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Conserved domains on  [gi|392887044|ref|NP_492773|]
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Kringle domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KR super family cl00100
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 98-173 7.57e-10

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 smart00130:

Pssm-ID: 412161  Cd Length: 83  Bit Score: 55.47  E-value: 7.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044    98 YRGKKNVDFKDRPCLFWSS----IPNSTFDISDsssssysmNRILPdeyENFCRNPDKNPLGPWCYVGNDTTApcFQPCR 173
Cdd:smart00130  11 YRGTVSVTKSGKPCQRWDSqtphLHRFTPESFP--------DLGLE---ENYCRNPDGDSEGPWCYTTDPNVR--WEYCD 77
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 98-173 7.57e-10

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: 55.47  E-value: 7.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044    98 YRGKKNVDFKDRPCLFWSS----IPNSTFDISDsssssysmNRILPdeyENFCRNPDKNPLGPWCYVGNDTTApcFQPCR 173
Cdd:smart00130  11 YRGTVSVTKSGKPCQRWDSqtphLHRFTPESFP--------DLGLE---ENYCRNPDGDSEGPWCYTTDPNVR--WEYCD 77
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 98-172 1.80e-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: 51.54  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044   98 YRGKKNVDFKDRPCLFWSS-IPNstfdisdsssssySMNRILPDEY------ENFCRNPDkNPLGPWCYVGNDTTApcFQ 170
Cdd:pfam00051   9 YRGTVSTTESGRPCQAWDSqTPH-------------RHSKYTPENFpakglgENYCRNPD-GDERPWCYTTDPRVR--WE 72


                  ..
gi 392887044  171 PC 172
Cdd:pfam00051  73 YC 74
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 98-173 1.94e-08

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: 51.22  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044  98 YRGKKNVDFKDRPCLFWSS-IPNStfdisdsssssysmNRILPDEY------ENFCRNPDKNPLGPWCYVGNDTTApcFQ 170
Cdd:cd00108   12 YRGTVSTTKSGKPCQRWNSqLPHQ--------------HKFNPERFpeglleENYCRNPDGDPEGPWCYTTDPNVR--WE 75


                 ...
gi 392887044 171 PCR 173
Cdd:cd00108   76 YCD 78
 
Name Accession Description Interval E-value
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 98-173 7.57e-10

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: 55.47  E-value: 7.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044    98 YRGKKNVDFKDRPCLFWSS----IPNSTFDISDsssssysmNRILPdeyENFCRNPDKNPLGPWCYVGNDTTApcFQPCR 173
Cdd:smart00130  11 YRGTVSVTKSGKPCQRWDSqtphLHRFTPESFP--------DLGLE---ENYCRNPDGDSEGPWCYTTDPNVR--WEYCD 77
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 98-172 1.80e-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: 51.54  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044   98 YRGKKNVDFKDRPCLFWSS-IPNstfdisdsssssySMNRILPDEY------ENFCRNPDkNPLGPWCYVGNDTTApcFQ 170
Cdd:pfam00051   9 YRGTVSTTESGRPCQAWDSqTPH-------------RHSKYTPENFpakglgENYCRNPD-GDERPWCYTTDPRVR--WE 72


                  ..
gi 392887044  171 PC 172
Cdd:pfam00051  73 YC 74
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 98-173 1.94e-08

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: 51.22  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392887044  98 YRGKKNVDFKDRPCLFWSS-IPNStfdisdsssssysmNRILPDEY------ENFCRNPDKNPLGPWCYVGNDTTApcFQ 170
Cdd:cd00108   12 YRGTVSTTKSGKPCQRWNSqLPHQ--------------HKFNPERFpeglleENYCRNPDGDPEGPWCYTTDPNVR--WE 75


                 ...
gi 392887044 171 PCR 173
Cdd:cd00108   76 YCD 78
 
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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