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Conserved domains on  [gi|1004350211|ref|NP_001307902|]
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golgin-45 isoform 1 [Homo sapiens]

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

Gene Ontology:  GO:0051301|GO:0045787

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 ...
 181-226 1.78e-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: 44.48  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1004350211 181 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 226
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-260 2.41e-06

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: 49.91  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  121 KELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLqyhfERLAREKNQLILENEALGRNTAQ 200
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL----EQLEREIERLERELEERERRRAR 363

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004350211  201 LSEQLERMSIQCDVWRSKFLA----SRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQE 260
Cdd:COG4913    364 LEALLAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
 
Name Accession Description Interval E-value
DASH_Hsk3 pfam08227
DASH complex subunit Hsk3 like; The DASH complex is a ~10 subunit microtubule-binding complex ...
 181-226 1.78e-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: 44.48  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1004350211 181 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 226
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-260 2.41e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  121 KELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLqyhfERLAREKNQLILENEALGRNTAQ 200
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL----EQLEREIERLERELEERERRRAR 363

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004350211  201 LSEQLERMSIQCDVWRSKFLA----SRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQE 260
Cdd:COG4913    364 LEALLAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-271 2.15e-05

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  121 KELSEVKNVLEKLKNSERRLLQDKEGLSNQL-RVQTEVNRELKKLLVASVGD-DLQYHFERLAREKNQLILENEALGRNT 198
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLaRLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004350211  199 AQLSEQLERMSIQCDVWRSkflasrvmadELTNSRAALQRQNRDAHgaiqDLLSEREQFRQEMIATQKLLEEL 271
Cdd:TIGR02168  785 EELEAQIEQLKEELKALRE----------ALDELRAELTLLNEEAA----NLRERLESLERRIAATERRLEDL 843
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-250 7.47e-04

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: 41.70  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  132 KLKNSERRLLQDKEGL--SNQLRVQTEVNR-ELKKLLVASVGDD--LQYHFERLAREKNQLILENEALGRNTAQLSEQLE 206
Cdd:pfam01576  834 KLKNLEAELLQLQEDLaaSERARRQAQQERdELADEIASGASGKsaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR 913

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1004350211  207 RMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDL 250
Cdd:pfam01576  914 KSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 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 ...
 181-226 1.78e-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: 44.48  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1004350211 181 AREKNQLILENEALGRNTAQLSEQLERMSIQCDVwrSKFLASRVMA 226
Cdd:pfam08227   1 QRQYSHLASQLAQLQANLADTEELLRMTSEQANS--IRKLGKYHAS 44
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-260 2.41e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  121 KELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLVASVGDDLqyhfERLAREKNQLILENEALGRNTAQ 200
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL----EQLEREIERLERELEERERRRAR 363

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004350211  201 LSEQLERMSIQCDVWRSKFLA----SRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQE 260
Cdd:COG4913    364 LEALLAALGLPLPASAEEFAAlraeAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-271 2.15e-05

chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  121 KELSEVKNVLEKLKNSERRLLQDKEGLSNQL-RVQTEVNRELKKLLVASVGD-DLQYHFERLAREKNQLILENEALGRNT 198
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLaRLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004350211  199 AQLSEQLERMSIQCDVWRSkflasrvmadELTNSRAALQRQNRDAHgaiqDLLSEREQFRQEMIATQKLLEEL 271
Cdd:TIGR02168  785 EELEAQIEQLKEELKALRE----------ALDELRAELTLLNEEAA----NLRERLESLERRIAATERRLEDL 843
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-272 9.37e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211 122 ELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLvasvgddlqyhfERLAREKNQLILENEALGRNTAQL 201
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL------------EELEEELAELEEELEELEEELEEL 342

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004350211 202 SEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQEMIATQKLLEELL 272
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 120-276 5.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211 120 NKELSEVKNVLEKLKNSERRLLQDKEGLSNQLRVQTEVNRELKKLLvasvgddlqyhfERLAREKNQLILENEALGRNTA 199
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL------------EELEEELEEAEEELEEAEAELA 361

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004350211 200 QLSEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDLLSEREQFRQEMIATQKLLEELLVSLQ 276
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 132-250 7.47e-04

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: 41.70  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  132 KLKNSERRLLQDKEGL--SNQLRVQTEVNR-ELKKLLVASVGDD--LQYHFERLAREKNQLILENEALGRNTAQLSEQLE 206
Cdd:pfam01576  834 KLKNLEAELLQLQEDLaaSERARRQAQQERdELADEIASGASGKsaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR 913

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1004350211  207 RMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHGAIQDL 250
Cdd:pfam01576  914 KSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 86-261 2.07e-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: 40.44  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211   86 AAITHDIPNKNTKVKSLGhhkgeflgqSEGVIEPNKELSEVKNVLEKLKNSERRLLQDKEGLSNQLRvQTEVNRELKKLL 165
Cdd:TIGR02169  268 EEIEQLLEELNKKIKDLG---------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-KLEAEIDKLLAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004350211  166 VASVGDDLqyhfERLAREKNQLILENEALGRNTAQLSEQLERMSIQCDVWRSKFLASRVMADELTNSRAALQRQNRDAHG 245
Cdd:TIGR02169  338 IEELEREI----EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413

                          170
                   ....*....|....*.
gi 1004350211  246 AIQDLLSEREQFRQEM 261
Cdd:TIGR02169  414 ELQRLSEELADLNAAI 429
 
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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