NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21312474|ref|NP_081539|]
View 

centromere protein S [Mus musculus]

Protein Classification

CENP-S family protein( domain architecture ID 10634920)

CENP-S family protein similar to centromere protein S, a DNA-binding component of the Fanconi anemia (FA) core complex; it is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 16-91 2.54e-40

CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


:

Pssm-ID: 464782  Cd Length: 76  Bit Score: 129.62  E-value: 2.54e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312474    16 QRLKAAVHYTVGCLCQEVTLNKQVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRNNSL 91
Cdd:pfam15630   1 QRLKAALWYSVGKIVEEETLDLGVNATPQFIAALTELVYKQLENLAKDLEAFAKHAGRSTITTDDVKLLARRNPSL 76
 
Name Accession Description Interval E-value
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 16-91 2.54e-40

CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


Pssm-ID: 464782  Cd Length: 76  Bit Score: 129.62  E-value: 2.54e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312474    16 QRLKAAVHYTVGCLCQEVTLNKQVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRNNSL 91
Cdd:pfam15630   1 QRLKAALWYSVGKIVEEETLDLGVNATPQFIAALTELVYKQLENLAKDLEAFAKHAGRSTITTDDVKLLARRNPSL 76
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 18-94 3.94e-35

histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also called MHF1, apoptosis-inducing TAF9-like domain-containing protein 1 (APITD1), FANCM-associated histone fold protein 1, FANCM-interacting histone fold protein 1, or Fanconi anemia-associated polypeptide of 16 kDa (FAAP16), is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-S, together with CENP-X, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-S acts as a crucial cofactor for FANCM, in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-S also forms a discrete complex with FANCM and CENP-X, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-X (CENP-T-W-S-X heterotetramer), CENP-S is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, CENP-S binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-X. It does not bind DNA on its own.


Pssm-ID: 467044  Cd Length: 77  Bit Score: 116.51  E-value: 3.94e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312474  18 LKAAVHYTVGCLCQEVTLNKQVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRNNSLLKY 94
Cdd:cd22919   1 LKAALHYTVGKICEEEAEEKGVTVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKLLARRNPSLLEE 77
 
Name Accession Description Interval E-value
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 16-91 2.54e-40

CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


Pssm-ID: 464782  Cd Length: 76  Bit Score: 129.62  E-value: 2.54e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21312474    16 QRLKAAVHYTVGCLCQEVTLNKQVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRNNSL 91
Cdd:pfam15630   1 QRLKAALWYSVGKIVEEETLDLGVNATPQFIAALTELVYKQLENLAKDLEAFAKHAGRSTITTDDVKLLARRNPSL 76
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 18-94 3.94e-35

histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also called MHF1, apoptosis-inducing TAF9-like domain-containing protein 1 (APITD1), FANCM-associated histone fold protein 1, FANCM-interacting histone fold protein 1, or Fanconi anemia-associated polypeptide of 16 kDa (FAAP16), is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-S, together with CENP-X, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-S acts as a crucial cofactor for FANCM, in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-S also forms a discrete complex with FANCM and CENP-X, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-X (CENP-T-W-S-X heterotetramer), CENP-S is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, CENP-S binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-X. It does not bind DNA on its own.


Pssm-ID: 467044  Cd Length: 77  Bit Score: 116.51  E-value: 3.94e-35
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21312474  18 LKAAVHYTVGCLCQEVTLNKQVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRNNSLLKY 94
Cdd:cd22919   1 LKAALHYTVGKICEEEAEEKGVTVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKLLARRNPSLLEE 77
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 38-107 5.98e-09

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 49.86  E-value: 5.98e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21312474  38 QVNFSKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARRnnslLKYITEKN--EEIAQLNL 107
Cdd:cd22920  17 KRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKR----QRLVTDKQslESLARKYL 84
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 42-87 2.74e-04

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 434768  Cd Length: 108  Bit Score: 38.18  E-value: 2.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 21312474    42 SKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKLLARR 87
Cdd:pfam15511  31 SKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKR 76
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 37-83 2.39e-03

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 34.50  E-value: 2.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21312474  37 KQVNF---SKQTIAAISEVTFRQCENFAKDLEMFARHAKRSTVTTEDVKL 83
Cdd:cd00076  11 KSAGFdsvSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVEL 60
TFIID-31kDa pfam02291
Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of ...
 62-99 5.83e-03

Transcription initiation factor IID, 31kD subunit; This family represents the N-terminus of the 31kD subunit (42kD in drosophila) of transcription initiation factor IID (TAFII31). TAFII31 binds to p53, and is an essential requirement for p53 mediated transcription activation.


Pssm-ID: 460525  Cd Length: 122  Bit Score: 34.41  E-value: 5.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 21312474    62 KDLEMFARHAKRSTVTTEDVKLL--ARRNNS---------LLKYITEKN 99
Cdd:pfam02291  44 EDALVYSEHAGKKQIDVDDVRLAiqSRVNHQftgppprefLLELARERN 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH