Conserved Protein Domain Family
DD_AK7

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cd22967: DD_AK7 
dimerization/docking (D/D) domain found in adenylate kinase 7 and similar proteins
Adenylate kinase (AK7, EC2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 7, is a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK7 is involved in maintaining ciliary structure and function. This model corresponds to the C-terminal domain of AK7, which shows high sequence similarity to the dimerization/docking (D/D) domain of protein DPY-30/SDC1.
Statistics
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PSSM-Id: 438536
Aligned: 74 rows
Threshold Bit Score: 42.0893
Created: 27-Apr-2021
Updated: 17-Oct-2022
Structure
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Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Q96M32        679 PLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNN 719  human
SUZ43094     1472 PVETYLMKYVLPNLTPVMTDVVRMRPNDPVSTLADALFERR 1512 Leishmania infantum
GBP44396      412 PLRDYLVKYIFPALTPALLQVAETRPEDPVDYLKGIRGTGP 452  Eumeta japonica
VVC36926       40 SCEEYLMKYVTSTLTKLIVQVAKVRPRNPVDFLAYMALKEN 80   Cinara cedri
GAU93539      738 SPLAYLVKYVFPSVQEALQQTARVKPNNPVDYFAELLISST 778  Ramazzottius varieornatus
XP_002508377  254 SLRAYLASEVMPVVTDAMLQMLRIRPEDPALALSDYLLRYD 294  Micromonas commoda
EPY16950      348 PMETYLMEYVLPSVTPLLADVTRLRPADPVTTMADLLFSHQ 388  Angomonas deanei
CCW70492       41 PMETYLVTYVLPSLTPALNEVVKLRPDDPITVLADILYDYK 81   Phytomonas sp. isolate Hart1
VDO08136      162 TAKYYLSKNVLPTLLSCLTEVCKRKPLDPIMFLADSLLRNN 202  Rodentolepis nana
XP_013902045  540 PLRRYLLQMVMPTVTAGLTQCVVDQPPDPVQVLARRLLEAA 580  Monoraphidium neglectum
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