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Conserved domains on  [gi|2257819982|ref|XP_001638507|]
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mediator of RNA polymerase II transcription subunit 30 [Nematostella vectensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Med30 super family cl12855
Mediator complex subunit 30; Med30 is a metazoan-specific subunit of Mediator, having no ...
 34-175 1.16e-56

Mediator complex subunit 30; Med30 is a metazoan-specific subunit of Mediator, having no homologs in yeasts.


The actual alignment was detected with superfamily member pfam11315:

Pssm-ID: 463259  Cd Length: 147  Bit Score: 174.87  E-value: 1.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257819982  34 NPITLTIQGQRTVQEIVDKAIELFRKLQNARLSTDTT--SRQSQAQTKDIRDQLNTLKGLLAKLRNVYNDTKRAVTIPAG 111
Cdd:pfam11315   1 NPASLCRIGQETVQDIVSRTQEIFQLLKNIQLPNGVTqgSNTSQDRKNKLQDQLRTLKVLFKKLRLIYEKCNENCQGLEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257819982 112 ENVENLIPL---ECSPRNEMDTSDGGGPVEQERAELQKKLKEKNDQLKEVIDKLRIAVWDINTMIML 175
Cdd:pfam11315  81 TPVESLIPYveeLDSKREERSKSEQYRVALQERKELLEKLKQKNQQLKEIMDQLRNLIWDINTMLAM 147
 
Name Accession Description Interval E-value
Med30 pfam11315
Mediator complex subunit 30; Med30 is a metazoan-specific subunit of Mediator, having no ...
 34-175 1.16e-56

Mediator complex subunit 30; Med30 is a metazoan-specific subunit of Mediator, having no homologs in yeasts.


Pssm-ID: 463259  Cd Length: 147  Bit Score: 174.87  E-value: 1.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257819982  34 NPITLTIQGQRTVQEIVDKAIELFRKLQNARLSTDTT--SRQSQAQTKDIRDQLNTLKGLLAKLRNVYNDTKRAVTIPAG 111
Cdd:pfam11315   1 NPASLCRIGQETVQDIVSRTQEIFQLLKNIQLPNGVTqgSNTSQDRKNKLQDQLRTLKVLFKKLRLIYEKCNENCQGLEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257819982 112 ENVENLIPL---ECSPRNEMDTSDGGGPVEQERAELQKKLKEKNDQLKEVIDKLRIAVWDINTMIML 175
Cdd:pfam11315  81 TPVESLIPYveeLDSKREERSKSEQYRVALQERKELLEKLKQKNQQLKEIMDQLRNLIWDINTMLAM 147
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 97-170 3.61e-03

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 37.27  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257819982  97 NVYNDTKRAVTIPAGENVEnlIPlecSPRNEMdtsdggGPVEQERAELQKKLKEKNDQLKEVIDKLRIAVWDIN 170
Cdd:cd02083   208 NVAAGKARGVVVGTGLNTE--IG---KIRDEM------AETEEEKTPLQQKLDEFGEQLSKVISVICVAVWAIN 270
 
Name Accession Description Interval E-value
Med30 pfam11315
Mediator complex subunit 30; Med30 is a metazoan-specific subunit of Mediator, having no ...
 34-175 1.16e-56

Mediator complex subunit 30; Med30 is a metazoan-specific subunit of Mediator, having no homologs in yeasts.


Pssm-ID: 463259  Cd Length: 147  Bit Score: 174.87  E-value: 1.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257819982  34 NPITLTIQGQRTVQEIVDKAIELFRKLQNARLSTDTT--SRQSQAQTKDIRDQLNTLKGLLAKLRNVYNDTKRAVTIPAG 111
Cdd:pfam11315   1 NPASLCRIGQETVQDIVSRTQEIFQLLKNIQLPNGVTqgSNTSQDRKNKLQDQLRTLKVLFKKLRLIYEKCNENCQGLEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257819982 112 ENVENLIPL---ECSPRNEMDTSDGGGPVEQERAELQKKLKEKNDQLKEVIDKLRIAVWDINTMIML 175
Cdd:pfam11315  81 TPVESLIPYveeLDSKREERSKSEQYRVALQERKELLEKLKQKNQQLKEIMDQLRNLIWDINTMLAM 147
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 97-170 3.61e-03

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 37.27  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257819982  97 NVYNDTKRAVTIPAGENVEnlIPlecSPRNEMdtsdggGPVEQERAELQKKLKEKNDQLKEVIDKLRIAVWDIN 170
Cdd:cd02083   208 NVAAGKARGVVVGTGLNTE--IG---KIRDEM------AETEEEKTPLQQKLDEFGEQLSKVISVICVAVWAIN 270
 
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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