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Conserved domains on  [gi|82207873|sp|Q7SXB3|]
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RecName: Full=Phosphoinositide-3-kinase-interacting protein 1; AltName: Full=Kringle domain-containing protein HGFL; Flags: Precursor

Protein Classification

inactive tyrosine-protein kinase transmembrane receptor ROR1( domain architecture ID 10639013)

inactive tyrosine-protein kinase transmembrane receptor ROR1 maybe a receptor for ligand WNT5A which activate downstream NFkB signaling pathway and may result in the inhibition of WNT3A-mediated signaling; has very low kinase activity in vitro

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 ...
24-101 4.91e-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: 94.76  E-value: 4.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873     24 DCITNNGEDYRGTQQKTSSGSTCLSWRS--------LNLKFKDSQtgvGDHNFCRNPDG-SNKPWCYVSGSsgETKKEAC 94
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtphlhrfTPESFPDLG---LEENYCRNPDGdSEGPWCYTTDP--NVRWEYC 76

                   ....*..
gi 82207873     95 DIRICQD 101
Cdd:smart00130  77 DIPQCEE 83
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
24-101 4.91e-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: 94.76  E-value: 4.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873     24 DCITNNGEDYRGTQQKTSSGSTCLSWRS--------LNLKFKDSQtgvGDHNFCRNPDG-SNKPWCYVSGSsgETKKEAC 94
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtphlhrfTPESFPDLG---LEENYCRNPDGdSEGPWCYTTDP--NVRWEYC 76

                   ....*..
gi 82207873     95 DIRICQD 101
Cdd:smart00130  77 DIPQCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
24-99 1.55e-23

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 90.90  E-value: 1.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873  24 DCITNNGEDYRGTQQKTSSGSTCLSWRSlNLKFKDSQT------GVGDHNFCRNPDG-SNKPWCYVSGssGETKKEACDI 96
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNS-QLPHQHKFNperfpeGLLEENYCRNPDGdPEGPWCYTTD--PNVRWEYCDI 79

                ...
gi 82207873  97 RIC 99
Cdd:cd00108  80 PRC 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
25-99 7.25e-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: 81.20  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873    25 CITNNGEDYRGTQQKTSSGSTCLSWRS-----LNLKFKDSQTGVG-DHNFCRNPDGSNKPWCYVSGSSGETkkEACDIRI 98
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSqtphrHSKYTPENFPAKGlGENYCRNPDGDERPWCYTTDPRVRW--EYCDIPR 78

                  .
gi 82207873    99 C 99
Cdd:pfam00051  79 C 79
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
24-101 4.91e-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: 94.76  E-value: 4.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873     24 DCITNNGEDYRGTQQKTSSGSTCLSWRS--------LNLKFKDSQtgvGDHNFCRNPDG-SNKPWCYVSGSsgETKKEAC 94
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSqtphlhrfTPESFPDLG---LEENYCRNPDGdSEGPWCYTTDP--NVRWEYC 76

                   ....*..
gi 82207873     95 DIRICQD 101
Cdd:smart00130  77 DIPQCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
24-99 1.55e-23

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 90.90  E-value: 1.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873  24 DCITNNGEDYRGTQQKTSSGSTCLSWRSlNLKFKDSQT------GVGDHNFCRNPDG-SNKPWCYVSGssGETKKEACDI 96
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNS-QLPHQHKFNperfpeGLLEENYCRNPDGdPEGPWCYTTD--PNVRWEYCDI 79

                ...
gi 82207873  97 RIC 99
Cdd:cd00108  80 PRC 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
25-99 7.25e-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: 81.20  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82207873    25 CITNNGEDYRGTQQKTSSGSTCLSWRS-----LNLKFKDSQTGVG-DHNFCRNPDGSNKPWCYVSGSSGETkkEACDIRI 98
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSqtphrHSKYTPENFPAKGlGENYCRNPDGDERPWCYTTDPRVRW--EYCDIPR 78

                  .
gi 82207873    99 C 99
Cdd:pfam00051  79 C 79
 
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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