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Conserved domains on  [gi|58865624|ref|NP_001012028|]
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kinetochore protein Nuf2 [Rattus norvegicus]

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 8.41e-44

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: 150.39  E-value: 8.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624     3 TLSFPRYNIAEIVVHIRNKLLTgADGKNLSKsdflpnPKPEVLYMIYMRALQLVYGVRLEHFYMMPVNIEVM--YPHIME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAAAALleYPELHE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624    81 GFLPVSNLFFHLDSFMPICRVNDFEIADILYPKANRTSRFLSGIINFIHFRETCLEKYEEFLLQNK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-447 5.12e-09

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: 58.91  E-value: 5.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    150 DKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQdfrqkttlLQERYTKMKSDFSEKTKHVNELKLS 229
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ--------LKEELKALREALDELRAELTLLNEE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    230 VVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEvMEKYDIYRDsvdclpscQLEVQLyQKKSQDLADNREK 309
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE-IEELEELIE--------ELESEL-EALLNERASLEEA 888

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    310 LSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDV-KQYKRTM---IEDCNKVQEKRD 385
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLeeaEALENKIEDDEE 968

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624    386 AVCEQVTAINQDIHKIK----SGIQQLRDAEKREKLKSQEIlVDLKSALEKYHEGIEKTTEECCTR 447
Cdd:TIGR02168  969 EARRRLKRLENKIKELGpvnlAAIEEYEELKERYDFLTAQK-EDLTEAKETLEEAIEEIDREARER 1033
 
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 8.41e-44

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: 150.39  E-value: 8.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624     3 TLSFPRYNIAEIVVHIRNKLLTgADGKNLSKsdflpnPKPEVLYMIYMRALQLVYGVRLEHFYMMPVNIEVM--YPHIME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAAAALleYPELHE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624    81 GFLPVSNLFFHLDSFMPICRVNDFEIADILYPKANRTSRFLSGIINFIHFRETCLEKYEEFLLQNK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-447 5.12e-09

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: 58.91  E-value: 5.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    150 DKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQdfrqkttlLQERYTKMKSDFSEKTKHVNELKLS 229
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ--------LKEELKALREALDELRAELTLLNEE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    230 VVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEvMEKYDIYRDsvdclpscQLEVQLyQKKSQDLADNREK 309
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE-IEELEELIE--------ELESEL-EALLNERASLEEA 888

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    310 LSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDV-KQYKRTM---IEDCNKVQEKRD 385
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLeeaEALENKIEDDEE 968

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624    386 AVCEQVTAINQDIHKIK----SGIQQLRDAEKREKLKSQEIlVDLKSALEKYHEGIEKTTEECCTR 447
Cdd:TIGR02168  969 EARRRLKRLENKIKELGpvnlAAIEEYEELKERYDFLTAQK-EDLTEAKETLEEAIEEIDREARER 1033
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 169-398 1.40e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 169 LNSVPVEEQEEFKQLKDDIQELQHLLNQdfrqkttlLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSP 248
Cdd:COG3883   7 AAPTPAFADPQIQAKQKELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 249 EKLKNYKEKMKDTVQklrsareevmekyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDS 328
Cdd:COG3883  79 AEIEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADK 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 329 SELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDI 398
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 173-443 1.92e-04

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: 43.95  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    173 PVEEQEEfkQLKDDIQELQHLLnqdfrqkttlLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLK 252
Cdd:pfam15921  242 PVEDQLE--ALKSESQNKIELL----------LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    253 N----YKEKMKDTVQKLRSAREEVMEKYDIYRDSVDclpscQLEVQLYQKKSQdLADNREKLSSILKESLNLEGQIDSDS 328
Cdd:pfam15921  310 NqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIE-----ELEKQLVLANSE-LTEARTERDQFSQESGNLDDQLQKLL 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    329 SELKKLKTEenslirlMTLKKERlatmqfkiNKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQL 408
Cdd:pfam15921  384 ADLHKREKE-------LSLEKEQ--------NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER 448

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 58865624    409 RDAEKREKLKSQEILVDLKSALEKYHEGIEKTTEE 443
Cdd:pfam15921  449 QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-459 4.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  175 EEQEEFKQLKDDIQELQHLLNQDFRQKTTLLQERYTKMKsDFSEKTKHVNELKLSVVSLKEVQDSLKSKIvdspEKLKNY 254
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP-ELREELEKLEKEVKELEELKEEIEELEKEL----ESLEGS 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  255 KEKMKDTVQKLRSAREEVMEKYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKKL 334
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  335 KTEENSLIRLmtlkKERLATMQFKINKKQEDVKQYKRtmiedcnkvqekrdavceqvtainqdihkIKSGIQQLRDAEKR 414
Cdd:PRK03918 334 EEKEERLEEL----KKKLKELEKRLEELEERHELYEE-----------------------------AKAKKEELERLKKR 380

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 58865624  415 EKLKSQEILVDLKSALEKYHEGIEKTTEECCTRIGGKTAELKRRM 459
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
 
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 8.41e-44

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: 150.39  E-value: 8.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624     3 TLSFPRYNIAEIVVHIRNKLLTgADGKNLSKsdflpnPKPEVLYMIYMRALQLVYGVRLEHFYMMPVNIEVM--YPHIME 80
Cdd:pfam03800   1 KDSFPRLSVDEIVACLRELGIP-VTEEDLKK------PTPDFVQKLYERFLELLMGITREDIEPPQLAAAALleYPELHE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624    81 GFLPVSNLFFHLDSFMPICRVNDFEIADILYPKANRTSRFLSGIINFIHFRETCLEKYEEFLLQNK 146
Cdd:pfam03800  74 DSLPLLNLYRHLKRFLKACGVDDFSLKDLLKPDPKRTRRILSALINFARFREERLELYDELLEESE 139
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-447 5.12e-09

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: 58.91  E-value: 5.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    150 DKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQdfrqkttlLQERYTKMKSDFSEKTKHVNELKLS 229
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ--------LKEELKALREALDELRAELTLLNEE 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    230 VVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEvMEKYDIYRDsvdclpscQLEVQLyQKKSQDLADNREK 309
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE-IEELEELIE--------ELESEL-EALLNERASLEEA 888

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    310 LSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDV-KQYKRTM---IEDCNKVQEKRD 385
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLeeaEALENKIEDDEE 968

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624    386 AVCEQVTAINQDIHKIK----SGIQQLRDAEKREKLKSQEIlVDLKSALEKYHEGIEKTTEECCTR 447
Cdd:TIGR02168  969 EARRRLKRLENKIKELGpvnlAAIEEYEELKERYDFLTAQK-EDLTEAKETLEEAIEEIDREARER 1033
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 136-370 5.88e-09

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: 58.53  E-value: 5.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    136 EKYEEFLLQNKSSVDKIQQLSNAHQEALMKLEKLNS--VPVEE-----QEEFKQLKDDIQELQHLLnQDFRQKTTLLQER 208
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLevSELEEeieelQKELYALANEISRLEQQK-QILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    209 YTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEVMEKYDIYRDSVDCLPS 288
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    289 CQLEVQLYQKKSQDLADNREKLSSILKESLN---------LEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKI 359
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKkleeaelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477

                          250
                   ....*....|.
gi 58865624    360 NKKQEDVKQYK 370
Cdd:TIGR02168  478 DAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 160-437 1.78e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    160 QEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQdFRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDS 239
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    240 LKSKIV---DSPEKLKNYKEKMKDTVQKLRSAREEVMEKYDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSILKE 316
Cdd:TIGR02168  314 LERQLEeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLETLRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    317 slnLEGQIDSDSSELKKLKTEENSL-IRLMTLKKERLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAIN 395
Cdd:TIGR02168  391 ---LELQIASLNNEIERLEARLERLeDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 58865624    396 QDIHKIKSGIQQLRDAEKREKLKsQEILVDLKSALEKYHEGI 437
Cdd:TIGR02168  468 EELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSEGV 508
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 169-398 1.40e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 169 LNSVPVEEQEEFKQLKDDIQELQHLLNQdfrqkttlLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSP 248
Cdd:COG3883   7 AAPTPAFADPQIQAKQKELSELQAELEA--------AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 249 EKLKNYKEKMKDTVQklrsareevmekyDIYRDSVDclpSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDS 328
Cdd:COG3883  79 AEIEERREELGERAR-------------ALYRSGGS---VSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADK 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 329 SELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDI 398
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 135-444 2.32e-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: 50.07  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    135 LEKYEEFLLQNKSSV--------DKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLnQDFRQKTTLLQ 206
Cdd:TIGR02169  686 LKRELSSLQSELRRIenrldelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-ENVKSELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    207 ERYTKMKSDFSEKTKHVNELK--LSVVSLKEVQ---DSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEVMEKYDIYRD 281
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALNDLEarLSHSRIPEIQaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    282 svdclpsCQLEVQLYQKKSQDLADNREKLSSILKES-----------LNLEGQIDSDSSELKKLKTEENSLIRLMTLKKE 350
Cdd:TIGR02169  845 -------LKEQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    351 RLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDA--VCEQVTAINQDIHKIKS----GIQQLRDAEKReklksQEILV 424
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedVQAELQRVEEEIRALEPvnmlAIQEYEEVLKR-----LDELK 992

                          330       340
                   ....*....|....*....|
gi 58865624    425 DLKSALEKYHEGIEKTTEEC 444
Cdd:TIGR02169  993 EKRAKLEEERKAILERIEEY 1012
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 178-443 2.67e-06

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: 50.06  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    178 EEFKQLKDDIQELQHLLN----QDFRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKN 253
Cdd:TIGR02168  213 ERYKELKAELRELELALLvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    254 YKEKMKDTVQKLRSAREEvmekydiyRDSVDCLPScQLEVQLYQKKSQ------DLADNREKLSSILKESLNLEGQIDSD 327
Cdd:TIGR02168  293 LANEISRLEQQKQILRER--------LANLERQLE-ELEAQLEELESKldelaeELAELEEKLEELKEELESLEAELEEL 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    328 SSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTmIEDCNKVQEKRDAVCEQVTAiNQDIHKIKSGIQQ 407
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQEIEELLK-KLEEAELKELQAE 441

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 58865624    408 LrDAEKREKLKSQEILVDLKSALEKYHEGIEKTTEE 443
Cdd:TIGR02168  442 L-EELEEELEELQEELERLEEALEELREELEEAEQA 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 137-432 1.20e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 137 KYEEFLLQNKSSVDKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQdFRQKTTLLQERYTKMKSDF 216
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-AQAEEYELLAELARLEQDI 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 217 SEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEvmekydiyrdsvdclpscqlevqly 296
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------------------------- 359

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 297 qkksqdLADNREKLSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIED 376
Cdd:COG1196 360 ------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624 377 CNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEKREKLKSQEILVDLKSALEK 432
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 135-401 1.31e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    135 LEKYEEFLLQNKSSVDKIQQLSNAHQEALMKLE-KLNSVPVEE-QEEFKQLKDDIQELQHLLnQDFRQKTTLLQERYTKM 212
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEiQAELSKLEEEVSRIEARL-REIEQKLNRLTLEKEYL 831

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    213 KSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMKD---TVQKLRSAREEVMEKYDIYRDSVDclpsc 289
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIE----- 906

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    290 QLEVQLYQKKSQ--DLADNREKLSSILKESLNLEGQIDSDSSE---LKKLKTE-ENSLIRLMTLK-------------KE 350
Cdd:TIGR02169  907 ELEAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEEIPEEelsLEDVQAElQRVEEEIRALEpvnmlaiqeyeevLK 986

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 58865624    351 RLATMQFKINKKQEDVKQYKRTmIEDCNKvqEKRDAVCEQVTAINQDIHKI 401
Cdd:TIGR02169  987 RLDELKEKRAKLEEERKAILER-IEEYEK--KKREVFMEAFEAINENFNEI 1034
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 150-424 1.51e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 44.24  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   150 DKIQQLSNAHQEALMKLEKLNS------VPVEEQEEFKQLKDD-IQELQHLLNQDFRQKTTLLQERyTKMKSDFSEKTKH 222
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESqindleSKIQNQEKLNQQKDEqIKKLQQEKELLEKEIERLKETI-IKNNSEIKDLTNQ 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   223 VNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEVM----------EKYDIYRDSVDCLPSCQ-- 290
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKklneekkeleEKVKDLTKKISSLKEKIek 528

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   291 LEVQLYQKKSQ--DLADNREKLSSILKESlNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKIN-------- 360
Cdd:TIGR04523 529 LESEKKEKESKisDLEDELNKDDFELKKE-NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlikeiee 607

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865624   361 ---------KKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEKREKLKSQEILV 424
Cdd:TIGR04523 608 kekkissleKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 173-443 1.92e-04

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: 43.95  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    173 PVEEQEEfkQLKDDIQELQHLLnqdfrqkttlLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLK 252
Cdd:pfam15921  242 PVEDQLE--ALKSESQNKIELL----------LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQAR 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    253 N----YKEKMKDTVQKLRSAREEVMEKYDIYRDSVDclpscQLEVQLYQKKSQdLADNREKLSSILKESLNLEGQIDSDS 328
Cdd:pfam15921  310 NqnsmYMRQLSDLESTVSQLRSELREAKRMYEDKIE-----ELEKQLVLANSE-LTEARTERDQFSQESGNLDDQLQKLL 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    329 SELKKLKTEenslirlMTLKKERlatmqfkiNKKQEDVKQYKRTMIEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQL 408
Cdd:pfam15921  384 ADLHKREKE-------LSLEKEQ--------NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER 448

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 58865624    409 RDAEKREKLKSQEILVDLKSALEKYHEGIEKTTEE 443
Cdd:pfam15921  449 QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 175-419 2.29e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 2.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 175 EEQEEFKQLKDDIQELQHLLNQDFRQKTTLLQERytkmksdfsektkhvNELKLSVVSLKEVQDSLKSKIVDSPEKLKNY 254
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQL---------------AALERRIAALARRIRALEQELAALEAELAEL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 255 KEKMKDTVQKLRSAREEVMEK-YDIYRDSvdclPSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKK 333
Cdd:COG4942  89 EKEIAELRAELEAQKEELAELlRALYRLG----RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 334 LKTEensLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMiedcNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEK 413
Cdd:COG4942 165 LRAE---LEAERAELEALLAELEEERAALEALKAERQKLL----ARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237


                ....*.
gi 58865624 414 REKLKS 419
Cdd:COG4942 238 AAAERT 243
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 155-459 3.80e-04

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 43.20  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   155 LSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQDfRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLK 234
Cdd:pfam07111 308 LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQ-SQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQ 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   235 EVQDSLKSKIVDSPEKLKNYKEKMKDTVQKLRSareeVMEKYDiyrDSVDCLPSCQLEVQLYQKKS---QDLADNREKLS 311
Cdd:pfam07111 387 EARRRQQQQTASAEEQLKFVVNAMSSTQIWLET----TMTRVE---QAVARIPSLSNRLSYAVRKVhtiKGLMARKVALA 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   312 SILKESLNLEGQ---IDSD-SSELKKLKTEENSLIRLMTLKKErlaTMQFKINKKQEDVKQYKRTMIEDCNKVQEKRDAV 387
Cdd:pfam07111 460 QLRQESCPPPPPappVDADlSLELEQLREERNRLDAELQLSAH---LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA 536

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58865624   388 CEQVTAINQDIHKIKSGIQQLRD--AEKREKLKSQEilvdlksalEKYHEGIEKTTEECCTRIGGKTAELKRRM 459
Cdd:pfam07111 537 QESLASVGQQLEVARQGQQESTEeaASLRQELTQQQ---------EIYGQALQEKVAEVETRLREQLSDTKRRL 601
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 297-443 4.11e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 297 QKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIED 376
Cdd:COG3883  19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 377 CNKVQ---------------EKRDAVCEQVTAINQDIHKIKSGIQQLrDAEKREKLKSQEILVDLKSALEKYHEGIEKTT 441
Cdd:COG3883  99 GGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAEL-EAKKAELEAKLAELEALKAELEAAKAELEAQQ 177


                ..
gi 58865624 442 EE 443
Cdd:COG3883 178 AE 179
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
175-459 4.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  175 EEQEEFKQLKDDIQELQHLLNQDFRQKTTLLQERYTKMKsDFSEKTKHVNELKLSVVSLKEVQDSLKSKIvdspEKLKNY 254
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP-ELREELEKLEKEVKELEELKEEIEELEKEL----ESLEGS 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  255 KEKMKDTVQKLRSAREEVMEKYDIYRDSVDCLPSCQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKKL 334
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  335 KTEENSLIRLmtlkKERLATMQFKINKKQEDVKQYKRtmiedcnkvqekrdavceqvtainqdihkIKSGIQQLRDAEKR 414
Cdd:PRK03918 334 EEKEERLEEL----KKKLKELEKRLEELEERHELYEE-----------------------------AKAKKEELERLKKR 380

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 58865624  415 EKLKSQEILVDLKSALEKYHEGIEKTTEECCTRIGGKTAELKRRM 459
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 254-432 5.79e-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: 42.35  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    254 YKEKMKDTVQKLRSAREEVMEKYDIYRDSVDCLPSCQLEVQL---YQKKSQDLadnREKLSSILKESLN-LEGQIDSDSS 329
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerYKELKAEL---RELELALLVLRLEeLREELEELQE 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    330 ELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTM------IEDCNK----VQEKRDAVCEQVTAINQDIH 399
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalaneISRLEQqkqiLRERLANLERQLEELEAQLE 326

                          170       180       190
                   ....*....|....*....|....*....|...
gi 58865624    400 KIKSGIQQLRDAEKREKLKSQEILVDLKSALEK 432
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAE 359
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 145-435 1.05e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    145 NKSSVDKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQDFRQKTTLLQERYTKMKSDFSEKTKHV- 223
Cdd:pfam12128  239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVa 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    224 ---NELKLSVVSLKEVQDSLKSKIVDSPEKLKNYK---EKMKDTVQKLRSAREEVMEKYDIYRDSVDclpscqlevqlyQ 297
Cdd:pfam12128  319 kdrSELEALEDQHGAFLDADIETAAADQEQLPSWQselENLEERLKALTGKHQDVTAKYNRRRSKIK------------E 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    298 KKSQDLADNREKLSSILKESLNLEGQIDSDSSELKK-LKTEENSLIRLMT----LKKERLATMQFKINKKQ--EDVKQYK 370
Cdd:pfam12128  387 QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESeLREQLEAGKLEFNeeeyRLKSRLGELKLRLNQATatPELLLQL 466

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58865624    371 RTMIEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEKREKLKSQEilvdLKSALEKYHE 435
Cdd:pfam12128  467 ENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE----RQSALDELEL 527
mukB PRK04863
chromosome partition protein MukB;
130-334 1.64e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   130 FRETCLEKYEE------FLLQNKSSVDKiqqlsnaHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLNQDFRQK-- 201
Cdd:PRK04863  888 ADETLADRVEEireqldEAEEAKRFVQQ-------HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfa 960

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   202 -TTLLQER----YTKMKSDFSEKTKHVNELKLSVVSLKEVQDSLKSKIVDSPEKLKNYKEKMkdtvQKLRSAreevmekY 276
Cdd:PRK04863  961 lTEVVQRRahfsYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVL----ASLKSS-------Y 1029

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58865624   277 DIYRDSVDCL---------PSCQ-LEVQLYQKKS---QDLADNREKLSSILKESLNLEGQIDSDSSELKKL 334
Cdd:PRK04863 1030 DAKRQMLQELkqelqdlgvPADSgAEERARARRDelhARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL 1100
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
135-432 1.94e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  135 LEKYEEFLLQNKSSVDKIQQLSNAHQEALMKLEKLNSVPVEEQEEFKQLKDDIQELQ--HLLNQDFRQKTTLLQERYTKM 212
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerHELYEEAKAKKEELERLKKRL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  213 KSDFSEKTKhvNELKLSVVSLKEVQDSLKsKIVDSPEKLKNYKEKMKDTVQKLRSAREEVmekydiyrdsvdclPSCQLE 292
Cdd:PRK03918 382 TGLTPEKLE--KELEELEKAKEEIEEEIS-KITARIGELKKEIKELKKAIEELKKAKGKC--------------PVCGRE 444

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  293 VQLYQKKSQdLADNREKLSSILKESLNLEGQIDSDSSELKKLKTEENSLIRLMTLKK--ERLATMQFKINK-KQEDVKQY 369
Cdd:PRK03918 445 LTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKyNLEELEKK 523

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58865624  370 KrtmiEDCNKVQEKRDAVCEQVTAINQDIHKIKSGIQQLRDAEKrEKLKSQEILVDLKSALEK 432
Cdd:PRK03918 524 A----EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK-KLDELEEELAELLKELEE 581
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-443 4.56e-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: 4.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 166 LEKLnsvpvEEQ----EEFKQLKDDIQELQHLLN----QDFRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQ 237
Cdd:COG1196 202 LEPL-----ERQaekaERYRELKEELKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 238 DSLKSKIVDSPEKLKNYKEKMKDTVQKLRSAREEVMekydiyrdsvdclpscQLEVQLyQKKSQDLADNREKLSSILKES 317
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRR----------------ELEERL-EELEEELAELEEELEELEEEL 339

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624 318 LNLEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVKQYKRTMIEDCNKVQEKRdavcEQVTAINQD 397
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE----EAEEALLER 415

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 58865624 398 IHKIKSGIQQLRDAEKREKLKSQEILVDLKSALEKYHEGIEKTTEE 443
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 189-443 6.39e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 39.26  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    189 ELQHLLNQDFRQKTTLLQERYTK--MKSDFSEKTKHVNELklsvvsLKEVQDsLKSKIVDSPEKlknYKEKMKDTVQKLR 266
Cdd:TIGR01612 1510 EKNKELFEQYKKDVTELLNKYSAlaIKNKFAKTKKDSEII------IKEIKD-AHKKFILEAEK---SEQKIKEIKKEKF 1579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    267 SAREEVMEKYDIYRDSVDClpscQLEVQLYQKKSQDLADNREKLSSILKESLNLEGQ-----IDSDSSELKKLKTEENSL 341
Cdd:TIGR01612 1580 RIEDDAAKNDKSNKAAIDI----QLSLENFENKFLKISDIKKKINDCLKETESIEKKissfsIDSQDTELKENGDNLNSL 1655

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624    342 IRLMTL----------KKERLATMQFKINKKQEDVKQYKRTM-IEDCNKVQEKRDAVCEQVTAINQdihKIKSGIQQLRD 410
Cdd:TIGR01612 1656 QEFLESlkdqkkniedKKKELDELDSEIEKIEIDVDQHKKNYeIGIIEKIKEIAIANKEEIESIKE---LIEPTIENLIS 1732

                          250       260       270
                   ....*....|....*....|....*....|...
gi 58865624    411 AEKREKLKSqeilVDLKSALEKYHEGIEKTTEE 443
Cdd:TIGR01612 1733 SFNTNDLEG----IDPNEKLEEYNTEIGDIYEE 1761
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 160-443 7.46e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   160 QEALMKLEKLNSVPVEEQEEFKQLKDDIQELQHLLnQDFRQKTTLLQERYTKMKSDFSEKTKHVNELKLSVVSLKEVQDS 239
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   240 LKSKIVDspeklknykekMKDTVQKLRSAREEVMEKYDIYRDSVDCLPSCQlevqlyQKKSQDLADNREKLSSILKESLN 319
Cdd:TIGR04523 445 LTNQDSV-----------KELIIKNLDNTRESLETQLKVLSRSINKIKQNL------EQKQKELKSKEKELKKLNEEKKE 507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624   320 LEGQIDSDSSELKKLKTEENSLIRLMTLKKERLATMQFKINKKQEDVkqykrtmiedcnkvqeKRDAVCEQVTAINQDIH 399
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL----------------KKENLEKEIDEKNKEIE 571

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 58865624   400 KIKSGIQQLRDA--EKREKLKSQEI-LVDLKSALEKYHEGIEKTTEE 443
Cdd:TIGR04523 572 ELKQTQKSLKKKqeEKQELIDQKEKeKKDLIKEIEEKEKKISSLEKE 618
46 PHA02562
endonuclease subunit; Provisional
 148-351 8.11e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.46  E-value: 8.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  148 SVDKIQQLSNAHQEALMKLEKLNSVPVEE-QEEFKQLKDDIQELQHLLNQdfrqkttlLQERYTKMKSDFSEKTKHVNEL 226
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARkQNKYDELVEEAKTIKAEIEE--------LTDELLNLVMDIEDPSAALNKL 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865624  227 KLSVVSLKEVQDSL----------------KSKIVDSPEKLKNYKEKMKDTVQKLR---SAREEVMEKYDIYRDsvdcLP 287
Cdd:PHA02562 261 NTAAAKIKSKIEQFqkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEkldTAIDELEEIMDEFNE----QS 336

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58865624  288 SCQLEVQL-YQKKSQDLADNREKLSSILKESLNLEGQIDSDSSELKKLKTEENSLI-RLMTLKKER 351
Cdd:PHA02562 337 KKLLELKNkISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVkTKSELVKEK 402
 
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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