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Conserved domains on  [gi|71989640|ref|NP_508164|]
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Pericentrin [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
156-426 2.58e-04

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    156 LRKELTEYKKANQFLQHSHANLEREMEE--NRFSVNEKVVNMLSEERDHFHQEISNLKHTCSQLTKEKIELEEKYQNSTD 233
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    234 SWHRTQDVLQYFRNQISQMKGALQKTEEtfiSDFETFGAEIKRSLENQAKRKSSSPKIIQlPCNCENKSREQTNQVVkhD 313
Cdd:TIGR02169  759 ELKELEARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLEEEVSRIEARLR-EIEQKLNRLTLEKEYL--E 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    314 ESTQTKSVYIDEshrWEREEKEIASSPNGKNGNVTDLLQIIEQLEMEKRLLLAQRRSDKAEIERLQEQLNETLIMHGE-- 391
Cdd:TIGR02169  833 KEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEle 909
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 71989640    392 -KIEQLDEILVDNEELKDILKQQALALTDNIAQSDE 426
Cdd:TIGR02169  910 aQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
156-426 2.58e-04

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: 43.52  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    156 LRKELTEYKKANQFLQHSHANLEREMEE--NRFSVNEKVVNMLSEERDHFHQEISNLKHTCSQLTKEKIELEEKYQNSTD 233
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    234 SWHRTQDVLQYFRNQISQMKGALQKTEEtfiSDFETFGAEIKRSLENQAKRKSSSPKIIQlPCNCENKSREQTNQVVkhD 313
Cdd:TIGR02169  759 ELKELEARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLEEEVSRIEARLR-EIEQKLNRLTLEKEYL--E 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    314 ESTQTKSVYIDEshrWEREEKEIASSPNGKNGNVTDLLQIIEQLEMEKRLLLAQRRSDKAEIERLQEQLNETLIMHGE-- 391
Cdd:TIGR02169  833 KEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEle 909
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 71989640    392 -KIEQLDEILVDNEELKDILKQQALALTDNIAQSDE 426
Cdd:TIGR02169  910 aQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
360-413 6.71e-04

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 39.07  E-value: 6.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71989640   360 EKRLLLAQRRSDKAEIERLQEQLNETLIMHGEKIEQLDEILVDNEELKDILKQQ 413
Cdd:pfam12325  58 ELKELKKELEELEKELKELEQRYETTLELLGEKSEEVEELKADVEDLKEMYREQ 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-429 7.72e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640 156 LRKELTEYKKANQFLQHSHANLEREMEE--NRFSVNEKVVNMLSEERDHFHQEISNLKHTCSQLTKEKIELEEKYQNSTD 233
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640 234 SWHRTQDVLQYFRNQISQMKGALQKTEETFISDFETFGAEIKRSLENQAKRkssspkiiqlpcncENKSREQTNQVVKHD 313
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--------------LEALRAAAELAAQLE 403
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640 314 ESTQTKSVYIDESHRWEREEKEIASSpngkngnvtdlLQIIEQLEMEKRLLLAQRRSDKAEIERLQEQLNETLIMHGEKI 393
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEA-----------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71989640 394 EQLDEILVDNEELKDILKQQALALTDNIAQSDEKGS 429
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
156-426 2.58e-04

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: 43.52  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    156 LRKELTEYKKANQFLQHSHANLEREMEE--NRFSVNEKVVNMLSEERDHFHQEISNLKHTCSQLTKEKIELEEKYQNSTD 233
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    234 SWHRTQDVLQYFRNQISQMKGALQKTEEtfiSDFETFGAEIKRSLENQAKRKSSSPKIIQlPCNCENKSREQTNQVVkhD 313
Cdd:TIGR02169  759 ELKELEARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLEEEVSRIEARLR-EIEQKLNRLTLEKEYL--E 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640    314 ESTQTKSVYIDEshrWEREEKEIASSPNGKNGNVTDLLQIIEQLEMEKRLLLAQRRSDKAEIERLQEQLNETLIMHGE-- 391
Cdd:TIGR02169  833 KEIQELQEQRID---LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEle 909
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 71989640    392 -KIEQLDEILVDNEELKDILKQQALALTDNIAQSDE 426
Cdd:TIGR02169  910 aQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
360-413 6.71e-04

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 39.07  E-value: 6.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71989640   360 EKRLLLAQRRSDKAEIERLQEQLNETLIMHGEKIEQLDEILVDNEELKDILKQQ 413
Cdd:pfam12325  58 ELKELKKELEELEKELKELEQRYETTLELLGEKSEEVEELKADVEDLKEMYREQ 111
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
156-429 7.72e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640 156 LRKELTEYKKANQFLQHSHANLEREMEE--NRFSVNEKVVNMLSEERDHFHQEISNLKHTCSQLTKEKIELEEKYQNSTD 233
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEaqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640 234 SWHRTQDVLQYFRNQISQMKGALQKTEETFISDFETFGAEIKRSLENQAKRkssspkiiqlpcncENKSREQTNQVVKHD 313
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL--------------LEALRAAAELAAQLE 403
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640 314 ESTQTKSVYIDESHRWEREEKEIASSpngkngnvtdlLQIIEQLEMEKRLLLAQRRSDKAEIERLQEQLNETLIMHGEKI 393
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEA-----------LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71989640 394 EQLDEILVDNEELKDILKQQALALTDNIAQSDEKGS 429
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
156-339 1.28e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.51  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640   156 LRKELTEYK-KANQFLQHSH---ANLEREMEENRFS---VNEKVVNMLSEERDHFHQEISNLKHTCSQLTKEKIELEEKY 228
Cdd:pfam09787   5 AKQELADYKqKAARILQSKEkliASLKEGSGVEGLDsstALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989640   229 QNSTDSWHR------------------TQDVLQYFRNQISQMKGALQKTEETFISDFETFGAEIKRsLENQAKRKS-SSP 289
Cdd:pfam09787  85 QEEAESSREqlqeleeqlatersarreAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEK-LRNQLTSKSqSSS 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 71989640   290 KIIQLpcncENKSREQTNQVVKHD---ESTQT-KSVYIDESHRWEREEKEIASS 339
Cdd:pfam09787 164 SQSEL----ENRLHQLTETLIQKQtmlEALSTeKNSLVLQLERMEQQIKELQGE 213
 
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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