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Conserved domains on  [gi|1622921859|ref|XP_028701326|]
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mitotic spindle assembly checkpoint protein MAD1 isoform X3 [Macaca mulatta]

Protein Classification

mitotic spindle assembly checkpoint protein MAD1( domain architecture ID 1000521)

mitotic spindle assembly checkpoint protein MAD1 is a component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MAD super family cl37733
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1-306 2.94e-117

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


The actual alignment was detected with superfamily member pfam05557:

Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 351.74  E-value: 2.94e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   1 MRAILGSYDSELTSAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQS 80
Cdd:pfam05557 358 YRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPS 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  81 FlfSREEVDTLRLKVEELEGERRRLEEEKRMLEAQLERRVLQGDYDQSRTKVLHMSLNPASVARQRLREDHSQLQAECER 160
Cdd:pfam05557 438 Y--SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIER 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859 161 LRGLLRAMErggtvpTDLEAAAASLPSS-----KEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITT 235
Cdd:pfam05557 516 LKRLLKKLE------DDLEQVLRLPETTstmnfKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITT 589
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622921859 236 ENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRHQDSIPAFLSSLTLELFSRQT 306
Cdd:pfam05557 590 NSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLIDLHLAAQKSIPAFLSALTLELFSRQT 660
 
Name Accession Description Interval E-value
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1-306 2.94e-117

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 351.74  E-value: 2.94e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   1 MRAILGSYDSELTSAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQS 80
Cdd:pfam05557 358 YRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPS 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  81 FlfSREEVDTLRLKVEELEGERRRLEEEKRMLEAQLERRVLQGDYDQSRTKVLHMSLNPASVARQRLREDHSQLQAECER 160
Cdd:pfam05557 438 Y--SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIER 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859 161 LRGLLRAMErggtvpTDLEAAAASLPSS-----KEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITT 235
Cdd:pfam05557 516 LKRLLKKLE------DDLEQVLRLPETTstmnfKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITT 589
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622921859 236 ENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRHQDSIPAFLSSLTLELFSRQT 306
Cdd:pfam05557 590 NSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLIDLHLAAQKSIPAFLSALTLELFSRQT 660
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-217 2.25e-03

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: 39.65  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   40 AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEVDTLRLKVEELEGERRRLEEEKRMLEAQLERR 119
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  120 V-----LQGDYDQSRTKVLHMSLNPASVARQRLREDHSQLQAECERLRGLLRAMERggtvptDLEAAAASLPSSK-EVAE 193
Cdd:TIGR02168  420 QqeieeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ------ALDAAERELAQLQaRLDS 493
                          170       180
                   ....*....|....*....|....
gi 1622921859  194 LKKQVESAELKNQRLKEVFQTKIQ 217
Cdd:TIGR02168  494 LERLQENLEGFSEGVKALLKNQSG 517
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-222 6.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   40 AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEVDTLRLKVEELEGERRRLEEEK-----RMLEA 114
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  115 QLERrvLQGDYDQSRTKvlhmsLNPASVARQRLREDHSQLQAECERLRGLLRAMERGGTVPT------DLEAAAASLPSS 188
Cdd:COG4913    693 QLEE--LEAELEELEEE-----LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleeRFAAALGDAVER 765
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1622921859  189 KEVAELKKQVESAELKNQRLKEVFQTKIQEFRKA 222
Cdd:COG4913    766 ELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
 
Name Accession Description Interval E-value
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1-306 2.94e-117

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 351.74  E-value: 2.94e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   1 MRAILGSYDSELTSAEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQS 80
Cdd:pfam05557 358 YRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPS 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  81 FlfSREEVDTLRLKVEELEGERRRLEEEKRMLEAQLERRVLQGDYDQSRTKVLHMSLNPASVARQRLREDHSQLQAECER 160
Cdd:pfam05557 438 Y--SKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIER 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859 161 LRGLLRAMErggtvpTDLEAAAASLPSS-----KEVAELKKQVESAELKNQRLKEVFQTKIQEFRKACYTLTGYQIDITT 235
Cdd:pfam05557 516 LKRLLKKLE------DDLEQVLRLPETTstmnfKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITT 589
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622921859 236 ENQYRLTSLYAEHPGDCLIFKATSPSGSKMQLLETEFSHTVGELIEVHLRHQDSIPAFLSSLTLELFSRQT 306
Cdd:pfam05557 590 NSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLIDLHLAAQKSIPAFLSALTLELFSRQT 660
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
40-217 2.25e-03

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: 39.65  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   40 AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEVDTLRLKVEELEGERRRLEEEKRMLEAQLERR 119
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  120 V-----LQGDYDQSRTKVLHMSLNPASVARQRLREDHSQLQAECERLRGLLRAMERggtvptDLEAAAASLPSSK-EVAE 193
Cdd:TIGR02168  420 QqeieeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ------ALDAAERELAQLQaRLDS 493
                          170       180
                   ....*....|....*....|....
gi 1622921859  194 LKKQVESAELKNQRLKEVFQTKIQ 217
Cdd:TIGR02168  494 LERLQENLEGFSEGVKALLKNQSG 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
15-221 3.39e-03

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: 39.27  E-value: 3.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   15 AEYSPQLTRRMREAEDMVQKVHSHSAEMEAQLSQALEELGGQKQRADMLEMEL--------------KMLKSQSSSAEQS 80
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerlESLERRIAATERR 839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   81 FLFSREEVDTLRLKVEELEGERRRLEEEKRMLEAQLE------------RRVLQGDYDQSRTKVLHMS--LNPASVARQR 146
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallnerasleeaLALLRSELEELSEELRELEskRSELRRELEE 919
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  147 LREDHSQLQAECERLRGLL-----RAMERGGTVPTDLEAAAASLPSskEVAELKKQVESAELKNQRLKEVFQTKIQEFRK 221
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIdnlqeRLSEEYSLTLEEAEALENKIED--DEEEARRRLKRLENKIKELGPVNLAAIEEYEE 997
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
40-222 6.00e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859   40 AEMEAQLSQALEELGGQKQRADMLEMELKMLKSQSSSAEQSFLFSREEVDTLRLKVEELEGERRRLEEEK-----RMLEA 114
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlAALEE 692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622921859  115 QLERrvLQGDYDQSRTKvlhmsLNPASVARQRLREDHSQLQAECERLRGLLRAMERGGTVPT------DLEAAAASLPSS 188
Cdd:COG4913    693 QLEE--LEAELEELEEE-----LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELralleeRFAAALGDAVER 765
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1622921859  189 KEVAELKKQVESAELKNQRLKEVFQTKIQEFRKA 222
Cdd:COG4913    766 ELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
 
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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