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Conserved domains on  [gi|1845979180|ref|NP_001370082|]
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KA1 domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AMPKA_C_like super family cl17070
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and ...
 44-140 1.23e-44

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and similar domains; This family is composed of AMPKs, microtubule-associated protein/microtubule affinity regulating kinases (MARKs), yeast Kcc4p-like proteins, plant calcineurin B-Like (CBL)-interacting protein kinases (CIPKs), and similar proteins. They are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. AMPKs act as sensors for the energy status of the cell and are activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. MARKs phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Kcc4p and related proteins are septin-associated proteins that are involved in septin organization and in the yeast morphogenesis checkpoint coordinating the cell cycle with bud formation. CIPKs interact with the calcineurin B-like (CBL) calcium sensors to form a signaling network that decode specific calcium signals triggered by a variety of environmental stimuli including salinity, drought, cold, light, and mechanical perturbation, among others. All members of this family contain an N-terminal catalytic kinase domain and a C-terminal regulatory domain which is also called kinase associated domain 1 (KA1) in some cases. The C-terminal regulatory domain serves as a protein interaction domain in AMPKs and CIPKs. In MARKs and Kcc4p-like proteins, this domain binds phospholipids and may be involved in membrane localization.


The actual alignment was detected with superfamily member cd12196:

Pssm-ID: 473060  Cd Length: 98  Bit Score: 141.43  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  44 PRAVRFTWNLKKTSMLEPDEILKEIQKVLGSYGIDYEQQKRFLLRCSHVDPLTDASVKWEIEVCTLPRLYLNGVHFQRIS 123
Cdd:cd12196     2 PRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQRERFLLFCVHGDGRTDSLVQWEMEVCKLPRLSLNGVRFKRIS 81

                          90
                  ....*....|....*..
gi 1845979180 124 GSSSDFKNIITKISEEL 140
Cdd:cd12196    82 GTSIAFKNIASKIANEL 98
 
Name Accession Description Interval E-value
MARK1-3_C cd12196
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
 44-140 1.23e-44

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases 1-3; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK1/2, through their activation by death-associated protein kinase (DAPK), modulates polarized neurite outgrowth. MARK1, also called Par-1c, is also involved in axon-dendrite specification, and SNPs on the MARK1 gene is associated with autism spectrum disorders. MARK2, also called Par-1b, is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. MARK3, also called Par-1a, is implicated in gluconeogenesis and adiposity; mice deficient with MARK3 display reduced adiposity, resistance to hepatic steatosis, and defective gluconeogensis. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213381  Cd Length: 98  Bit Score: 141.43  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  44 PRAVRFTWNLKKTSMLEPDEILKEIQKVLGSYGIDYEQQKRFLLRCSHVDPLTDASVKWEIEVCTLPRLYLNGVHFQRIS 123
Cdd:cd12196     2 PRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQRERFLLFCVHGDGRTDSLVQWEMEVCKLPRLSLNGVRFKRIS 81

                          90
                  ....*....|....*..
gi 1845979180 124 GSSSDFKNIITKISEEL 140
Cdd:cd12196    82 GTSIAFKNIASKIANEL 98
KA1 pfam02149
Kinase associated domain 1;
100-140 1.92e-15

Kinase associated domain 1;


Pssm-ID: 460465  Cd Length: 44  Bit Score: 65.57  E-value: 1.92e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1845979180 100 VKWEIEVCTLPRLYLNGVHFQRISGSSSDFKNIITKISEEL 140
Cdd:pfam02149   2 VKFEIEVCKLPRLSLYGVDFKRLSGDTWQYKDLASKILSEL 42
 
Name Accession Description Interval E-value
MARK1-3_C cd12196
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
 44-140 1.23e-44

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases 1-3; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK1/2, through their activation by death-associated protein kinase (DAPK), modulates polarized neurite outgrowth. MARK1, also called Par-1c, is also involved in axon-dendrite specification, and SNPs on the MARK1 gene is associated with autism spectrum disorders. MARK2, also called Par-1b, is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. MARK3, also called Par-1a, is implicated in gluconeogenesis and adiposity; mice deficient with MARK3 display reduced adiposity, resistance to hepatic steatosis, and defective gluconeogensis. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213381  Cd Length: 98  Bit Score: 141.43  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  44 PRAVRFTWNLKKTSMLEPDEILKEIQKVLGSYGIDYEQQKRFLLRCSHVDPLTDASVKWEIEVCTLPRLYLNGVHFQRIS 123
Cdd:cd12196     2 PRSLRFTWSMKTTSSMDPNDMMREIRKVLDANNCDYEQRERFLLFCVHGDGRTDSLVQWEMEVCKLPRLSLNGVRFKRIS 81

                          90
                  ....*....|....*..
gi 1845979180 124 GSSSDFKNIITKISEEL 140
Cdd:cd12196    82 GTSIAFKNIASKIANEL 98
MARK_C_like cd12121
C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
 45-140 7.88e-42

C-terminal kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinases, and similar domains; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. In yeast, MARK/Par-1 homologs are called Kin1/2 kinases. Kin1 is a membrane-associated kinase that is involved in regulating cytokinesis and the cell surface. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213377  Cd Length: 96  Bit Score: 133.89  E-value: 7.88e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  45 RAVRFTWNLKKTSMLEPDEILKEIQKVLGSYGIDYEQQKRFLLRCSHVDPLTDASVKWEIEVCTLPRLYLNGVHFQRISG 124
Cdd:cd12121     1 RSLRGPFSVATTSTKSPEEIMNEIKRVLRSNGIDYEEVGGYLLECKHGDSSGGEFVIFEIEICKLPRLGLNGIRFKRISG 80

                          90
                  ....*....|....*.
gi 1845979180 125 SSSDFKNIITKISEEL 140
Cdd:cd12121    81 DSWQYKRLCKKILNEL 96
MARK2_C cd12201
C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule ...
 44-140 6.04e-40

C-terminal, kinase associated domain 1 (KA1), a phospholipid binding domain, of microtubule affinity-regulating kinase 2; Microtubule-associated protein/microtubule affinity regulating kinases (MARKs), also called partition-defective (Par-1) kinases, are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. They phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Mammals contain four proteins, MARK1-4, encoded by distinct genes belonging to this subfamily, with additional isoforms arising from alternative splicing. MARK2, also called Par-1b or ELKL motif kinase 1 (EMK-1), is implicated in many physiological processes including fertility, immune system homeostasis, learning and memory, growth, and metabolism. It also regulates axon formation and has been implicated in neurodegeneration. MARKs contain an N-terminal catalytic kinase domain, a ubiquitin-associated domain (UBA), and a C-terminal kinase associated domain (KA1). The KA1 domain binds anionic phospholipids and may be involved in membrane localization as well as in auto-inhibition of the kinase domain.


Pssm-ID: 213386  Cd Length: 99  Bit Score: 129.39  E-value: 6.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  44 PRAVRFTWNLKKTSMLEPDEILKEIQKVLGSYGIDYEQQKRFLLRCSHVDPLTDASVKWEIEVCTLPRLYLNGVHFQRIS 123
Cdd:cd12201     2 PRSLRFTWSMKTTSSMEPNEMMKEIRKVLDANNCQYELQEKYMLLCMHGTPGHDDFVQWEMEVCKLPRLSLNGVRFKRIS 81

                          90
                  ....*....|....*..
gi 1845979180 124 GSSSDFKNIITKISEEL 140
Cdd:cd12201    82 GTSIAFKNIASKIANEL 98
AMPKA_C_like cd12120
C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and ...
 48-140 9.69e-21

C-terminal regulatory domain of 5'-AMP-activated protein kinase (AMPK) alpha subunit and similar domains; This family is composed of AMPKs, microtubule-associated protein/microtubule affinity regulating kinases (MARKs), yeast Kcc4p-like proteins, plant calcineurin B-Like (CBL)-interacting protein kinases (CIPKs), and similar proteins. They are serine/threonine protein kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. AMPKs act as sensors for the energy status of the cell and are activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. MARKs phosphorylate the tau protein and related microtubule-associated proteins (MAPs) on tubulin binding sites to induce detachment from microtubules, and are involved in the regulation of cell shape and polarity, cell cycle control, transport, and the cytoskeleton. Kcc4p and related proteins are septin-associated proteins that are involved in septin organization and in the yeast morphogenesis checkpoint coordinating the cell cycle with bud formation. CIPKs interact with the calcineurin B-like (CBL) calcium sensors to form a signaling network that decode specific calcium signals triggered by a variety of environmental stimuli including salinity, drought, cold, light, and mechanical perturbation, among others. All members of this family contain an N-terminal catalytic kinase domain and a C-terminal regulatory domain which is also called kinase associated domain 1 (KA1) in some cases. The C-terminal regulatory domain serves as a protein interaction domain in AMPKs and CIPKs. In MARKs and Kcc4p-like proteins, this domain binds phospholipids and may be involved in membrane localization.


Pssm-ID: 213376  Cd Length: 95  Bit Score: 80.67  E-value: 9.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  48 RFTWNLKKTSMLEPDEILKEIQKVLGSYGIDYEQQKR-FLLRCSHVDP--LTDASVKWEIEVCTLPRlYLNGVHFQRISG 124
Cdd:cd12120     1 RKKWELEIHSRIDPSEIYEGIHKVLEGWGKNLVFRITnFIITGKLVNDhiLFLRSTLFEIEVYEVGP-GLFMVDFKKKTG 79

                          90
                  ....*....|....*.
gi 1845979180 125 SSSDFKNIITKISEEL 140
Cdd:cd12120    80 STKTFTKLATKIQIKL 95
KA1 pfam02149
Kinase associated domain 1;
100-140 1.92e-15

Kinase associated domain 1;


Pssm-ID: 460465  Cd Length: 44  Bit Score: 65.57  E-value: 1.92e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1845979180 100 VKWEIEVCTLPRLYLNGVHFQRISGSSSDFKNIITKISEEL 140
Cdd:pfam02149   2 VKFEIEVCKLPRLSLYGVDFKRLSGDTWQYKDLASKILSEL 42
MELK_C cd12198
C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, ...
 52-136 3.18e-12

C-terminal kinase associated domain 1 (KA1) of Maternal embryonic leucine zipper kinase; MELK, also called protein kinase 38 (PK38) or pEg3 kinase, is a cell cycle-regulated serine/threonine protein kinase (STK) that catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It is phosphorylated and maximally active during mitosis and is involved in regulating cell cycle progression, division, proliferation, tumor growth, and mRNA splicing. MELK shows a broad substrate specificity, including the zinc finger-like protein ZPR9, the transcription and splicing factor NIPP1, and the protein-tyrosine phosphatase Cdc25B, among others. MELK contains an N-terminal catalytic domain followed by a ubiquitin-associated (UBA) domain, a TP dipeptide-rich region, and a C-terminal KA1 domain. The KA1 domain of MELK, together with its TP dipeptide-rich region, functions as an autoinhibitory domain. The KA1 domain of the related microtubule affinity-regulating kinases (MARKs) has been shown to bind anionic phospholipids and may be involved in membrane localization.


Pssm-ID: 213383  Cd Length: 96  Bit Score: 58.78  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979180  52 NLKKTSMLEPDEILKEIQKVLGSYGIDYEqQKRFLLRCSHVDPLTDASVKWEIEVCTLPRLY-LNGVHFQRISGSSSDFK 130
Cdd:cd12198     8 NVSTTSSKDPEQVLNELKRVLAKKGIDCK-QKGYTLRCKTKDDFGKVKLTFELEVCRLPGLDeVVGIRRKRLKGDAWVYK 86


                  ....*.
gi 1845979180 131 NIITKI 136
Cdd:cd12198    87 KVCEDI 92
 
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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