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Conserved domains on  [gi|237649005|ref|NP_001153680|]
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golgin-45 isoform b [Mus musculus]

Protein Classification

DASH complex subunit HSK3 family protein( domain architecture ID 10548802)

DASH complex subunit HSK3 is a component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 184-229 2.56e-06

DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. This family also includes several higher eukaryotic proteins. However, other DASH subunits do not appear to be conserved in higher eukaryotes.


:

Pssm-ID: 429874 [Multi-domain]  Cd Length: 45  Bit Score: 44.09  E-value: 2.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 237649005  184 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 229
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
123-269 9.80e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005  123 RKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEINRELKKLLVASVGDDpqyhFERLAREKNQLILENEALGRNTA 202
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR----LEQLEREIERLERELEERERRRA 362

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237649005  203 QLSEQLERMSIQCDVWRSKFLA----SRVMADELTNFRVVLQRQNRDAQSAIQDLLSEREQFRQEMTSTQK 269
Cdd:COG4913   363 RLEALLAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
 
Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 184-229 2.56e-06

DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. This family also includes several higher eukaryotic proteins. However, other DASH subunits do not appear to be conserved in higher eukaryotes.


Pssm-ID: 429874 [Multi-domain]  Cd Length: 45  Bit Score: 44.09  E-value: 2.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 237649005  184 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 229
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
123-269 9.80e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005  123 RKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEINRELKKLLVASVGDDpqyhFERLAREKNQLILENEALGRNTA 202
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR----LEQLEREIERLERELEERERRRA 362

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237649005  203 QLSEQLERMSIQCDVWRSKFLA----SRVMADELTNFRVVLQRQNRDAQSAIQDLLSEREQFRQEMTSTQK 269
Cdd:COG4913   363 RLEALLAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-274 3.36e-03

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: 39.67  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005    89 AAITHDIPTKNTKVKSLGHHReelhnQAEVvtdpRKELSEVKKVLEKLKNSERRLLQDKEGLSNQLR-VQTEINRELKKL 167
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEE-----QLRV----KEKIGELEAEIASLERSIAEKERELEDAEERLAkLEAEIDKLLAEI 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005   168 lvasvgDDPQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQRQNRDAQ 247
Cdd:TIGR02169  339 ------EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412

                          170       180
                   ....*....|....*....|....*..
gi 237649005   248 SAIQDLLSEREQFRQEMTSTQKFLEEL 274
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINEL 439
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 123-253 7.72e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.62  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005   123 RKE-LSEVKKVLEKLKNSERRLLQDKEGL--SNQLRVQTEINR-ELKKLLVASVGDDPQYHFE--RLAREKNQLILENEA 196
Cdd:pfam01576  821 RDEiLAQSKESEKKLKNLEAELLQLQEDLaaSERARRQAQQERdELADEIASGASGKSALQDEkrRLEARIAQLEEELEE 900

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 237649005   197 LGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQRQNRDAQSAIQDL 253
Cdd:pfam01576  901 EQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
 
Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 184-229 2.56e-06

DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. This family also includes several higher eukaryotic proteins. However, other DASH subunits do not appear to be conserved in higher eukaryotes.


Pssm-ID: 429874 [Multi-domain]  Cd Length: 45  Bit Score: 44.09  E-value: 2.56e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 237649005  184 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 229
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
123-269 9.80e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005  123 RKELSEVKKVLEKLKNSERRLLQDKEGLSNQLRVQTEINRELKKLLVASVGDDpqyhFERLAREKNQLILENEALGRNTA 202
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR----LEQLEREIERLERELEERERRRA 362

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237649005  203 QLSEQLERMSIQCDVWRSKFLA----SRVMADELTNFRVVLQRQNRDAQSAIQDLLSEREQFRQEMTSTQK 269
Cdd:COG4913   363 RLEALLAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 109-279 2.66e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005 109 REELHNQAEVVTDPRKELSEVKKVLEKLKNSERRLLQDKEGLSNQL-RVQTEINRELKKLLVASVGDdpqyhfERLAREK 187
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLeELEEELAELEEELEELEEEL------EELEEEL 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005 188 NQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQRQNRDAQSAIQDLLSEREQFRQEMTST 267
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                        170
                 ....*....|..
gi 237649005 268 QKFLEELLVSLQ 279
Cdd:COG1196  427 EEALAELEEEEE 438
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 89-274 3.36e-03

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: 39.67  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005    89 AAITHDIPTKNTKVKSLGHHReelhnQAEVvtdpRKELSEVKKVLEKLKNSERRLLQDKEGLSNQLR-VQTEINRELKKL 167
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLGEEE-----QLRV----KEKIGELEAEIASLERSIAEKERELEDAEERLAkLEAEIDKLLAEI 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005   168 lvasvgDDPQYHFERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQRQNRDAQ 247
Cdd:TIGR02169  339 ------EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412

                          170       180
                   ....*....|....*....|....*..
gi 237649005   248 SAIQDLLSEREQFRQEMTSTQKFLEEL 274
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINEL 439
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 123-253 7.72e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.62  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649005   123 RKE-LSEVKKVLEKLKNSERRLLQDKEGL--SNQLRVQTEINR-ELKKLLVASVGDDPQYHFE--RLAREKNQLILENEA 196
Cdd:pfam01576  821 RDEiLAQSKESEKKLKNLEAELLQLQEDLaaSERARRQAQQERdELADEIASGASGKSALQDEkrRLEARIAQLEEELEE 900

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 237649005   197 LGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNFRVVLQRQNRDAQSAIQDL 253
Cdd:pfam01576  901 EQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
 
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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