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Conserved domains on  [gi|15831478|ref|NP_310251|]
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transposase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

IS66 family transposase( domain architecture ID 15445763)

IS66 family transposase binds to the end of a transposon and catalyze the movement of the transposon to another part of the genome by a cut and paste mechanism or a replicative transposition mechanism

Gene Ontology:  GO:0004803|GO:0032196|GO:0003677|GO:0006313|GO:0046872|GO:0015074|GO:0006310
PubMed:  20615441|17165262|20079432|11774877|20215432|20885819|16381877

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
transpos_IS66 NF033517
IS66 family transposase; Members of this protein family are DDE transposases from the IS66 ...
 91-488 8.05e-170

IS66 family transposase; Members of this protein family are DDE transposases from the IS66 family insertion sequences, which typically consist of two accessary genes (TnpA and TnpB) and the third gene encoding the transposase.


:

Pssm-ID: 468053 [Multi-domain]  Cd Length: 388  Bit Score: 484.39  E-value: 8.05e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   91 RPLRQTRTRKPFPESLPRDEKRLLPAapCCPNCGGS-LSYLGEDTAEQLELMRSAFRVIRTVREKHACTQCDAIVQAPAP 169
Cdd:NF033517   1 QPGHKGKTRKPLPDHLPREEVVHEPE--SCPCCGGAlLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCGTVVQAPAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  170 SRPIERGIAGPGLLARVLTSKYAEHTPLYRQSEIYGRQ-GVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADD 248
Cdd:NF033517  79 ARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLfGIELSRGTLANWVGRAAELLEPLYDALKEELLAAPVLHADE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  249 TPVQVLLPGnkKTKTGRLWAYVRDDrnagsalaPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRnggITEA 328
Cdd:NF033517 159 TGVPVLEPG--RGKTGWLWVYASAP--------PAVLFDYAPSRGGEVPEALLEGFNGVLQSDGYAGYNKLAA---VTHA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  329 ACWAHARRKIHDVHVRIPSALTEEALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLKSLESWLREKMKTLSRHSELA 408
Cdd:NF033517 226 GCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERSRPLLDELKAWLEAGLAGVLPKSPLG 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  409 KAFAYALNQWPALTYYANDGWVEIDNNIAENALRAVSLGRKNFLFFGSDHGGERGALLYSLIGTCKLNDVDPESYLRHVL 488
Cdd:NF033517 306 KAIRYLLNRWDALLRFLDDGRVPIDNNAAERAIRPVVLGRKNSLFAGSDRGAEAAARIYSLIETAKLNGLNPYAYLRDVL 385
LZ_Tnp_IS66 pfam13007
Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region ...
 39-110 1.56e-11

Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region of transposase TnpC of insertion element IS66.


:

Pssm-ID: 463771 [Multi-domain]  Cd Length: 67  Bit Score: 59.59  E-value: 1.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831478    39 HLQAQLDKLRRMNFGSRSEKvsRRIAQMEADLNRLQKESDTLTGRvydpAVQRPLRQTRTRKPFPESLPRDE 110
Cdd:pfam13007   1 RLEEQLALLKRRLFGRSSEK--LDPEQLELALEELEAEEAEVEAE----ARASKKRKKPGRKPLPAHLPREE 66
DD_cGKI super family cl17044
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 12-48 4.05e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


The actual alignment was detected with superfamily member cd12083:

Pssm-ID: 473057 [Multi-domain]  Cd Length: 48  Bit Score: 35.24  E-value: 4.05e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLR 48
Cdd:cd12083   7 KTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQ 43
 
Name Accession Description Interval E-value
transpos_IS66 NF033517
IS66 family transposase; Members of this protein family are DDE transposases from the IS66 ...
 91-488 8.05e-170

IS66 family transposase; Members of this protein family are DDE transposases from the IS66 family insertion sequences, which typically consist of two accessary genes (TnpA and TnpB) and the third gene encoding the transposase.


Pssm-ID: 468053 [Multi-domain]  Cd Length: 388  Bit Score: 484.39  E-value: 8.05e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   91 RPLRQTRTRKPFPESLPRDEKRLLPAapCCPNCGGS-LSYLGEDTAEQLELMRSAFRVIRTVREKHACTQCDAIVQAPAP 169
Cdd:NF033517   1 QPGHKGKTRKPLPDHLPREEVVHEPE--SCPCCGGAlLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCGTVVQAPAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  170 SRPIERGIAGPGLLARVLTSKYAEHTPLYRQSEIYGRQ-GVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADD 248
Cdd:NF033517  79 ARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLfGIELSRGTLANWVGRAAELLEPLYDALKEELLAAPVLHADE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  249 TPVQVLLPGnkKTKTGRLWAYVRDDrnagsalaPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRnggITEA 328
Cdd:NF033517 159 TGVPVLEPG--RGKTGWLWVYASAP--------PAVLFDYAPSRGGEVPEALLEGFNGVLQSDGYAGYNKLAA---VTHA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  329 ACWAHARRKIHDVHVRIPSALTEEALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLKSLESWLREKMKTLSRHSELA 408
Cdd:NF033517 226 GCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERSRPLLDELKAWLEAGLAGVLPKSPLG 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  409 KAFAYALNQWPALTYYANDGWVEIDNNIAENALRAVSLGRKNFLFFGSDHGGERGALLYSLIGTCKLNDVDPESYLRHVL 488
Cdd:NF033517 306 KAIRYLLNRWDALLRFLDDGRVPIDNNAAERAIRPVVLGRKNSLFAGSDRGAEAAARIYSLIETAKLNGLNPYAYLRDVL 385
DDE_Tnp_IS66 pfam03050
Transposase IS66 family; Transposase proteins are necessary for efficient DNA transposition. ...
 175-462 1.62e-130

Transposase IS66 family; Transposase proteins are necessary for efficient DNA transposition. This family includes IS66 from Agrobacterium tumefaciens.


Pssm-ID: 427113 [Multi-domain]  Cd Length: 281  Bit Score: 380.44  E-value: 1.62e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   175 RGIAGPGLLARVLTSKYAEHTPLYRQSEIYGRQGVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADDTPVQVL 254
Cdd:pfam03050   1 KSLAGPSLLALILVLKYADHLPLYRQEDILARLGVELSRGTLANWVGRAAELLEPLVDALRAALLESPVIHADETPLRVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   255 LPGNKKTKTGRLWAYVRDDRNAgsalaPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRnGGITEAACWAHA 334
Cdd:pfam03050  81 KPGRGKGKKGWLWVYVTDDRPP-----PAVLFHYHPSRGGEHPQALLGGFRGVLQTDGYAGYNKLAR-GQVTHAGCWAHA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   335 RRKIHDVHVRIPSALTEeALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLKSLESWLREKMKTLSRHSELAKAFAYA 414
Cdd:pfam03050 155 RRKFFDAHKAGSPLAAQ-ALARIGKLYAIEREIRDLTPEERLALRQEYSRPLLDELEAWLEEQLRGVLPKSALGKAIRYL 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 15831478   415 LNQWPALTYYANDGWVEIDNNIAENALRAVSLGRKNFLFFGSDHGGER 462
Cdd:pfam03050 234 LNRWEALLRFLEDGRVPIDNNQAERAIRPVVLGRKNWLFAGSDEGAEA 281
COG3436 COG3436
Transposase [Mobilome: prophages, transposons];
34-454 6.42e-89

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442662 [Multi-domain]  Cd Length: 416  Bit Score: 278.84  E-value: 6.42e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  34 EREIDHLQAQLDKLRRMNFGSRSEKVSRRIAQMEADLNRLQ-KESDTLTGRVYDPAVQRPLRQTRTRKPFPESLPRDEKR 112
Cdd:COG3436   1 EEEEEELILLLLLLERLRLRRLRERESRLESQPELQLLELEeEAEEEEEAAEEAEAKTTKKKPKPGRKPMPEHLPREEVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 113 LLPAAPCCPNcggSLSYLGEDTAEQLELMRSAFRVIRTVREKHACTQCDA--IVQAPAPSRPIERGIAGPGLLARVLTSK 190
Cdd:COG3436  81 HEPTDMRKID---GLAAIGEEVSEELDLDPGALFVFRNRRDKYKCLYCDGtgLVYAPAPAKRLEKGLAGPGLLAHILVSK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 191 YAEHTPLYRQSEIYGRQGVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADDTPVQVLLPGNKKTKTGRLWAYV 270
Cdd:COG3436 158 FVDHLPLYRQEEIFARLGVELSRSTLLNWVGRAAELLEPLLEGLDERLLAAPVLHADETPVQVLDEGKGKTVTASYWWVY 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 271 RDDRNAGSALAPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRNGGITEAACWAHARRKIHDVHVRIPSALT 350
Cdd:COG3436 238 RDGRPSRGPVVYDAYRSRRGARAGLVLDGGLGGGLGDDYADGYAALLRLAELGCAAAARRRRKAAAAALKKLAKKAAAAA 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 351 EEALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLkslesWLREKMKTLSRHSELAKAFAYALNQWPALTYYANDGWV 430
Cdd:COG3436 318 AGLAAEEALLRIEELRKEERLRERRRERRPRRLLLLK-----ALLLLLLLLLPLLPPGKALLYAALARAARLLALLDRLL 392

                       410       420
                ....*....|....*....|....
gi 15831478 431 EIDNNIAENALRAVSLGRKNFLFF 454
Cdd:COG3436 393 DLLRNNDENNAERNALRRRNNLFA 416
LZ_Tnp_IS66 pfam13007
Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region ...
 39-110 1.56e-11

Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region of transposase TnpC of insertion element IS66.


Pssm-ID: 463771 [Multi-domain]  Cd Length: 67  Bit Score: 59.59  E-value: 1.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831478    39 HLQAQLDKLRRMNFGSRSEKvsRRIAQMEADLNRLQKESDTLTGRvydpAVQRPLRQTRTRKPFPESLPRDE 110
Cdd:pfam13007   1 RLEEQLALLKRRLFGRSSEK--LDPEQLELALEELEAEEAEVEAE----ARASKKRKKPGRKPLPAHLPREE 66
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 12-80 8.79e-05

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 41.40  E-value: 8.79e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRMNFGSRSEKVSRRIA--QMEADLNRLQKESDTL 80
Cdd:cd22887   2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIEnnLLEEKLRKLQEENDEL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-84 3.71e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.71e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831478     12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNRLQKESDTLTGRV 84
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----ELEELSRQISALRKDLARLEAEVEQLEERI 749
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-83 9.12e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831478   11 LLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgSRSEKVSRRIAQMEADLNRLQKESDTLTGR 83
Cdd:COG4913  292 LLEAELEELRAELARLEAELERLEARLDALREELDELEA----QIRGNGGDRLEQLEREIERLERELEERERR 360
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 12-48 4.05e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373 [Multi-domain]  Cd Length: 48  Bit Score: 35.24  E-value: 4.05e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLR 48
Cdd:cd12083   7 KTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQ 43
 
Name Accession Description Interval E-value
transpos_IS66 NF033517
IS66 family transposase; Members of this protein family are DDE transposases from the IS66 ...
 91-488 8.05e-170

IS66 family transposase; Members of this protein family are DDE transposases from the IS66 family insertion sequences, which typically consist of two accessary genes (TnpA and TnpB) and the third gene encoding the transposase.


Pssm-ID: 468053 [Multi-domain]  Cd Length: 388  Bit Score: 484.39  E-value: 8.05e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   91 RPLRQTRTRKPFPESLPRDEKRLLPAapCCPNCGGS-LSYLGEDTAEQLELMRSAFRVIRTVREKHACTQCDAIVQAPAP 169
Cdd:NF033517   1 QPGHKGKTRKPLPDHLPREEVVHEPE--SCPCCGGAlLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCGTVVQAPAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  170 SRPIERGIAGPGLLARVLTSKYAEHTPLYRQSEIYGRQ-GVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADD 248
Cdd:NF033517  79 ARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLfGIELSRGTLANWVGRAAELLEPLYDALKEELLAAPVLHADE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  249 TPVQVLLPGnkKTKTGRLWAYVRDDrnagsalaPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRnggITEA 328
Cdd:NF033517 159 TGVPVLEPG--RGKTGWLWVYASAP--------PAVLFDYAPSRGGEVPEALLEGFNGVLQSDGYAGYNKLAA---VTHA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  329 ACWAHARRKIHDVHVRIPSALTEEALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLKSLESWLREKMKTLSRHSELA 408
Cdd:NF033517 226 GCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERSRPLLDELKAWLEAGLAGVLPKSPLG 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  409 KAFAYALNQWPALTYYANDGWVEIDNNIAENALRAVSLGRKNFLFFGSDHGGERGALLYSLIGTCKLNDVDPESYLRHVL 488
Cdd:NF033517 306 KAIRYLLNRWDALLRFLDDGRVPIDNNAAERAIRPVVLGRKNSLFAGSDRGAEAAARIYSLIETAKLNGLNPYAYLRDVL 385
DDE_Tnp_IS66 pfam03050
Transposase IS66 family; Transposase proteins are necessary for efficient DNA transposition. ...
 175-462 1.62e-130

Transposase IS66 family; Transposase proteins are necessary for efficient DNA transposition. This family includes IS66 from Agrobacterium tumefaciens.


Pssm-ID: 427113 [Multi-domain]  Cd Length: 281  Bit Score: 380.44  E-value: 1.62e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   175 RGIAGPGLLARVLTSKYAEHTPLYRQSEIYGRQGVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADDTPVQVL 254
Cdd:pfam03050   1 KSLAGPSLLALILVLKYADHLPLYRQEDILARLGVELSRGTLANWVGRAAELLEPLVDALRAALLESPVIHADETPLRVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   255 LPGNKKTKTGRLWAYVRDDRNAgsalaPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRnGGITEAACWAHA 334
Cdd:pfam03050  81 KPGRGKGKKGWLWVYVTDDRPP-----PAVLFHYHPSRGGEHPQALLGGFRGVLQTDGYAGYNKLAR-GQVTHAGCWAHA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478   335 RRKIHDVHVRIPSALTEeALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLKSLESWLREKMKTLSRHSELAKAFAYA 414
Cdd:pfam03050 155 RRKFFDAHKAGSPLAAQ-ALARIGKLYAIEREIRDLTPEERLALRQEYSRPLLDELEAWLEEQLRGVLPKSALGKAIRYL 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 15831478   415 LNQWPALTYYANDGWVEIDNNIAENALRAVSLGRKNFLFFGSDHGGER 462
Cdd:pfam03050 234 LNRWEALLRFLEDGRVPIDNNQAERAIRPVVLGRKNWLFAGSDEGAEA 281
COG3436 COG3436
Transposase [Mobilome: prophages, transposons];
34-454 6.42e-89

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442662 [Multi-domain]  Cd Length: 416  Bit Score: 278.84  E-value: 6.42e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478  34 EREIDHLQAQLDKLRRMNFGSRSEKVSRRIAQMEADLNRLQ-KESDTLTGRVYDPAVQRPLRQTRTRKPFPESLPRDEKR 112
Cdd:COG3436   1 EEEEEELILLLLLLERLRLRRLRERESRLESQPELQLLELEeEAEEEEEAAEEAEAKTTKKKPKPGRKPMPEHLPREEVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 113 LLPAAPCCPNcggSLSYLGEDTAEQLELMRSAFRVIRTVREKHACTQCDA--IVQAPAPSRPIERGIAGPGLLARVLTSK 190
Cdd:COG3436  81 HEPTDMRKID---GLAAIGEEVSEELDLDPGALFVFRNRRDKYKCLYCDGtgLVYAPAPAKRLEKGLAGPGLLAHILVSK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 191 YAEHTPLYRQSEIYGRQGVELRRSLLSGWVDACCRLLSPLEEALHGYVMTDGKLHADDTPVQVLLPGNKKTKTGRLWAYV 270
Cdd:COG3436 158 FVDHLPLYRQEEIFARLGVELSRSTLLNWVGRAAELLEPLLEGLDERLLAAPVLHADETPVQVLDEGKGKTVTASYWWVY 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 271 RDDRNAGSALAPAVWFAYSPDRKGIHPQTHLACFSGVLQADAYAGFNELYRNGGITEAACWAHARRKIHDVHVRIPSALT 350
Cdd:COG3436 238 RDGRPSRGPVVYDAYRSRRGARAGLVLDGGLGGGLGDDYADGYAALLRLAELGCAAAARRRRKAAAAALKKLAKKAAAAA 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831478 351 EEALEQIGQLYAIEADIRGMPAEQRLAERQRKTKPLLkslesWLREKMKTLSRHSELAKAFAYALNQWPALTYYANDGWV 430
Cdd:COG3436 318 AGLAAEEALLRIEELRKEERLRERRRERRPRRLLLLK-----ALLLLLLLLLPLLPPGKALLYAALARAARLLALLDRLL 392

                       410       420
                ....*....|....*....|....
gi 15831478 431 EIDNNIAENALRAVSLGRKNFLFF 454
Cdd:COG3436 393 DLLRNNDENNAERNALRRRNNLFA 416
DDE_Tnp_IS66_C pfam13817
IS66 C-terminal element;
468-505 6.01e-14

IS66 C-terminal element;


Pssm-ID: 433500  Cd Length: 39  Bit Score: 65.88  E-value: 6.01e-14
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 15831478   468 SLIGTCKLNDVDPESYLRHVLGVIAD-WPVNRVSELLPW 505
Cdd:pfam13817   1 SLIETAKLNGLDPYAYLTDVLERLPDhHPAERLDELLPW 39
LZ_Tnp_IS66 pfam13007
Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region ...
 39-110 1.56e-11

Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region of transposase TnpC of insertion element IS66.


Pssm-ID: 463771 [Multi-domain]  Cd Length: 67  Bit Score: 59.59  E-value: 1.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15831478    39 HLQAQLDKLRRMNFGSRSEKvsRRIAQMEADLNRLQKESDTLTGRvydpAVQRPLRQTRTRKPFPESLPRDE 110
Cdd:pfam13007   1 RLEEQLALLKRRLFGRSSEK--LDPEQLELALEELEAEEAEVEAE----ARASKKRKKPGRKPLPAHLPREE 66
zf-IS66 pfam13005
zinc-finger binding domain of transposase IS66; This is a zinc-finger region of the N-terminus ...
 119-161 6.47e-11

zinc-finger binding domain of transposase IS66; This is a zinc-finger region of the N-terminus of the insertion element IS66 transposase.


Pssm-ID: 463770 [Multi-domain]  Cd Length: 46  Bit Score: 57.32  E-value: 6.47e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15831478   119 CCPNCGGSLSYLGED-TAEQLELMRSAFRVIRTVREKHACTQCD 161
Cdd:pfam13005   3 VCPCCGGLLHPIGEDeVREELDIPPAKFRVIEHIRPKYACRHCE 46
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 12-80 8.79e-05

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 41.40  E-value: 8.79e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRMNFGSRSEKVSRRIA--QMEADLNRLQKESDTL 80
Cdd:cd22887   2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIEnnLLEEKLRKLQEENDEL 72
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-84 3.71e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 3.71e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831478     12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNRLQKESDTLTGRV 84
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----ELEELSRQISALRKDLARLEAEVEQLEERI 749
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-83 9.12e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831478   11 LLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgSRSEKVSRRIAQMEADLNRLQKESDTLTGR 83
Cdd:COG4913  292 LLEAELEELRAELARLEAELERLEARLDALREELDELEA----QIRGNGGDRLEQLEREIERLERELEERERR 360
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
12-84 2.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 2.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNRLQKESDTLTGRV 84
Cdd:COG4372  50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNE-----QLQAAQAELAQAQEELESLQEEAEELQEEL 117
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 12-48 4.05e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373 [Multi-domain]  Cd Length: 48  Bit Score: 35.24  E-value: 4.05e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLR 48
Cdd:cd12083   7 KTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQ 43
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 14-77 4.92e-03

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 1; ROCK1 is a serine/threonine kinase and is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK1 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. It is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212029 [Multi-domain]  Cd Length: 66  Bit Score: 35.76  E-value: 4.92e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831478  14 QRLAEQEAlihalqEKLSNREREIDHLQAQLDKLRRMNfgSRSEKVSRRIAQMEADLNRLQKES 77
Cdd:cd11639  11 QRKAEQES------EKRRNVENEVSTLKDQLEDLKKIS--QNSQITNEKINQLQKQLEEANDLL 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-83 6.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 6.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15831478   5 SSDDIFLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNRLQKESDTLTGR 83
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAELAELEKE 91
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 8-84 6.83e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 6.83e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15831478   8 DIFLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNRLQKESDTLTGRV 84
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----ELAALEAELAELEKEIAELRAELEAQKEEL 106
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
12-68 6.84e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 6.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15831478  12 LKQRLAEQEALIHALQEKL-----------------SNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEA 68
Cdd:COG2433 432 LEAELEEKDERIERLERELsearseerreirkdreiSRLDREIERLERELEEERE-----RIEELKRKLERLKE 500
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 12-76 7.75e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 7.75e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15831478  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNRLQKE 76
Cdd:COG3883  28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQA-----EIDKLQAEIAEAEAEIEERREE 87
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 7-84 9.94e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 9.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831478   7 DDIFLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKlrrmnfgsrsekvsrRIAQMEADLNRLQKESDTLTGRV 84
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---------------ELAELEAELEELEAEREELAAKI 172
 
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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