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Conserved domains on  [gi|2462589922|ref|XP_054202555|]
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hepatocyte growth factor-like protein isoform X10 [Homo sapiens]

Protein Classification

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 ...
 122-202 1.15e-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: 130.59  E-value: 1.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  122 RTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLRN--GLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKS 199
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPdlGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 2462589922  200 CRE 202
Cdd:smart00130  81 CEE 83
KR super family cl00100
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 202-241 6.11e-14

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.


The actual alignment was detected with superfamily member cd00108:

Pssm-ID: 412161  Cd Length: 83  Bit Score: 67.02  E-value: 6.11e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462589922 202 EAACVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEP 241
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNP 40
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 37-118 1.22e-13

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: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  37 LNDFQVLRgtELQHLLHAVVPgpWQEDVADAEECAGRCG--PLMDCRAFHYNVSSHGCQLLPWTQHSPHTRLRRSGRCDL 114
Cdd:cd01099     1 LNDFKFVL--VLNKILVSEVK--TEITVASLEECLRKCLeeTEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                  ....
gi 2462589922 115 FQKK 118
Cdd:cd01099    77 YENK 80
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 234-457 1.36e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  234 PHQHPFEPGSSTKVWTTTIAGILTAPSGHGATLRIRRSSESSVTSPAAGPR--HSPAKRPQL-SAASAGRVRATGAQPIP 310
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrpRRRAARPTVgSLTSLADPPPPPPTPEP 2710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  311 PLRAYLASVGTRKSLISTDLRQKNTRAKTFGRTSAGTPTAQRRPGASHCGPACARPFATRSGVVQTTCGPRTATTAQGSS 390
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462589922  391 tAARSARPARVSSASAGPLRRRTSRSSRLPPNrmhnwRRTSAGTQMGIAMGPGATRWTQGPHSTTVP 457
Cdd:PHA03247  2791 -LSESRESLPSPWDPADPPAAVLAPAAALPPA-----ASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 122-202 1.15e-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: 130.59  E-value: 1.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  122 RTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLRN--GLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKS 199
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPdlGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 2462589922  200 CRE 202
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 122-200 5.37e-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: 129.04  E-value: 5.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922 122 RTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLR--NGLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKS 199
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFpeGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                  .
gi 2462589922 200 C 200
Cdd:cd00108    82 C 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 124-200 2.91e-32

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: 118.56  E-value: 2.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922 124 CIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDH-KYTPT--LRNGLEENFCRNPDGDPgGPWCYTTDPAVRFQSCGIKSC 200
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPEnfPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 202-241 6.11e-14

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: 67.02  E-value: 6.11e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462589922 202 EAACVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEP 241
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNP 40
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 37-118 1.22e-13

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: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  37 LNDFQVLRgtELQHLLHAVVPgpWQEDVADAEECAGRCG--PLMDCRAFHYNVSSHGCQLLPWTQHSPHTRLRRSGRCDL 114
Cdd:cd01099     1 LNDFKFVL--VLNKILVSEVK--TEITVASLEECLRKCLeeTEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                  ....
gi 2462589922 115 FQKK 118
Cdd:cd01099    77 YENK 80
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 205-243 1.27e-13

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: 66.26  E-value: 1.27e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462589922  205 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGS 243
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPES 41
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 39-117 1.63e-12

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: 62.96  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  39 DFQVLRGTELQHLLhavvpgPWQEDVADAEECAGRCGPLMDCRAFHYNVSSHGCQLLPWTQHSPhTRLRRSG-RCDLFQK 117
Cdd:pfam00024   2 DFERVPGSSLSGVD------VSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSL-PRLKRSDnKVDYYEK 74
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 205-239 2.69e-12

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: 62.32  E-value: 2.69e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462589922 205 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPF 239
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSK 35
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 38-118 1.36e-11

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: 60.29  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922   38 NDFQVLRGTELqhllhaVVPGPWQEDVADAEECAGRC-GPLMDCRAFHYNVSSHGCQLLpWTQHSPHTRLRRSGRCDLFQ 116
Cdd:smart00473   4 DCFVRLPNTKL------PGFSRIVISVASLEECASKClNSNCSCRSFTYNNGTKGCLLW-SESSLGDARLFPSGGVDLYE 76


                   ..
gi 2462589922  117 KK 118
Cdd:smart00473  77 KI 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
 234-457 1.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  234 PHQHPFEPGSSTKVWTTTIAGILTAPSGHGATLRIRRSSESSVTSPAAGPR--HSPAKRPQL-SAASAGRVRATGAQPIP 310
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrpRRRAARPTVgSLTSLADPPPPPPTPEP 2710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  311 PLRAYLASVGTRKSLISTDLRQKNTRAKTFGRTSAGTPTAQRRPGASHCGPACARPFATRSGVVQTTCGPRTATTAQGSS 390
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462589922  391 tAARSARPARVSSASAGPLRRRTSRSSRLPPNrmhnwRRTSAGTQMGIAMGPGATRWTQGPHSTTVP 457
Cdd:PHA03247  2791 -LSESRESLPSPWDPADPPAAVLAPAAALPPA-----ASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 122-202 1.15e-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: 130.59  E-value: 1.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  122 RTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLRN--GLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKS 199
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPdlGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 2462589922  200 CRE 202
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 122-200 5.37e-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: 129.04  E-value: 5.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922 122 RTCIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDHKYTPTLR--NGLEENFCRNPDGDPGGPWCYTTDPAVRFQSCGIKS 199
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFpeGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                  .
gi 2462589922 200 C 200
Cdd:cd00108    82 C 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 124-200 2.91e-32

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: 118.56  E-value: 2.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922 124 CIMNNGVGYRGTMATTVGGLPCQAWSHKFPNDH-KYTPT--LRNGLEENFCRNPDGDPgGPWCYTTDPAVRFQSCGIKSC 200
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPEnfPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 202-241 6.11e-14

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: 67.02  E-value: 6.11e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462589922 202 EAACVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEP 241
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNP 40
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 37-118 1.22e-13

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: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  37 LNDFQVLRgtELQHLLHAVVPgpWQEDVADAEECAGRCG--PLMDCRAFHYNVSSHGCQLLPWTQHSPHTRLRRSGRCDL 114
Cdd:cd01099     1 LNDFKFVL--VLNKILVSEVK--TEITVASLEECLRKCLeeTEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                  ....
gi 2462589922 115 FQKK 118
Cdd:cd01099    77 YENK 80
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 205-243 1.27e-13

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: 66.26  E-value: 1.27e-13
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2462589922  205 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPFEPGS 243
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPES 41
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 39-117 1.63e-12

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: 62.96  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  39 DFQVLRGTELQHLLhavvpgPWQEDVADAEECAGRCGPLMDCRAFHYNVSSHGCQLLPWTQHSPhTRLRRSG-RCDLFQK 117
Cdd:pfam00024   2 DFERVPGSSLSGVD------VSTVTVSSAEECAQRCTNEPRCRSFTYNPKSKKCHLKSSSSGSL-PRLKRSDnKVDYYEK 74
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 205-239 2.69e-12

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: 62.32  E-value: 2.69e-12
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462589922 205 CVWCNGEEYRGAVDRTESGRECQRWDLQHPHQHPF 239
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSK 35
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 38-118 1.36e-11

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: 60.29  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922   38 NDFQVLRGTELqhllhaVVPGPWQEDVADAEECAGRC-GPLMDCRAFHYNVSSHGCQLLpWTQHSPHTRLRRSGRCDLFQ 116
Cdd:smart00473   4 DCFVRLPNTKL------PGFSRIVISVASLEECASKClNSNCSCRSFTYNNGTKGCLLW-SESSLGDARLFPSGGVDLYE 76


                   ..
gi 2462589922  117 KK 118
Cdd:smart00473  77 KI 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
 234-457 1.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  234 PHQHPFEPGSSTKVWTTTIAGILTAPSGHGATLRIRRSSESSVTSPAAGPR--HSPAKRPQL-SAASAGRVRATGAQPIP 310
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrpRRRAARPTVgSLTSLADPPPPPPTPEP 2710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922  311 PLRAYLASVGTRKSLISTDLRQKNTRAKTFGRTSAGTPTAQRRPGASHCGPACARPFATRSGVVQTTCGPRTATTAQGSS 390
Cdd:PHA03247  2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462589922  391 tAARSARPARVSSASAGPLRRRTSRSSRLPPNrmhnwRRTSAGTQMGIAMGPGATRWTQGPHSTTVP 457
Cdd:PHA03247  2791 -LSESRESLPSPWDPADPPAAVLAPAAALPPA-----ASPAGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
PHA03378 PHA03378
EBNA-3B; Provisional
 234-398 2.44e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922 234 PHQHP-FEPGSSTKVWTTtIAGILTAPSGHGA-TLRIRRSSESSVTSPAAGPrhSPAKRPQLSAASAGRVRATGAQPIPP 311
Cdd:PHA03378  651 PHQPPqVEITPYKPTWTQ-IGHIPYQPSPTGAnTMLPIQWAPGTMQPPPRAP--TPMRPPAAPPGRAQRPAAATGRARPP 727

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462589922 312 LRAYLASvgtrkslistdlrQKNTRAKTFGRTSAGTPTAQRRPGAShcgPACARPFATRSGVVQTTCGPRTATTAQGSST 391
Cdd:PHA03378  728 AAAPGRA-------------RPPAAAPGRARPPAAAPGRARPPAAA---PGRARPPAAAPGAPTPQPPPQAPPAPQQRPR 791


                  ....*..
gi 2462589922 392 AARSARP 398
Cdd:PHA03378  792 GAPTPQP 798
 
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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