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Conserved domains on  [gi|45356151|ref|NP_056076|]
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condensin-2 complex subunit D3 isoform 1 [Homo sapiens]

Protein Classification

Cnd1 domain-containing protein( domain architecture ID 11196605)

Cnd1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
 956-1120 1.46e-17

non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of chromosomes) subunits of the mitotic condensation complex are Cnd1-3. The whole complex is essential for viability and the condensing of chromosomes in mitosis.


:

Pssm-ID: 463677 [Multi-domain]  Cd Length: 162  Bit Score: 81.35  E-value: 1.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151    956 AVRNNVIIVMCdlCIRYTIMVDKYIPNISMCLKDSDPFIRKQTLILLTNLLQEEFVKWKGsLFFRFVSTLIDSHPDIASf 1035
Cdd:pfam12717    1 LIRALAIRTMG--CIRFPNLVEYLTEPLYRRLKDEDPYVRKTAAMCVAKLILPDMVKVKG-FISELAKLLEDPNPMVVA- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151   1036 geFCLAHL--LLKRNPVMFFQHFIECIFHFNNyekhekynkfpqserekrlfsLKGKSNKERRMKIYKFLLEHFTDEQR- 1112
Cdd:pfam12717   77 --NALAALteISEKDPNAIYNLLPDIISKLSD---------------------ALNECSEWGQIYILDFLASYIPKDKQe 133


                   ....*....
gi 45356151   1113 -FNITSKIC 1120
Cdd:pfam12717  134 aESLVEKLC 142
PDS5 super family cl47186
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 542-606 5.77e-03

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


The actual alignment was detected with superfamily member cd19953:

Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 41.36  E-value: 5.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45356151  542 VMAMLRRRIRDEKTNVRKSALQVLVSILKHCDVSGMKEDLW-ILQDQCRDPAVSVRKQALQSLTEL 606
Cdd:cd19953  325 ILEALKKRLLDPDEKVRLAAVKAICDLAYEDLLHKVPEELLsTLAERLRDKKASVRKEALQGLARL 390
 
Name Accession Description Interval E-value
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
 956-1120 1.46e-17

non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of chromosomes) subunits of the mitotic condensation complex are Cnd1-3. The whole complex is essential for viability and the condensing of chromosomes in mitosis.


Pssm-ID: 463677 [Multi-domain]  Cd Length: 162  Bit Score: 81.35  E-value: 1.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151    956 AVRNNVIIVMCdlCIRYTIMVDKYIPNISMCLKDSDPFIRKQTLILLTNLLQEEFVKWKGsLFFRFVSTLIDSHPDIASf 1035
Cdd:pfam12717    1 LIRALAIRTMG--CIRFPNLVEYLTEPLYRRLKDEDPYVRKTAAMCVAKLILPDMVKVKG-FISELAKLLEDPNPMVVA- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151   1036 geFCLAHL--LLKRNPVMFFQHFIECIFHFNNyekhekynkfpqserekrlfsLKGKSNKERRMKIYKFLLEHFTDEQR- 1112
Cdd:pfam12717   77 --NALAALteISEKDPNAIYNLLPDIISKLSD---------------------ALNECSEWGQIYILDFLASYIPKDKQe 133


                   ....*....
gi 45356151   1113 -FNITSKIC 1120
Cdd:pfam12717  134 aESLVEKLC 142
COG5098 COG5098
Chromosome condensation complex Condensin, subunit D2 [Chromatin structure and dynamics / Cell ...
 916-1050 1.65e-06

Chromosome condensation complex Condensin, subunit D2 [Chromatin structure and dynamics / Cell division and chromosome partitioning];


Pssm-ID: 227429 [Multi-domain]  Cd Length: 1128  Bit Score: 53.06  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151  916 PSVIRAhAIITLGKL-CLQHEdLAKKSIPALVRELEVCEDVAVRNNVIIVMCDLCIRYTIMVDKYIPNISMCLKDSDPFI 994
Cdd:COG5098  910 EELQVA-AYLSLYKLmCLSFE-FCSEHLPLLITSMEKHPIPRIRANAVVGLGDFLVCFNTTADEHTHYLYRRLGDEDADV 987

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 45356151  995 RKQTLILLTNLLQEEFVKWKGSLfFRFVSTLIDSHPDIASFGEFCLAHLLLKRNPV 1050
Cdd:COG5098  988 RRTCLMTIHFLILAGQLKVKGQL-GKMALLLTDEDAEISDMARHFFTQIAKKDNTM 1042
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 542-606 5.77e-03

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 41.36  E-value: 5.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45356151  542 VMAMLRRRIRDEKTNVRKSALQVLVSILKHCDVSGMKEDLW-ILQDQCRDPAVSVRKQALQSLTEL 606
Cdd:cd19953  325 ILEALKKRLLDPDEKVRLAAVKAICDLAYEDLLHKVPEELLsTLAERLRDKKASVRKEALQGLARL 390
 
Name Accession Description Interval E-value
Cnd1 pfam12717
non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of ...
 956-1120 1.46e-17

non-SMC mitotic condensation complex subunit 1; The three non-SMC (structural maintenance of chromosomes) subunits of the mitotic condensation complex are Cnd1-3. The whole complex is essential for viability and the condensing of chromosomes in mitosis.


Pssm-ID: 463677 [Multi-domain]  Cd Length: 162  Bit Score: 81.35  E-value: 1.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151    956 AVRNNVIIVMCdlCIRYTIMVDKYIPNISMCLKDSDPFIRKQTLILLTNLLQEEFVKWKGsLFFRFVSTLIDSHPDIASf 1035
Cdd:pfam12717    1 LIRALAIRTMG--CIRFPNLVEYLTEPLYRRLKDEDPYVRKTAAMCVAKLILPDMVKVKG-FISELAKLLEDPNPMVVA- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151   1036 geFCLAHL--LLKRNPVMFFQHFIECIFHFNNyekhekynkfpqserekrlfsLKGKSNKERRMKIYKFLLEHFTDEQR- 1112
Cdd:pfam12717   77 --NALAALteISEKDPNAIYNLLPDIISKLSD---------------------ALNECSEWGQIYILDFLASYIPKDKQe 133


                   ....*....
gi 45356151   1113 -FNITSKIC 1120
Cdd:pfam12717  134 aESLVEKLC 142
COG5098 COG5098
Chromosome condensation complex Condensin, subunit D2 [Chromatin structure and dynamics / Cell ...
 916-1050 1.65e-06

Chromosome condensation complex Condensin, subunit D2 [Chromatin structure and dynamics / Cell division and chromosome partitioning];


Pssm-ID: 227429 [Multi-domain]  Cd Length: 1128  Bit Score: 53.06  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45356151  916 PSVIRAhAIITLGKL-CLQHEdLAKKSIPALVRELEVCEDVAVRNNVIIVMCDLCIRYTIMVDKYIPNISMCLKDSDPFI 994
Cdd:COG5098  910 EELQVA-AYLSLYKLmCLSFE-FCSEHLPLLITSMEKHPIPRIRANAVVGLGDFLVCFNTTADEHTHYLYRRLGDEDADV 987

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 45356151  995 RKQTLILLTNLLQEEFVKWKGSLfFRFVSTLIDSHPDIASFGEFCLAHLLLKRNPV 1050
Cdd:COG5098  988 RRTCLMTIHFLILAGQLKVKGQL-GKMALLLTDEDAEISDMARHFFTQIAKKDNTM 1042
PDS5 cd19953
Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. ...
 542-606 5.77e-03

Sister chromatid cohesion protein PDS5; Pds5 plays a crucial role in sister chromatid cohesion. Together with WapI and Scc3, it is involved in the release of the cohesin complex from chromosomes during S phase. The core of the cohesin complex consists of a coiled-coiled heterodimer of Smc1 and Smc30, together with Scc1 (also called kleisin). Pds5 interacts with Scc1 via a conserved patch on the surface of its heat repeats. Pds5 also promotes the acetylation of Smc3 that protects cohesin from releasing activity in G2 phase.


Pssm-ID: 410996 [Multi-domain]  Cd Length: 630  Bit Score: 41.36  E-value: 5.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45356151  542 VMAMLRRRIRDEKTNVRKSALQVLVSILKHCDVSGMKEDLW-ILQDQCRDPAVSVRKQALQSLTEL 606
Cdd:cd19953  325 ILEALKKRLLDPDEKVRLAAVKAICDLAYEDLLHKVPEELLsTLAERLRDKKASVRKEALQGLARL 390
 
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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