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Conserved domains on  [gi|18414476|ref|NP_567470|]
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PH-response transcription factor [Arabidopsis thaliana]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 711891)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
51-135 6.54e-05

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


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 6.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476  51 LSTRVSALESESSDLRELLAEKEKEFEELQShvesleaslsdafhKLSLADGEKENLIRENA---SLSNTVKRLQRDVSK 127
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLER--------------ELSEARSEERREIRKDReisRLDREIERLERELEE 483

                ....*...
gi 18414476 128 LEGFRKTL 135
Cdd:COG2433 484 ERERIEEL 491
CwlO1 super family cl25603
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
33-264 5.99e-04

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


The actual alignment was detected with superfamily member COG3883:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476  33 PSDPFEQLDVARKITS------IALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLSLADGEKEN 106
Cdd:COG3883 114 FSDFLDRLSALSKIADadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476 107 LIRENASLSNTVKRLQRDVSKLEGFRKTLMMSLQDDDQNAGTTQIIAKPTPNDDDTPFQPSRHSSIQSQQASEAIEPAAT 186
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414476 187 DNENDAPKPSLSASLPLVSQTTTPRLTPPGSPPILSASGTPKTTSRPISPRRHSVSFATTRGMFDDTRSSISISEPGS 264
Cdd:COG3883 274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGG 351
 
Name Accession Description Interval E-value
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
51-135 6.54e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 6.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476  51 LSTRVSALESESSDLRELLAEKEKEFEELQShvesleaslsdafhKLSLADGEKENLIRENA---SLSNTVKRLQRDVSK 127
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLER--------------ELSEARSEERREIRKDReisRLDREIERLERELEE 483

                ....*...
gi 18414476 128 LEGFRKTL 135
Cdd:COG2433 484 ERERIEEL 491
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
49-128 6.86e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476     49 IALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLsladgEKENLIREnaSLSNTVKRLQRDVSKL 128
Cdd:pfam01576  485 LNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-----EEDAGTLE--ALEEGKKRLQRELEAL 557
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-141 5.98e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476   54 RVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHklsladgekENLIRENASLSNTVKRLQRDVSKLEGFRK 133
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY---------EELREEYLELSRELAGLRAELEELEKRRE 690

                 ....*...
gi 18414476  134 TLMMSLQD 141
Cdd:PRK03918 691 EIKKTLEK 698
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
33-264 5.99e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476  33 PSDPFEQLDVARKITS------IALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLSLADGEKEN 106
Cdd:COG3883 114 FSDFLDRLSALSKIADadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476 107 LIRENASLSNTVKRLQRDVSKLEGFRKTLMMSLQDDDQNAGTTQIIAKPTPNDDDTPFQPSRHSSIQSQQASEAIEPAAT 186
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414476 187 DNENDAPKPSLSASLPLVSQTTTPRLTPPGSPPILSASGTPKTTSRPISPRRHSVSFATTRGMFDDTRSSISISEPGS 264
Cdd:COG3883 274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGG 351
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-135 1.02e-03

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: 41.20  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476     34 SDPFEQLDVARKITSIALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLSLADGEKENLIRENAS 113
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100
                   ....*....|....*....|..
gi 18414476    114 LSNTVKRLQRDVSKLEGFRKTL 135
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEEL 766
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
155-262 8.94e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 37.84  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476   155 PTPNDDDTPFQPSRHSSIQSQQASEAIEPAATDNENDAPKPSLSASLPL--VSQTT----TPRLTPPGSPPILSASGTPK 228
Cdd:PHA03307  128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLssPEETArapsSPPAEPPPSTPPAAASPRPP 207
                          90       100       110
                  ....*....|....*....|....*....|....
gi 18414476   229 TTSRPISPRRHSVSFATTRGMFDDTRSSISISEP 262
Cdd:PHA03307  208 RRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241
 
Name Accession Description Interval E-value
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
51-135 6.54e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 6.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476  51 LSTRVSALESESSDLRELLAEKEKEFEELQShvesleaslsdafhKLSLADGEKENLIRENA---SLSNTVKRLQRDVSK 127
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLER--------------ELSEARSEERREIRKDReisRLDREIERLERELEE 483

                ....*...
gi 18414476 128 LEGFRKTL 135
Cdd:COG2433 484 ERERIEEL 491
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
49-128 6.86e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.78  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476     49 IALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLsladgEKENLIREnaSLSNTVKRLQRDVSKL 128
Cdd:pfam01576  485 LNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-----EEDAGTLE--ALEEGKKRLQRELEAL 557
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
54-141 5.98e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476   54 RVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHklsladgekENLIRENASLSNTVKRLQRDVSKLEGFRK 133
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY---------EELREEYLELSRELAGLRAELEELEKRRE 690

                 ....*...
gi 18414476  134 TLMMSLQD 141
Cdd:PRK03918 691 EIKKTLEK 698
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
33-264 5.99e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476  33 PSDPFEQLDVARKITS------IALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLSLADGEKEN 106
Cdd:COG3883 114 FSDFLDRLSALSKIADadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476 107 LIRENASLSNTVKRLQRDVSKLEGFRKTLMMSLQDDDQNAGTTQIIAKPTPNDDDTPFQPSRHSSIQSQQASEAIEPAAT 186
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18414476 187 DNENDAPKPSLSASLPLVSQTTTPRLTPPGSPPILSASGTPKTTSRPISPRRHSVSFATTRGMFDDTRSSISISEPGS 264
Cdd:COG3883 274 AGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGG 351
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-135 1.02e-03

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: 41.20  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476     34 SDPFEQLDVARKITSIALSTRVSALESESSDLRELLAEKEKEFEELQSHVESLEASLSDAFHKLSLADGEKENLIRENAS 113
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
                           90       100
                   ....*....|....*....|..
gi 18414476    114 LSNTVKRLQRDVSKLEGFRKTL 135
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEEL 766
PRK14147 PRK14147
heat shock protein GrpE; Provisional
67-183 2.09e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237625 [Multi-domain]  Cd Length: 172  Bit Score: 38.39  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476   67 ELLAEKEKEFEELQSHVESLEASLSDAfhklsladgeKENLIRENASLSNTVKRLQRDVSKLEGF-RKTLMMSLQD--DD 143
Cdd:PRK14147  11 EDLAQNPPETDPLKAEVESLRSEIALV----------KADALRERADLENQRKRIARDVEQARKFaNEKLLGELLPvfDS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18414476  144 QNAGTTQIIAKPTPNDD------------------------DTPFQPSRHSSIqSQQASEAIEP 183
Cdd:PRK14147  81 LDAGLTAAGTEPSPLRDgleltykqllkvaadngltlldpvGQPFNPEHHQAI-SQGEAEGVAP 143
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
155-262 8.94e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 37.84  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414476   155 PTPNDDDTPFQPSRHSSIQSQQASEAIEPAATDNENDAPKPSLSASLPL--VSQTT----TPRLTPPGSPPILSASGTPK 228
Cdd:PHA03307  128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLssPEETArapsSPPAEPPPSTPPAAASPRPP 207
                          90       100       110
                  ....*....|....*....|....*....|....
gi 18414476   229 TTSRPISPRRHSVSFATTRGMFDDTRSSISISEP 262
Cdd:PHA03307  208 RRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241
 
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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