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Conserved domains on  [gi|1201891973|ref|XP_021255924|]
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hyaluronan-binding protein 2 [Numida meleagris]

Protein Classification

calcium-binding EGF-like domain-containing protein; serine protease( domain architecture ID 11076412)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions; trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile; contains C-terminal DNA polymerase III subunits gamma and tau

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 303-538 9.85e-92

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: 280.70  E-value: 9.85e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 303 IYGGTKSTAGKHPWMVSLQRKFSRrekHFCGGVLIQSCWVLTAAHCVEH-EAENLQVALGKQNLKRREHQEQIFDVEKVI 381
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSsAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 382 MHHRYRTKDNvpYNDIALLKLKpidgQCATETKYVKTACLPDF--EFPVGTNCFISGWGATETDD-LSHQLLDARVRLIS 458
Cdd:cd00190    78 VHPNYNPSTY--DNDIALLKLK----RPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 459 HKQCNAPRAYDQRLDESMFCAGNLRRpGTDSCQGDSGGPLICVESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRWIK 538
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 191-274 4.22e-22

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


:

Pssm-ID: 238056  Cd Length: 83  Bit Score: 90.52  E-value: 4.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 191 DCYEEDSFYYRGRVNQAENGRTCLHWNSHMLLDFSINAFMEDAesyGIGEHNFCRNPDEDQK-PWCFIrKNGKVEWDFCD 269
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPE---GLLEENYCRNPDGDPEgPWCYT-TDPNVRWEYCD 78


                  ....*
gi 1201891973 270 VSLCS 274
Cdd:cd00108    79 IPRCE 83
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 75-105 3.68e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.53  E-value: 3.68e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1201891973  75 CSSNPCKNNGQCEMRGNNFTCHCPMPYTGDT 105
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 152-184 7.77e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.67  E-value: 7.77e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1201891973 152 CRPNPCKNGGTCIrhRIRSKFTCKCPEPYKGRF 184
Cdd:pfam00008   1 CAPNPCSNGGTCV--DTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 303-538 9.85e-92

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: 280.70  E-value: 9.85e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 303 IYGGTKSTAGKHPWMVSLQRKFSRrekHFCGGVLIQSCWVLTAAHCVEH-EAENLQVALGKQNLKRREHQEQIFDVEKVI 381
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSsAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 382 MHHRYRTKDNvpYNDIALLKLKpidgQCATETKYVKTACLPDF--EFPVGTNCFISGWGATETDD-LSHQLLDARVRLIS 458
Cdd:cd00190    78 VHPNYNPSTY--DNDIALLKLK----RPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 459 HKQCNAPRAYDQRLDESMFCAGNLRRpGTDSCQGDSGGPLICVESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRWIK 538
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 302-537 3.33e-87

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: 268.78  E-value: 3.33e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  302 RIYGGTKSTAGKHPWMVSLQRkfsRREKHFCGGVLIQSCWVLTAAHCVE-HEAENLQVALGKQNLKRREHQeQIFDVEKV 380
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRgSDPSNIRVRLGSHDLSSGEEG-QVIKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  381 IMHHRYRTKDNvpYNDIALLKLKPIdgqcATETKYVKTACLPDF--EFPVGTNCFISGWGATETDD--LSHQLLDARVRL 456
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEP----VTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAgsLPDTLQEVNVPI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  457 ISHKQCNAPRAYDQRLDESMFCAGNLRRpGTDSCQGDSGGPLICvESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRW 536
Cdd:smart00020 151 VSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228


                   .
gi 1201891973  537 I 537
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
303-537 4.64e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 229.25  E-value: 4.64e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 303 IYGGTKSTAGKHPWMVSLQRkfsRREKHFCGGVLIQSCWVLTAAHCVeHEAENLQVALGKQNLKRREHQEQIFDVEKVIM 382
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCV-SGASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 383 HHRYRTKDNvpYNDIALLKLKpidgQCATETKYVKTACLPDFE--FPVGTNCFISGWGATETDDLSHQLLDARVRLISHK 460
Cdd:pfam00089  77 HPNYNPDTL--DNDIALLKLE----SPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201891973 461 QCNapRAYDQRLDESMFCAGNlrrPGTDSCQGDSGGPLICvesGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRWI 537
Cdd:pfam00089 151 TCR--SAYGGTVTDTMICAGA---GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 302-538 1.73e-64

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.05  E-value: 1.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 302 RIYGGTKSTAGKHPWMVSLQRKFSRREkHFCGGVLIQSCWVLTAAHCVEHE-AENLQVALGkqNLKRREHQEQIFDVEKV 380
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPSG-QFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIG--STDLSTSGGTVVKVARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 381 IMHHRYRtkDNVPYNDIALLKL-KPIDGqcatetkyVKTACLPD--FEFPVGTNCFISGWGATETDD--LSHQLLDARVR 455
Cdd:COG5640   107 VVHPDYD--PATPGNDIALLKLaTPVPG--------VAPAPLATsaDAAAPGTPATVAGWGRTSEGPgsQSGTLRKADVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 456 LISHKQCNApraYDQRLDESMFCAGNlRRPGTDSCQGDSGGPLICVESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLR 535
Cdd:COG5640   177 VVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252


                  ...
gi 1201891973 536 WIK 538
Cdd:COG5640   253 WIK 255
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 191-274 4.22e-22

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 90.52  E-value: 4.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 191 DCYEEDSFYYRGRVNQAENGRTCLHWNSHMLLDFSINAFMEDAesyGIGEHNFCRNPDEDQK-PWCFIrKNGKVEWDFCD 269
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPE---GLLEENYCRNPDGDPEgPWCYT-TDPNVRWEYCD 78


                  ....*
gi 1201891973 270 VSLCS 274
Cdd:cd00108    79 IPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 191-275 1.92e-19

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 82.82  E-value: 1.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  191 DCYEEDSFYYRGRVNQAENGRTCLHWNSHM-LLDFSINAFMEDAesygIGEHNFCRNPDED-QKPWCFIrKNGKVEWDFC 268
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTpHLHRFTPESFPDL----GLEENYCRNPDGDsEGPWCYT-TDPNVRWEYC 76


                   ....*..
gi 1201891973  269 DVSLCSG 275
Cdd:smart00130  77 DIPQCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 192-273 4.44e-16

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 73.11  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 192 CYEEDSFYYRGRVNQAENGRTCLHWNSHMLLDFSinafMEDAESY---GIGEhNFCRNPDEDQKPWCFIrKNGKVEWDFC 268
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHS----KYTPENFpakGLGE-NYCRNPDGDERPWCYT-TDPRVRWEYC 74


                  ....*
gi 1201891973 269 DVSLC 273
Cdd:pfam00051  75 DIPRC 79
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 75-105 3.68e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.53  E-value: 3.68e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1201891973  75 CSSNPCKNNGQCEMRGNNFTCHCPMPYTGDT 105
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 73-107 4.87e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 4.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1201891973  73 DLCSS-NPCKNNGQCEMRGNNFTCHCPMPYTGDTCE 107
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 152-184 7.77e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.67  E-value: 7.77e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1201891973 152 CRPNPCKNGGTCIrhRIRSKFTCKCPEPYKGRF 184
Cdd:pfam00008   1 CAPNPCSNGGTCV--DTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
76-107 6.09e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 6.09e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1201891973   76 SSNPCKNNGQCEMRGNNFTCHCPMPYT-GDTCE 107
Cdd:smart00179   7 SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 154-186 1.67e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1201891973 154 PNPCKNGGTCIRhrIRSKFTCKCPEPYKGRFCE 186
Cdd:cd00054     8 GNPCQNGGTCVN--TVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 303-538 9.85e-92

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: 280.70  E-value: 9.85e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 303 IYGGTKSTAGKHPWMVSLQRKFSRrekHFCGGVLIQSCWVLTAAHCVEH-EAENLQVALGKQNLKRREHQEQIFDVEKVI 381
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYSsAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 382 MHHRYRTKDNvpYNDIALLKLKpidgQCATETKYVKTACLPDF--EFPVGTNCFISGWGATETDD-LSHQLLDARVRLIS 458
Cdd:cd00190    78 VHPNYNPSTY--DNDIALLKLK----RPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGpLPDVLQEVNVPIVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 459 HKQCNAPRAYDQRLDESMFCAGNLRRpGTDSCQGDSGGPLICVESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRWIK 538
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 302-537 3.33e-87

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: 268.78  E-value: 3.33e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  302 RIYGGTKSTAGKHPWMVSLQRkfsRREKHFCGGVLIQSCWVLTAAHCVE-HEAENLQVALGKQNLKRREHQeQIFDVEKV 380
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCVRgSDPSNIRVRLGSHDLSSGEEG-QVIKVSKV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  381 IMHHRYRTKDNvpYNDIALLKLKPIdgqcATETKYVKTACLPDF--EFPVGTNCFISGWGATETDD--LSHQLLDARVRL 456
Cdd:smart00020  77 IIHPNYNPSTY--DNDIALLKLKEP----VTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAgsLPDTLQEVNVPI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  457 ISHKQCNAPRAYDQRLDESMFCAGNLRRpGTDSCQGDSGGPLICvESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRW 536
Cdd:smart00020 151 VSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228


                   .
gi 1201891973  537 I 537
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
303-537 4.64e-72

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 229.25  E-value: 4.64e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 303 IYGGTKSTAGKHPWMVSLQRkfsRREKHFCGGVLIQSCWVLTAAHCVeHEAENLQVALGKQNLKRREHQEQIFDVEKVIM 382
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQL---SSGKHFCGGSLISENWVLTAAHCV-SGASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 383 HHRYRTKDNvpYNDIALLKLKpidgQCATETKYVKTACLPDFE--FPVGTNCFISGWGATETDDLSHQLLDARVRLISHK 460
Cdd:pfam00089  77 HPNYNPDTL--DNDIALLKLE----SPVTLGDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1201891973 461 QCNapRAYDQRLDESMFCAGNlrrPGTDSCQGDSGGPLICvesGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLRWI 537
Cdd:pfam00089 151 TCR--SAYGGTVTDTMICAGA---GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 302-538 1.73e-64

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.05  E-value: 1.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 302 RIYGGTKSTAGKHPWMVSLQRKFSRREkHFCGGVLIQSCWVLTAAHCVEHE-AENLQVALGkqNLKRREHQEQIFDVEKV 380
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPSG-QFCGGTLIAPRWVLTAAHCVDGDgPSDLRVVIG--STDLSTSGGTVVKVARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 381 IMHHRYRtkDNVPYNDIALLKL-KPIDGqcatetkyVKTACLPD--FEFPVGTNCFISGWGATETDD--LSHQLLDARVR 455
Cdd:COG5640   107 VVHPDYD--PATPGNDIALLKLaTPVPG--------VAPAPLATsaDAAAPGTPATVAGWGRTSEGPgsQSGTLRKADVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 456 LISHKQCNApraYDQRLDESMFCAGNlRRPGTDSCQGDSGGPLICVESGSYYVYGIVSWGDQCGLKNKPGVYTQVTTFLR 535
Cdd:COG5640   177 VVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRD 252


                  ...
gi 1201891973 536 WIK 538
Cdd:COG5640   253 WIK 255
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 191-274 4.22e-22

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 90.52  E-value: 4.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 191 DCYEEDSFYYRGRVNQAENGRTCLHWNSHMLLDFSINAFMEDAesyGIGEHNFCRNPDEDQK-PWCFIrKNGKVEWDFCD 269
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPE---GLLEENYCRNPDGDPEgPWCYT-TDPNVRWEYCD 78


                  ....*
gi 1201891973 270 VSLCS 274
Cdd:cd00108    79 IPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 191-275 1.92e-19

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 82.82  E-value: 1.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973  191 DCYEEDSFYYRGRVNQAENGRTCLHWNSHM-LLDFSINAFMEDAesygIGEHNFCRNPDED-QKPWCFIrKNGKVEWDFC 268
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTpHLHRFTPESFPDL----GLEENYCRNPDGDsEGPWCYT-TDPNVRWEYC 76


                   ....*..
gi 1201891973  269 DVSLCSG 275
Cdd:smart00130  77 DIPQCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 192-273 4.44e-16

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 73.11  E-value: 4.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 192 CYEEDSFYYRGRVNQAENGRTCLHWNSHMLLDFSinafMEDAESY---GIGEhNFCRNPDEDQKPWCFIrKNGKVEWDFC 268
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHS----KYTPENFpakGLGE-NYCRNPDGDERPWCYT-TDPRVRWEYC 74


                  ....*
gi 1201891973 269 DVSLC 273
Cdd:pfam00051  75 DIPRC 79
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 324-516 5.42e-12

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 64.70  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 324 FSRREKHFCGGVLIQSCWVLTAAHCVE-----HEAENLQVALGKQNLKRREHQeqifdVEKVIMHHRYRTKDNVPYnDIA 398
Cdd:COG3591     6 ETDGGGGVCTGTLIGPNLVLTAGHCVYdgaggGWATNIVFVPGYNGGPYGTAT-----ATRFRVPPGWVASGDAGY-DYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1201891973 399 LLKLKPidgqcatetkyvktaclpdfefPVGTNcfisgWGATETDDLSHQLLDARVRLISHkqcnaPRAYDQRLdeSMFC 478
Cdd:COG3591    80 LLRLDE----------------------PLGDT-----TGWLGLAFNDAPLAGEPVTIIGY-----PGDRPKDL--SLDC 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1201891973 479 AGNLRRPGT-------DSCQGDSGGPLICVESGSYYVYGIVSWGD 516
Cdd:COG3591   126 SGRVTGVQGnrlsydcDTTGGSSGSPVLDDSDGGGRVVGVHSAGG 170
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 75-105 3.68e-06

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 43.53  E-value: 3.68e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1201891973  75 CSSNPCKNNGQCEMRGNNFTCHCPMPYTGDT 105
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 73-107 4.87e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 4.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1201891973  73 DLCSS-NPCKNNGQCEMRGNNFTCHCPMPYTGDTCE 107
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 152-184 7.77e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 39.67  E-value: 7.77e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1201891973 152 CRPNPCKNGGTCIrhRIRSKFTCKCPEPYKGRF 184
Cdd:pfam00008   1 CAPNPCSNGGTCV--DTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 76-107 5.60e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 37.46  E-value: 5.60e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1201891973  76 SSNPCKNNGQCEMRGNNFTCHCPMPYTGD-TCE 107
Cdd:cd00053     4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
76-107 6.09e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 6.09e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1201891973   76 SSNPCKNNGQCEMRGNNFTCHCPMPYT-GDTCE 107
Cdd:smart00179   7 SGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 154-186 1.67e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1201891973 154 PNPCKNGGTCIRhrIRSKFTCKCPEPYKGRFCE 186
Cdd:cd00054     8 GNPCQNGGTCVN--TVGSYRCSCPPGYTGRNCE 38
 
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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