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Conserved domains on  [gi|795344047|ref|XP_011783085|]
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PREDICTED: hepatocyte growth factor isoform X2 [Colobus angolensis palliatus]

Protein Classification

PAN/Apple domain-containing protein( domain architecture ID 10820474)

PAN/Apple domain-containing protein contains a conserved core of three disulphide bridges and may mediate protein-protein or protein-carbohydrate interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
210-289 1.16e-43

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: 143.68  E-value: 1.16e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   210 ECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 288
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81

                   .
gi 795344047   289 E 289
Cdd:smart00130  82 E 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
126-208 8.44e-41

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: 136.37  E-value: 8.44e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80

                   ...
gi 795344047   206 CSE 208
Cdd:smart00130  81 CEE 83
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
39-122 3.26e-27

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


:

Pssm-ID: 238074  Cd Length: 80  Bit Score: 101.23  E-value: 3.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNnGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129    1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76

                 ....
gi 795344047 119 YENK 122
Cdd:cd00129   77 YENK 80
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
210-289 1.16e-43

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: 143.68  E-value: 1.16e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   210 ECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 288
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81

                   .
gi 795344047   289 E 289
Cdd:smart00130  82 E 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
211-288 1.67e-41

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: 137.82  E-value: 1.67e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795344047  211 CMTCNGESYRGLMDHTESGKSCQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 288
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
208-289 5.41e-41

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: 136.74  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047 208 EVECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 286
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80

                 ...
gi 795344047 287 TCE 289
Cdd:cd00108   81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
126-208 8.44e-41

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: 136.37  E-value: 8.44e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80

                   ...
gi 795344047   206 CSE 208
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
126-207 4.15e-40

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: 134.43  E-value: 4.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047 126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81

                 ..
gi 795344047 206 CS 207
Cdd:cd00108   82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
128-206 1.90e-35

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: 122.42  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047  128 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSF-LPSSYRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 206
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
39-122 3.26e-27

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238074  Cd Length: 80  Bit Score: 101.23  E-value: 3.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNnGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129    1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76

                 ....
gi 795344047 119 YENK 122
Cdd:cd00129   77 YENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
37-122 1.10e-09

divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans hypothetical ORFs and the extracellular portion of plant receptor-like protein kinases. Predicted to possess protein- and/or carbohydrate-binding functions.


Pssm-ID: 214680  Cd Length: 78  Bit Score: 54.12  E-value: 1.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047    37 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNNglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72

                   ....*.
gi 795344047   117 DLYENK 122
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
41-121 3.95e-08

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 49.47  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   41 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNNGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73

                  .
gi 795344047  121 N 121
Cdd:pfam00024  74 K 74
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
210-289 1.16e-43

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: 143.68  E-value: 1.16e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   210 ECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 288
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81

                   .
gi 795344047   289 E 289
Cdd:smart00130  82 E 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
211-288 1.67e-41

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: 137.82  E-value: 1.67e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795344047  211 CMTCNGESYRGLMDHTESGKSCQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 288
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
208-289 5.41e-41

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: 136.74  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047 208 EVECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 286
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80

                 ...
gi 795344047 287 TCE 289
Cdd:cd00108   81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
126-208 8.44e-41

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: 136.37  E-value: 8.44e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80

                   ...
gi 795344047   206 CSE 208
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
126-207 4.15e-40

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: 134.43  E-value: 4.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047 126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81

                 ..
gi 795344047 206 CS 207
Cdd:cd00108   82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
128-206 1.90e-35

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: 122.42  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047  128 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSF-LPSSYRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 206
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
39-122 3.26e-27

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238074  Cd Length: 80  Bit Score: 101.23  E-value: 3.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNnGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129    1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76

                 ....
gi 795344047 119 YENK 122
Cdd:cd00129   77 YENK 80
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
40-122 3.51e-14

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238532  Cd Length: 80  Bit Score: 66.34  E-value: 3.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047  40 HEFKKSAktTLIKIDPALKIKTKKVNTADQCANRCTRNNglPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLY 119
Cdd:cd01099    2 NDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEET--EFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYY 77

                 ...
gi 795344047 120 ENK 122
Cdd:cd01099   78 ENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
37-122 1.10e-09

divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans hypothetical ORFs and the extracellular portion of plant receptor-like protein kinases. Predicted to possess protein- and/or carbohydrate-binding functions.


Pssm-ID: 214680  Cd Length: 78  Bit Score: 54.12  E-value: 1.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047    37 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNNglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72

                   ....*.
gi 795344047   117 DLYENK 122
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
41-121 3.95e-08

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 49.47  E-value: 3.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795344047   41 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNNGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73

                  .
gi 795344047  121 N 121
Cdd:pfam00024  74 K 74
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
59-97 2.05e-03

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 36.26  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 795344047  59 IKTKKVNTADQCANRCTRNNGlpftCKAFVFDKARKQCL 97
Cdd:cd01100   19 LSTVFASSAEQCQAACTADPG----CLAFTYNTKSKKCF 53
 
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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