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Conserved domains on  [gi|1034626970|ref|XP_016883761|]
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heat shock factor 2-binding protein isoform X10 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12704 super family cl36166
phosphodiesterase; Provisional
 17-118 1.54e-03

phosphodiesterase; Provisional


The actual alignment was detected with superfamily member PRK12704:

Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970  17 KEEFVKvRKKDLERlttEVmqirdflpRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQaDNIREK 96
Cdd:PRK12704   63 KEEIHK-LRNEFEK---EL--------RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ-QELEKK 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034626970  97 KEKL-ALRQQLN------------EAKQQLLQQAE 118
Cdd:PRK12704  130 EEELeELIEEQLqelerisgltaeEAKEILLEKVE 164
 
Name Accession Description Interval E-value
PRK12704 PRK12704
phosphodiesterase; Provisional
 17-118 1.54e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970  17 KEEFVKvRKKDLERlttEVmqirdflpRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQaDNIREK 96
Cdd:PRK12704   63 KEEIHK-LRNEFEK---EL--------RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ-QELEKK 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034626970  97 KEKL-ALRQQLN------------EAKQQLLQQAE 118
Cdd:PRK12704  130 EEELeELIEEQLqelerisgltaeEAKEILLEKVE 164
COG6 pfam06419
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ...
 47-106 1.89e-03

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localization.


Pssm-ID: 461904  Cd Length: 611  Bit Score: 39.13  E-value: 1.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034626970  47 NGEVLESFQKLKiveKNLERKEQELEQLKMDCEHFKARLETV---------QADNIREKKEKLALRQQL 106
Cdd:pfam06419  32 NGEFLKEFGPVV---EQLKRIETDVEKLNNSCDEMRKRLSAAkedtaplleEASSLQEQKKKIELKQKL 97
COG6 smart01087
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ...
 47-118 1.90e-03

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.


Pssm-ID: 215018  Cd Length: 598  Bit Score: 39.23  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970   47 NGEVLESFQKLKiveKNLERKEQELEQLKMDCEHFKARLETV---------QADNIREKKEKLALRQQ----------LN 107
Cdd:smart01087  20 NGEFLSEFKPVA---EQLQRLSEDVQKLNNSCDSMKDQLNTAknqtqdlisEASELQEELALLELKKKlldaflskftLS 96

                           90
                   ....*....|.
gi 1034626970  108 EAKQQLLQQAE 118
Cdd:smart01087  97 QDELDVLTSRE 107
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 40-127 3.72e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970  40 DFLPRIL--------NGEVLESFQKLKiveKNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQ 111
Cdd:COG3883   116 DFLDRLSalskiadaDADLLEELKADK---AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192

                          90
                  ....*....|....*.
gi 1034626970 112 QLLQQAEYCTEMGAAA 127
Cdd:COG3883   193 AAEAQLAELEAELAAA 208
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-119 6.89e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.74  E-value: 6.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970    6 AAEEACRHMGTKEEFVKVRKK--------------------DLERLTTEVMQIRDFLPRILnGEVLESFQKLKIVEKNLE 65
Cdd:TIGR02169  373 LEEVDKEFAETRDELKDYREKleklkreinelkreldrlqeELQRLSEELADLNAAIAGIE-AKINELEEEKEDKALEIK 451

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034626970   66 RKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQLLQQAEY 119
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
 
Name Accession Description Interval E-value
PRK12704 PRK12704
phosphodiesterase; Provisional
 17-118 1.54e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970  17 KEEFVKvRKKDLERlttEVmqirdflpRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQaDNIREK 96
Cdd:PRK12704   63 KEEIHK-LRNEFEK---EL--------RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQ-QELEKK 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034626970  97 KEKL-ALRQQLN------------EAKQQLLQQAE 118
Cdd:PRK12704  130 EEELeELIEEQLqelerisgltaeEAKEILLEKVE 164
COG6 pfam06419
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ...
 47-106 1.89e-03

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localization.


Pssm-ID: 461904  Cd Length: 611  Bit Score: 39.13  E-value: 1.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034626970  47 NGEVLESFQKLKiveKNLERKEQELEQLKMDCEHFKARLETV---------QADNIREKKEKLALRQQL 106
Cdd:pfam06419  32 NGEFLKEFGPVV---EQLKRIETDVEKLNNSCDEMRKRLSAAkedtaplleEASSLQEQKKKIELKQKL 97
COG6 smart01087
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ...
 47-118 1.90e-03

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.


Pssm-ID: 215018  Cd Length: 598  Bit Score: 39.23  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970   47 NGEVLESFQKLKiveKNLERKEQELEQLKMDCEHFKARLETV---------QADNIREKKEKLALRQQ----------LN 107
Cdd:smart01087  20 NGEFLSEFKPVA---EQLQRLSEDVQKLNNSCDSMKDQLNTAknqtqdlisEASELQEELALLELKKKlldaflskftLS 96

                           90
                   ....*....|.
gi 1034626970  108 EAKQQLLQQAE 118
Cdd:smart01087  97 QDELDVLTSRE 107
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 40-127 3.72e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970  40 DFLPRIL--------NGEVLESFQKLKiveKNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQ 111
Cdd:COG3883   116 DFLDRLSalskiadaDADLLEELKADK---AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192

                          90
                  ....*....|....*.
gi 1034626970 112 QLLQQAEYCTEMGAAA 127
Cdd:COG3883   193 AAEAQLAELEAELAAA 208
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-118 5.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 5.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034626970  55 QKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQLLQQAE 118
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 19-119 5.68e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.03  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970   19 EFVKVRKKDLERLTTEVMQIRDFLprILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKA-RLETVQADNIREKK 97
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELI--IDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYlDYLKLNEERIDLLQ 243

                           90       100
                   ....*....|....*....|..
gi 1034626970   98 EKLALRQQLNEAKQQLLQQAEY 119
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEE 265
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-119 6.89e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.74  E-value: 6.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970    6 AAEEACRHMGTKEEFVKVRKK--------------------DLERLTTEVMQIRDFLPRILnGEVLESFQKLKIVEKNLE 65
Cdd:TIGR02169  373 LEEVDKEFAETRDELKDYREKleklkreinelkreldrlqeELQRLSEELADLNAAIAGIE-AKINELEEEKEDKALEIK 451

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034626970   66 RKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQLLQQAEY 119
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-117 7.46e-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: 37.34  E-value: 7.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970   25 KKDLERLTTEVMQIRDFLPRI------LNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLEtvqadniREKKE 98
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLerqleeLEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE-------ELEAE 366

                           90
                   ....*....|....*....
gi 1034626970   99 KLALRQQLNEAKQQLLQQA 117
Cdd:TIGR02168  367 LEELESRLEELEEQLETLR 385
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 17-101 8.37e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.35  E-value: 8.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034626970   17 KEEFVKVRKKDLERLTTEVMQIRdflpRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQADnIREK 96
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED-LSSL 749


                   ....*
gi 1034626970   97 KEKLA 101
Cdd:TIGR02169  750 EQEIE 754
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 62-113 8.48e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 37.19  E-value: 8.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034626970  62 KNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQL 113
Cdd:pfam15964 481 RQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQL 532
 
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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