 429
Cdd:cd00036 1 AWPNPTHYTAGQSVVYNGNLYTANWYTAGSVPGSDSSW 38
|
|
| CBD_like |
cd12204 |
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related ... |
399-429 |
4.55e-05 |
|
Cellulose-binding domain, chitinase and related proteins; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18.
Pssm-ID: 213176 Cd Length: 48 Bit Score: 40.77 E-value: 4.55e-05
10 20 30
....*....|....*....|....*....|.
gi 516229815 399 YLKGDTVTWNGKVWQAQWWTQGDnPADSGPW 429
Cdd:cd12204 15 AAGGDLVSYNGAVYQAKWWTQSA-PGSDSSW 44
|
|
| choice_anch_D |
NF012200 |
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long ... |
263-368 |
3.07e-04 |
|
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM.
Pssm-ID: 467954 [Multi-domain] Cd Length: 107 Bit Score: 39.91 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 263 VIGTATPPKENVSVGYTTEQTLASFNVGELQQHSFVIQNSGSTTFTVENVRAFASGVTDAAVIANdqcSQATLAMNASCR 342
Cdd:NF012200 5 LTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTIEGLTISGTNAGDFTVSGN---SPTTLAAGGSCT 81
|
90 100
....*....|....*....|....*.
gi 516229815 343 VDVEFGATQSGEARVALNFNVDKTST 368
Cdd:NF012200 82 LTVTFDPTAAGARSGTLTIASNDAGE 107
|
|
| Trypsin_2 |
pfam13365 |
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains. |
67-168 |
5.96e-04 |
|
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
Pssm-ID: 433149 [Multi-domain] Cd Length: 142 Bit Score: 40.10 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516229815 67 GNGYVLTAAHCVEGDSPSQIAVkiggVVYNGSDGVRANVSEIHMHPAyrratlsHDLAVLKLDSVPQGVSSVEIANGSLt 146
Cdd:pfam13365 8 SDGLVLTNAHVVDDAEEAAVEL----VSVVLADGREYPATVVARDPD-------LDLALLRVSGDGRGLPPLPLGDSEP- 75
|
90 100
....*....|....*....|..
gi 516229815 147 qyASIGDWLSVAGLGRTSEGGS 168
Cdd:pfam13365 76 --LVGGERVYAVGYPLGGEKLS 95
|
|
| |
