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Conserved domains on  [gi|1240700485|ref|NP_001342088|]
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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 1240700485   3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1240700485  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 1240700485  185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168  186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168  264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1240700485  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 1240700485   3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1240700485  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 1240700485  185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168  186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168  264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1240700485  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 1240700485 132 ETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLE-----------KLNTVPAEEREEFKQFMDDIQELQH--LLNEEF 198
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekeihdleiQLTAIKTSEEHYLKEVEDLKTELEKekLKNIEL 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 199 RQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDI 278
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 279 YRDSVDCLPSCQLEVQLYQKKSQDLADNreklssllkeslnLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFK 358
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNN-------------LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 359 INKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE 438
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYD 717
                         330
                  ....*....|
gi 1240700485 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 1240700485 171 TVPAEEREEFKQfmDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEK 250
Cdd:COG3883    11 PAFADPQIQAKQ--KELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 251 LKNYKDKMKGTVQklrsarekvmeqyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSE 330
Cdd:COG3883    81 IEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240700485 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 1240700485 175 EEREEFKQFMDDIQELQHLLNEEFRQKTTLLQE--EYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIvdspEKLK 252
Cdd:PRK03918  176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 253 NYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQI-------- 324
Cdd:PRK03918  252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerik 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 325 --ESDSSELKKLKTEENSLIRMTTVKKEK---LATARFKINKKQEDVKHYKQAMIEDCNK-----------VQEKRDAVC 388
Cdd:PRK03918  332 elEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKIT 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 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 1240700485   3 TLSFPRYNVAELVVHIRNKLLTgADGKNLSKsdflpnPKSDVLYMIYMKALQLVYGVRLEHFYMMPMN--IEVTYPHLME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAaaALLEYPELHE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1240700485  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 1240700485  185 DDIQELQHLLNEEFRQKTTL-LQ----EEYAKMKSDISEKTKHLneQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMK 259
Cdd:TIGR02168  186 ENLDRLEDILNELERQLKSLeRQaekaERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQ 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  260 GT---VQKLRSAREKVMEQYDIYRDSVDCLpscqleVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKT 336
Cdd:TIGR02168  264 ELeekLEELRLEVSELEEEIEELQKELYAL------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  337 EENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEqvttVNQEIHKIKSAIQQLRDTKKReI 416
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER-L 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1240700485  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 1240700485  174 AEEREEFKQFMDDIQELQHLLNEeFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKN 253
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  254 YKDKMKGTVQKLRSA----------REKVMEQYDIYRDSVDCLPSCQLEVQ-LYQKKSQDLADNREKLSSLLKESLNLED 322
Cdd:TIGR02168  759 LEAEIEELEERLEEAeeelaeaeaeIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATER 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  323 QIESDSSELKKLKTEENSLirmtTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIK 402
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1240700485  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 1240700485 132 ETCLEKCEEFLLQNKSSMVRMQQLSNVHQEALMKLE-----------KLNTVPAEEREEFKQFMDDIQELQH--LLNEEF 198
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekeihdleiQLTAIKTSEEHYLKEVEDLKTELEKekLKNIEL 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 199 RQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDI 278
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 279 YRDSVDCLPSCQLEVQLYQKKSQDLADNreklssllkeslnLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFK 358
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNN-------------LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 359 INKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIE 438
Cdd:pfam05483 638 VNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYD 717
                         330
                  ....*....|
gi 1240700485 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 1240700485  135 LEKCEEFLLQNKSSM--------VRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQhllneefrQKTTLLQ 206
Cdd:TIGR02169  686 LKRELSSLQSELRRIenrldelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------QEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  207 EEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLK-SKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDC 285
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  286 LPSCQLEVQLyQKKS--QDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEENSL---IRMTTVKKEKLATARFKIN 360
Cdd:TIGR02169  838 LQEQRIDLKE-QIKSieKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELeaqLRELERKIEELEAQIEKKR 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  361 KKQEDVKHYKQAMIE-----DCNKVQEKRDAVCEQVT-TVNQEIHKIKSAIQQLRDTKKREIlksqEIFVNLKSALEKYH 434
Cdd:TIGR02169  917 KRLSELKAKLEALEEelseiEDPKGEDEEIPEEELSLeDVQAELQRVEEEIRALEPVNMLAI----QEYEEVLKRLDELK 992
                          330       340       350
                   ....*....|....*....|....*....|
gi 1240700485  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 1240700485 171 TVPAEEREEFKQfmDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEK 250
Cdd:COG3883    11 PAFADPQIQAKQ--KELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 251 LKNYKDKMKGTVQklrsarekvmeqyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSE 330
Cdd:COG3883    81 IEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240700485 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 1240700485 175 EEREEFKQFMDDIQELQHLLNEEFRQKTTLLQE--EYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIvdspEKLK 252
Cdd:PRK03918  176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREinEISSELPELREELEKLEKEVKELEELKEEIEELEKEL----ESLE 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 253 NYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQI-------- 324
Cdd:PRK03918  252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngieerik 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 325 --ESDSSELKKLKTEENSLIRMTTVKKEK---LATARFKINKKQEDVKHYKQAMIEDCNK-----------VQEKRDAVC 388
Cdd:PRK03918  332 elEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKeleelekakeeIEEEISKIT 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 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 1240700485  254 YKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQL---YQKKSQDLadnREKLSSLLKESLN-LEDQIESDSS 329
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerYKELKAEL---RELELALLVLRLEeLREELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  330 ELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVkhykqamiedcNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLR 409
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-----------EELQKELYALANEISRLEQQKQILRERLANLE 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1240700485  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 1240700485  150 VRMQQLSNVHQEALMKLEKLNTvPAEEREEFKQFMDDIQE-----LQHLLNEEFRQKTTL------LQEEYAKMKSDISE 218
Cdd:TIGR02169  184 ENIERLDLIIDEKRQQLERLRR-EREKAERYQALLKEKREyegyeLLKEKEALERQKEAIerqlasLEEELEKLTEEISE 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  219 KTKHLNEqklSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSA-REKVMEQYDIYRDSVdclpscQLEVQLYQ 297
Cdd:TIGR02169  263 LEKRLEE---IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSiAEKERELEDAEERLA------KLEAEIDK 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  298 KKSQdLADNREKLSSLLKESLNLEDqiesdssELKKLKTEENSLIRMTTVKKEKLATARFKINKKQ---EDVKHYKQAMI 374
Cdd:TIGR02169  334 LLAE-IEELEREIEEERKRRDKLTE-------EYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREINELK 405
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  375 EDCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSA---LEKYHEGIEKVAEERSaKLEEK 451
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLaadLSKYEQELYDLKEEYD-RVEKE 484
                          330
                   ....*....|
gi 1240700485  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 1240700485  189 ELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYK-------DKMKGT 261
Cdd:pfam15921  246 QLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymrqlSDLEST 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  262 VQKLRSareKVMEQYDIYRDSVDclpscQLEVQLYQKKSQdLADNREKLSSLLKESLNLEDQIESDSSELKK------LK 335
Cdd:pfam15921  326 VSQLRS---ELREAKRMYEDKIE-----ELEKQLVLANSE-LTEARTERDQFSQESGNLDDQLQKLLADLHKrekelsLE 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  336 TEENS-LIRMTTVKKEKLATARFKINKKQEDVKHYK---QAMIEDCNKVQEKRDAVceqVTTVNQEIHKIKSAIQQLRDT 411
Cdd:pfam15921  397 KEQNKrLWDRDTGNSITIDHLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAA---IQGKNESLEKVSSLTAQLEST 473
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1240700485  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 1240700485 151 RMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEefrqkttlLQEEYAKMKSDISEKTKHLNEQKLSL 230
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE--------LLAELARLEQDIARLEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 231 VSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDsvdclpscqlEVQLYQKKSQDLADNREKL 310
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----------AEAELAEAEEELEELAEEL 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 311 SSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVCEQ 390
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1240700485 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 1240700485 290 QLEVQLYQKKSQDLADNREKLSSLLKEslnLEDQIESDSSELKKLKTEENSLirmttvkKEKLATARFKINKKQEDVKHY 369
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEE---LEAELEELEAELAELEAELEEL-------RLELEELELELEEAQAEEYEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 370 KQAMIE---DCNKVQEKRDAVCEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIFVNLKSALEKYHEGIEKVAEERSA 446
Cdd:COG1196   294 LAELARleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         170
                  ....*....|..
gi 1240700485 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 1240700485 234 KEVEDNLKSKIVDSPEKLKnyKDKMKGTVQKLRSAREK---VMEQYDIYRDSVDclpscqlevQLYQKKSQDLADNREKL 310
Cdd:PHA02562  154 KLVEDLLDISVLSEMDKLN--KDKIRELNQQIQTLDMKidhIQQQIKTYNKNIE---------EQRKKNGENIARKQNKY 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 311 SSLLKESLNLEDQIESDSSELKKLKTEENSlirmTTVKKEKLATARFKINKK----QEDVKHY---------KQAMIEDC 377
Cdd:PHA02562  223 DELVEEAKTIKAEIEELTDELLNLVMDIED----PSAALNKLNTAAAKIKSKieqfQKVIKMYekggvcptcTQQISEGP 298
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1240700485 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 1240700485 309 KLSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAvc 388
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-- 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 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 1240700485  150 VRMQQLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQELQHLLNEEFRQKTTLLQEEYAKMKSDISEK---TKHLNEQ 226
Cdd:TIGR00618  594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHalsIRVLPKE 673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  227 KLSLVSLKEVE-DNLKSKIVDSPEKLKNYKDKMKGTVQKLRSAREKVMEQYDIYRDSVDCLPSCQLEVQLYQKKSQDLAD 305
Cdd:TIGR00618  674 LLASRQLALQKmQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485  306 NREKLSSLLKESLNLEDQIESDS-SELKKLKTEENSLIRMTTVKKEKLATARFKInkkQEDVKHYKQAMIEDCNKVQEKR 384
Cdd:TIGR00618  754 TVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEI---GQEIPSDEDILNLQCETLVQEE 830
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1240700485  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 1240700485 185 DDIQELQHLLnEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKSKIVDSPEKLKNYKDKMKGTVQK 264
Cdd:COG4942    20 DAAAEAEAEL-EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 265 LRSAREKVMEQ-YDIYRDSvdclPSCQLEVQLYQKKSQDLADNREKLSSLLKESLNLEDQIESDSSELKKLKTEenslir 343
Cdd:COG4942    99 LEAQKEELAELlRALYRLG----RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE------ 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1240700485 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 1240700485 188 QELQHLLNEEFRQKTTLLQEEYAKMKSDISEKTKHLNEQKLSLVSLKEVEDNLKskivdspEKLKNYKDKMKGTVQKLRS 267
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-------LELEELELELEEAQAEEYE 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 268 AREKVMEQydiyrdsvdclpscQLEVQLYQKKSQDLADNREKLS----SLLKESLNLEDQIESDSSELKKLKTEENSLIR 343
Cdd:COG1196   293 LLAELARL--------------EQDIARLEERRRELEERLEELEeelaELEEELEELEEELEELEEELEEAEEELEEAEA 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 344 MTTVKKEKLATARFKINKKQEDVKHYKQAMIEDCNKVQEKRDAVcEQVTTVNQEIHKIKSAIQQLRDTKKREILKSQEIF 423
Cdd:COG1196   359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1240700485 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 1240700485 154 QLSNVHQEALMKLEKLNTVPAEEREEFKQFMDDIQEL-----QHLLNEEFRQKttLLQEEYAKMKSDISEKTKHLNEQKL 228
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELlrteqQRLEKNEDQLK--IITMELQKKSSELEEMTKFKNNKEV 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 229 SLVSLKEVEDNlKSKIVDSPEKLKNYKDKMKGTVQKLR---SAREKvmEQYDiyrdsvdclpscqLEVQLYQKKSQDlad 305
Cdd:pfam05483 406 ELEELKKILAE-DEKLLDEKKQFEKIAEELKGKEQELIfllQAREK--EIHD-------------LEIQLTAIKTSE--- 466
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 306 nreklSSLLKESLNLEDQIESDSSELKKLKTEENSLIRMTTVKKEKLATARFKINKKQEDV---KHYKQAMIEDCNKVQE 382
Cdd:pfam05483 467 -----EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIincKKQEERMLKQIENLEE 541
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1240700485 383 KRDAVCEQVTTVNQEIH--------KIKSAIQQLRDTKKREILKSQEIFV------NLKSALEKYHEGIEKVAEERSAKL 448
Cdd:pfam05483 542 KEMNLRDELESVREEFIqkgdevkcKLDKSEENARSIEYEVLKKEKQMKIlenkcnNLKKQIENKNKNIEELHQENKALK 621

                  ....*....
gi 1240700485 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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