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Conserved domains on  [gi|442624875|ref|NP_001259799|]
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uncharacterized protein Dmel_CG31974, isoform C [Drosophila melanogaster]

Protein Classification

protein kinase family protein( domain architecture ID 10503049)

protein kinase family protein, similar to Bombyx mori EcKinase that catalyzes the phosphorylation of the steroid hormone and together with ecdysteroid-phosphate phosphatase, plays an important role in ecdysteroid economy of the ovary-egg system

CATH:  1.10.510.10
EC:  2.7.-.-
Gene Ontology:  GO:0016310|GO:0005524|GO:0016301
PubMed:  16244704
SCOP:  4003661

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
35-334 5.26e-89

Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes.


:

Pssm-ID: 397213 [Multi-domain]  Cd Length: 293  Bit Score: 271.45  E-value: 5.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   35 PGDNYGSIMLSVQAKIRSADGGIRDLPLIAKLPPlTNDLYWQIFQPERTCITENAVYQYLSPELDKLQLESGilpaQIFD 114
Cdd:pfam02958   1 KGDNYASVMLRVTIEYEKGDGSKRTKSLIVKTMP-DNEERREMFSSLNLFTREINMYEKVLPELEALYREAG----DPFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  115 GFPRYYGSRvsldnratKVDRDAVLVQENVTTRGYRPGNRHRPYNLAETVLILHYLAQYHALPIALRLKKPQVYEEYVRP 194
Cdd:pfam02958  76 LAPKCYYAD--------LEPEDQVIILEDLSLKGYKNADRLKGLDLEHTKLVLEKLAKFHAASAALKELQPEVFKQLKKG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  195 YFKKFDMNSNIDQAETEIMNKEILKDIKLVTSD----ERDVNRVKELLD-IFQAFQASNDVDDGPFTTLVHGDLWINNMM 269
Cdd:pfam02958 148 LFEEDYVNGAIKEFFEPLMETGLDAAAEALREQlpeyEKYAEKLEKLKDnYFDRLLRLVEPTPGEFNVLNHGDLWVNNIM 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442624875  270 LKYGEEGTPLKVKIVDFQIAQYGSLVHDIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRSVN 334
Cdd:pfam02958 228 FKYDDEGEPEDVILVDFQLSRYGSPAIDLNYFLYTSTELELRLEHFDELLRYYHSSLVETLKKLG 292
 
Name Accession Description Interval E-value
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
35-334 5.26e-89

Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes.


Pssm-ID: 397213 [Multi-domain]  Cd Length: 293  Bit Score: 271.45  E-value: 5.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   35 PGDNYGSIMLSVQAKIRSADGGIRDLPLIAKLPPlTNDLYWQIFQPERTCITENAVYQYLSPELDKLQLESGilpaQIFD 114
Cdd:pfam02958   1 KGDNYASVMLRVTIEYEKGDGSKRTKSLIVKTMP-DNEERREMFSSLNLFTREINMYEKVLPELEALYREAG----DPFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  115 GFPRYYGSRvsldnratKVDRDAVLVQENVTTRGYRPGNRHRPYNLAETVLILHYLAQYHALPIALRLKKPQVYEEYVRP 194
Cdd:pfam02958  76 LAPKCYYAD--------LEPEDQVIILEDLSLKGYKNADRLKGLDLEHTKLVLEKLAKFHAASAALKELQPEVFKQLKKG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  195 YFKKFDMNSNIDQAETEIMNKEILKDIKLVTSD----ERDVNRVKELLD-IFQAFQASNDVDDGPFTTLVHGDLWINNMM 269
Cdd:pfam02958 148 LFEEDYVNGAIKEFFEPLMETGLDAAAEALREQlpeyEKYAEKLEKLKDnYFDRLLRLVEPTPGEFNVLNHGDLWVNNIM 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442624875  270 LKYGEEGTPLKVKIVDFQIAQYGSLVHDIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRSVN 334
Cdd:pfam02958 228 FKYDDEGEPEDVILVDFQLSRYGSPAIDLNYFLYTSTELELRLEHFDELLRYYHSSLVETLKKLG 292
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
139-332 5.57e-48

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 162.11  E-value: 5.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   139 LVQENVTTRGYRPGNRHRPYNLAETVLILHYLAQYHALPIALR-LKKPQVYEEYVRPYFKKFDMNSNIDQAETEIMNKEI 217
Cdd:smart00587   1 IIFEDLSPKGYVNADRLKGLDLEHTSLVLKKLAKLHAASAVLIeEEKGSYLEEFDEGLFERFKRMFSEEFIGGLENFLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   218 LKDIKLVTSDERDVNRVKELLDIFQAFQA-SNDVDDGPFTTLVHGDLWINNMMLKYGEEGTPLKVKIVDFQIAQYGSLVH 296
Cdd:smart00587  81 LLSQPELLKVEEYIEKLDKLLDNLEDLKKeDKEPDEGEFNVLNHGDLWANNIMFKYDDEGKPEDVALIDFQLSHYGSPAE 160
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 442624875   297 DIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRS 332
Cdd:smart00587 161 DLHYFLLTSLSVEIRREHFDELLKFYYETLVETLKK 196
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
127-304 6.87e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 39.98  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875 127 DNRATKVDRDAVLVqenVTTRGYRPGNRHRPYnlaetVLILHYLAQYHALPIalrlkkPQVYeeyvrpYFKKFDMNSNId 206
Cdd:cd05120   11 DNKVYLLGDPREYV---LKIGPPRLKKDLEKE-----AAMLQLLAGKLSLPV------PKVY------GFGESDGWEYL- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875 207 qaeteIMNK---EILKDIKLVTSDERDVNRVKELLDIFQAFQasndvdDGPFTTLVHGDLWINNMMLKYGEEGTplkvKI 283
Cdd:cd05120   70 -----LMERiegETLSEVWPRLSEEEKEKIADQLAEILAALH------RIDSSVLTHGDLHPGNILVKPDGKLS----GI 134
                        170       180
                 ....*....|....*....|.
gi 442624875 284 VDFQIAQYGSLVHDIIFVLFS 304
Cdd:cd05120  135 IDWEFAGYGPPAFDYAAALRD 155
 
Name Accession Description Interval E-value
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
35-334 5.26e-89

Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes.


Pssm-ID: 397213 [Multi-domain]  Cd Length: 293  Bit Score: 271.45  E-value: 5.26e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   35 PGDNYGSIMLSVQAKIRSADGGIRDLPLIAKLPPlTNDLYWQIFQPERTCITENAVYQYLSPELDKLQLESGilpaQIFD 114
Cdd:pfam02958   1 KGDNYASVMLRVTIEYEKGDGSKRTKSLIVKTMP-DNEERREMFSSLNLFTREINMYEKVLPELEALYREAG----DPFK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  115 GFPRYYGSRvsldnratKVDRDAVLVQENVTTRGYRPGNRHRPYNLAETVLILHYLAQYHALPIALRLKKPQVYEEYVRP 194
Cdd:pfam02958  76 LAPKCYYAD--------LEPEDQVIILEDLSLKGYKNADRLKGLDLEHTKLVLEKLAKFHAASAALKELQPEVFKQLKKG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  195 YFKKFDMNSNIDQAETEIMNKEILKDIKLVTSD----ERDVNRVKELLD-IFQAFQASNDVDDGPFTTLVHGDLWINNMM 269
Cdd:pfam02958 148 LFEEDYVNGAIKEFFEPLMETGLDAAAEALREQlpeyEKYAEKLEKLKDnYFDRLLRLVEPTPGEFNVLNHGDLWVNNIM 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442624875  270 LKYGEEGTPLKVKIVDFQIAQYGSLVHDIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRSVN 334
Cdd:pfam02958 228 FKYDDEGEPEDVILVDFQLSRYGSPAIDLNYFLYTSTELELRLEHFDELLRYYHSSLVETLKKLG 292
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
139-332 5.57e-48

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 162.11  E-value: 5.57e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   139 LVQENVTTRGYRPGNRHRPYNLAETVLILHYLAQYHALPIALR-LKKPQVYEEYVRPYFKKFDMNSNIDQAETEIMNKEI 217
Cdd:smart00587   1 IIFEDLSPKGYVNADRLKGLDLEHTSLVLKKLAKLHAASAVLIeEEKGSYLEEFDEGLFERFKRMFSEEFIGGLENFLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875   218 LKDIKLVTSDERDVNRVKELLDIFQAFQA-SNDVDDGPFTTLVHGDLWINNMMLKYGEEGTPLKVKIVDFQIAQYGSLVH 296
Cdd:smart00587  81 LLSQPELLKVEEYIEKLDKLLDNLEDLKKeDKEPDEGEFNVLNHGDLWANNIMFKYDDEGKPEDVALIDFQLSHYGSPAE 160
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 442624875   297 DIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRS 332
Cdd:smart00587 161 DLHYFLLTSLSVEIRREHFDELLKFYYETLVETLKK 196
DUF1679 pfam07914
Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number ...
205-380 1.91e-06

Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number of C. elegans proteins, in one case as a repeat. In many of the family members, this region is associated with the CHK region described by SMART as being found in ZnF_C4 and HLH domain-containing kinases. In fact, one member of this family is annotated as being a member of the nuclear hormone receptor family, and contains regions typical of such proteins (Interpro:IPR000536, Interpro:IPR008946, and Interpro:IPR001628).


Pssm-ID: 369592  Cd Length: 413  Bit Score: 49.58  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  205 IDQAETEIMNKEILKDIKLVTSD---ERDVNRVKELLDIFQAFQAS-NDVDD--------GPFTTLVHGDLWINNMMLKY 272
Cdd:pfam07914 205 LEEMFETFMSEEGLKGIFEQLRNifgAAYPEKVEELVDIFEHYGPEiLIFKKytnlnkvlGIKPVLVHGDLWQSNILWTL 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  273 GEEGTPLKVKIVDFQIAQYGSLVHDIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRSVNVDtsnYTyelfLEEVQQT 352
Cdd:pfam07914 285 ENDGKLKLKAIIDYQTVHMGNPAEDLVRLLLSCLSGADRRAHWEELLEQYYETFTKALGDNEEP---YT----LEQLKDS 357
                         170       180       190
                  ....*....|....*....|....*....|.
gi 442624875  353 AHVQLP-HAIFMMKVI--LADNSTIPKDYKD 380
Cdd:pfam07914 358 YNLYFPmMSLLLLPLIgpFLDMKSMSEEEKE 388
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
149-304 2.64e-06

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 48.27  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875  149 YRPGNRHRPYNLAETVLilHYLAQYHALPIALRlkkPQVYEEYVRPYFKKFDMNSNIDqaeteimnkeilkdikLVTSDE 228
Cdd:pfam01636  84 ARPLLPEERGALLEALG--RALARLHAVDPAAL---PLAGRLARLLELLRQLEAALAR----------------LLAAEL 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442624875  229 RDvnRVKELLDIFQAFQASNDVDDGPfTTLVHGDLWINNMMLKYGEEGTplkvKIVDFQIAQYGSLVHDIIFVLFS 304
Cdd:pfam01636 143 LD--RLEELEERLLAALLALLPAELP-PVLVHGDLHPGNLLVDPGGRVS----GVIDFEDAGLGDPAYDLAILLNS 211
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
127-304 6.87e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 39.98  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875 127 DNRATKVDRDAVLVqenVTTRGYRPGNRHRPYnlaetVLILHYLAQYHALPIalrlkkPQVYeeyvrpYFKKFDMNSNId 206
Cdd:cd05120   11 DNKVYLLGDPREYV---LKIGPPRLKKDLEKE-----AAMLQLLAGKLSLPV------PKVY------GFGESDGWEYL- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624875 207 qaeteIMNK---EILKDIKLVTSDERDVNRVKELLDIFQAFQasndvdDGPFTTLVHGDLWINNMMLKYGEEGTplkvKI 283
Cdd:cd05120   70 -----LMERiegETLSEVWPRLSEEEKEKIADQLAEILAALH------RIDSSVLTHGDLHPGNILVKPDGKLS----GI 134
                        170       180
                 ....*....|....*....|.
gi 442624875 284 VDFQIAQYGSLVHDIIFVLFS 304
Cdd:cd05120  135 IDWEFAGYGPPAFDYAAALRD 155
 
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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