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Conserved domains on  [gi|356582454|ref|NP_001239202|]
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divergent protein kinase domain 1A isoform 5 [Homo sapiens]

Protein Classification

PIP49_N domain-containing protein( domain architecture ID 10632810)

PIP49_N domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 19-159 4.46e-82

N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane proteins localize to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).


:

Pssm-ID: 464353  Cd Length: 158  Bit Score: 238.80  E-value: 4.46e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582454   19 ARFSYVRMKYLFFSWLVVFVGSWIIYVQYSTYTELCRGKDCKKIICDKYKTGVIDGPACNSLCVTETLYFGKCLSTKPNN 98
Cdd:pfam14875   1 ARFSYRRVKYLFLVWLAVFVGSWVVYVQYSSYTELCRGHDCENIICDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356582454   99 QMYLGIWDNLPGVVKCQMEQALHLDFGTELEPRKEIVLFDKPTRGTTVQKFKEMVYSLFKD 159
Cdd:pfam14875  81 QVYTGLWGDLEVVIKCGIEEVPRSNYEPLSWPRSEYVLFDKPTRGTSVEEFKEMVKSFLKA 141
 
Name Accession Description Interval E-value
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 19-159 4.46e-82

N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane proteins localize to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).


Pssm-ID: 464353  Cd Length: 158  Bit Score: 238.80  E-value: 4.46e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582454   19 ARFSYVRMKYLFFSWLVVFVGSWIIYVQYSTYTELCRGKDCKKIICDKYKTGVIDGPACNSLCVTETLYFGKCLSTKPNN 98
Cdd:pfam14875   1 ARFSYRRVKYLFLVWLAVFVGSWVVYVQYSSYTELCRGHDCENIICDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356582454   99 QMYLGIWDNLPGVVKCQMEQALHLDFGTELEPRKEIVLFDKPTRGTTVQKFKEMVYSLFKD 159
Cdd:pfam14875  81 QVYTGLWGDLEVVIKCGIEEVPRSNYEPLSWPRSEYVLFDKPTRGTSVEEFKEMVKSFLKA 141
 
Name Accession Description Interval E-value
PIP49_N pfam14875
N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane ...
 19-159 4.46e-82

N-term cysteine-rich ER, FAM69; The FAM69 family of cysteine-rich type II transmembrane proteins localize to the endoplasmic reticulum (ER) in cultured cells, probably via N-terminal di-arginine motifs. These proteins carry at least 14 luminal cysteines which are conserved in all FAM69s. There are currently few indications of the involvement of FAM69 members in human diseases. It would appear that FAM69 proteins are predicted to be have a protein kinase structure and function. Analysis of three-dimensional structure models and conservation of the classic catalytic motifs of protein kinases in four of human FAM69 proteins suggests they might have retained catalytic phosphotransferase activity. An EF-hand Ca2+-binding domain, inserted within the structure of the kinase domain, suggests they function as Ca2+-dependent kinases (unpublished).


Pssm-ID: 464353  Cd Length: 158  Bit Score: 238.80  E-value: 4.46e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356582454   19 ARFSYVRMKYLFFSWLVVFVGSWIIYVQYSTYTELCRGKDCKKIICDKYKTGVIDGPACNSLCVTETLYFGKCLSTKPNN 98
Cdd:pfam14875   1 ARFSYRRVKYLFLVWLAVFVGSWVVYVQYSSYTELCRGHDCENIICDKYRKGIISGSACSSLCEKSTLYLGRCLSTKPNN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356582454   99 QMYLGIWDNLPGVVKCQMEQALHLDFGTELEPRKEIVLFDKPTRGTTVQKFKEMVYSLFKD 159
Cdd:pfam14875  81 QVYTGLWGDLEVVIKCGIEEVPRSNYEPLSWPRSEYVLFDKPTRGTSVEEFKEMVKSFLKA 141
 
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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