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Conserved domains on  [gi|528510169|ref|XP_005159684|]
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tumor protein D52 isoform X1 [Danio rerio]

Protein Classification

D52 family tumor protein( domain architecture ID 10514819)

D52 family tumor protein similar to Homo sapiens tumor protein D52 (TPD52) that may play roles in calcium-mediated signal transduction and cell proliferation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPD52 pfam04201
Tumour protein D52 family; The hD52 gene was originally identified through its elevated ...
 69-199 2.29e-50

Tumour protein D52 family; The hD52 gene was originally identified through its elevated expression level in human breast carcinoma. Cloning of D52 homologs from other species has indicated that D52 may play roles in calcium-mediated signal transduction and cell proliferation. Two human homologs of hD52, hD53 and hD54, have also been identified, demonstrating the existence of a novel gene/protein family. These proteins have an amino terminal coiled-coil that allows members to form homo- and heterodimers with each other.


:

Pssm-ID: 461225  Cd Length: 99  Bit Score: 159.93  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510169   69 LTEQEQAELHSELQKVEEEIQTLSQVLAAKEKQVAEIKRKLGITPLNELKQNLSKGWHDVTTSTAYKKtsetlsqvgQKA 148
Cdd:pfam04201   1 LTEAEQEELKSELTKLEEEIVTLRQVLAAKEKHCAELKRKLGLTPLVELKQNLSKSWHDVQVSNAYKK---------QKT 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528510169  149 TTAFSSVGTAITRKLEDvrlqsfsnsfgirsiqhsasmpvMRNTPSFKSFE 199
Cdd:pfam04201  72 SAALSTVGSAICRKLGD-----------------------MRNSPTFKSFE 99
 
Name Accession Description Interval E-value
TPD52 pfam04201
Tumour protein D52 family; The hD52 gene was originally identified through its elevated ...
 69-199 2.29e-50

Tumour protein D52 family; The hD52 gene was originally identified through its elevated expression level in human breast carcinoma. Cloning of D52 homologs from other species has indicated that D52 may play roles in calcium-mediated signal transduction and cell proliferation. Two human homologs of hD52, hD53 and hD54, have also been identified, demonstrating the existence of a novel gene/protein family. These proteins have an amino terminal coiled-coil that allows members to form homo- and heterodimers with each other.


Pssm-ID: 461225  Cd Length: 99  Bit Score: 159.93  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510169   69 LTEQEQAELHSELQKVEEEIQTLSQVLAAKEKQVAEIKRKLGITPLNELKQNLSKGWHDVTTSTAYKKtsetlsqvgQKA 148
Cdd:pfam04201   1 LTEAEQEELKSELTKLEEEIVTLRQVLAAKEKHCAELKRKLGLTPLVELKQNLSKSWHDVQVSNAYKK---------QKT 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528510169  149 TTAFSSVGTAITRKLEDvrlqsfsnsfgirsiqhsasmpvMRNTPSFKSFE 199
Cdd:pfam04201  72 SAALSTVGSAICRKLGD-----------------------MRNSPTFKSFE 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 70-123 2.08e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 2.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 528510169    70 TEQEQAELHSELQKVEEEIQTLSQVLAAKEKQVAEIKRKLGITPLNELKQNLSK 123
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK 802
 
Name Accession Description Interval E-value
TPD52 pfam04201
Tumour protein D52 family; The hD52 gene was originally identified through its elevated ...
 69-199 2.29e-50

Tumour protein D52 family; The hD52 gene was originally identified through its elevated expression level in human breast carcinoma. Cloning of D52 homologs from other species has indicated that D52 may play roles in calcium-mediated signal transduction and cell proliferation. Two human homologs of hD52, hD53 and hD54, have also been identified, demonstrating the existence of a novel gene/protein family. These proteins have an amino terminal coiled-coil that allows members to form homo- and heterodimers with each other.


Pssm-ID: 461225  Cd Length: 99  Bit Score: 159.93  E-value: 2.29e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528510169   69 LTEQEQAELHSELQKVEEEIQTLSQVLAAKEKQVAEIKRKLGITPLNELKQNLSKGWHDVTTSTAYKKtsetlsqvgQKA 148
Cdd:pfam04201   1 LTEAEQEELKSELTKLEEEIVTLRQVLAAKEKHCAELKRKLGLTPLVELKQNLSKSWHDVQVSNAYKK---------QKT 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528510169  149 TTAFSSVGTAITRKLEDvrlqsfsnsfgirsiqhsasmpvMRNTPSFKSFE 199
Cdd:pfam04201  72 SAALSTVGSAICRKLGD-----------------------MRNSPTFKSFE 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 70-123 2.08e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 2.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 528510169    70 TEQEQAELHSELQKVEEEIQTLSQVLAAKEKQVAEIKRKLGITPLNELKQNLSK 123
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK 802
 
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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