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Conserved domains on  [gi|530413077|ref|XP_005257836|]
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centrosomal protein of 95 kDa isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
 51-107 2.85e-24

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


:

Pssm-ID: 465945  Cd Length: 59  Bit Score: 96.10  E-value: 2.85e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413077   51 LIVIPRSQEDDAHNVQAVIDSLALDYLQVSLSHITGENIVKGDKESIKNLLEIFDGL 107
Cdd:pfam19016   3 VIRNPSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
TPH super family cl38442
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 584-771 6.81e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


The actual alignment was detected with superfamily member pfam13868:

Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077  584 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 663
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077  664 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLL 743
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164

                         170       180
                  ....*....|....*....|....*...
gi 530413077  744 AEAISQEHQELKAREKSQAQVIIKIEAK 771
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQ 192
 
Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
 51-107 2.85e-24

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


Pssm-ID: 465945  Cd Length: 59  Bit Score: 96.10  E-value: 2.85e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413077   51 LIVIPRSQEDDAHNVQAVIDSLALDYLQVSLSHITGENIVKGDKESIKNLLEIFDGL 107
Cdd:pfam19016   3 VIRNPSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 584-771 6.81e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077  584 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 663
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077  664 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLL 743
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164

                         170       180
                  ....*....|....*....|....*...
gi 530413077  744 AEAISQEHQELKAREKSQAQVIIKIEAK 771
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQ 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 587-761 6.86e-05

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: 46.59  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077   587 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077   661 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 732
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 530413077   733 EN----------YYKDQFSLLAEAISQEHQELKAREKSQ 761
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKL 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 588-771 4.61e-04

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: 43.21  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077 588 KQQIAQVEQLKKEAcreNRSKKKLQDEIEEALRRHDLLTTLVKkeyEHNKRLQDFKDCIRRqrlTQSKIKENRQQIVRAR 667
Cdd:COG4942   33 QQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIR---ALEQELAALEAELAE---LEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077 668 KYYddyrVQLCAKMMRMRTREEMIFKKLFEEGLNIQKqRLRDLRNYAKEKRD--EQRRRHQDELDSMENYYKDQFSLLAE 745
Cdd:COG4942  104 EEL----AELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREqaEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|....*....
gi 530413077 746 AIS---QEHQELKAREKSQAQVIIKIEAK 771
Cdd:COG4942  179 LLAeleEERAALEALKAERQKLLARLEKE 207
 
Name Accession Description Interval E-value
DUF5745 pfam19016
Domain of unknown function (DUF5745); This is a domain of unknown function found in ...
 51-107 2.85e-24

Domain of unknown function (DUF5745); This is a domain of unknown function found in Platyhelminthes. It shows homology with the calponin homology (CH) domain.


Pssm-ID: 465945  Cd Length: 59  Bit Score: 96.10  E-value: 2.85e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530413077   51 LIVIPRSQEDDAHNVQAVIDSLALDYLQVSLSHITGENIVKGDKESIKNLLEIFDGL 107
Cdd:pfam19016   3 VIRNPSSVEDRIHNIQAVIDSLANDVLNVDLSHITPEDIVDGDPEAIRNLLEIFVGI 59
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 584-771 6.81e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077  584 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 663
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077  664 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLL 743
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164

                         170       180
                  ....*....|....*....|....*...
gi 530413077  744 AEAISQEHQELKAREKSQAQVIIKIEAK 771
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQ 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 587-761 6.86e-05

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: 46.59  E-value: 6.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077   587 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 660
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077   661 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 732
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 530413077   733 EN----------YYKDQFSLLAEAISQEHQELKAREKSQ 761
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKL 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 588-771 4.61e-04

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: 43.21  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077 588 KQQIAQVEQLKKEAcreNRSKKKLQDEIEEALRRHDLLTTLVKkeyEHNKRLQDFKDCIRRqrlTQSKIKENRQQIVRAR 667
Cdd:COG4942   33 QQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIR---ALEQELAALEAELAE---LEKEIAELRAELEAQK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077 668 KYYddyrVQLCAKMMRMRTREEMIFKKLFEEGLNIQKqRLRDLRNYAKEKRD--EQRRRHQDELDSMENYYKDQFSLLAE 745
Cdd:COG4942  104 EEL----AELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREqaEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|....*....
gi 530413077 746 AIS---QEHQELKAREKSQAQVIIKIEAK 771
Cdd:COG4942  179 LLAeleEERAALEALKAERQKLLARLEKE 207
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
 684-764 6.28e-03

Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 38.04  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413077 684 MRTREEMIFKKLFEeGLNI---QKQRLRDLRNYAKEKRDEQRRRHQDELDSM------ENYYKDQFSLLAEAISQEHQEL 754
Cdd:COG3678   28 GGPRGGRGLRRMLE-GLNLteeQRQQIRAIRQQYRKQMRALRQQLREAREELrallaaDKFDEAAVRALADKIAALRAQL 106

                         90
                 ....*....|.
gi 530413077 755 -KAREKSQAQV 764
Cdd:COG3678  107 aVERAEARNQM 117
 
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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