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Conserved domains on  [gi|110625714|ref|NP_075773|]
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kinetochore protein Nuf2 [Mus musculus]

Protein Classification

Nuf2 and DUF460 domain-containing protein( domain architecture ID 13691607)

protein containing domains Nuf2, DUF460, and FapA

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 1.13e-40

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: 142.30  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714    3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625714   81 GFLPVRSLFFYMDSFMPICRVNDFEIVDILNPRTNRTSRFLSGIINFIHFRETCLEKCEEFLLQNK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-457 3.52e-08

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: 56.22  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168  186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168  264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 110625714   417 LKSQEIFVNLKSALEKyhEGIEKVAEERSAKLEEKTAELKK 457
Cdd:TIGR02168  413 EDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEE 451
 
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 1.13e-40

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: 142.30  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714    3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625714   81 GFLPVRSLFFYMDSFMPICRVNDFEIVDILNPRTNRTSRFLSGIINFIHFRETCLEKCEEFLLQNK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-457 3.52e-08

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: 56.22  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168  186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168  264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 110625714   417 LKSQEIFVNLKSALEKyhEGIEKVAEERSAKLEEKTAELKK 457
Cdd:TIGR02168  413 EDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEE 451
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 132-448 1.11e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 54.34  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  132 ETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLE-----------KLNTVPAEEREEFKQFMDDIQELQH--LLNEEF 198
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekeihdleiQLTAIKTSEEHYLKEVEDLKTELEKekLKNIEL 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  199 RQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDI 278
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  279 YRDSVDCLPSCQLEVQLYQKKSQDLADNreklssllkeslnLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFK 358
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNN-------------LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  359 INKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE 438
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYD 717

                         330
                  ....*....|
gi 110625714  439 KVAEERSAKL 448
Cdd:pfam05483 718 KIIEERDSEL 727
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 171-404 3.95e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 171 TVPAEEREEFKQfmDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEK 250
Cdd:COG3883   11 PAFADPQIQAKQ--KELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 251 LKNYKDKMKGTVQklrsarekvmeqyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSE 330
Cdd:COG3883   81 IEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110625714 331 LKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSA 404
Cdd:COG3883  145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-462 4.09e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 175 EEREEFKQFMDDIQELQHLLNEEFRQKTTLLQE--EYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIvdspEKLK 252
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 253 NYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQI-------- 324
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerik 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 325 --ESDSSELKKLKTEENSLIRMTTVKKEK---LATARFKINKKQEDVKHYKQAMIEDCNK-----------VQEKRDAVC 388
Cdd:PRK03918 332 elEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKIT 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 389 EQVTTVNQEIHKIKSAIQQLRDTK------KREILKSQEifvnlKSALEKYHEGIEKVAEERsAKLEEKTAELKKRMVRM 462
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEEHR-----KELLEEYTAELKRIEKEL-KEIEEKERKLRKELREL 485
 
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 1.13e-40

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: 142.30  E-value: 1.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714    3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625714   81 GFLPVRSLFFYMDSFMPICRVNDFEIVDILNPRTNRTSRFLSGIINFIHFRETCLEKCEEFLLQNK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 185-457 3.52e-08

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: 56.22  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168  186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168  264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 110625714   417 LKSQEIFVNLKSALEKyhEGIEKVAEERSAKLEEKTAELKK 457
Cdd:TIGR02168  413 EDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-458 7.92e-08

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: 55.06  E-value: 7.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   174 AEEREEFKQFMDDIQELQHLLNEeFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKN 253
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   254 YKDKMKGTVQKLRSA----------REKVMEQYDIYRDSVDCLPSCQLEVQ-LYQKKSQDLADNREKLSSLLKESLNLED 322
Cdd:TIGR02168  759 LEAEIEELEERLEEAeeelaeaeaeIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   323 QIESDSSELKKLKTEENSLirmtTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIK 402
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 110625714   403 SAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE---KVAEERSAKLEEKTAELKKR 458
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRR 973
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 132-448 1.11e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 54.34  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  132 ETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLE-----------KLNTVPAEEREEFKQFMDDIQELQH--LLNEEF 198
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekeihdleiQLTAIKTSEEHYLKEVEDLKTELEKekLKNIEL 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  199 RQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDI 278
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  279 YRDSVDCLPSCQLEVQLYQKKSQDLADNreklssllkeslnLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFK 358
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNN-------------LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  359 INKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE 438
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYD 717

                         330
                  ....*....|
gi 110625714  439 KVAEERSAKL 448
Cdd:pfam05483 718 KIIEERDSEL 727
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 135-462 1.31e-06

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: 51.22  E-value: 1.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   135 LEKCEEFLLQNKSSM--------VRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQhllneefrQKTTLLQ 206
Cdd:TIGR02169  686 LKRELSSLQSELRRIenrldelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------QEIENVK 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   207 EEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLK-SKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDC 285
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   286 LPSCQLEVQLyQKKS--QDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEENSL---IRMTTVKKEKLATARFKIN 360
Cdd:TIGR02169  838 LQEQRIDLKE-QIKSieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeaqLRELERKIEELEAQIEKKR 916

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   361 KKQEDVKHYKQAMIE-----DCNKVQEKRDAVCEQVT-TVNQEIHKIKSAIQQLRDTKKREIlksqEIFVNLKSALEKYH 434
Cdd:TIGR02169  917 KRLSELKAKLEALEEelseiEDPKGEDEEIPEEELSLeDVQAELQRVEEEIRALEPVNMLAI----QEYEEVLKRLDELK 992

                          330       340       350
                   ....*....|....*....|....*....|
gi 110625714   435 EGIEKVAEERSAkLEEKTAEL--KKRMVRM 462
Cdd:TIGR02169  993 EKRAKLEEERKA-ILERIEEYekKKREVFM 1021
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 171-404 3.95e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 171 TVPAEEREEFKQfmDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEK 250
Cdd:COG3883   11 PAFADPQIQAKQ--KELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 251 LKNYKDKMKGTVQklrsarekvmeqyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSE 330
Cdd:COG3883   81 IEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110625714 331 LKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSA 404
Cdd:COG3883  145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-462 4.09e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 175 EEREEFKQFMDDIQELQHLLNEEFRQKTTLLQE--EYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIvdspEKLK 252
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 253 NYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQI-------- 324
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerik 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 325 --ESDSSELKKLKTEENSLIRMTTVKKEK---LATARFKINKKQEDVKHYKQAMIEDCNK-----------VQEKRDAVC 388
Cdd:PRK03918 332 elEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKIT 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 389 EQVTTVNQEIHKIKSAIQQLRDTK------KREILKSQEifvnlKSALEKYHEGIEKVAEERsAKLEEKTAELKKRMVRM 462
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKgkcpvcGRELTEEHR-----KELLEEYTAELKRIEKEL-KEIEEKERKLRKELREL 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 254-462 2.95e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 2.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   254 YKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQL---YQKKSQDLadnREKLSSLLKESLN-LEDQIESDSS 329
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerYKELKAEL---RELELALLVLRLEeLREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   330 ELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVkhykqamiedcNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLR 409
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-----------EELQKELYALANEISRLEQQKQILRERLANLE 315

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 110625714   410 DTKKReilkSQEIFVNLKSALEKYhegiekvaEERSAKLEEKTAELKKRMVRM 462
Cdd:TIGR02168  316 RQLEE----LEAQLEELESKLDEL--------AEELAELEEKLEELKEELESL 356
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 150-461 3.85e-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: 43.13  E-value: 3.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   150 VRMQQLSNVHQEALMKLEKLNTvPAEEREEFKQFMDDIQE-----LQHLLNEEFRQKTTL------LQEEYAKMKSDISE 218
Cdd:TIGR02169  184 ENIERLDLIIDEKRQQLERLRR-EREKAERYQALLKEKREyegyeLLKEKEALERQKEAIerqlasLEEELEKLTEEISE 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   219 KTKHLNEqklSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSA-REKVMEQYDIYRDSVdclpscQLEVQLYQ 297
Cdd:TIGR02169  263 LEKRLEE---IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSiAEKERELEDAEERLA------KLEAEIDK 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   298 KKSQdLADNREKLSSLLKESLNLEDqiesdssELKKLKTEENSLIRMTTVKKEKLATARFKINKKQ---EDVKHYKQAMI 374
Cdd:TIGR02169  334 LLAE-IEELEREIEEERKRRDKLTE-------EYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELK 405

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   375 EDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSA---LEKYHEGIEKVAEERSaKLEEK 451
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYD-RVEKE 484

                          330
                   ....*....|
gi 110625714   452 TAELKKRMVR 461
Cdd:TIGR02169  485 LSKLQRELAE 494
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 189-451 1.60e-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: 41.26  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   189 ELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYK-------DKMKGT 261
Cdd:pfam15921  246 QLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymrqlSDLEST 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   262 VQKLRSareKVMEQYDIYRDSVDclpscQLEVQLYQKKSQdLADNREKLSSLLKESLNLEDQIESDSSELKK------LK 335
Cdd:pfam15921  326 VSQLRS---ELREAKRMYEDKIE-----ELEKQLVLANSE-LTEARTERDQFSQESGNLDDQLQKLLADLHKrekelsLE 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   336 TEENS-LIRMTTVKKEKLATARFKINKKQEDVKHYK---QAMIEDCNKVQEKRDAVceqVTTVNQEIHKIKSAIQQLRDT 411
Cdd:pfam15921  397 KEQNKrLWDRDTGNSITIDHLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAA---IQGKNESLEKVSSLTAQLEST 473

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 110625714   412 KkrEILKSqeiFVNLKSALEKYHEGIEKVAEERSAKLEEK 451
Cdd:pfam15921  474 K--EMLRK---VVEELTAKKMTLESSERTVSDLTASLQEK 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-422 1.84e-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: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 151 RMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSL 230
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE--------LLAELARLEQDIARLEERRRELEERL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 231 VSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDsvdclpscqlEVQLYQKKSQDLADNREKL 310
Cdd:COG1196  319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----------AEAELAEAEEELEELAEEL 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 311 SSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQ 390
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                        250       260       270
                 ....*....|....*....|....*....|..
gi 110625714 391 VTTVNQEIHKIKSAIQQLRDTKKREILKSQEI 422
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-458 1.89e-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: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 290 QLEVQLYQKKSQDLADNREKLSSLLKEslnLEDQIESDSSELKKLKTEENSLirmttvkKEKLATARFKINKKQEDVKHY 369
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEE---LEAELEELEAELAELEAELEEL-------RLELEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 370 KQAMIE---DCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIEKVAEERSA 446
Cdd:COG1196  294 LAELARleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                        170
                 ....*....|..
gi 110625714 447 KLEEKTAELKKR 458
Cdd:COG1196  374 LAEAEEELEELA 385
46 PHA02562
endonuclease subunit; Provisional
 234-451 1.97e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 234 KEVEDNLKSKIVDSPEKLKnyKDKMKGTVQKLRSAREK---VMEQYDIYRDSVDclpscqlevQLYQKKSQDLADNREKL 310
Cdd:PHA02562 154 KLVEDLLDISVLSEMDKLN--KDKIRELNQQIQTLDMKidhIQQQIKTYNKNIE---------EQRKKNGENIARKQNKY 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 311 SSLLKESLNLEDQIESDSSELKKLKTEENSlirmTTVKKEKLATARFKINKK----QEDVKHY---------KQAMIEDC 377
Cdd:PHA02562 223 DELVEEAKTIKAEIEELTDELLNLVMDIED----PSAALNKLNTAAAKIKSKieqfQKVIKMYekggvcptcTQQISEGP 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110625714 378 NKVQEKRDavceQVTTVNQEIHKIKSAIQQLRDtKKREILKSQEIFVNLKSALEKYHEGIekVAEERSAKLEEK 451
Cdd:PHA02562 299 DRITKIKD----KLKELQHSLEKLDTAIDELEE-IMDEFNEQSKKLLELKNKISTNKQSL--ITLVDKAKKVKA 365
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 309-458 2.15e-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: 39.52  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 309 KLSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAvc 388
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-- 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 389 EQVTTVNQEIHKIKSAIQQLRDtkkrEILKSQEIfvnlKSALEKYHEGIEKVAEERSAKLEEKTAELKKR 458
Cdd:COG1579   89 KEYEALQKEIESLKRRISDLED----EILELMER----IEELEEELAELEAELAELEAELEEKKAELDEE 150
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 150-423 2.28e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   150 VRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEEFRQKTTLLQEEYAKMKSDISEK---TKHLNEQ 226
Cdd:TIGR00618  594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsIRVLPKE 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   227 KLSLVSLKEVE-DNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLAD 305
Cdd:TIGR00618  674 LLASRQLALQKmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714   306 NREKLSSLLKESLNLEDQIESDS-SELKKLKTEENSLIRMTTVKKEKLATARFKInkkQEDVKHYKQAMIEDCNKVQEKR 384
Cdd:TIGR00618  754 TVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEE 830

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 110625714   385 DAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIF 423
Cdd:TIGR00618  831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 185-421 2.48e-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: 40.13  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 185 DDIQELQHLLnEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQK 264
Cdd:COG4942   20 DAAAEAEAEL-EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 265 LRSAREKVMEQ-YDIYRDSvdclPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEenslir 343
Cdd:COG4942   99 LEAQKEELAELlRALYRLG----RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE------ 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625714 344 mttvkkekLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQE 421
Cdd:COG4942  169 --------LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-458 4.40e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 188 QELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKskivdspEKLKNYKDKMKGTVQKLRS 267
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-------LELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 268 AREKVMEQydiyrdsvdclpscQLEVQLYQKKSQDLADNREKLS----SLLKESLNLEDQIESDSSELKKLKTEENSLIR 343
Cdd:COG1196  293 LLAELARL--------------EQDIARLEERRRELEERLEELEeelaELEEELEELEEELEELEEELEEAEEELEEAEA 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714 344 MTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVcEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIF 423
Cdd:COG1196  359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 110625714 424 VNLKSALEKYHEGIEKVAEERSAKLEEKTAELKKR 458
Cdd:COG1196  438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 154-457 6.79e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  154 QLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQEL-----QHLLNEEFRQKttLLQEEYAKMKSDISEKTKHLNEQKL 228
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteqQRLEKNEDQLK--IITMELQKKSSELEEMTKFKNNKEV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  229 SLVSLKEVEDNlKSKIVDSPEKLKNYKDKMKGTVQKLR---SAREKvmEQYDiyrdsvdclpscqLEVQLYQKKSQDlad 305
Cdd:pfam05483 406 ELEELKKILAE-DEKLLDEKKQFEKIAEELKGKEQELIfllQAREK--EIHD-------------LEIQLTAIKTSE--- 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  306 nreklSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDV---KHYKQAMIEDCNKVQE 382
Cdd:pfam05483 467 -----EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEE 541

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625714  383 KRDAVCEQVTTVNQEIH--------KIKSAIQQLRDTKKREILKSQEIFV------NLKSALEKYHEGIEKVAEERSAKL 448
Cdd:pfam05483 542 KEMNLRDELESVREEFIqkgdevkcKLDKSEENARSIEYEVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALK 621


                  ....*....
gi 110625714  449 EEKTAELKK 457
Cdd:pfam05483 622 KKGSAENKQ 630
 
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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