NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18490837|gb|AAH22308|]
View 

Hepatocyte growth factor (hepapoietin A; scatter factor) [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 205-284 2.19e-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: 142.91  E-value: 2.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    205 ECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 283
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   .
gi 18490837    284 E 284
Cdd:smart00130  82 E 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-203 1.92e-36

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: 124.81  E-value: 1.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 18490837    201 CSE 203
Cdd:smart00130  81 CEE 83
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 39-122 4.30e-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: 100.85  E-value: 4.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNkGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129   1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                ....
gi 18490837 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 ...
 205-284 2.19e-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: 142.91  E-value: 2.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    205 ECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 283
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   .
gi 18490837    284 E 284
Cdd:smart00130  82 E 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 206-283 3.64e-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: 137.05  E-value: 3.64e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18490837   206 CMTCNGESYRGLMDHTESGKICQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 283
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 203-284 1.32e-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: 135.58  E-value: 1.32e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837 203 EVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 281
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                ...
gi 18490837 282 TCE 284
Cdd:cd00108  81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-203 1.92e-36

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: 124.81  E-value: 1.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 18490837    201 CSE 203
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 126-202 5.54e-36

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: 123.64  E-value: 5.54e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837 126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 18490837 201 CS 202
Cdd:cd00108  82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 128-201 3.85e-33

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: 116.25  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837   128 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 201
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 4.30e-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: 100.85  E-value: 4.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNkGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129   1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                ....
gi 18490837 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 3.01e-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: 52.58  E-value: 3.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837     37 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNKglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 18490837    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 1.08e-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: 51.01  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    41 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNKGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 18490837   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 ...
 205-284 2.19e-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: 142.91  E-value: 2.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    205 ECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 283
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   .
gi 18490837    284 E 284
Cdd:smart00130  82 E 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 206-283 3.64e-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: 137.05  E-value: 3.64e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18490837   206 CMTCNGESYRGLMDHTESGKICQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 283
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 203-284 1.32e-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: 135.58  E-value: 1.32e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837 203 EVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 281
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                ...
gi 18490837 282 TCE 284
Cdd:cd00108  81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-203 1.92e-36

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: 124.81  E-value: 1.92e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 18490837    201 CSE 203
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 126-202 5.54e-36

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: 123.64  E-value: 5.54e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837 126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 18490837 201 CS 202
Cdd:cd00108  82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 128-201 3.85e-33

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: 116.25  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837   128 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 201
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 4.30e-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: 100.85  E-value: 4.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNkGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129   1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                ....
gi 18490837 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 3.32e-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: 3.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837  40 HEFKKSAktTLIKIDPALKIKTKKVNTADQCANRCTRNKglPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLY 119
Cdd:cd01099   2 NDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEET--EFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYY 77


                ...
gi 18490837 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 3.01e-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: 52.58  E-value: 3.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837     37 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNKglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 18490837    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 1.08e-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: 51.01  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18490837    41 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNKGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 18490837   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 2.60e-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: 35.87  E-value: 2.60e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18490837  59 IKTKKVNTADQCANRCTRNKGlpftCKAFVFDKARKQCL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH