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Conserved domains on  [gi|22760294|dbj|BAC11140|]
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unnamed protein product [Homo sapiens]

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 ...
 23-103 6.98e-23

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: 88.99  E-value: 6.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760294     23 GGCFWDNGHLYREDQTSPAPGLRCLNWLDAQSGL-----ASAPVSGaGNHSYCRNPDEDPRGPWCYVSGEAGVPEkrPCE 97
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLhrftpESFPDLG-LEENYCRNPDGDSEGPWCYTTDPNVRWE--YCD 77


                   ....*.
gi 22760294     98 GLRCPE 103
Cdd:smart00130  78 IPQCEE 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 ...
 23-103 6.98e-23

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: 88.99  E-value: 6.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760294     23 GGCFWDNGHLYREDQTSPAPGLRCLNWLDAQSGL-----ASAPVSGaGNHSYCRNPDEDPRGPWCYVSGEAGVPEkrPCE 97
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLhrftpESFPDLG-LEENYCRNPDGDSEGPWCYTTDPNVRWE--YCD 77


                   ....*.
gi 22760294     98 GLRCPE 103
Cdd:smart00130  78 IPQCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 22-102 7.99e-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: 88.97  E-value: 7.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760294  22 SGGCFWDNGHLYREDQTSPAPGLRCLNWLDA----QSGLASAPVSGAGNHSYCRNPDEDPRGPWCYVSGEagVPEKRPCE 97
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQlphqHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDP--NVRWEYCD 78


                ....*
gi 22760294  98 GLRCP 102
Cdd:cd00108  79 IPRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 25-84 3.24e-08

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: 49.61  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22760294    25 CFWDNGHLYREDQTSPAPGLRCLNWlDAQSgLASAPVSGAGNHS-------YCRNPDEDPRgPWCYV 84
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAW-DSQT-PHRHSKYTPENFPakglgenYCRNPDGDER-PWCYT 64
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 23-103 6.98e-23

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: 88.99  E-value: 6.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760294     23 GGCFWDNGHLYREDQTSPAPGLRCLNWLDAQSGL-----ASAPVSGaGNHSYCRNPDEDPRGPWCYVSGEAGVPEkrPCE 97
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLhrftpESFPDLG-LEENYCRNPDGDSEGPWCYTTDPNVRWE--YCD 77


                   ....*.
gi 22760294     98 GLRCPE 103
Cdd:smart00130  78 IPQCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 22-102 7.99e-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: 88.97  E-value: 7.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22760294  22 SGGCFWDNGHLYREDQTSPAPGLRCLNWLDA----QSGLASAPVSGAGNHSYCRNPDEDPRGPWCYVSGEagVPEKRPCE 97
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQlphqHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDP--NVRWEYCD 78


                ....*
gi 22760294  98 GLRCP 102
Cdd:cd00108  79 IPRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 25-84 3.24e-08

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: 49.61  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22760294    25 CFWDNGHLYREDQTSPAPGLRCLNWlDAQSgLASAPVSGAGNHS-------YCRNPDEDPRgPWCYV 84
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAW-DSQT-PHRHSKYTPENFPakglgenYCRNPDGDER-PWCYT 64
 
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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