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Conserved domains on  [gi|966923612|ref|XP_014979956|]
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kinetochore protein Nuf2 isoform X1 [Macaca mulatta]

Protein Classification

kinetochore protein Nuf2( domain architecture ID 10510382)

kinetochore protein Nuf2 acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity

Gene Symbol:  NUF2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nuf2 pfam03800
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ...
3-146 1.42e-45

Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.


:

Pssm-ID: 461057  Cd Length: 139  Bit Score: 155.01  E-value: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612    3 TLSFPRYNVAEIVIHIRNKILTgADGKNLTKndlypnPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVM--YPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAAAALleYPELHE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966923612   81 GFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-370 1.17e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   144 QYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQ---DFHQKTIVLQEGNSQKKS------ 214
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQQKQIlrerla 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   215 -----------NISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSV 283
Cdd:TIGR02168  313 nlerqleeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   284 DCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLN---------LEDQIESDESELKKLKTEENSFKRLMIVKKEKLAT 354
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250
                   ....*....|....*.
gi 966923612   355 AQFKINKKHEDVKQYK 370
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
DR0291 super family cl34310
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
309-458 3.48e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


The actual alignment was detected with superfamily member COG1579:

Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 309 KLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTViedcNKVQEKRGAV- 387
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEEQLGNVr 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966923612 388 -YERVTTINQEIQKIKLGIQQLKDaAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRK 458
Cdd:COG1579   87 nNKEYEALQKEIESLKRRISDLED-EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
 
Name Accession Description Interval E-value
Nuf2 pfam03800
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ...
3-146 1.42e-45

Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.


Pssm-ID: 461057  Cd Length: 139  Bit Score: 155.01  E-value: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612    3 TLSFPRYNVAEIVIHIRNKILTgADGKNLTKndlypnPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVM--YPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAAAALleYPELHE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966923612   81 GFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-370 1.17e-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: 54.29  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   144 QYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQ---DFHQKTIVLQEGNSQKKS------ 214
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQQKQIlrerla 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   215 -----------NISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSV 283
Cdd:TIGR02168  313 nlerqleeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   284 DCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLN---------LEDQIESDESELKKLKTEENSFKRLMIVKKEKLAT 354
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250
                   ....*....|....*.
gi 966923612   355 AQFKINKKHEDVKQYK 370
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
142-422 1.67e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 142 LWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQ------DFHQKTIVLQEGNSQKKSN 215
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyELLAELARLEQDIARLEER 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 216 ISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEkyeiygdsvdclpscqlEVQL 295
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE-----------------AEAE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 296 YQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIE 375
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 966923612 376 DCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEI 422
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-462 3.74e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 175 EEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSqKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIvdspEKLKNY 254
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISS-ELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLEGS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 255 KEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQI---------- 324
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerikel 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 325 ESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLG 404
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923612 405 IQQLKDAAER-----EKLKSQEIFLNL----------KTALEKYHDGIEKAAEDsYAKIDEKTAELKRKMFKM 462
Cdd:PRK03918 414 IGELKKEIKElkkaiEELKKAKGKCPVcgrelteehrKELLEEYTAELKRIEKE-LKEIEEKERKLRKELREL 485
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
309-458 3.48e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 309 KLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTViedcNKVQEKRGAV- 387
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEEQLGNVr 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966923612 388 -YERVTTINQEIQKIKLGIQQLKDaAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRK 458
Cdd:COG1579   87 nNKEYEALQKEIESLKRRISDLED-EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
138-422 3.76e-03

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: 40.10  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   138 YMEFLWQYKSSADKMQ-QLNAAHQEALMKLERLDSVPV----------EEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQ 206
Cdd:pfam15921  315 YMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVlanseltearTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   207 EGNSQKKS----------NISEKTKRLNELKLSVVSLKEIQESLKTKIV--------------DSPEKLKNYKEKMKDTV 262
Cdd:pfam15921  395 LEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaaiqgknESLEKVSSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   263 QKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFK 342
Cdd:pfam15921  475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   343 RLMIVKKEKLATAQFKINKKHEDVKQYKRTViedcnkvqekrGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEI 422
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTA-----------GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
 
Name Accession Description Interval E-value
Nuf2 pfam03800
Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown ...
3-146 1.42e-45

Nuf2 family; Members of this family are components of the mitotic spindle. It has been shown that Nuf2 from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle. An arabidopsis protein has been included in this family that has previously not been identified as a member of this family, Swiss:Q9C953. The match is not strong, but in common with other members of this family contains coiled-coil to the C terminus of this region.


Pssm-ID: 461057  Cd Length: 139  Bit Score: 155.01  E-value: 1.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612    3 TLSFPRYNVAEIVIHIRNKILTgADGKNLTKndlypnPKPEVLHMIYMRALQIVYGIRLEHFYMMPVNSEVM--YPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAAAALleYPELHE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966923612   81 GFLPFSNLVTHLDSFLPICRVNDFETADILCPKAKRTSRFLSGIINFIHFREACRETYMEFLWQYK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
144-370 1.17e-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: 54.29  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   144 QYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQ---DFHQKTIVLQEGNSQKKS------ 214
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkELYALANEISRLEQQKQIlrerla 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   215 -----------NISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSV 283
Cdd:TIGR02168  313 nlerqleeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   284 DCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLN---------LEDQIESDESELKKLKTEENSFKRLMIVKKEKLAT 354
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaelkeLQAELEELEEELEELQEELERLEEALEELREELEE 472
                          250
                   ....*....|....*.
gi 966923612   355 AQFKINKKHEDVKQYK 370
Cdd:TIGR02168  473 AEQALDAAERELAQLQ 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
142-422 1.67e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 142 LWQYKSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQ------DFHQKTIVLQEGNSQKKSN 215
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyELLAELARLEQDIARLEER 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 216 ISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEkyeiygdsvdclpscqlEVQL 295
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE-----------------AEAE 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 296 YQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIE 375
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 966923612 376 DCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEI 422
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
210-421 6.78e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 210 SQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSV-----D 284
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 285 CLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHE 364
Cdd:COG3883   99 GGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966923612 365 DVKQYKrtviedcNKVQEKRGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQE 421
Cdd:COG3883  179 EQEALL-------AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
175-450 2.59e-05

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: 46.55  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  175 EEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEgNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNY 254
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  255 KEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKEslnLEDQIESDESELKKL 334
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD---LEDELNKDDFELKKE 557
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  335 KTEE---NSFKRLMIVK--KEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLGIQQLK 409
Cdd:TIGR04523 558 NLEKeidEKNKEIEELKqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 966923612  410 DAAEREKLKSQEIFLNLKTALEKYHDgIEKAAEDSYAKIDE 450
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKWPE-IIKKIKESKTKIDD 677
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-462 3.74e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 175 EEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSqKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIvdspEKLKNY 254
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISS-ELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLEGS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 255 KEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQI---------- 324
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerikel 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 325 ESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLG 404
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923612 405 IQQLKDAAER-----EKLKSQEIFLNL----------KTALEKYHDGIEKAAEDsYAKIDEKTAELKRKMFKM 462
Cdd:PRK03918 414 IGELKKEIKElkkaiEELKKAKGKCPVcgrelteehrKELLEEYTAELKRIEKE-LKEIEEKERKLRKELREL 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
175-430 7.90e-05

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: 44.75  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 175 EEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEGNSQKKSnISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNY 254
Cdd:COG4942   24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 255 KEKMKDTVQKL-KNARQEvvekyeiygdsvdclpscQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKK 333
Cdd:COG4942  103 KEELAELLRALyRLGRQP------------------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 334 LKTEENSFKRlmivKKEKLATAQFKINKKHEDVKQYKRTVIedcNKVQEKRGAVYERVTTINQEIQKIKLGIQQL-KDAA 412
Cdd:COG4942  165 LRAELEAERA----ELEALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLeAEAA 237
                        250
                 ....*....|....*...
gi 966923612 413 EREKLKSQEIFLNLKTAL 430
Cdd:COG4942  238 AAAERTPAAGFAALKGKL 255
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
254-458 1.61e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 254 YKEKMKDTVQKLKNARQ-----------------------EVVEKYEIYGDSVDclpscQLEVQLYQKKIQDLSDNREKL 310
Cdd:COG1196  170 YKERKEEAERKLEATEEnlerledilgelerqleplerqaEKAERYRELKEELK-----ELEAELLLLKLRELEAELEEL 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 311 ASILKEslnLEDQIESDESELKKLKTEENSfkrlmivKKEKLATAQFKINKKHEDVKQYKRTVIE---DCNKVQEKRGAV 387
Cdd:COG1196  245 EAELEE---LEAELEELEAELAELEAELEE-------LRLELEELELELEEAQAEEYELLAELARleqDIARLEERRREL 314
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966923612 388 YERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRK 458
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
150-402 1.65e-04

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: 44.29  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   150 DKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQEgnsqkksnISEKTKRLNELKLS 229
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------IEELEEDLHKLEEA 780
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   230 VVSLK-EIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQL----YQKKIQDLS 304
Cdd:TIGR02169  781 LNDLEaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqiksIEKEIENLN 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   305 DNREKLASILKEslnLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKrtviedcnkvqEKR 384
Cdd:TIGR02169  861 GKKEELEEELEE---LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK-----------AKL 926
                          250
                   ....*....|....*...
gi 966923612   385 GAVYERVTTINQEIQKIK 402
Cdd:TIGR02169  927 EALEEELSEIEDPKGEDE 944
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
150-420 1.97e-03

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: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 150 DKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNqdfhqktivlqegnsQKKSNISEKTKRLNELKLS 229
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA---------------ELEEELEELEEELEELEEE 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 230 VVSLKEIQESLKTKIVDSPEKLKNYKEKMKDTVQKLKNARQEVVEKyeiygdsvdclpscQLEVQLYQKKIQDLsdnREK 309
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--------------LRAAAELAAQLEEL---EEA 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 310 LASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYE 389
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                        250       260       270
                 ....*....|....*....|....*....|.
gi 966923612 390 RVTTINQEIQKIKLGIQQLKDAAEREKLKSQ 420
Cdd:COG1196  489 AAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-456 2.45e-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: 40.43  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   254 YKEKMKDTVQKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLN-LEDQIESDESELK 332
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEeLREELEELQEELK 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   333 KLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVkqykrtviedcNKVQEKRGAVYERVTTINQEIQKIK-----LGIQQ 407
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEI-----------EELQKELYALANEISRLEQQKQILRerlanLERQL 318
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 966923612   408 LKDAAEREKLKSQEIFLNLKTA-LEKYHDGIEKAAEDSYAKIDEKTAELK 456
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAeLEEKLEELKEELESLEAELEELEAELE 368
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
179-427 3.26e-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: 40.00  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  179 EFKQLSDGIQELQQSLNQDFHQKTIVLQegnsqKKSNISEKTKRLNELKLSVVSLKEIQESLKTKIVDSPEKLKNYKEKM 258
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLEL-----LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  259 KDTVQKLKNARQEVVEkyeiygdSVDCLPSCQLEVQLYQKKIQDLSDNREKLASilkESLNLEDQIESDESelKKLKTEE 338
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNK-------IKKQLSEKQKELEQNNKKIKELEKQLNQLKS---EISDLNNQKEQDWN--KELKSEL 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  339 NSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERvttiNQEIQKIKLGIQQLKDaaEREKLK 418
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQ--EIKNLE 390

                  ....*....
gi 966923612  419 SQEIFLNLK 427
Cdd:TIGR04523 391 SQINDLESK 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
146-460 3.42e-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: 40.04  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   146 KSSADKMQQLNAAHQEALMKLERLDSVPVEEQEEFKQLSDGIQELQQSLNqdfhqktivlqegnsQKKSNISEKTKRLNE 225
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE---------------SLERRIAATERRLED 842
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   226 LKLSVVSLKEIQESLKTKIvdspEKLKNYKEKMKDTVQKLKNARQEVvekyeiygdsvdclpscqlevqlyQKKIQDLSD 305
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEI----EELEELIEELESELEALLNERASL------------------------EEALALLRS 894
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   306 NREKLASILKEslnLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQykrTVIEDCNKVQEKRG 385
Cdd:TIGR02168  895 ELEELSEELRE---LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEE 968
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   386 AVYERVTTINQEIQKIK----LGIQQLKDAAER-EKLKSQeiFLNLKTALEKYHDGIEKAAE-------DSYAKIDEKTA 453
Cdd:TIGR02168  969 EARRRLKRLENKIKELGpvnlAAIEEYEELKERyDFLTAQ--KEDLTEAKETLEEAIEEIDRearerfkDTFDQVNENFQ 1046

                   ....*..
gi 966923612   454 ELKRKMF 460
Cdd:TIGR02168 1047 RVFPKLF 1053
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
309-458 3.48e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 3.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612 309 KLASILKESLNLEDQIESDESELKKLKTEENSFKRLMIVKKEKLATAQFKINKKHEDVKQYKRTViedcNKVQEKRGAV- 387
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEEQLGNVr 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966923612 388 -YERVTTINQEIQKIKLGIQQLKDaAEREKLKSQEIFLNLKTALEKYHDGIEKAAEDSYAKIDEKTAELKRK 458
Cdd:COG1579   87 nNKEYEALQKEIESLKRRISDLED-EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
138-422 3.76e-03

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: 40.10  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   138 YMEFLWQYKSSADKMQ-QLNAAHQEALMKLERLDSVPV----------EEQEEFKQLSDGIQELQQSLNQDFHQKTIVLQ 206
Cdd:pfam15921  315 YMRQLSDLESTVSQLRsELREAKRMYEDKIEELEKQLVlanseltearTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   207 EGNSQKKS----------NISEKTKRLNELKLSVVSLKEIQESLKTKIV--------------DSPEKLKNYKEKMKDTV 262
Cdd:pfam15921  395 LEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaaiqgknESLEKVSSLTAQLESTK 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   263 QKLKNARQEVVEKYEIYGDSVDCLPSCQLEVQLYQKKIQDLSDNREKLASILKESLNLEDQIESDESELKKLKTEENSFK 342
Cdd:pfam15921  475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612   343 RLMIVKKEKLATAQFKINKKHEDVKQYKRTViedcnkvqekrGAVYERVTTINQEIQKIKLGIQQLKDAAEREKLKSQEI 422
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTA-----------GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
165-456 6.28e-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: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  165 KLERLDSVPVEEQEEFKQLSDGIQELQQSLNQdfhqktivLQEGNSQKKSNISEKTKRLNELKLSVVSLKEIQESLKTKI 244
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTN--------SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  245 VDSPEKLKNYKEKMKDTVQKLKNArqevvekyeiygdsvdclpscQLEVQLYQKKIQDLSDNREKLASILKeslNLEDQI 324
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKL---------------------QQEKELLEKEIERLKETIIKNNSEIK---DLTNQD 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923612  325 ESDESELKKLKTEENSFKRlmivKKEKLATAQFKINKKHEDVKQYKRTVIEDCNKVQEKRGAVYERVTTINQEIQKIKLG 404
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLET----QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 966923612  405 IQQLkdaaEREKLKSQEIFLNLKTALEKYHDGIEKAA-EDSYAKIDEKTAELK 456
Cdd:TIGR04523 526 IEKL----ESEKKEKESKISDLEDELNKDDFELKKENlEKEIDEKNKEIEELK 574
 
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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