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Conserved domains on  [gi|398364335|ref|NP_010934|]
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kinetochore-associated Ndc80 complex subunit SPC25 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RWD_DRWD_ELF-like super family cl45901
RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF ...
 133-214 1.31e-06

RWD, DRWD, and ELF domain family; The family includes the RWD, double-RWD (DRWD), and ELF domains. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. The RWD domain (named after three major RWD-containing proteins: RING finger, WD-repeat-containing proteins and DEXD-like helicases) mediates protein-protein interactions in a variety of pathways in eukaryotes. The DRWD domain is responsible for substrate binding. It is involved in interactions with other kinetochore proteins. The ELF (N-terminal E2-like fold) domain is found in all Fanconi anemia group L protein (FANCL) homologs. It is required to promote efficient DNA damage-induced FANCD2 (Fanconi anemia group D2 protein) monoubiquitination in vertebrate cells.


The actual alignment was detected with superfamily member cd23784:

Pssm-ID: 480265  Cd Length: 87  Bit Score: 44.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335 133 NDAAEVALYERLLQLRVLPGASDVhdVRFVFG-----DDSR-CWIEVAMHGDH-VIGNSHPALDpkSRATLEHVLTVQGD 205
Cdd:cd23784    3 ELEKELELYEKLLGLRIEKTKDDR--LKFVFTnidpkDPEReFSFVLDVSEDDyKVVECDPPLE--DLDELLEELNETRD 78


                 ....*....
gi 398364335 206 LAAFLVVAR 214
Cdd:cd23784   79 FSAFLKRMR 87
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-148 2.68e-03

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335  22 AQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQST 101
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 398364335 102 LAAQSRELDSLLQQRGKECVQLRARWAAQSGNDAAEVALYERLLQLR 148
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
 
Name Accession Description Interval E-value
RWD_Spc25 cd23784
RWD domain of kinetochore protein Spc25 and related proteins; Spc25 is a component of the ...
 133-214 1.31e-06

RWD domain of kinetochore protein Spc25 and related proteins; Spc25 is a component of the nuclear division cycle 80 (NDC80) kinetochore complex, which is essential for the stable formation of kinetochore-microtubule anchoring and correct chromosome segregation during mitosis. NDC80 has two subcomplexes, NDC80/NUF2 which binds directly to microtubules, and Spc24/Spc25 which interacts with the kinetochore. The inner kinetochore centromere protein T (CENP-T) has been shown to interact directly with the Spc24/25 RWD domains; these RWD domains serve as interaction modules at the kinetochores.


Pssm-ID: 467646  Cd Length: 87  Bit Score: 44.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335 133 NDAAEVALYERLLQLRVLPGASDVhdVRFVFG-----DDSR-CWIEVAMHGDH-VIGNSHPALDpkSRATLEHVLTVQGD 205
Cdd:cd23784    3 ELEKELELYEKLLGLRIEKTKDDR--LKFVFTnidpkDPEReFSFVLDVSEDDyKVVECDPPLE--DLDELLEELNETRD 78


                 ....*....
gi 398364335 206 LAAFLVVAR 214
Cdd:cd23784   79 FSAFLKRMR 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-148 2.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335  22 AQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQST 101
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 398364335 102 LAAQSRELDSLLQQRGKECVQLRARWAAQSGNDAAEVALYERLLQLR 148
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 32-147 3.15e-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: 37.82  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335   32 ARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRtalqqqihaaQQATNTTREQWRSYHER-ESELSRRQST---LAAQSR 107
Cdd:pfam09787  52 LRQERDLLREEIQKLRGQIQQLRTELQELEAQQ----------QEEAESSREQLQELEEQlATERSARREAeaeLERLQE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 398364335  108 ELDSL--------------LQQRGKECVQLRARWAAQSGNDAAEVALYERLLQL 147
Cdd:pfam09787 122 ELRYLeeelrrskatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL 175
 
Name Accession Description Interval E-value
RWD_Spc25 cd23784
RWD domain of kinetochore protein Spc25 and related proteins; Spc25 is a component of the ...
 133-214 1.31e-06

RWD domain of kinetochore protein Spc25 and related proteins; Spc25 is a component of the nuclear division cycle 80 (NDC80) kinetochore complex, which is essential for the stable formation of kinetochore-microtubule anchoring and correct chromosome segregation during mitosis. NDC80 has two subcomplexes, NDC80/NUF2 which binds directly to microtubules, and Spc24/Spc25 which interacts with the kinetochore. The inner kinetochore centromere protein T (CENP-T) has been shown to interact directly with the Spc24/25 RWD domains; these RWD domains serve as interaction modules at the kinetochores.


Pssm-ID: 467646  Cd Length: 87  Bit Score: 44.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335 133 NDAAEVALYERLLQLRVLPGASDVhdVRFVFG-----DDSR-CWIEVAMHGDH-VIGNSHPALDpkSRATLEHVLTVQGD 205
Cdd:cd23784    3 ELEKELELYEKLLGLRIEKTKDDR--LKFVFTnidpkDPEReFSFVLDVSEDDyKVVECDPPLE--DLDELLEELNETRD 78


                 ....*....
gi 398364335 206 LAAFLVVAR 214
Cdd:cd23784   79 FSAFLKRMR 87
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-148 2.68e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335  22 AQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQST 101
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 398364335 102 LAAQSRELDSLLQQRGKECVQLRARWAAQSGNDAAEVALYERLLQLR 148
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 32-147 3.15e-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: 37.82  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364335   32 ARQQLQQFQAEMRQLHNQHQHLIDELQRLATQRtalqqqihaaQQATNTTREQWRSYHER-ESELSRRQST---LAAQSR 107
Cdd:pfam09787  52 LRQERDLLREEIQKLRGQIQQLRTELQELEAQQ----------QEEAESSREQLQELEEQlATERSARREAeaeLERLQE 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 398364335  108 ELDSL--------------LQQRGKECVQLRARWAAQSGNDAAEVALYERLLQL 147
Cdd:pfam09787 122 ELRYLeeelrrskatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL 175
 
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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