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Conserved domains on  [gi|295054188|ref|NP_001171131|]
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hyaluronan-binding protein 2 isoform 2 [Homo sapiens]

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 ...
288-527 1.20e-88

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: 272.23  E-value: 1.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 288 IYGGFKSTAGKHPWQASLQSSLpltismpQGHFCGGALIHPCWVLTAAHCT-DIKTRHLKVVLGDQDLKKEEFHEQSFRV 366
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 367 EKIFKYSHYNerDEIPHNDIALLKLKpvdgHCALESKYVKTVCLPDGS--FPSGSECHISGWGVT-ETGKGSRQLLDAKV 443
Cdd:cd00190   74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 444 KLIANTLCNSRQLYDHMIDDSMICAGNLQKpGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGK--RPGVYTQVTKFL 521
Cdd:cd00190  148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226

                 ....*.
gi 295054188 522 NWIKAT 527
Cdd:cd00190  227 DWIQKT 232
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
165-251 4.27e-29

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: 109.78  E-value: 4.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 165 SDDCYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENYNMFMEDaetHGIGEHNFCRNPDAD-EKPWCFikVTNDKVKWE 243
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCY--TTDPNVRWE 75

                 ....*...
gi 295054188 244 YCDVSACS 251
Cdd:cd00108   76 YCDIPRCE 83
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
51-80 2.88e-04

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: 38.13  E-value: 2.88e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 295054188   51 CQPNPCEHGGDCLVHGSTFTCSCLAPFSGN 80
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
288-527 1.20e-88

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: 272.23  E-value: 1.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 288 IYGGFKSTAGKHPWQASLQSSLpltismpQGHFCGGALIHPCWVLTAAHCT-DIKTRHLKVVLGDQDLKKEEFHEQSFRV 366
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 367 EKIFKYSHYNerDEIPHNDIALLKLKpvdgHCALESKYVKTVCLPDGS--FPSGSECHISGWGVT-ETGKGSRQLLDAKV 443
Cdd:cd00190   74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 444 KLIANTLCNSRQLYDHMIDDSMICAGNLQKpGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGK--RPGVYTQVTKFL 521
Cdd:cd00190  148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226

                 ....*.
gi 295054188 522 NWIKAT 527
Cdd:cd00190  227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
287-524 1.02e-84

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: 261.84  E-value: 1.02e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   287 RIYGGFKSTAGKHPWQASLQSSLpltismpQGHFCGGALIHPCWVLTAAHCTDIKTRH-LKVVLGDQDLKKEEfHEQSFR 365
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG-------GRHFCGGSLISPRWVLTAAHCVRGSDPSnIRVRLGSHDLSSGE-EGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   366 VEKIFKYSHYNerDEIPHNDIALLKLK-PVDghcalESKYVKTVCLPDGS--FPSGSECHISGWGVTETGKG--SRQLLD 440
Cdd:smart00020  73 VSKVIIHPNYN--PSTYDNDIALLKLKePVT-----LSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGslPDTLQE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   441 AKVKLIANTLCNSRQLYDHMIDDSMICAGNLQKpGQDTCQGDSGGPLTCeKDGTYYVYGIVSWGLECGK--RPGVYTQVT 518
Cdd:smart00020 146 VNVPIVSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARpgKPGVYTRVS 223

                   ....*.
gi 295054188   519 KFLNWI 524
Cdd:smart00020 224 SYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
287-530 2.56e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.98  E-value: 2.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 287 RIYGGFKSTAGKHPWQASLQSSlpltiSMPQGHFCGGALIHPCWVLTAAHC-TDIKTRHLKVVLGDQDLKKEEfhEQSFR 365
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSS-----NGPSGQFCGGTLIAPRWVLTAAHCvDGDGPSDLRVVIGSTDLSTSG--GTVVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 366 VEKIFKYSHYNERDeiPHNDIALLKL-KPVDGhcaleskyVKTVCLPDGSFPS--GSECHISGWGVTETGKG--SRQLLD 440
Cdd:COG5640  103 VARIVVHPDYDPAT--PGNDIALLKLaTPVPG--------VAPAPLATSADAAapGTPATVAGWGRTSEGPGsqSGTLRK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 441 AKVKLIANTLCNSrqlYDHMIDDSMICAGNlQKPGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGL-EC-GKRPGVYTQVT 518
Cdd:COG5640  173 ADVPVVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCaAGYPGVYTRVS 248
                        250
                 ....*....|..
gi 295054188 519 KFLNWIKATIKS 530
Cdd:COG5640  249 AYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
288-524 1.53e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.21  E-value: 1.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  288 IYGGFKSTAGKHPWQASLQSSLPltismpqGHFCGGALIHPCWVLTAAHCTDiKTRHLKVVLGDQDLKKEEFHEQSFRVE 367
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG-------KHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEQKFDVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  368 KIFKYSHYNERDEipHNDIALLKLK-PVDGhcaleSKYVKTVCLPDGS--FPSGSECHISGWGVTETGKGSRQLLDAKVK 444
Cdd:pfam00089  73 KIIVHPNYNPDTL--DNDIALLKLEsPVTL-----GDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  445 LIANTLCNSRqlYDHMIDDSMICAGNlqkPGQDTCQGDSGGPLTCEKDgtyYVYGIVSWGLEC--GKRPGVYTQVTKFLN 522
Cdd:pfam00089 146 VVSRETCRSA--YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCasGNYPGVYTPVSSYLD 217

                  ..
gi 295054188  523 WI 524
Cdd:pfam00089 218 WI 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
165-251 4.27e-29

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: 109.78  E-value: 4.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 165 SDDCYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENYNMFMEDaetHGIGEHNFCRNPDAD-EKPWCFikVTNDKVKWE 243
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCY--TTDPNVRWE 75

                 ....*...
gi 295054188 244 YCDVSACS 251
Cdd:cd00108   76 YCDIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
167-251 3.88e-25

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: 99.00  E-value: 3.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   167 DCYVGDGYSYRGKMNRTVNQHACLYWNS---HLLLQenYNMFMEDAethgIGEHNFCRNPDAD-EKPWCFikVTNDKVKW 242
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtpHLHRF--TPESFPDL----GLEENYCRNPDGDsEGPWCY--TTDPNVRW 73

                   ....*....
gi 295054188   243 EYCDVSACS 251
Cdd:smart00130  74 EYCDIPQCE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
168-250 2.15e-20

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: 85.44  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  168 CYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENynmfMEDAETH---GIGEhNFCRNPDADEKPWCFikVTNDKVKWEY 244
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHS----KYTPENFpakGLGE-NYCRNPDGDERPWCY--TTDPRVRWEY 73

                  ....*.
gi 295054188  245 CDVSAC 250
Cdd:pfam00051  74 CDIPRC 79
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
51-80 2.88e-04

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: 38.13  E-value: 2.88e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 295054188   51 CQPNPCEHGGDCLVHGSTFTCSCLAPFSGN 80
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
49-83 5.51e-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: 34.92  E-value: 5.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 295054188  49 DPCQ-PNPCEHGGDCLVHGSTFTCSCLAPFSGNKCQ 83
Cdd:cd00054    3 DECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
288-527 1.20e-88

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: 272.23  E-value: 1.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 288 IYGGFKSTAGKHPWQASLQSSLpltismpQGHFCGGALIHPCWVLTAAHCT-DIKTRHLKVVLGDQDLKKEEFHEQSFRV 366
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTG-------GRHFCGGSLISPRWVLTAAHCVySSAPSNYTVRLGSHDLSSNEGGGQVIKV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 367 EKIFKYSHYNerDEIPHNDIALLKLKpvdgHCALESKYVKTVCLPDGS--FPSGSECHISGWGVT-ETGKGSRQLLDAKV 443
Cdd:cd00190   74 KKVIVHPNYN--PSTYDNDIALLKLK----RPVTLSDNVRPICLPSSGynLPAGTTCTVSGWGRTsEGGPLPDVLQEVNV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 444 KLIANTLCNSRQLYDHMIDDSMICAGNLQKpGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGK--RPGVYTQVTKFL 521
Cdd:cd00190  148 PIVSNAECKRAYSYGGTITDNMLCAGGLEG-GKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARpnYPGVYTRVSSYL 226

                 ....*.
gi 295054188 522 NWIKAT 527
Cdd:cd00190  227 DWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
287-524 1.02e-84

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: 261.84  E-value: 1.02e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   287 RIYGGFKSTAGKHPWQASLQSSLpltismpQGHFCGGALIHPCWVLTAAHCTDIKTRH-LKVVLGDQDLKKEEfHEQSFR 365
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGG-------GRHFCGGSLISPRWVLTAAHCVRGSDPSnIRVRLGSHDLSSGE-EGQVIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   366 VEKIFKYSHYNerDEIPHNDIALLKLK-PVDghcalESKYVKTVCLPDGS--FPSGSECHISGWGVTETGKG--SRQLLD 440
Cdd:smart00020  73 VSKVIIHPNYN--PSTYDNDIALLKLKePVT-----LSDNVRPICLPSSNynVPAGTTCTVSGWGRTSEGAGslPDTLQE 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   441 AKVKLIANTLCNSRQLYDHMIDDSMICAGNLQKpGQDTCQGDSGGPLTCeKDGTYYVYGIVSWGLECGK--RPGVYTQVT 518
Cdd:smart00020 146 VNVPIVSNATCRRAYSGGGAITDNMLCAGGLEG-GKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARpgKPGVYTRVS 223

                   ....*.
gi 295054188   519 KFLNWI 524
Cdd:smart00020 224 SYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
287-530 2.56e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 217.98  E-value: 2.56e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 287 RIYGGFKSTAGKHPWQASLQSSlpltiSMPQGHFCGGALIHPCWVLTAAHC-TDIKTRHLKVVLGDQDLKKEEfhEQSFR 365
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSS-----NGPSGQFCGGTLIAPRWVLTAAHCvDGDGPSDLRVVIGSTDLSTSG--GTVVK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 366 VEKIFKYSHYNERDeiPHNDIALLKL-KPVDGhcaleskyVKTVCLPDGSFPS--GSECHISGWGVTETGKG--SRQLLD 440
Cdd:COG5640  103 VARIVVHPDYDPAT--PGNDIALLKLaTPVPG--------VAPAPLATSADAAapGTPATVAGWGRTSEGPGsqSGTLRK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 441 AKVKLIANTLCNSrqlYDHMIDDSMICAGNlQKPGQDTCQGDSGGPLTCEKDGTYYVYGIVSWGL-EC-GKRPGVYTQVT 518
Cdd:COG5640  173 ADVPVVSDATCAA---YGGFDGGTMLCAGY-PEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCaAGYPGVYTRVS 248
                        250
                 ....*....|..
gi 295054188 519 KFLNWIKATIKS 530
Cdd:COG5640  249 AYRDWIKSTAGG 260
Trypsin pfam00089
Trypsin;
288-524 1.53e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 204.21  E-value: 1.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  288 IYGGFKSTAGKHPWQASLQSSLPltismpqGHFCGGALIHPCWVLTAAHCTDiKTRHLKVVLGDQDLKKEEFHEQSFRVE 367
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG-------KHFCGGSLISENWVLTAAHCVS-GASDVKVVLGAHNIVLREGGEQKFDVE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  368 KIFKYSHYNERDEipHNDIALLKLK-PVDGhcaleSKYVKTVCLPDGS--FPSGSECHISGWGVTETGKGSRQLLDAKVK 444
Cdd:pfam00089  73 KIIVHPNYNPDTL--DNDIALLKLEsPVTL-----GDTVRPICLPDASsdLPVGTTCTVSGWGNTKTLGPSDTLQEVTVP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  445 LIANTLCNSRqlYDHMIDDSMICAGNlqkPGQDTCQGDSGGPLTCEKDgtyYVYGIVSWGLEC--GKRPGVYTQVTKFLN 522
Cdd:pfam00089 146 VVSRETCRSA--YGGTVTDTMICAGA---GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCasGNYPGVYTPVSSYLD 217

                  ..
gi 295054188  523 WI 524
Cdd:pfam00089 218 WI 219
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
165-251 4.27e-29

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: 109.78  E-value: 4.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 165 SDDCYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENYNMFMEDaetHGIGEHNFCRNPDAD-EKPWCFikVTNDKVKWE 243
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFP---EGLLEENYCRNPDGDpEGPWCY--TTDPNVRWE 75

                 ....*...
gi 295054188 244 YCDVSACS 251
Cdd:cd00108   76 YCDIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
167-251 3.88e-25

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: 99.00  E-value: 3.88e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188   167 DCYVGDGYSYRGKMNRTVNQHACLYWNS---HLLLQenYNMFMEDAethgIGEHNFCRNPDAD-EKPWCFikVTNDKVKW 242
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtpHLHRF--TPESFPDL----GLEENYCRNPDGDsEGPWCY--TTDPNVRW 73

                   ....*....
gi 295054188   243 EYCDVSACS 251
Cdd:smart00130  74 EYCDIPQCE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
168-250 2.15e-20

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: 85.44  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188  168 CYVGDGYSYRGKMNRTVNQHACLYWNSHLLLQENynmfMEDAETH---GIGEhNFCRNPDADEKPWCFikVTNDKVKWEY 244
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHS----KYTPENFpakGLGE-NYCRNPDGDERPWCY--TTDPRVRWEY 73

                  ....*.
gi 295054188  245 CDVSAC 250
Cdd:pfam00051  74 CDIPRC 79
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
317-528 1.95e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.38  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 317 QGHFCGGALIHPCWVLTAAHCTDIKT-----RHLKVVLGDQDLKKEEFHEQSFRVEKIFKyshyneRDEIPHNDIALLKL 391
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVYDGAgggwaTNIVFVPGYNGGPYGTATATRFRVPPGWV------ASGDAGYDYALLRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295054188 392 K----PVDGHCALeskyvktvcLPDGSFPSGSECHISGWGVTETGKGSRQlldakvklianTLCNSRQLYDHMIddSMIC 467
Cdd:COG3591   84 DeplgDTTGWLGL---------AFNDAPLAGEPVTIIGYPGDRPKDLSLD-----------CSGRVTGVQGNRL--SYDC 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295054188 468 agnlqkpgqDTCQGDSGGPLTCEKDGTYYVYGIVSWGLECGKRPGVYTqVTKFLNWIKATI 528
Cdd:COG3591  142 ---------DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRANTGVRL-TSAIVAALRAWA 192
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
51-80 2.88e-04

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: 38.13  E-value: 2.88e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 295054188   51 CQPNPCEHGGDCLVHGSTFTCSCLAPFSGN 80
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
49-83 5.51e-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: 34.92  E-value: 5.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 295054188  49 DPCQ-PNPCEHGGDCLVHGSTFTCSCLAPFSGNKCQ 83
Cdd:cd00054    3 DECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 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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