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Conserved domains on  [gi|1314817969|ref|NP_001345956|]
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mitotic spindle assembly checkpoint protein MAD1 isoform b [Mus musculus]

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 ...
27-292 3.29e-106

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: 322.85  E-value: 3.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  27 SVSQAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSfcKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKL 106
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYS--KEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 107 TLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVES 186
Cdd:pfam05557 475 CLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 187 AELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELI 266
Cdd:pfam05557 555 AELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLI 634
                         250       260
                  ....*....|....*....|....*.
gi 1314817969 267 ELHLLQQDSIPAFLSALTIELFSRQT 292
Cdd:pfam05557 635 DLHLAAQKSIPAFLSALTLELFSRQT 660
 
Name Accession Description Interval E-value
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
27-292 3.29e-106

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: 322.85  E-value: 3.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  27 SVSQAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSfcKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKL 106
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYS--KEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 107 TLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVES 186
Cdd:pfam05557 475 CLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 187 AELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELI 266
Cdd:pfam05557 555 AELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLI 634
                         250       260
                  ....*....|....*....|....*.
gi 1314817969 267 ELHLLQQDSIPAFLSALTIELFSRQT 292
Cdd:pfam05557 635 DLHLAAQKSIPAFLSALTLELFSRQT 660
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-207 7.26e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   30 QAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVD--ALRLKVEELEGERSRLEQEKQVLemqmEKLT 107
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDL----AALE 691
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  108 LQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIP------ADLEAASSLPSSKEVAE-L 180
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleERFAAALGDAVERELREnL 771
                          170       180
                   ....*....|....*....|....*..
gi 1314817969  181 RKQVESAELKNQRLKEVFQTKIQEFRK 207
Cdd:COG4913    772 EERIDALRARLNRAEEELERAMRAFNR 798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-196 1.14e-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: 46.59  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   30 QAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQV-------LEMQ 102
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlanLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  103 MEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGgpiPADLEAAsSLPSSKEVAELRK 182
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR---LEELEEQ-LETLRSKVAQLEL 393
                          170
                   ....*....|....
gi 1314817969  183 QVESAELKNQRLKE 196
Cdd:TIGR02168  394 QIASLNNEIERLEA 407
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-188 4.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  32 QLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGD 111
Cdd:PRK02224  238 EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 112 YNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHAL-ERGGPIPADLEAASSLPSSKE--VAELRKQVESAE 188
Cdd:PRK02224  318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELrEEAAELESELEEAREAVEDRReeIEELEEEIEELR 397
 
Name Accession Description Interval E-value
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
27-292 3.29e-106

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: 322.85  E-value: 3.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  27 SVSQAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSfcKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKL 106
Cdd:pfam05557 397 EEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYS--KEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 107 TLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIPADLEAASSLPSSKEVAELRKQVES 186
Cdd:pfam05557 475 CLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 187 AELKNQRLKEVFQTKIQEFRKVCYTLTGYQIDVTTESQYRLTSRYAEHQTDCLIFKATGPSGSKMQLLETEFSRSVPELI 266
Cdd:pfam05557 555 AELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYAEHPDDYLLFKLSGSNGSTMQLLETPFSRTLEPLI 634
                         250       260
                  ....*....|....*....|....*.
gi 1314817969 267 ELHLLQQDSIPAFLSALTIELFSRQT 292
Cdd:pfam05557 635 DLHLAAQKSIPAFLSALTLELFSRQT 660
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-207 7.26e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 7.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   30 QAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVD--ALRLKVEELEGERSRLEQEKQVLemqmEKLT 107
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDL----AALE 691
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  108 LQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGGPIP------ADLEAASSLPSSKEVAE-L 180
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleERFAAALGDAVERELREnL 771
                          170       180
                   ....*....|....*....|....*..
gi 1314817969  181 RKQVESAELKNQRLKEVFQTKIQEFRK 207
Cdd:COG4913    772 EERIDALRARLNRAEEELERAMRAFNR 798
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-196 1.14e-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: 46.59  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   30 QAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQV-------LEMQ 102
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlanLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  103 MEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERGgpiPADLEAAsSLPSSKEVAELRK 182
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR---LEELEEQ-LETLRSKVAQLEL 393
                          170
                   ....*....|....
gi 1314817969  183 QVESAELKNQRLKE 196
Cdd:TIGR02168  394 QIASLNNEIERLEA 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-206 1.68e-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: 46.20  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   30 QAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQ 109
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  110 GDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERggpipadleaasslpsskEVAELRKQVESAEL 189
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR------------------ELEELREKLAQLEL 929
                          170
                   ....*....|....*..
gi 1314817969  190 KNQRLKEVFQTKIQEFR 206
Cdd:TIGR02168  930 RLEGLEVRIDNLQERLS 946
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
33-197 7.53e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  33 LSQALEELgvqKQRADTLEMELKMLKAQTSSAESSFSfcKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQgdy 112
Cdd:COG2433   378 IEEALEEL---IEKELPEEEPEAEREKEHEERELTEE--EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE--- 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 113 nqsrtkvlhmslnpISMARQRQHEDHdRLQEECERLRGLVHALERggpipadleaasslpsskEVAELRKQVESAELKNQ 192
Cdd:COG2433   450 --------------LSEARSEERREI-RKDREISRLDREIERLER------------------ELEEERERIEELKRKLE 496

                  ....*
gi 1314817969 193 RLKEV 197
Cdd:COG2433   497 RLKEL 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-207 9.43e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 9.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  31 AQLSQALEELGVQKQRADTLEMELKMLKAQTSSAEssfsfckEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQG 110
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELE-------AELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 111 DYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERggpipadlEAASSLPSSKEVAELRKQVESAELK 190
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE--------ELEEAEAELAEAEEALLEAEAELAE 376
                         170
                  ....*....|....*..
gi 1314817969 191 NQRLKEVFQTKIQEFRK 207
Cdd:COG1196   377 AEEELEELAEELLEALR 393
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
28-193 9.63e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 9.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   28 VSQAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGER-SRLEQEKQVLEMQMEKL 106
Cdd:COG4913    278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEER 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  107 TLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALErggpipADLEAASSlPSSKEVAELRKQVES 186
Cdd:COG4913    358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL------AEAEAALR-DLRRELRELEAEIAS 430

                   ....*..
gi 1314817969  187 aeLKNQR 193
Cdd:COG4913    431 --LERRK 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
29-157 1.63e-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: 40.05  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   29 SQAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGE----RSRLEQEKQVLEM--- 101
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKlkr 399
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1314817969  102 QMEKLTLQGDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALER 157
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-237 4.15e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 4.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969   81 KVEELEGERSRLEQEKQVLEMQMEKLTLQGDYNQSRtkvlHMSLNPISMARQRQhEDHDRLQEECERLRGLVHALERGgp 160
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQER----REALQRLAEYSWDE-IDVASAEREIAELEAELERLDAS-- 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  161 iPADLEAAsslpsSKEVAELRKQVESAELKNQRLKE---VFQTKIQEFRKVC----YTLTGYQIDVTTESQYRLTSRYAE 233
Cdd:COG4913    684 -SDDLAAL-----EEQLEELEAELEELEEELDELKGeigRLEKELEQAEEELdelqDRLEAAEDLARLELRALLEERFAA 757

                   ....
gi 1314817969  234 HQTD 237
Cdd:COG4913    758 ALGD 761
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-188 4.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  32 QLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGD 111
Cdd:PRK02224  238 EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 112 YNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHAL-ERGGPIPADLEAASSLPSSKE--VAELRKQVESAE 188
Cdd:PRK02224  318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELrEEAAELESELEEAREAVEDRReeIEELEEEIEELR 397
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
30-204 7.66e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  30 QAQLSQALEELGVQKQRADTLEMELKMLKAQTSSAESSFSFCKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQ 109
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 110 GDYNQSRTKVLHMSLNPISMARQRQHEDHDRLQEECERLRGLVHALERggpipADLEAASSLpssKEVAELRKQVESAEL 189
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE-----ALLEAEAEL---AEAEEELEELAEELL 389
                         170
                  ....*....|....*
gi 1314817969 190 KNQRLKEVFQTKIQE 204
Cdd:COG1196   390 EALRAAAELAAQLEE 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
44-204 7.72e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 7.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969  44 KQRADTLEMELKMLKAQTSSAESSFSfcKEEVDALRLKVEELEGERSRLEQEKQVLEMQMEKLTLQGDYNQSRTKVLHMS 123
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEEL--EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1314817969 124 LNPISMARQRQHEDHDRLQEECERLRGLVHALErggpipADLEAAsslpsSKEVAELRKQVESAELKNQRLKEVFQTKIQ 203
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELE------EELEEL-----EEELEELEEELEEAEEELEEAEAELAEAEE 365

                  .
gi 1314817969 204 E 204
Cdd:COG1196   366 A 366
 
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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