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Conserved domains on  [gi|1483692262|ref|XP_026332431|]
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uncharacterized protein LOC113239591 [Hyposmocoma kahamanoa]

Protein Classification

transposase( domain architecture ID 1750089)

transposase binds to the end of a transposon and catalyzes the movement of the transposon to another part of the genome by a cut and paste mechanism or a replicative transposition mechanism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3335 super family cl41994
Transposase [Mobilome: prophages, transposons];
63-194 4.81e-09

Transposase [Mobilome: prophages, transposons];


The actual alignment was detected with superfamily member COG3335:

Pssm-ID: 442564 [Multi-domain]  Cd Length: 292  Bit Score: 54.49  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  63 ALLAFESKSTKEYHEEMDANKFKEWFKTLL-QNLPEQCTIIMDNASYHsvqidraptqanKKADLVAWLQrngveadmel 141
Cdd:COG3335   164 ALNLDGGLAVMVFDGSINGEVFIAFLEQLLlPYLKPGIVVILDNASFH------------KSKAVREWLE---------- 221
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1483692262 142 lkvellrlvrehrptklryeidelalEHGHKIIRTPPYHCQYNAIELIWAQIK 194
Cdd:COG3335   222 --------------------------EAGIELLFLPPYSPDLNPIERLWSKLK 248
 
Name Accession Description Interval E-value
COG3335 COG3335
Transposase [Mobilome: prophages, transposons];
63-194 4.81e-09

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442564 [Multi-domain]  Cd Length: 292  Bit Score: 54.49  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  63 ALLAFESKSTKEYHEEMDANKFKEWFKTLL-QNLPEQCTIIMDNASYHsvqidraptqanKKADLVAWLQrngveadmel 141
Cdd:COG3335   164 ALNLDGGLAVMVFDGSINGEVFIAFLEQLLlPYLKPGIVVILDNASFH------------KSKAVREWLE---------- 221
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1483692262 142 lkvellrlvrehrptklryeidelalEHGHKIIRTPPYHCQYNAIELIWAQIK 194
Cdd:COG3335   222 --------------------------EAGIELLFLPPYSPDLNPIERLWSKLK 248
transpos_IS630 NF033545
IS630 family transposase;
10-194 4.04e-07

IS630 family transposase;


Pssm-ID: 468076 [Multi-domain]  Cd Length: 298  Bit Score: 48.79  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  10 VVFIDETWLNSNHTVPQSWTDDTKASSSKVPMGKGGRLIICHAGSAGGGFVnnaLLAFESKSTKEYheemdankFKEWFK 89
Cdd:NF033545  146 VVFIDESGIQLLDTRGRGWAPKGQRRPRVHVYGRRGTLNLFGALDPLTGKV---FVLFTGRINSED--------FIEFLE 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  90 TLLQNLPEQ-CTIIMDNASYHsvqidraptqanKKADLVAWLQRNGveadmellKVELLRLvrehrptklryeidelale 168
Cdd:NF033545  215 ELLAAYPGKkIHLILDNASTH------------KSKKVREWLEEHG--------RIELHYL------------------- 255
                         170       180
                  ....*....|....*....|....*.
gi 1483692262 169 hghkiirtPPYHCQYNAIELIWAQIK 194
Cdd:NF033545  256 --------PPYSPWLNPIERVWAVLK 273
DDE_3 pfam13358
DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are ...
9-194 1.04e-06

DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are probably endonucleases of the DDE superfamily. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction.


Pssm-ID: 433142 [Multi-domain]  Cd Length: 146  Bit Score: 46.13  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262   9 NVVFIDETWLNSNHTVPQSW--TDDTKasSSKVPMGKGGRLIIChagsagGGFVNNALLAFEsksTKEyhEEMDANKFKE 86
Cdd:pfam13358   1 PLVFLDESGFNLGTVRRYGWapKGRRP--RGLKPYGRGGRVNVI------GALTYKGGLAFV---TFE--ETVNAEDFIA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  87 WFKTLLQNLPEQCT-IIMDNASYHsvqidraptqanKKADLVAWLQRNGveadmellkvellrlvrehrptklryeidel 165
Cdd:pfam13358  68 FLEQLLKPYLQPKIvLVLDNASYH------------KSKAVRELVEAEA------------------------------- 104
                         170       180
                  ....*....|....*....|....*....
gi 1483692262 166 aleHGHKIIRTPPYHCQYNAIELIWAQIK 194
Cdd:pfam13358 105 ---DGLELHYLPPYSPELNPIEILWSVLK 130
 
Name Accession Description Interval E-value
COG3335 COG3335
Transposase [Mobilome: prophages, transposons];
63-194 4.81e-09

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442564 [Multi-domain]  Cd Length: 292  Bit Score: 54.49  E-value: 4.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  63 ALLAFESKSTKEYHEEMDANKFKEWFKTLL-QNLPEQCTIIMDNASYHsvqidraptqanKKADLVAWLQrngveadmel 141
Cdd:COG3335   164 ALNLDGGLAVMVFDGSINGEVFIAFLEQLLlPYLKPGIVVILDNASFH------------KSKAVREWLE---------- 221
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1483692262 142 lkvellrlvrehrptklryeidelalEHGHKIIRTPPYHCQYNAIELIWAQIK 194
Cdd:COG3335   222 --------------------------EAGIELLFLPPYSPDLNPIERLWSKLK 248
transpos_IS630 NF033545
IS630 family transposase;
10-194 4.04e-07

IS630 family transposase;


Pssm-ID: 468076 [Multi-domain]  Cd Length: 298  Bit Score: 48.79  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  10 VVFIDETWLNSNHTVPQSWTDDTKASSSKVPMGKGGRLIICHAGSAGGGFVnnaLLAFESKSTKEYheemdankFKEWFK 89
Cdd:NF033545  146 VVFIDESGIQLLDTRGRGWAPKGQRRPRVHVYGRRGTLNLFGALDPLTGKV---FVLFTGRINSED--------FIEFLE 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  90 TLLQNLPEQ-CTIIMDNASYHsvqidraptqanKKADLVAWLQRNGveadmellKVELLRLvrehrptklryeidelale 168
Cdd:NF033545  215 ELLAAYPGKkIHLILDNASTH------------KSKKVREWLEEHG--------RIELHYL------------------- 255
                         170       180
                  ....*....|....*....|....*.
gi 1483692262 169 hghkiirtPPYHCQYNAIELIWAQIK 194
Cdd:NF033545  256 --------PPYSPWLNPIERVWAVLK 273
DDE_3 pfam13358
DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are ...
9-194 1.04e-06

DDE superfamily endonuclease; This family of proteins are related to pfam00665 and are probably endonucleases of the DDE superfamily. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction.


Pssm-ID: 433142 [Multi-domain]  Cd Length: 146  Bit Score: 46.13  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262   9 NVVFIDETWLNSNHTVPQSW--TDDTKasSSKVPMGKGGRLIIChagsagGGFVNNALLAFEsksTKEyhEEMDANKFKE 86
Cdd:pfam13358   1 PLVFLDESGFNLGTVRRYGWapKGRRP--RGLKPYGRGGRVNVI------GALTYKGGLAFV---TFE--ETVNAEDFIA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483692262  87 WFKTLLQNLPEQCT-IIMDNASYHsvqidraptqanKKADLVAWLQRNGveadmellkvellrlvrehrptklryeidel 165
Cdd:pfam13358  68 FLEQLLKPYLQPKIvLVLDNASYH------------KSKAVRELVEAEA------------------------------- 104
                         170       180
                  ....*....|....*....|....*....
gi 1483692262 166 aleHGHKIIRTPPYHCQYNAIELIWAQIK 194
Cdd:pfam13358 105 ---DGLELHYLPPYSPELNPIEILWSVLK 130
 
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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