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Conserved domains on  [gi|766453913|gb|AJR78032|]
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Mad1p [Saccharomyces cerevisiae YJM248]

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 ...
83-747 4.75e-16

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: 82.10  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   83 LQLQKQTNILEKKYKATIDELEKALNDTKYLYE----SNDKLEQELKSLKERsansmndkdkciEELRTTLQNKDLEMET 158
Cdd:pfam05557  12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDresdRNQELQKRIRLLEKR------------EAEAEEALREQAELNR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  159 LRQQYDSKLSKVTNQCDHFKLEAESSHSLLMKyekeikrqsvDIKDLQHQVMEKDDELSSVkaskminshpNYSTEEFNE 238
Cdd:pfam05557  80 LKKKYLEALNKKLNEKESQLADAREVISCLKN----------ELSELRRQIQRAELELQST----------NSELEELQE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  239 --------LTEMNKMIQDQVQYTKELELANmQQANELKKLKQSQDTstfWKLENEKLQNKLSQLHVLESQYENLQLENID 310
Cdd:pfam05557 140 rldllkakASEAEQLRQNLEKQQSSLAEAE-QRIKELEFEIQSQEQ---DSEIVKNSKSELARIPELEKELERLREHNKH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  311 LKSKLTKWEIYNDSDDDDDNNVNNNDNNNNNKNDNNNDNNNDTSNNNNINNNNRTRNNIRNNPEEIIRDWKLTKKECLIL 390
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  391 ----TDMNDKLRLDNNNLKLLNDEMALERNQILDLNKNYENnivnLKRLNHELEQQKSLSFEECRLLREQLDGLHSAQNN 466
Cdd:pfam05557 296 keenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKR----HKALVRRLQRRVLLLTKERDGYRAILESYDKELTM 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  467 ALLEVENTETHASNKNVNEDMNNLIDTYKNKTEDLTNELKKLNDQLlsNSNDVETQRKKRKLTSDQIGL------NYSQR 540
Cdd:pfam05557 372 SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA--QTLERELQALRQQESLADPSYskeevdSLRRK 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  541 LNELQLENvsvsRELSKAQTTIQLLQEKLEKLTKLKEKKIRILQLRDGPFIKDQFIKKNKLRLLEKENA---DLLNELKK 617
Cdd:pfam05557 450 LETLELER----QRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlkRLLKKLED 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  618 NNPAVETVPISVYDSLNFELKQFEQEVFKSNKRFSRLKQVFNNKSLEFIDVVNSLLGFKLEFQQDGRVKIFSCF--KPEK 695
Cdd:pfam05557 526 DLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYaeHPDD 605
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 766453913  696 YLIADLNENT------LKSNLDADIEGwddLMNLWVEDRGQLPCFLATITLRLWeQRQ 747
Cdd:pfam05557 606 YLLFKLSGSNgstmqlLETPFSRTLEP---LIDLHLAAQKSIPAFLSALTLELF-SRQ 659
 
Name Accession Description Interval E-value
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
83-747 4.75e-16

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: 82.10  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   83 LQLQKQTNILEKKYKATIDELEKALNDTKYLYE----SNDKLEQELKSLKERsansmndkdkciEELRTTLQNKDLEMET 158
Cdd:pfam05557  12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDresdRNQELQKRIRLLEKR------------EAEAEEALREQAELNR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  159 LRQQYDSKLSKVTNQCDHFKLEAESSHSLLMKyekeikrqsvDIKDLQHQVMEKDDELSSVkaskminshpNYSTEEFNE 238
Cdd:pfam05557  80 LKKKYLEALNKKLNEKESQLADAREVISCLKN----------ELSELRRQIQRAELELQST----------NSELEELQE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  239 --------LTEMNKMIQDQVQYTKELELANmQQANELKKLKQSQDTstfWKLENEKLQNKLSQLHVLESQYENLQLENID 310
Cdd:pfam05557 140 rldllkakASEAEQLRQNLEKQQSSLAEAE-QRIKELEFEIQSQEQ---DSEIVKNSKSELARIPELEKELERLREHNKH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  311 LKSKLTKWEIYNDSDDDDDNNVNNNDNNNNNKNDNNNDNNNDTSNNNNINNNNRTRNNIRNNPEEIIRDWKLTKKECLIL 390
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  391 ----TDMNDKLRLDNNNLKLLNDEMALERNQILDLNKNYENnivnLKRLNHELEQQKSLSFEECRLLREQLDGLHSAQNN 466
Cdd:pfam05557 296 keenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKR----HKALVRRLQRRVLLLTKERDGYRAILESYDKELTM 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  467 ALLEVENTETHASNKNVNEDMNNLIDTYKNKTEDLTNELKKLNDQLlsNSNDVETQRKKRKLTSDQIGL------NYSQR 540
Cdd:pfam05557 372 SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA--QTLERELQALRQQESLADPSYskeevdSLRRK 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  541 LNELQLENvsvsRELSKAQTTIQLLQEKLEKLTKLKEKKIRILQLRDGPFIKDQFIKKNKLRLLEKENA---DLLNELKK 617
Cdd:pfam05557 450 LETLELER----QRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlkRLLKKLED 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  618 NNPAVETVPISVYDSLNFELKQFEQEVFKSNKRFSRLKQVFNNKSLEFIDVVNSLLGFKLEFQQDGRVKIFSCF--KPEK 695
Cdd:pfam05557 526 DLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYaeHPDD 605
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 766453913  696 YLIADLNENT------LKSNLDADIEGwddLMNLWVEDRGQLPCFLATITLRLWeQRQ 747
Cdd:pfam05557 606 YLLFKLSGSNgstmqlLETPFSRTLEP---LIDLHLAAQKSIPAFLSALTLELF-SRQ 659
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
62-305 2.57e-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: 47.74  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913    62 RQIQALQFKLNTLQNEYEIEKLQLQKQTNILEKKYK---ATIDELEKALNDTKYLYESNDKLEQELKSLKERSANSMNDK 138
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   139 DKCIEELRTTLQNKDLEMETLRQQYDSKLSKVTNQcdhfkleaesshsllmkyEKEIKRQSVDIKDLQHQVMEKDDELSS 218
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASL------------------NNEIERLEARLERLEDRRERLQQEIEE 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   219 VKASKminsHPNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDTstfwklENEKLQNKLSQLHVLE 298
Cdd:TIGR02168  426 LLKKL----EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA------AERELAQLQARLDSLE 495

                   ....*..
gi 766453913   299 SQYENLQ 305
Cdd:TIGR02168  496 RLQENLE 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
67-297 4.05e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  67 LQFKLNTLQNEYEIEKLQLQKQTNILEKKYKATIDELEKALNDTKYLYESNDKLEQELKSLKERSANsmndkdkcIEELR 146
Cdd:COG4717   40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE--------LEAEL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913 147 TTLQNKDLEMETLRQQYD--SKLSKVTNQCDHFKLEAESshslLMKYEKEIKRQSVDIKDLQHQVMEKDDELSSVKASKm 224
Cdd:COG4717  112 EELREELEKLEKLLQLLPlyQELEALEAELAELPERLEE----LEERLEELRELEEELEELEAELAELQEELEELLEQL- 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 766453913 225 inshpnySTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQsQDTSTFWKLENEKLQNKLSQLHVL 297
Cdd:COG4717  187 -------SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLL 251
 
Name Accession Description Interval E-value
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
83-747 4.75e-16

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: 82.10  E-value: 4.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   83 LQLQKQTNILEKKYKATIDELEKALNDTKYLYE----SNDKLEQELKSLKERsansmndkdkciEELRTTLQNKDLEMET 158
Cdd:pfam05557  12 SQLQNEKKQMELEHKRARIELEKKASALKRQLDresdRNQELQKRIRLLEKR------------EAEAEEALREQAELNR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  159 LRQQYDSKLSKVTNQCDHFKLEAESSHSLLMKyekeikrqsvDIKDLQHQVMEKDDELSSVkaskminshpNYSTEEFNE 238
Cdd:pfam05557  80 LKKKYLEALNKKLNEKESQLADAREVISCLKN----------ELSELRRQIQRAELELQST----------NSELEELQE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  239 --------LTEMNKMIQDQVQYTKELELANmQQANELKKLKQSQDTstfWKLENEKLQNKLSQLHVLESQYENLQLENID 310
Cdd:pfam05557 140 rldllkakASEAEQLRQNLEKQQSSLAEAE-QRIKELEFEIQSQEQ---DSEIVKNSKSELARIPELEKELERLREHNKH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  311 LKSKLTKWEIYNDSDDDDDNNVNNNDNNNNNKNDNNNDNNNDTSNNNNINNNNRTRNNIRNNPEEIIRDWKLTKKECLIL 390
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  391 ----TDMNDKLRLDNNNLKLLNDEMALERNQILDLNKNYENnivnLKRLNHELEQQKSLSFEECRLLREQLDGLHSAQNN 466
Cdd:pfam05557 296 keenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKR----HKALVRRLQRRVLLLTKERDGYRAILESYDKELTM 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  467 ALLEVENTETHASNKNVNEDMNNLIDTYKNKTEDLTNELKKLNDQLlsNSNDVETQRKKRKLTSDQIGL------NYSQR 540
Cdd:pfam05557 372 SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA--QTLERELQALRQQESLADPSYskeevdSLRRK 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  541 LNELQLENvsvsRELSKAQTTIQLLQEKLEKLTKLKEKKIRILQLRDGPFIKDQFIKKNKLRLLEKENA---DLLNELKK 617
Cdd:pfam05557 450 LETLELER----QRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlkRLLKKLED 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  618 NNPAVETVPISVYDSLNFELKQFEQEVFKSNKRFSRLKQVFNNKSLEFIDVVNSLLGFKLEFQQDGRVKIFSCF--KPEK 695
Cdd:pfam05557 526 DLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDVCYMLTGYQIDITTNSQYRLTSMYaeHPDD 605
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 766453913  696 YLIADLNENT------LKSNLDADIEGwddLMNLWVEDRGQLPCFLATITLRLWeQRQ 747
Cdd:pfam05557 606 YLLFKLSGSNgstmqlLETPFSRTLEP---LIDLHLAAQKSIPAFLSALTLELF-SRQ 659
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
58-300 7.20e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.73  E-value: 7.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913    58 GQSNRQIQALQFKLNTLQNEYEIEKLQLQkQTNILEKKYKATIDELEKALND------------------TKYLYESNDK 119
Cdd:pfam15921  579 GQHGRTAGAMQVEKAQLEKEINDRRLELQ-EFKILKDKKDAKIRELEARVSDlelekvklvnagserlraVKDIKQERDQ 657
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   120 LEQELKSlkerSANSMNDKDKCIEELRTTLQNKDLEMET----LRQQYDSKLSKVTNQCDHFK-LEAESSHSL--LMKYE 192
Cdd:pfam15921  658 LLNEVKT----SRNELNSLSEDYEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKsMEGSDGHAMkvAMGMQ 733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   193 KEIKRQSVDIKDLQHQVMEKDDELSSVKASK-MINSHPNYSTEEFNEL-TEMNKM------IQDQVQYTKElELANMQQA 264
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKhFLKEEKNKLSQELSTVaTEKNKMagelevLRSQERRLKE-KVANMEVA 812
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 766453913   265 NELKKLKQSQDTSTFWKLENEKLQNKLSQ-LHVLESQ 300
Cdd:pfam15921  813 LDKASLQFAECQDIIQRQEQESVRLKLQHtLDVKELQ 849
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
62-305 2.57e-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: 47.74  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913    62 RQIQALQFKLNTLQNEYEIEKLQLQKQTNILEKKYK---ATIDELEKALNDTKYLYESNDKLEQELKSLKERSANSMNDK 138
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   139 DKCIEELRTTLQNKDLEMETLRQQYDSKLSKVTNQcdhfkleaesshsllmkyEKEIKRQSVDIKDLQHQVMEKDDELSS 218
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASL------------------NNEIERLEARLERLEDRRERLQQEIEE 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   219 VKASKminsHPNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDTstfwklENEKLQNKLSQLHVLE 298
Cdd:TIGR02168  426 LLKKL----EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA------AERELAQLQARLDSLE 495

                   ....*..
gi 766453913   299 SQYENLQ 305
Cdd:TIGR02168  496 RLQENLE 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
80-320 5.27e-04

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: 43.51  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913    80 IEKLQLQKQTNILEKKYKATIDELEKAL--NDTKYLYESNDKLEQELKSLKERsansmndkdkcIEELRTTLQNKDLEME 157
Cdd:TIGR02168  202 LKSLERQAEKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEE-----------LEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   158 TLR-----------------QQYDSKLSKVTNQCDHFKLEAESSHSLLMKYEKEIKRQSVDIKDLQHQVMEKDDELSSVK 220
Cdd:TIGR02168  271 ELRlevseleeeieelqkelYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   221 ASKminshpnysTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQdtstfwKLENEKLQNKLSQLHVLESQ 300
Cdd:TIGR02168  351 EEL---------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI------ASLNNEIERLEARLERLEDR 415
                          250       260
                   ....*....|....*....|
gi 766453913   301 YENLQLENIDLKSKLTKWEI 320
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAEL 435
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
62-304 2.21e-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: 41.59  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913    62 RQIQALQFKLNTLQNEYEIEKL-QLQKQTNILEK---KYKATIDELEKALNDTKYLYESNDKLEQELKSLKERSANSMND 137
Cdd:TIGR02169  772 EDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   138 KDKCIEELRTTLQNKDLEMETLR---QQYDSKLSKVTNQCDHFKLEAESSHSLLMKYEKEIKRQSVDIKDLQHQVMEKDD 214
Cdd:TIGR02169  852 IEKEIENLNGKKEELEEELEELEaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913   215 ELSSVKASKminSHPNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDTstfWKLENEKLQNKLSQL 294
Cdd:TIGR02169  932 ELSEIEDPK---GEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDE---LKEKRAKLEEERKAI 1005
                          250
                   ....*....|
gi 766453913   295 HVLESQYENL 304
Cdd:TIGR02169 1006 LERIEEYEKK 1015
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
67-297 4.05e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  67 LQFKLNTLQNEYEIEKLQLQKQTNILEKKYKATIDELEKALNDTKYLYESNDKLEQELKSLKERSANsmndkdkcIEELR 146
Cdd:COG4717   40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE--------LEAEL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913 147 TTLQNKDLEMETLRQQYD--SKLSKVTNQCDHFKLEAESshslLMKYEKEIKRQSVDIKDLQHQVMEKDDELSSVKASKm 224
Cdd:COG4717  112 EELREELEKLEKLLQLLPlyQELEALEAELAELPERLEE----LEERLEELRELEEELEELEAELAELQEELEELLEQL- 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 766453913 225 inshpnySTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQsQDTSTFWKLENEKLQNKLSQLHVL 297
Cdd:COG4717  187 -------SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLL 251
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
59-276 8.26e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913  59 QSNRQIQALQFKLNTLQNEYEieklQLQKQTNILEKKykatIDELEKALNDTKylyESNDKLEQELKSLKERsansmndk 138
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEK----ALLKQLAALERR----IAALARRIRALE---QELAALEAELAELEKE-------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766453913 139 dkcIEELRTTL-QNKDLEMETLRQQY----DSKLSKVTNQCDhfKLEAESSHSLLMKYEKEIKRQSVDIKDLQHQVMEKD 213
Cdd:COG4942   92 ---IAELRAELeAQKEELAELLRALYrlgrQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 766453913 214 DELSSVKASKMinshpNYSTEEFNELTEMNKMIQDQVQYTKELELANMQQANELKKLKQSQDT 276
Cdd:COG4942  167 AELEAERAELE-----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
 
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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