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Conserved domains on  [gi|2241884808|emb|CAH3960249|]
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hypothetical protein AI2666V1_5182 (plasmid) [Citrobacter freundii]

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 1.04e-167

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: 479.00  E-value: 1.04e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808  91 RPLRQTRTRKPFPESLPRDEKRLLPtePCCPECGGS-LSYLGEDAAEQLELMRSAFRVIRTVREKHACRRCDRIVQAPAP 169
Cdd:NF033517    1 QPGHKGKTRKPLPDHLPREEVVHEP--ESCPCCGGAlLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCGTVVQAPAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 170 SRPIERGIAGPGLLARVLTSKYAEHTPLYRQSEIYARQ-GVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADD 248
Cdd:NF033517   79 ARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLfGIELSRGTLANWVGRAAELLEPLYDALKEELLAAPVLHADE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 249 TPVPVLLPGnkKTKTGRLWTYVRDDrnagsalaPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRdghIKEA 328
Cdd:NF033517  159 TGVPVLEPG--RGKTGWLWVYASAP--------PAVLFDYAPSRGGEVPEALLEGFNGVLQSDGYAGYNKLAA---VTHA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 329 ACWAHARRKIHDVHVRTPSVLTEEALKRIGELYAIESEIRGKRAEERQAVRHQKVLPLLASLEGWLREKQKTLSRHSELA 408
Cdd:NF033517  226 GCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERSRPLLDELKAWLEAGLAGVLPKSPLG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 409 KAFGYALNQWPALIRYAEDGWVEVDNNIAENALRRVSLGRKNWLFFGSDHGGERGASLYSLIGTCKLNGVDPERYLHYVL 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 1.36e-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: 59.97  E-value: 1.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241884808  39 HLQAQLDKLRRMNFGSRSEKvsRRIAQMEADLNLLQQESDTLTGRvddpAVQRPLRQTRTRKPFPESLPRDE 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 ...
 6-48 4.55e-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: 4.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2241884808   6 SDDILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLR 48
Cdd:cd12083     1 SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQ 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 1.04e-167

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: 479.00  E-value: 1.04e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808  91 RPLRQTRTRKPFPESLPRDEKRLLPtePCCPECGGS-LSYLGEDAAEQLELMRSAFRVIRTVREKHACRRCDRIVQAPAP 169
Cdd:NF033517    1 QPGHKGKTRKPLPDHLPREEVVHEP--ESCPCCGGAlLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCGTVVQAPAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 170 SRPIERGIAGPGLLARVLTSKYAEHTPLYRQSEIYARQ-GVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADD 248
Cdd:NF033517   79 ARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLfGIELSRGTLANWVGRAAELLEPLYDALKEELLAAPVLHADE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 249 TPVPVLLPGnkKTKTGRLWTYVRDDrnagsalaPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRdghIKEA 328
Cdd:NF033517  159 TGVPVLEPG--RGKTGWLWVYASAP--------PAVLFDYAPSRGGEVPEALLEGFNGVLQSDGYAGYNKLAA---VTHA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 329 ACWAHARRKIHDVHVRTPSVLTEEALKRIGELYAIESEIRGKRAEERQAVRHQKVLPLLASLEGWLREKQKTLSRHSELA 408
Cdd:NF033517  226 GCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERSRPLLDELKAWLEAGLAGVLPKSPLG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 409 KAFGYALNQWPALIRYAEDGWVEVDNNIAENALRRVSLGRKNWLFFGSDHGGERGASLYSLIGTCKLNGVDPERYLHYVL 488
Cdd:NF033517  306 KAIRYLLNRWDALLRFLDDGRVPIDNNAAERAIRPVVLGRKNSLFAGSDRGAEAAARIYSLIETAKLNGLNPYAYLRDVL 385
DDE_Tnp_IS66 pfam03050
Transposase IS66 family; Transposase proteins are necessary for efficient DNA transposition. ...
 175-462 1.49e-125

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: 367.73  E-value: 1.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 175 RGIAGPGLLARVLTSKYAEHTPLYRQSEIYARQGVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADDTPVPVL 254
Cdd:pfam03050   1 KSLAGPSLLALILVLKYADHLPLYRQEDILARLGVELSRGTLANWVGRAAELLEPLVDALRAALLESPVIHADETPLRVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 255 LPGNKKTKTGRLWTYVRDDRNAgsalaPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRdGHIKEAACWAHA 334
Cdd:pfam03050  81 KPGRGKGKKGWLWVYVTDDRPP-----PAVLFHYHPSRGGEHPQALLGGFRGVLQTDGYAGYNKLAR-GQVTHAGCWAHA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 335 RRKIHDVHVRTPSVLTEeALKRIGELYAIESEIRGKRAEERQAVRHQKVLPLLASLEGWLREKQKTLSRHSELAKAFGYA 414
Cdd:pfam03050 155 RRKFFDAHKAGSPLAAQ-ALARIGKLYAIEREIRDLTPEERLALRQEYSRPLLDELEAWLEEQLRGVLPKSALGKAIRYL 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2241884808 415 LNQWPALIRYAEDGWVEVDNNIAENALRRVSLGRKNWLFFGSDHGGER 462
Cdd:pfam03050 234 LNRWEALLRFLEDGRVPIDNNQAERAIRPVVLGRKNWLFAGSDEGAEA 281
COG3436 COG3436
Transposase [Mobilome: prophages, transposons];
34-454 9.41e-91

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442662 [Multi-domain]  Cd Length: 416  Bit Score: 283.46  E-value: 9.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808  34 EREIDHLQAQLDKLRRMNFGSRSEKVSRRIAQMEADLNLLQQESDTLTGRVDDPAVQRPLRQTR-TRKPFPESLPRDEKR 112
Cdd:COG3436     1 EEEEEELILLLLLLERLRLRRLRERESRLESQPELQLLELEEEAEEEEEAAEEAEAKTTKKKPKpGRKPMPEHLPREEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 113 LLPTEPCCPEcggSLSYLGEDAAEQLELMRSAFRVIRTVREKHACRRCDR--IVQAPAPSRPIERGIAGPGLLARVLTSK 190
Cdd:COG3436    81 HEPTDMRKID---GLAAIGEEVSEELDLDPGALFVFRNRRDKYKCLYCDGtgLVYAPAPAKRLEKGLAGPGLLAHILVSK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 191 YAEHTPLYRQSEIYARQGVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADDTPVPVLLPGNKKTKTGRLWTYV 270
Cdd:COG3436   158 FVDHLPLYRQEEIFARLGVELSRSTLLNWVGRAAELLEPLLEGLDERLLAAPVLHADETPVQVLDEGKGKTVTASYWWVY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 271 RDDRNAGSALAPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRDGHIKEAACWAHARRKIHDVHVRTPSVLT 350
Cdd:COG3436   238 RDGRPSRGPVVYDAYRSRRGARAGLVLDGGLGGGLGDDYADGYAALLRLAELGCAAAARRRRKAAAAALKKLAKKAAAAA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 351 EEALKRIGELYAIESEIRGKRAEERQAVRhqkvlPLLASLEGWLREKQKTLSRHSELAKAFGYALNQWPALIRYAEDGWV 430
Cdd:COG3436   318 AGLAAEEALLRIEELRKEERLRERRRERR-----PRRLLLLKALLLLLLLLLPLLPPGKALLYAALARAARLLALLDRLL 392

                         410       420
                  ....*....|....*....|....
gi 2241884808 431 EVDNNIAENALRRVSLGRKNWLFF 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 1.36e-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: 59.97  E-value: 1.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241884808  39 HLQAQLDKLRRMNFGSRSEKvsRRIAQMEADLNLLQQESDTLTGRvddpAVQRPLRQTRTRKPFPESLPRDE 110
Cdd:pfam13007   1 RLEEQLALLKRRLFGRSSEK--LDPEQLELALEELEAEEAEVEAE----ARASKKRKKPGRKPLPAHLPREE 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-86 7.10e-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: 42.35  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2241884808   12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNLLQQESDTLTGRVDD 86
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----ELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 14-77 1.71e-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: 36.91  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241884808  14 QRLAEQEAlihalqEKLSNREREIDHLQAQLDKLRRMNfgSRSEKVSRRIAQMEADLNLLQQES 77
Cdd:cd11639    11 QRKAEQES------EKRRNVENEVSTLKDQLEDLKKIS--QNSQITNEKINQLQKQLEEANDLL 66
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
9-86 2.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808    9 ILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRM---NFGSRSEKVSRRIAQMEADLNLLQQESDTLTGRVD 85
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgNGGDRLEQLEREIERLERELEERERRRARLEALLA 369


                   .
gi 2241884808   86 D 86
Cdd:COG4913    370 A 370
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 6-48 4.55e-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: 4.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2241884808   6 SDDILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLR 48
Cdd:cd12083     1 SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQ 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 1.04e-167

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: 479.00  E-value: 1.04e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808  91 RPLRQTRTRKPFPESLPRDEKRLLPtePCCPECGGS-LSYLGEDAAEQLELMRSAFRVIRTVREKHACRRCDRIVQAPAP 169
Cdd:NF033517    1 QPGHKGKTRKPLPDHLPREEVVHEP--ESCPCCGGAlLHRIGEEVSEQLEIIPAKFEVTEYVRPKYACRHCGTVVQAPAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 170 SRPIERGIAGPGLLARVLTSKYAEHTPLYRQSEIYARQ-GVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADD 248
Cdd:NF033517   79 ARVIPKGQAGPRLLAHVAVLKYADHLPLYRQQQILARLfGIELSRGTLANWVGRAAELLEPLYDALKEELLAAPVLHADE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 249 TPVPVLLPGnkKTKTGRLWTYVRDDrnagsalaPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRdghIKEA 328
Cdd:NF033517  159 TGVPVLEPG--RGKTGWLWVYASAP--------PAVLFDYAPSRGGEVPEALLEGFNGVLQSDGYAGYNKLAA---VTHA 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 329 ACWAHARRKIHDVHVRTPSVLTEEALKRIGELYAIESEIRGKRAEERQAVRHQKVLPLLASLEGWLREKQKTLSRHSELA 408
Cdd:NF033517  226 GCWAHLRRKFQEAAERKGKSIAEEALKRIGELYAIERRIRGLSPEERRALRQERSRPLLDELKAWLEAGLAGVLPKSPLG 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 409 KAFGYALNQWPALIRYAEDGWVEVDNNIAENALRRVSLGRKNWLFFGSDHGGERGASLYSLIGTCKLNGVDPERYLHYVL 488
Cdd:NF033517  306 KAIRYLLNRWDALLRFLDDGRVPIDNNAAERAIRPVVLGRKNSLFAGSDRGAEAAARIYSLIETAKLNGLNPYAYLRDVL 385
DDE_Tnp_IS66 pfam03050
Transposase IS66 family; Transposase proteins are necessary for efficient DNA transposition. ...
 175-462 1.49e-125

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: 367.73  E-value: 1.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 175 RGIAGPGLLARVLTSKYAEHTPLYRQSEIYARQGVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADDTPVPVL 254
Cdd:pfam03050   1 KSLAGPSLLALILVLKYADHLPLYRQEDILARLGVELSRGTLANWVGRAAELLEPLVDALRAALLESPVIHADETPLRVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 255 LPGNKKTKTGRLWTYVRDDRNAgsalaPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRdGHIKEAACWAHA 334
Cdd:pfam03050  81 KPGRGKGKKGWLWVYVTDDRPP-----PAVLFHYHPSRGGEHPQALLGGFRGVLQTDGYAGYNKLAR-GQVTHAGCWAHA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 335 RRKIHDVHVRTPSVLTEeALKRIGELYAIESEIRGKRAEERQAVRHQKVLPLLASLEGWLREKQKTLSRHSELAKAFGYA 414
Cdd:pfam03050 155 RRKFFDAHKAGSPLAAQ-ALARIGKLYAIEREIRDLTPEERLALRQEYSRPLLDELEAWLEEQLRGVLPKSALGKAIRYL 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2241884808 415 LNQWPALIRYAEDGWVEVDNNIAENALRRVSLGRKNWLFFGSDHGGER 462
Cdd:pfam03050 234 LNRWEALLRFLEDGRVPIDNNQAERAIRPVVLGRKNWLFAGSDEGAEA 281
COG3436 COG3436
Transposase [Mobilome: prophages, transposons];
34-454 9.41e-91

Transposase [Mobilome: prophages, transposons];


Pssm-ID: 442662 [Multi-domain]  Cd Length: 416  Bit Score: 283.46  E-value: 9.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808  34 EREIDHLQAQLDKLRRMNFGSRSEKVSRRIAQMEADLNLLQQESDTLTGRVDDPAVQRPLRQTR-TRKPFPESLPRDEKR 112
Cdd:COG3436     1 EEEEEELILLLLLLERLRLRRLRERESRLESQPELQLLELEEEAEEEEEAAEEAEAKTTKKKPKpGRKPMPEHLPREEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 113 LLPTEPCCPEcggSLSYLGEDAAEQLELMRSAFRVIRTVREKHACRRCDR--IVQAPAPSRPIERGIAGPGLLARVLTSK 190
Cdd:COG3436    81 HEPTDMRKID---GLAAIGEEVSEELDLDPGALFVFRNRRDKYKCLYCDGtgLVYAPAPAKRLEKGLAGPGLLAHILVSK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 191 YAEHTPLYRQSEIYARQGVVLSRSVLSGWVDACCRLLAPLDEALQHYVLTDGKLHADDTPVPVLLPGNKKTKTGRLWTYV 270
Cdd:COG3436   158 FVDHLPLYRQEEIFARLGVELSRSTLLNWVGRAAELLEPLLEGLDERLLAAPVLHADETPVQVLDEGKGKTVTASYWWVY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 271 RDDRNAGSALAPAVWFAYSPDRKGIHPQTHLAGFSGVLQADAYAGFNELYRDGHIKEAACWAHARRKIHDVHVRTPSVLT 350
Cdd:COG3436   238 RDGRPSRGPVVYDAYRSRRGARAGLVLDGGLGGGLGDDYADGYAALLRLAELGCAAAARRRRKAAAAALKKLAKKAAAAA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808 351 EEALKRIGELYAIESEIRGKRAEERQAVRhqkvlPLLASLEGWLREKQKTLSRHSELAKAFGYALNQWPALIRYAEDGWV 430
Cdd:COG3436   318 AGLAAEEALLRIEELRKEERLRERRRERR-----PRRLLLLKALLLLLLLLLPLLPPGKALLYAALARAARLLALLDRLL 392

                         410       420
                  ....*....|....*....|....
gi 2241884808 431 EVDNNIAENALRRVSLGRKNWLFF 454
Cdd:COG3436   393 DLLRNNDENNAERNALRRRNNLFA 416
DDE_Tnp_IS66_C pfam13817
IS66 C-terminal element;
468-505 4.26e-14

IS66 C-terminal element;


Pssm-ID: 433500  Cd Length: 39  Bit Score: 66.26  E-value: 4.26e-14
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2241884808 468 SLIGTCKLNGVDPERYLHYVLDVIAD-WPVNRVGALLPW 505
Cdd:pfam13817   1 SLIETAKLNGLDPYAYLTDVLERLPDhHPAERLDELLPW 39
zf-IS66 pfam13005
zinc-finger binding domain of transposase IS66; This is a zinc-finger region of the N-terminus ...
 117-161 3.15e-12

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: 61.17  E-value: 3.15e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2241884808 117 EPCCPECGGSLSYLGEDA-AEQLELMRSAFRVIRTVREKHACRRCD 161
Cdd:pfam13005   1 ERVCPCCGGLLHPIGEDEvREELDIPPAKFRVIEHIRPKYACRHCE 46
LZ_Tnp_IS66 pfam13007
Transposase C of IS166 homeodomain; This is a leucine-zipper-like or homeodomain-like region ...
 39-110 1.36e-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: 59.97  E-value: 1.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2241884808  39 HLQAQLDKLRRMNFGSRSEKvsRRIAQMEADLNLLQQESDTLTGRvddpAVQRPLRQTRTRKPFPESLPRDE 110
Cdd:pfam13007   1 RLEEQLALLKRRLFGRSSEK--LDPEQLELALEELEAEEAEVEAE----ARASKKRKKPGRKPLPAHLPREE 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-86 7.10e-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: 42.35  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2241884808   12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNLLQQESDTLTGRVDD 86
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----ELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
HR1_ROCK1 cd11639
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 14-77 1.71e-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: 36.91  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2241884808  14 QRLAEQEAlihalqEKLSNREREIDHLQAQLDKLRRMNfgSRSEKVSRRIAQMEADLNLLQQES 77
Cdd:cd11639    11 QRKAEQES------EKRRNVENEVSTLKDQLEDLKKIS--QNSQITNEKINQLQKQLEEANDLL 66
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 12-80 1.98e-03

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: 37.55  E-value: 1.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2241884808  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRMNFGSRSEKVSRRIA--QMEADLNLLQQESDTL 80
Cdd:cd22887     2 LESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIEnnLLEEKLRKLQEENDEL 72
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
9-86 2.16e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808    9 ILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRM---NFGSRSEKVSRRIAQMEADLNLLQQESDTLTGRVD 85
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgNGGDRLEQLEREIERLERELEERERRRARLEALLA 369


                   .
gi 2241884808   86 D 86
Cdd:COG4913    370 A 370
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-99 2.49e-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: 40.13  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808   5 SSDDILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNLLQQESDTLTGRV 84
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----RIAALARRIRALEQELAALEAELAELEKEI 92

                          90
                  ....*....|....*
gi 2241884808  85 DdpAVQRPLRQTRTR 99
Cdd:COG4942    93 A--ELRAELEAQKEE 105
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 7-91 2.58e-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: 39.52  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808   7 DDILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKlrrmnfgsrsekvsrRIAQMEADLNLLQQESDTLTGRVDD 86
Cdd:COG1579   110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---------------ELAELEAELEELEAEREELAAKIPP 174


                  ....*
gi 2241884808  87 PAVQR 91
Cdd:COG1579   175 ELLAL 179
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
12-86 4.26e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2241884808  12 LKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNLLQQESDTLTGRVDD 86
Cdd:COG4372    50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNE-----QLQAAQAELAQAQEELESLQEEAEELQEELEE 119
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
 6-48 4.55e-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: 4.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2241884808   6 SDDILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLDKLR 48
Cdd:cd12083     1 SGLLEEKTEELRKKDERIRELEQELQEKDEEIQELRSQLDKFQ 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-86 8.26e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808   9 ILLLKQRLAEQEALIHALQEKLSNREREIDHLQAQLD--KLRRMNFGSRSEKVSRRIAQMEADLNLLQQESDTLTGRVDD 86
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
12-76 9.22e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241884808  12 LKQRLAEQEALIHALQEKL-----------------SNREREIDHLQAQLDKLRRmnfgsRSEKVSRRIAQMEADLNLLQ 74
Cdd:COG2433   432 LEAELEEKDERIERLERELsearseerreirkdreiSRLDREIERLERELEEERE-----RIEELKRKLERLKELWKLEH 506


                  ..
gi 2241884808  75 QE 76
Cdd:COG2433   507 SG 508
 
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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