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Conserved domains on  [gi|1115995402|ref|NP_001334795|]
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kinase non-catalytic C-lobe domain-containing protein 1 isoform 4 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 37-120 1.90e-25

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member smart00750:

Pssm-ID: 473864  Cd Length: 176  Bit Score: 94.39  E-value: 1.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115995402   37 VSLADILSLRDRGLSEQEAWAVCLECSLSMRSVAHAAIFQSLCITPDTLAFNtSGNVCFMEQLSDDPEGAFVPPEFDVTG 116
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKL-DGSVAFKTPEQSRPDPYFMAPEVIQGQ 79


                   ....
gi 1115995402  117 NTFE 120
Cdd:smart00750  80 SYTE 83
 
Name Accession Description Interval E-value
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
 37-120 1.90e-25

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 94.39  E-value: 1.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115995402   37 VSLADILSLRDRGLSEQEAWAVCLECSLSMRSVAHAAIFQSLCITPDTLAFNtSGNVCFMEQLSDDPEGAFVPPEFDVTG 116
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKL-DGSVAFKTPEQSRPDPYFMAPEVIQGQ 79


                   ....
gi 1115995402  117 NTFE 120
Cdd:smart00750  80 SYTE 83
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
 37-67 5.15e-03

Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) evolved from a catalytic protein kinase fold and functions as an interaction domain. In SPIRE1 (protein spire homolog 1) this domain interacts with FMN2 (formin-2).


Pssm-ID: 465129  Cd Length: 196  Bit Score: 34.97  E-value: 5.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1115995402  37 VSLADILSLRDRGLSEQEAWAVCLECSLSMR 67
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGLR 31
 
Name Accession Description Interval E-value
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
 37-120 1.90e-25

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 94.39  E-value: 1.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1115995402   37 VSLADILSLRDRGLSEQEAWAVCLECSLSMRSVAHAAIFQSLCITPDTLAFNtSGNVCFMEQLSDDPEGAFVPPEFDVTG 116
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKL-DGSVAFKTPEQSRPDPYFMAPEVIQGQ 79


                   ....
gi 1115995402  117 NTFE 120
Cdd:smart00750  80 SYTE 83
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
 37-67 5.15e-03

Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) evolved from a catalytic protein kinase fold and functions as an interaction domain. In SPIRE1 (protein spire homolog 1) this domain interacts with FMN2 (formin-2).


Pssm-ID: 465129  Cd Length: 196  Bit Score: 34.97  E-value: 5.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1115995402  37 VSLADILSLRDRGLSEQEAWAVCLECSLSMR 67
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGLR 31
 
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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