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Conserved domains on  [gi|1034601923|ref|XP_016880777|]
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centrosomal protein of 95 kDa isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
375-549 2.61e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923  375 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 448
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923  449 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 520
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034601923  521 EN----------YYKDQFSLLAEAISQEHQELKAREKSQ 549
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKL 430
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
375-549 2.61e-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: 47.36  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923  375 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 448
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923  449 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 520
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034601923  521 EN----------YYKDQFSLLAEAISQEHQELKAREKSQ 549
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKL 430
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
372-559 2.58e-04

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: 43.37  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 372 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 451
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 452 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLL 531
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
                         170       180
                  ....*....|....*....|....*...
gi 1034601923 532 AEAISQEHQELKAREKSQAQVIIKIEAK 559
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQ 192
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
376-559 4.76e-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: 42.83  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 376 KQQIAQVEQLKKEAcreNRSKKKLQDEIEEALRRHDLLTTLVKkeyEHNKRLQDFKDCIRRqrlTQSKIKENRQQIVRAR 455
Cdd:COG4942    33 QQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIR---ALEQELAALEAELAE---LEKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 456 KYYddyrVQLCAKMMRMRTREEMIFkKLFEEGLNIQKQRLRDLRNYAKEKRD--EQRRRHQDELDSMENYYKDQFSLLAE 533
Cdd:COG4942   104 EEL----AELLRALYRLGRQPPLAL-LLSPEDFLDAVRRLQYLKYLAPARREqaEELRADLAELAALRAELEAERAELEA 178
                         170       180
                  ....*....|....*....|....*....
gi 1034601923 534 AIS---QEHQELKAREKSQAQVIIKIEAK 559
Cdd:COG4942   179 LLAeleEERAALEALKAERQKLLARLEKE 207
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
375-549 2.61e-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: 47.36  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923  375 WKQQIAQVEQLKKEACRENRSKKKLQDEI---EEALRRHDLLTTLVKKEYEH-NKRLQDFKdcIRRQRLTQSK--IKENR 448
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELqelEEKLEELRLEVSELEEEIEElQKELYALA--NEISRLEQQKqiLRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923  449 QQIVRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFE-----EGLNIQKQRLRDLRNYAKEKRDEQRRRHQ---DELDSM 520
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeelESLEAELEELEAELEELESRLEELEEQLEtlrSKVAQL 391
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1034601923  521 EN----------YYKDQFSLLAEAISQEHQELKAREKSQ 549
Cdd:TIGR02168  392 ELqiaslnneieRLEARLERLEDRRERLQQEIEELLKKL 430
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
372-559 2.58e-04

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: 43.37  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 372 SKMWKQQIAQVEQLKKEACRENRSkkklQDEIEEALRRHDLLTTLVKKEYEHNKRLQdFKDCIRRQrltqskIKENRQQI 451
Cdd:pfam13868  21 NKERDAQIAEKKRIKAEEKEEERR----LDEMMEEERERALEEEEEKEEERKEERKR-YRQELEEQ------IEEREQKR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 452 VRARKYYDDYRVQLCAKMMRMRTREEMIFKKLFEEglniqKQRLRDLRNYAKEKRDEQRRRHQDELDSMENYYKDQFSLL 531
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK-----QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
                         170       180
                  ....*....|....*....|....*...
gi 1034601923 532 AEAISQEHQELKAREKSQAQVIIKIEAK 559
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIARLRAQ 192
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
376-559 4.76e-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: 42.83  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 376 KQQIAQVEQLKKEAcreNRSKKKLQDEIEEALRRHDLLTTLVKkeyEHNKRLQDFKDCIRRqrlTQSKIKENRQQIVRAR 455
Cdd:COG4942    33 QQEIAELEKELAAL---KKEEKALLKQLAALERRIAALARRIR---ALEQELAALEAELAE---LEKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 456 KYYddyrVQLCAKMMRMRTREEMIFkKLFEEGLNIQKQRLRDLRNYAKEKRD--EQRRRHQDELDSMENYYKDQFSLLAE 533
Cdd:COG4942   104 EEL----AELLRALYRLGRQPPLAL-LLSPEDFLDAVRRLQYLKYLAPARREqaEELRADLAELAALRAELEAERAELEA 178
                         170       180
                  ....*....|....*....|....*....
gi 1034601923 534 AIS---QEHQELKAREKSQAQVIIKIEAK 559
Cdd:COG4942   179 LLAeleEERAALEALKAERQKLLARLEKE 207
CpxP COG3678
Periplasmic chaperone Spy, Spy/CpxP family [Posttranslational modification, protein turnover, ...
472-552 9.47e-03

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


Pssm-ID: 442894 [Multi-domain]  Cd Length: 141  Bit Score: 36.88  E-value: 9.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601923 472 MRTREEMIFKKLFEeGLNI---QKQRLRDLRNYAKEKRDEQRRRHQDELDSM------ENYYKDQFSLLAEAISQEHQEL 542
Cdd:COG3678    28 GGPRGGRGLRRMLE-GLNLteeQRQQIRAIRQQYRKQMRALRQQLREAREELrallaaDKFDEAAVRALADKIAALRAQL 106
                          90
                  ....*....|.
gi 1034601923 543 -KAREKSQAQV 552
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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