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Conserved domains on  [gi|161077224|ref|NP_001097366|]
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TRPL translocation defect 14, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
68-295 5.07e-11

N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase superfamily is a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. The N-terminal domain contains the ATP-binding region.


The actual alignment was detected with superfamily member pfam13521:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 164  Bit Score: 61.13  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224   68 KIVLTGGPCGGKTTGQSRLctfFENLGWKVfrVPETATVLLSGGVKF--SDLTEKEDPptpttfvykdLPFAapehslid 145
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEAL---AARFGYPV--VPEAAREILEELGADggDALPWVEDL----------LAFA-------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224  146 ltascprclakaasrpngseaykfqenliRTMVQIENTYFELGNSSNrncLIICDRGVMDASAYISKDKWEKMMAGNNwn 225
Cdd:pfam13521  58 -----------------------------RGVLEAQLEDEAAAAAND---LLFFDRGPLDTLAYSRAYGGPCPPELEA-- 103
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224  226 pvEMRDNRYNQILHLvsaangAEDFYSTEDHAcRSEGVDLARELDYKSAAAWVGHPYFDVIDNSTNFETK 295
Cdd:pfam13521 104 --AARASRYDLVFLL------PPDPEIVQDGE-RREDPEERERFHERLREALRELGIPVIIVPRGSVEER 164
CYTH-like_Pase super family cl11964
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
323-481 2.41e-09

CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like superfamily enzymes hydrolyze triphosphate-containing substrates and require metal cations as cofactors. They have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB), and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions.


The actual alignment was detected with superfamily member cd07761:

Pssm-ID: 448368  Cd Length: 146  Bit Score: 55.70  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224 323 KYLVALLPPDSEFPPFQdfdvvhHYLQ---SAGPKVqaRLRKRGQKnhwsYIHTQRRPnvHGQARIEVKTQLTHRDYMNL 399
Cdd:cd07761    6 KFLVNELPAGLESYKKV------EIRQgylSINPEV--RIRSKGEK----YILTVKSG--GGLVREEIEIEIDKKEFEHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224 400 LAQRDDAhfTIYKKRRCF-LINNQYFQLDIYKepGHPrcKGLVLLET-YSSlTGDALKNCMPKFLNivKEVTGDPDYSMF 477
Cdd:cd07761   72 LEKTEGN--LIEKTRYLIpLEGGLLAELDVFE--GRL--TGLVYAEVeFPS-EEAARAFSPPAWFG--KEVTEDPRYKNK 142

                 ....
gi 161077224 478 NLSL 481
Cdd:cd07761  143 NLAL 146
 
Name Accession Description Interval E-value
AAA_28 pfam13521
AAA domain;
68-295 5.07e-11

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 61.13  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224   68 KIVLTGGPCGGKTTGQSRLctfFENLGWKVfrVPETATVLLSGGVKF--SDLTEKEDPptpttfvykdLPFAapehslid 145
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEAL---AARFGYPV--VPEAAREILEELGADggDALPWVEDL----------LAFA-------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224  146 ltascprclakaasrpngseaykfqenliRTMVQIENTYFELGNSSNrncLIICDRGVMDASAYISKDKWEKMMAGNNwn 225
Cdd:pfam13521  58 -----------------------------RGVLEAQLEDEAAAAAND---LLFFDRGPLDTLAYSRAYGGPCPPELEA-- 103
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224  226 pvEMRDNRYNQILHLvsaangAEDFYSTEDHAcRSEGVDLARELDYKSAAAWVGHPYFDVIDNSTNFETK 295
Cdd:pfam13521 104 --AARASRYDLVFLL------PPDPEIVQDGE-RREDPEERERFHERLREALRELGIPVIIVPRGSVEER 164
CYTH-like_CthTTM-like cd07761
Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like ...
323-481 2.41e-09

Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like superfamily; CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. Members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143626  Cd Length: 146  Bit Score: 55.70  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224 323 KYLVALLPPDSEFPPFQdfdvvhHYLQ---SAGPKVqaRLRKRGQKnhwsYIHTQRRPnvHGQARIEVKTQLTHRDYMNL 399
Cdd:cd07761    6 KFLVNELPAGLESYKKV------EIRQgylSINPEV--RIRSKGEK----YILTVKSG--GGLVREEIEIEIDKKEFEHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224 400 LAQRDDAhfTIYKKRRCF-LINNQYFQLDIYKepGHPrcKGLVLLET-YSSlTGDALKNCMPKFLNivKEVTGDPDYSMF 477
Cdd:cd07761   72 LEKTEGN--LIEKTRYLIpLEGGLLAELDVFE--GRL--TGLVYAEVeFPS-EEAARAFSPPAWFG--KEVTEDPRYKNK 142

                 ....
gi 161077224 478 NLSL 481
Cdd:cd07761  143 NLAL 146
 
Name Accession Description Interval E-value
AAA_28 pfam13521
AAA domain;
68-295 5.07e-11

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 61.13  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224   68 KIVLTGGPCGGKTTGQSRLctfFENLGWKVfrVPETATVLLSGGVKF--SDLTEKEDPptpttfvykdLPFAapehslid 145
Cdd:pfam13521   1 RIVITGGPSTGKTTLAEAL---AARFGYPV--VPEAAREILEELGADggDALPWVEDL----------LAFA-------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224  146 ltascprclakaasrpngseaykfqenliRTMVQIENTYFELGNSSNrncLIICDRGVMDASAYISKDKWEKMMAGNNwn 225
Cdd:pfam13521  58 -----------------------------RGVLEAQLEDEAAAAAND---LLFFDRGPLDTLAYSRAYGGPCPPELEA-- 103
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224  226 pvEMRDNRYNQILHLvsaangAEDFYSTEDHAcRSEGVDLARELDYKSAAAWVGHPYFDVIDNSTNFETK 295
Cdd:pfam13521 104 --AARASRYDLVFLL------PPDPEIVQDGE-RREDPEERERFHERLREALRELGIPVIIVPRGSVEER 164
CYTH-like_CthTTM-like cd07761
Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like ...
323-481 2.41e-09

Clostridium thermocellum (Cth)TTM and similar proteins, a subgroup of the CYTH-like superfamily; CthTTM is a metal dependent tripolyphosphatase, nucleoside triphosphatase, and nucleoside tetraphosphatase. It hydrolyzes the beta-gamma phosphoanhydride linkage of triphosphate-containing substrates including tripolyphosphate, nucleoside triphosphates and nucleoside tetraphosphates. These substrates are hydrolyzed, releasing Pi. Mg++ or Mn++ are required for the enzyme's activity. CthTTM appears to have no adenylate cyclase activity. This subgroup consists chiefly of bacterial sequences. Members of the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143626  Cd Length: 146  Bit Score: 55.70  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224 323 KYLVALLPPDSEFPPFQdfdvvhHYLQ---SAGPKVqaRLRKRGQKnhwsYIHTQRRPnvHGQARIEVKTQLTHRDYMNL 399
Cdd:cd07761    6 KFLVNELPAGLESYKKV------EIRQgylSINPEV--RIRSKGEK----YILTVKSG--GGLVREEIEIEIDKKEFEHL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161077224 400 LAQRDDAhfTIYKKRRCF-LINNQYFQLDIYKepGHPrcKGLVLLET-YSSlTGDALKNCMPKFLNivKEVTGDPDYSMF 477
Cdd:cd07761   72 LEKTEGN--LIEKTRYLIpLEGGLLAELDVFE--GRL--TGLVYAEVeFPS-EEAARAFSPPAWFG--KEVTEDPRYKNK 142

                 ....
gi 161077224 478 NLSL 481
Cdd:cd07761  143 NLAL 146
 
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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