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Conserved domains on  [gi|1622939062|ref|XP_028704206|]
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coiled-coil domain-containing protein 149 isoform X3 [Macaca mulatta]

Protein Classification

coiled-coil domain-containing family 149 protein( domain architecture ID 12102062)

coiled-coil domain-containing family 149 (CCDC149) protein is a DUF2353 domain-containing protein similar to Homo sapiens CCDC149

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
1-283 1.49e-120

Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.


:

Pssm-ID: 462902 [Multi-domain]  Cd Length: 314  Bit Score: 355.49  E-value: 1.49e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   1 MANQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789  31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  81 G---DEEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622939062 237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
 
Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
1-283 1.49e-120

Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.


Pssm-ID: 462902 [Multi-domain]  Cd Length: 314  Bit Score: 355.49  E-value: 1.49e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   1 MANQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789  31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  81 G---DEEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622939062 237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-195 8.85e-07

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: 51.60  E-value: 8.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGD--NKLLRMTIAKQRLGDEEIgvrhfaahEREDLVQQLERAKE 107
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaaNLRERLESLERRIAATER--------RLEDLEEQIEELSE 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  108 QIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                   ....*...
gi 1622939062  188 KYKNALER 195
Cdd:TIGR02168  933 GLEVRIDN 940
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
29-195 3.82e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEeigvRHFAAHEREDLVQQLERAKEQ 108
Cdd:COG4717    79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 109 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:COG4717   155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230

                  ....*...
gi 1622939062 188 KYKNALER 195
Cdd:COG4717   231 QLENELEA 238
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
46-184 1.22e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   46 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEEIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 113
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939062  114 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 184
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
mukB PRK04863
chromosome partition protein MukB;
31-195 3.09e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   31 RKQANLAQllRDSQDRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEEIGVRHFAAHE--REDLVQQLER 104
Cdd:PRK04863   506 REQRHLAE--QLQQLRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSE 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  105 AKEQIESLEH---DLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNL 181
Cdd:PRK04863   577 ARERRMALRQqleQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDE 649
                          170
                   ....*....|....
gi 1622939062  182 LKSNIAKYKNALER 195
Cdd:PRK04863   650 LAARKQALDEEIER 663
 
Name Accession Description Interval E-value
CC149 pfam09789
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ...
1-283 1.49e-120

Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.


Pssm-ID: 462902 [Multi-domain]  Cd Length: 314  Bit Score: 355.49  E-value: 1.49e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   1 MANQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRL 80
Cdd:pfam09789  31 MAEQLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLRDSREQNKCLRLEVEELRQKLNEAQGDIKLLREQIARQRL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  81 G---DEEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIID 157
Cdd:pfam09789 111 GgpdEGSISTRHFPLHEREELVKQLEKLRKKCQQLERDLQSVLDEKEELETERDAYKCKAHRLNHELNYILGGDESRIVD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 158 VDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLsedHGCSLPATPQ- 236
Cdd:pfam09789 191 IDALIMENRYLQERLKQLEEEKELAKQTLSKYKSMLEKKRNKGSLKLGNGSSGGLVISAKQVKELL---ESGSLSNTPQa 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622939062 237 SISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTL 283
Cdd:pfam09789 268 TISDLKSLCTALLETLNDKNLALSHQRKTNKILGNRVAELEKKLKTL 314
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-195 8.85e-07

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: 51.60  E-value: 8.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGD--NKLLRMTIAKQRLGDEEIgvrhfaahEREDLVQQLERAKE 107
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaaNLRERLESLERRIAATER--------RLEDLEEQIEELSE 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  108 QIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                   ....*...
gi 1622939062  188 KYKNALER 195
Cdd:TIGR02168  933 GLEVRIDN 940
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
29-195 3.82e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEeigvRHFAAHEREDLVQQLERAKEQ 108
Cdd:COG4717    79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE----LEALEAELAELPERLEELEER 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 109 IESLEHDLQasvdELQDVKEERSSYQDKVERLNQELNHILSGHENRII-DVDALCMENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:COG4717   155 LEELRELEE----ELEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELEELEEELE 230

                  ....*...
gi 1622939062 188 KYKNALER 195
Cdd:COG4717   231 QLENELEA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
30-195 4.57e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 4.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGdnklLRMTIAK-QRLGDEEIGVRHfAAHEREDLVQQLER---- 104
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE----RREALQRlAEYSWDEIDVAS-AEREIAELEAELERldas 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  105 ------AKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNH---ILSGHENRIIDVDALCMENRYLQERL--- 172
Cdd:COG4913    684 sddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALLEERFAAALGdav 763
                          170       180
                   ....*....|....*....|....*...
gi 1622939062  173 -----KQLHEEVNLLKSNIAKYKNALER 195
Cdd:COG4913    764 erelrENLEERIDALRARLNRAEEELER 791
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
4-187 6.52e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.35  E-value: 6.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   4 QLRERHQSLKKKYREMIDGDPSLPPEKRKqanLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDnkLLRMTIAKQRLGde 83
Cdd:pfam07888  91 QSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETE--LERMKERAKKAG-- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  84 eiGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCM 163
Cdd:pfam07888 164 --AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA----HRKEAENEALLE 237
                         170       180
                  ....*....|....*....|....
gi 1622939062 164 ENRYLQERLKQLHEEVNLLKSNIA 187
Cdd:pfam07888 238 ELRSLQERLNASERKVEGLGEELS 261
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
91-284 2.20e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  91 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRII----DVDALCM 163
Cdd:COG1196   230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELArleqDIARLEE 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 164 ENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALtgVLSAKQVQDLLSEDHGCSLPATpQSISDLKS 243
Cdd:COG1196   310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA--EAELAEAEEALLEAEAELAEAE-EELEELAE 386
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622939062 244 LATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
30-188 4.54e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 46.00  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLgevqgdnkllrmtiakqRLGDEEIGvrhfaaheredLVQQLErakEQI 109
Cdd:pfam06160 290 EKNLPEIEDYLEHAEEQNKELKEELERVQQSY-----------------TLNENELE-----------RVRGLE---KQL 338
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939062 110 ESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNIAK 188
Cdd:pfam06160 339 EELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3-284 1.53e-04

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: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   3 NQLRERHQSLKK------KYREMIDGdpslppEKRKQANLAQL-LRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI 75
Cdd:COG1196   196 GELERQLEPLERqaekaeRYRELKEE------LKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  76 AKQRLGDEEigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRI 155
Cdd:COG1196   270 EELRLELEE------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 156 IDVDALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLS--AKQVQDLLSEDHgcslpa 233
Cdd:COG1196   344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEelEEAEEALLERLE------ 417
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622939062 234 tpQSISDLKSLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG1196   418 --RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
3-198 1.96e-04

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: 43.60  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   3 NQLRERHQSLKKKYREMIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGD-----NKLLRMTIAK 77
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  78 QRLG------------DEEIGVRHFA-----AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERL 140
Cdd:COG4942   114 YRLGrqpplalllspeDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622939062 141 NQELNHILSGHENRIidvdalcmenRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 198
Cdd:COG4942   194 KAERQKLLARLEKEL----------AELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-195 3.66e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062    2 ANQLRERHQSLKKKYREMIDGDPSLPPEKRKQAnlAQLLRDSQDRNKhlgEEIKELQQRLGEvqgdnkllrmtiAKQRLG 81
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELR---AELARLEAELER------------LEARLD 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   82 DeeigvrhfAAHEREDLVQQLERAK-EQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDA 160
Cdd:COG4913    320 A--------LREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA 391
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622939062  161 LCMEnryLQERLKQLHEEVNLLKSNIAKYKNALER 195
Cdd:COG4913    392 LLEA---LEEELEALEEALAEAEAALRDLRRELRE 423
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
3-284 7.44e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 7.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   3 NQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgd 82
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN--- 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  83 EEIgvrhfaaherEDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELnhilsghENRIIDVDALC 162
Cdd:TIGR04523 440 SEI----------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL-------KSKEKELKKLN 502
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 163 MENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLSEDHgcslpatpQSISDLK 242
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN--------KEIEELK 574
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622939062 243 SLATALLETIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
91-284 7.83e-04

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: 41.67  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  91 AAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIidvdalcmenRYLQE 170
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQEL----------AALEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 171 RLKQLHEEVNLLKSNIAKYKNALERRkNSKGQGKSSSSALTGVLSAKQVQDLLSedhgcSLPATPQSISDLKSLATALLE 250
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVR-----RLQYLKYLAPARREQAEELRA 157
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622939062 251 TIHEKNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG4942   158 DLAELAALRAELEAERAELEALLAELEEERAALE 191
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-285 8.35e-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: 41.97  E-value: 8.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   30 KRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTI--AKQRLGDEEIGVRHF------AAHEREDLVQQ 101
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLeaeveqLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  102 LERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHenriidvDALCMENRYLQERLKQLHEEVNL 181
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-------DELRAELTLLNEEAANLRERLES 828
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  182 LKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQ--DLLSE--DHGCSLPATPQSISDLKSLATALLETIHEKNM 257
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieELESEleALLNERASLEEALALLRSELEELSEELRELES 908
                          250       260
                   ....*....|....*....|....*...
gi 1622939062  258 VIQHQRQTNKILGNRVAELEKKLRTLEV 285
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEV 936
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
99-284 9.76e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  99 VQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsgheNRIIDVDALCMENRYLQERLKQLHEE 178
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPER 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 179 VNLLKSNIAKYKNALERRKNSKGQgkssssaltgvlsAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIHEKNMV 258
Cdd:COG4717   148 LEELEERLEELRELEEELEELEAE-------------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
                         170       180
                  ....*....|....*....|....*.
gi 1622939062 259 IQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEAAA 240
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-198 1.09e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  27 PPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgdeeigvrhfaaHEREDLVQQLERAK 106
Cdd:COG4372    20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------------SELEQLEEELEELN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 107 EQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQLHEEVNLLKSNI 186
Cdd:COG4372    87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
                         170
                  ....*....|..
gi 1622939062 187 AKYKNALERRKN 198
Cdd:COG4372   167 AALEQELQALSE 178
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
52-313 1.12e-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: 41.29  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  52 EEIKELQQRLGEVQGDNKLLRMTIAKQRlgdeeiGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERS 131
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALK------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 132 SYQDKVERLNQELNHIL---------------------SGHENRIIDVDALcmeNRYLQERLKQLHEEVNLLKSNIAKYK 190
Cdd:COG4942    94 ELRAELEAQKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYL---APARREQAEELRADLAELAALRAELE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 191 NALERRKNSKGQGKSSSSALTgvlSAKQVQDLLSEDHGCSLPATPQSISDLKSLATALLETIheKNMVIQHQRQTNKILG 270
Cdd:COG4942   171 AERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEALI--ARLEAEAAAAAERTPA 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1622939062 271 NRVAELEKKLRtlevsglWSLPGlsyNVSVGFGRGKDTILFSD 313
Cdd:COG4942   246 AGFAALKGKLP-------WPVSG---RVVRRFGERDGGGGRNK 278
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
46-184 1.22e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.77  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   46 RNKHLGEEIKELQQRLGEVQGDNKLLRMTIA-----KQRLGDEEIGVRHFAAHERE--DLVQQ-----LERAKEQIESLE 113
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELEllnsiKPKLRDRKDALEEELRQLKQleDELEDcdpteLDRAKEKLKKLL 217
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939062  114 HDLQASVDELQDVKEERSSYQDKVERLNQELNHIlsghENRIIDVDALCMENRYLQER-LKQLHEEVNLLKS 184
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSEL----NTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQS 285
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
29-124 1.50e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 41.21  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  29 EKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDEEIGV--RHFAAHERE--DLVQQLER 104
Cdd:pfam05622 302 YRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLlkQKLEEHLEKlhEAQSELQK 381
                          90       100
                  ....*....|....*....|....
gi 1622939062 105 AKEQIESLEHDLQAS----VDELQ 124
Cdd:pfam05622 382 KKEQIEELEPKQDSNlaqkIDELQ 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
96-286 1.58e-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: 41.20  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   96 EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHENRIIDVDALCMENRYLQERLKQL 175
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  176 HEEVNLLKSNIAKyknaLERRKNSKGQGKSSSSALTGVLsAKQVQDLLSEdhgcsLPATPQSISDLKSLATALLETIHE- 254
Cdd:TIGR02168  315 ERQLEELEAQLEE----LESKLDELAEELAELEEKLEEL-KEELESLEAE-----LEELEAELEELESRLEELEEQLETl 384
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1622939062  255 KNMVIQHQRQTNKIlGNRVAELEKKLRTLEVS 286
Cdd:TIGR02168  385 RSKVAQLELQIASL-NNEIERLEARLERLEDR 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-140 2.34e-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: 40.81  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062    2 ANQLRERHQSLKKKYREMIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQgdNKLLRMTIAKQRLG 81
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASL---NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEE 448
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939062   82 DEEigvrhfAAHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERL 140
Cdd:TIGR02168  449 LEE------LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
4-288 2.68e-03

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: 40.49  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   4 QLRERHQSLKKKYREMIDGDPSLppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGDE 83
Cdd:pfam05557  59 LLEKREAEAEEALREQAELNRLK---KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  84 EIGVRHFAAHERedlVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDK---VERLNQELNhilsghenRIIDVDA 160
Cdd:pfam05557 136 ELQERLDLLKAK---ASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDseiVKNSKSELA--------RIPELEK 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 161 LCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGVLSAKQVQDLLSEDHGCSLPaTPQSISd 240
Cdd:pfam05557 205 ELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLR-SPEDLS- 282
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622939062 241 lkslatalletihekNMVIQHQrQTNKILGNRVAELEKKLRTLEVSGL 288
Cdd:pfam05557 283 ---------------RRIEQLQ-QREIVLKEENSSLTSSARQLEKARR 314
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3-148 2.85e-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: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062    3 NQLRERHQSLKKKYREMidgdpslppeKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRLGD 82
Cdd:TIGR02169  850 KSIEKEIENLNGKKEEL----------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   83 EEIGVRHFAAHER---------------------EDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLN 141
Cdd:TIGR02169  920 SELKAKLEALEEElseiedpkgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999

                   ....*..
gi 1622939062  142 QELNHIL 148
Cdd:TIGR02169 1000 EERKAIL 1006
mukB PRK04863
chromosome partition protein MukB;
31-195 3.09e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   31 RKQANLAQllRDSQDRNKHlgeeiKELQQRLGEVQGDNKLLRMtiAKQRLG----DEEIGVRHFAAHE--REDLVQQLER 104
Cdd:PRK04863   506 REQRHLAE--QLQQLRMRL-----SELEQRLRQQQRAERLLAE--FCKRLGknldDEDELEQLQEELEarLESLSESVSE 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  105 AKEQIESLEH---DLQASVDELQDVKEERSSYQDKVERLNQELNHILSGHEnriiDVDALcMENryLQERLKQLHEEVNL 181
Cdd:PRK04863   577 ARERRMALRQqleQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ----DVTEY-MQQ--LLERERELTVERDE 649
                          170
                   ....*....|....
gi 1622939062  182 LKSNIAKYKNALER 195
Cdd:PRK04863   650 LAARKQALDEEIER 663
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
3-225 3.89e-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: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   3 NQLRERHQSLKKKYREmidgdpslppEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQGDNKLLRMTIAKQRlgd 82
Cdd:COG1196   277 EELELELEEAQAEEYE----------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--- 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  83 EEIGVRHFAAHEREDLVQQLERAKEQIESLEHDLQASVDELQdvkEERSSYQDKVERLNQELNHILSGHENRIIDVDALC 162
Cdd:COG1196   344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622939062 163 MENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKNSKGQGKSSSSALTGV--LSAKQVQDLLSE 225
Cdd:COG1196   421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEaaLLEAALAELLEE 485
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-198 4.56e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   3 NQLRERHQSLKKKYREMIDGDPSLPPEKRKQANLAQLLRdsqdRNKHLGEEIKELQQRLGEVQGDNKLLrmtiaKQRLGD 82
Cdd:PRK03918  193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKL-----EEKIRE 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  83 EEigvrhfaaHEREDLVQQLERAKEQIESLEhDLQASVDELQDVKEERSSYQDKVERLNQELNHI---LSGHENRIIDVD 159
Cdd:PRK03918  264 LE--------ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLeeeINGIEERIKELE 334
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622939062 160 ALCMENRYLQERLKQLHEEVNLLKSNIAKYKNALERRKN 198
Cdd:PRK03918  335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
8-284 6.29e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062   8 RHQSLKKKYREMIdgdpsLPPEKRKQANLAQLLRDSQDRNKHLGEEIKELQQRLGEVQgdNKLLRMTIAKQRLGDEEIGV 87
Cdd:TIGR04523 193 KNKLLKLELLLSN-----LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT--TEISNTQTQLNQLKDEQNKI 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  88 RHfaahEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEErssyqdKVERLNQELNHILSGHENRIIDVDALCMENRY 167
Cdd:TIGR04523 266 KK----QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ------KEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062 168 ----LQERLKQLHEEVNLLKSNIAKYKNALERRKNskgqgkssssaltgvlsakQVQDLLSEDHGCSlpatpQSISDLKS 243
Cdd:TIGR04523 336 iisqLNEQISQLKKELTNSESENSEKQRELEEKQN-------------------EIEKLKKENQSYK-----QEIKNLES 391
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1622939062 244 LATALletihekNMVIQHQRQTNKILGNRVAELEKKLRTLE 284
Cdd:TIGR04523 392 QINDL-------ESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
TraB_PrgY_gumN pfam01963
TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora ...
23-172 6.34e-03

TraB/PrgY/gumN family; This entry includes Tiki1/2 from humans, TraB/PrgY from the gut flora Enterococcusfaecalis and gumN from the plant pathogen Xanthomonas. Tiki1 is homologous to TraB/PrgY. They have a pair of widely spaced GX2H motifs and a conserved glutamate. From the structural study, this group of proteins have been identified as an ancient metalloprotease clan with a common protein architecture (cobbled from the folds of the EreA/ChaN/PMT group) that mediates proteolytic activities. Tiki1 is a membrane-associated protease that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. TraB/PrgY is an inhibitor peptide that may act as a protease to inactivate the mating pheromone.


Pssm-ID: 426534  Cd Length: 262  Bit Score: 38.49  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  23 DPSLPPEKRKQANLAQLLRDSQDRN--KHLGEE-IKELQQRLGEVQ-GDNKLLRM------------TIAKQRLGDEEIG 86
Cdd:pfam01963  47 DLSRYTDPATQAALPKLGLLPDGKTlsDLLSPElYARLQKALAKRGlPLAALDRMkpwlaalllslaELAKQKAGLDPDL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939062  87 V-RHFA--AHEREDLVQQLERAKEQIESLEHDLQASVDELQDVKEERSSYQDKVERLnqeLNHILSGHENRIIDVDALCM 163
Cdd:pfam01963 127 VdRYLAktAKRAGKPVGGLETVEEQLALLSLPDEEQLEMLEETLDELEKGEDLLETL---VEAWAEGDLEALELEAELKE 203

                  ....*....
gi 1622939062 164 ENRYLQERL 172
Cdd:pfam01963 204 AYPELYEVL 212
 
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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