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Conserved domains on  [gi|1162495507|ref|XP_020398439|]
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uncharacterized protein LOC109941669 [Zea mays]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 160-382 5.64e-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: 59.69  E-value: 5.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  160 SAVRQIETEMATKWN-HQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEE 238
Cdd:TIGR02168  242 EELQEELKEAEEELEeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  239 KASL----KSREHDKFhhILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELA 314
Cdd:TIGR02168  322 EAQLeeleSKLDELAE--ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162495507  315 KEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVwreERVHMKLVDAKLTLENKYSQLSMLQNELE 382
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALE 464
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 160-382 5.64e-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: 59.69  E-value: 5.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  160 SAVRQIETEMATKWN-HQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEE 238
Cdd:TIGR02168  242 EELQEELKEAEEELEeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  239 KASL----KSREHDKFhhILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELA 314
Cdd:TIGR02168  322 EAQLeeleSKLDELAE--ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162495507  315 KEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVwreERVHMKLVDAKLTLENKYSQLSMLQNELE 382
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALE 464
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-383 1.52e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 190 ERKQRDA---GREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDkfhhiLDAVKEELNRERK 266
Cdd:COG1196   221 ELKELEAellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-----LEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 267 QRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDEL-EEEKKML 345
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALlEAEAELA 375

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1162495507 346 QMAEVWREERV-HMKLVDAKLTLENKYSQLSMLQNELED 383
Cdd:COG1196   376 EAEEELEELAEeLLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
189-342 2.42e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 189 IERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKFHHILDAVKEELNRERKQR 268
Cdd:PRK03918  610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162495507 269 HRAEMMNSKLLNDLSEMElaakRYSRDYEKERKARVLMEEVCDELAKEITEDR----AEVEAMRSEsmkIRDELEEEK 342
Cdd:PRK03918  690 EEIKKTLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKKYKALLKeralSKVGEIASE---IFEELTEGK 760
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 211-380 6.06e-05

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: 46.25  E-value: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 211 QDRIHELEAECRSTKKQLDHLAKNISEEKASLksrEHDKFHHI-LDAVKEELNRErkqrhraemmNSKLLNDLSEMELAA 289
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL---EKEKLKNIeLTAHCDKLLLE----------NKELTQEASDMTLEL 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 290 KRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDELE------EEKKMLQMAEVWREERVHMKLVDA 363
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckldksEENARSIEYEVLKKEKQMKILENK 595

                         170       180
                  ....*....|....*....|.
gi 1162495507 364 ----KLTLENKYSQLSMLQNE 380
Cdd:pfam05483 596 cnnlKKQIENKNKNIEELHQE 616
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 160-382 5.64e-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: 59.69  E-value: 5.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  160 SAVRQIETEMATKWN-HQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEE 238
Cdd:TIGR02168  242 EELQEELKEAEEELEeLTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  239 KASL----KSREHDKFhhILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELA 314
Cdd:TIGR02168  322 EAQLeeleSKLDELAE--ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162495507  315 KEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVwreERVHMKLVDAKLTLENKYSQLSMLQNELE 382
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALE 464
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 198-382 1.67e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  198 REIYTLREELVVAQDRIHELEAECRSTKKQLDhlakNISEEKASLKSREHDKFHHIlDAVKEELNRERKQRHRAEMMNSK 277
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  278 LLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVwREERVH 357
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE-RLESLE 830

                          170       180
                   ....*....|....*....|....*
gi 1162495507  358 MKLVDAKLTLENKYSQLSMLQNELE 382
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIE 855
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 191-465 2.14e-07

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: 54.30  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  191 RKQRDAG-REIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNI----SEEKASLKSREHD------KFHHILDAVKE 259
Cdd:TIGR02169  236 ERQKEAIeRQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQLRVKEKIGEleaeiaSLERSIAEKER 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  260 ELNRERKQRHRAEMMNSKLLNDLSEMElaakrysRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDELE 339
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  340 EEKKMLQMAEVWREE--RVHMKLVDaklTLENKYSQLSMLQNELEDFLRFHPGCNMEKGTVREAERLKEAICSSKINGIK 417
Cdd:TIGR02169  389 DYREKLEKLKREINElkRELDRLQE---ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1162495507  418 EFSYKLPPPSEDIYAVFEELKQREDTAEKVIVQCNGNRPKGRASRAQT 465
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-375 1.25e-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: 51.98  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  159 HSAVRQIETEMATKWNHQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAknisEE 238
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE----AE 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  239 KASLKSREHDKFHHI------LDAVKEELNRERKQRHRAEmmnsKLLNDLSEM--ELAAKRYSRDYEKERKARVLMEEVC 310
Cdd:TIGR02168  367 LEELESRLEELEEQLetlrskVAQLELQIASLNNEIERLE----ARLERLEDRreRLQQEIEELLKKLEEAELKELQAEL 442

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162495507  311 DELAKEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEvwREERVHMKLVDAKLTLENKYSQLS 375
Cdd:TIGR02168  443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAE--RELAQLQARLDSLERLQENLEGFS 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-383 1.52e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 190 ERKQRDA---GREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDkfhhiLDAVKEELNRERK 266
Cdd:COG1196   221 ELKELEAellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-----LEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 267 QRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDEL-EEEKKML 345
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALlEAEAELA 375

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1162495507 346 QMAEVWREERV-HMKLVDAKLTLENKYSQLSMLQNELED 383
Cdd:COG1196   376 EAEEELEELAEeLLEALRAAAELAAQLEELEEAEEALLE 414
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
189-342 2.42e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 189 IERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKFHHILDAVKEELNRERKQR 268
Cdd:PRK03918  610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR 689

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162495507 269 HRAEMMNSKLLNDLSEMElaakRYSRDYEKERKARVLMEEVCDELAKEITEDR----AEVEAMRSEsmkIRDELEEEK 342
Cdd:PRK03918  690 EEIKKTLEKLKEELEERE----KAKKELEKLEKALERVEELREKVKKYKALLKeralSKVGEIASE---IFEELTEGK 760
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 155-384 6.39e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 6.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 155 EMEAHSAVRQIETEMAtkwNHQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKN 234
Cdd:COG1196   290 EYELLAELARLEQDIA---RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 235 ISEEKASLKSREhdkfhhildavkEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELA 314
Cdd:COG1196   367 LLEAEAELAEAE------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 315 KEITEDRAEVEAMRSESMKIRDELEEEKKMLQmAEVWREERVHMKLVDAKLTLENKYSQLSMLQNELEDF 384
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLA-ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 198-365 6.72e-06

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: 48.00  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 198 REIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDkfhhiLDAVKEELNRERKQRHRAemMNSK 277
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-----IEEVEARIKKYEEQLGNV--RNNK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 278 LLNDLS-EMELAAKRYSrdyEKERKARVLMEEVcDELAKEITEDRAEVEAMRSESMKIRDELEEEKKML--QMAEVWREE 354
Cdd:COG1579    90 EYEALQkEIESLKRRIS---DLEDEILELMERI-EELEEELAELEAELAELEAELEEKKAELDEELAELeaELEELEAER 165

                         170
                  ....*....|.
gi 1162495507 355 RVHMKLVDAKL 365
Cdd:COG1579   166 EELAAKIPPEL 176
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
204-407 1.06e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.88  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 204 REELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKFHHILDAVKEELNRERKQRHRAEMMNSK--LLND 281
Cdd:PRK02224  250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDeeLRDR 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 282 LSEMELAAKRYSRDYEKERK-ARVLME------EVCDELAKEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVWREE 354
Cdd:PRK02224  330 LEECRVAAQAHNEEAESLREdADDLEEraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1162495507 355 rvhmkLVDAKLTLENKYSQLSMLQNELEDFLRfhpgcnMEKGTVREAERLKEA 407
Cdd:PRK02224  410 -----AEDFLEELREERDELREREAELEATLR------TARERVEEAEALLEA 451
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 211-380 6.06e-05

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: 46.25  E-value: 6.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 211 QDRIHELEAECRSTKKQLDHLAKNISEEKASLksrEHDKFHHI-LDAVKEELNRErkqrhraemmNSKLLNDLSEMELAA 289
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL---EKEKLKNIeLTAHCDKLLLE----------NKELTQEASDMTLEL 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 290 KRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDELE------EEKKMLQMAEVWREERVHMKLVDA 363
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckldksEENARSIEYEVLKKEKQMKILENK 595

                         170       180
                  ....*....|....*....|.
gi 1162495507 364 ----KLTLENKYSQLSMLQNE 380
Cdd:pfam05483 596 cnnlKKQIENKNKNIEELHQE 616
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 152-343 8.30e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 152 VPHEMEAHSAVRQIETEMATKWNHQfmkaslSADYDYIERKQRDA-GREIYTLREELVVAQDRIHELEAECRSTKKQLDH 230
Cdd:pfam17380 394 VRQELEAARKVKILEEERQRKIQQQ------KVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEEQERQQQVERLRQ 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 231 LAKNISEEKASLKSREHDKfhhildAVKEELNR--------ERKQRHRAEMMNSKLLNdlSEME-----LAAKRYSRDYE 297
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDR------KRAEEQRRkilekeleERKQAMIEEERKRKLLE--KEMEerqkaIYEEERRREAE 539

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1162495507 298 KERKARVLMEE--VCDELAKEITEDRAEVEAMRSESMKIRDELEEEKK 343
Cdd:pfam17380 540 EERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA 587
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 192-386 1.06e-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: 45.14  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 192 KQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDkfhhiLDAVKEELNRERKQRHRA 271
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-----LAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 272 EMMNSKLLNDLSEMELAAKR------------------------YSRDYEKERKARVlmeEVCDELAKEITEDRAEVEAM 327
Cdd:COG4942    96 RAELEAQKEELAELLRALYRlgrqpplalllspedfldavrrlqYLKYLAPARREQA---EELRADLAELAALRAELEAE 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1162495507 328 RSESMKIRDELEEEKKMLQMAEVWREERVhMKLVDAKLTLENKYSQLSMLQNELEDFLR 386
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLL-ARLEKELAELAAELAELQQEAEELEALIA 230
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
156-346 1.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  156 MEAHSAV----RQIET--EMATKWNhQFMKASLSADydyiERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLD 229
Cdd:COG4913    238 ERAHEALedarEQIELlePIRELAE-RYAAARERLA----ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  230 HLAKNISEEKASLKSREHDKFHH---ILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLM 306
Cdd:COG4913    313 RLEARLDALREELDELEAQIRGNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1162495507  307 EEVCDELAKEITEDRAEVEAMRSESMKIRDELEEEKKMLQ 346
Cdd:COG4913    393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 254-384 1.25e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 42.24  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 254 LDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKErkarvLMEEVcdELAKEITEDRAEVEAMRSESMK 333
Cdd:pfam07926   3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERE-----LVLHA--EDIKALQALREELNELKAEIAE 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162495507 334 IRDELEEEKKMLQMAEV-WREERVHMK--LVDAKLTLENKYSQLSMLQNELEDF 384
Cdd:pfam07926  76 LKAEAESAKAELEESEEsWEEQKKELEkeLSELEKRIEDLNEQNKLLHDQLESL 129
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
180-342 1.71e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 180 ASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDkfhhiLDAVKE 259
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE-----LAQAQE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 260 ELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDELE 339
Cdd:COG4372   102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181


                  ...
gi 1162495507 340 EEK 342
Cdd:COG4372   182 EQA 184
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
211-448 1.97e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 211 QDRIHELEAECRSTKKQLDHLAKNI---SEEKASLKSREHDkfhhiLDAVKEELNRERKQRHRAEMMNSKLLNDLSEMEl 287
Cdd:PRK03918  192 EELIKEKEKELEEVLREINEISSELpelREELEKLEKEVKE-----LEELKEEIEELEKELESLEGSKRKLEEKIRELE- 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 288 aakrySRDYEKERKARVLmEEVCDELaKEITEDRAEVEAMRSESMKIRDELEEEKKMLqmaEVWREERvhmKLVDAKLT- 366
Cdd:PRK03918  266 -----ERIEELKKEIEEL-EEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRL---SRLEEEI---NGIEERIKe 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 367 LENKYSQLSMLQNELEDFLRfhpGCNMEKGTVREAERLKEAIcsSKINGIKEFSYKLPPpsEDIYAVFEELKQREDTAEK 446
Cdd:PRK03918  333 LEEKEERLEELKKKLKELEK---RLEELEERHELYEEAKAKK--EELERLKKRLTGLTP--EKLEKELEELEKAKEEIEE 405


                  ..
gi 1162495507 447 VI 448
Cdd:PRK03918  406 EI 407
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 179-340 3.00e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 179 KASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASL-KSREHDK-------- 249
Cdd:COG4942    50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyRLGRQPPlalllspe 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 250 -----------FHHILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEIT 318
Cdd:COG4942   130 dfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                         170       180
                  ....*....|....*....|..
gi 1162495507 319 EDRAEVEAMRSESMKIRDELEE 340
Cdd:COG4942   210 ELAAELAELQQEAEELEALIAR 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 189-408 3.13e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  189 IERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKF---HHILDAVKEELNRER 265
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLeeeVSRIEARLREIEQKL 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  266 KQRHRAEmmnsKLLNDLSEMELAAKRYSRDYEKERKARV-LMEEVCDELAKEITEDRAEVEAMRSESMKIRDELEEEKKM 344
Cdd:TIGR02169  822 NRLTLEK----EYLEKEIQELQEQRIDLKEQIKSIEKEIeNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1162495507  345 LQMAEVWREE--------RVHMKLVDAKltLENKYSQLSmlqnELEDFLRF---HPGCNMEKGTVREA-ERLKEAI 408
Cdd:TIGR02169  898 LRELERKIEEleaqiekkRKRLSELKAK--LEALEEELS----EIEDPKGEdeeIPEEELSLEDVQAElQRVEEEI 967
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 188-386 9.10e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 188 YIERKqRDAGREIYTLREELVVAQDRIHELEaecrstkKQLDHLAK---------NISEE----KASLKSREHDKFHHIL 254
Cdd:COG1196   170 YKERK-EEAERKLEATEENLERLEDILGELE-------RQLEPLERqaekaeryrELKEElkelEAELLLLKLRELEAEL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 255 DAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKI 334
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1162495507 335 RDELEEEKKMLQMAEVwREERVHMKLVDAKLTLENKYSQLSMLQNELEDFLR 386
Cdd:COG1196   322 EEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 189-383 9.18e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 189 IERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLK-----------SREHDKFHHI---- 253
Cdd:COG1196   258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerleeleeELAELEEELEelee 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 254 -LDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESM 332
Cdd:COG1196   338 eLEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1162495507 333 KIRDELEEEKKMLQMAEVwREERVHMKLVDAKLTLENKYSQLSMLQNELED 383
Cdd:COG1196   418 RLEEELEELEEALAELEE-EEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 157-368 1.08e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  157 EAHSAVRQIETEMATKwnhQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNIS 236
Cdd:TIGR02168  807 ELRAELTLLNEEAANL---RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  237 EEKASLKSREH--DKFHHILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMEL--------AAKRYSRDYE--KERKARV 304
Cdd:TIGR02168  884 SLEEALALLRSelEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerLSEEYSLTLEeaEALENKI 963

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162495507  305 LMEEvcDELAKEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVWREErvhmkLVDAKLTLE 368
Cdd:TIGR02168  964 EDDE--EEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKED-----LTEAKETLE 1020
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
191-349 1.45e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 191 RKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKFHHILDAVKEELNRERKQRHR 270
Cdd:COG4717    81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 271 AEMMNSKLLNDLSEM--ELAAKRYSRDYEKERKARVLMEEVcDELAKEITEDRAEVEAMRSESMKIRDELEEEKKMLQMA 348
Cdd:COG4717   161 LEEELEELEAELAELqeELEELLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239


                  .
gi 1162495507 349 E 349
Cdd:COG4717   240 A 240
COG5022 COG5022
Myosin heavy chain [General function prediction only];
213-382 2.07e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.60  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  213 RIHELEAECRSTKKQLDHLAKNISEEKaSLKSREHDKFHHILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELA-AKR 291
Cdd:COG5022    804 SLLGSRKEYRSYLACIIKLQKTIKREK-KLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVElAER 882

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  292 YSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIR-DELEEEKKMLQMAEV-------WREERVHMKLVDA 363
Cdd:COG5022    883 QLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKtELIARLKKLLNNIDLeegpsieYVKLPELNKLHEV 962

                          170
                   ....*....|....*....
gi 1162495507  364 KLTLENKYSQLSMLQNELE 382
Cdd:COG5022    963 ESKLKETSEEYEDLLKKST 981
PRK12704 PRK12704
phosphodiesterase; Provisional
 209-358 3.52e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 209 VAQDRIHELEAECRSTKKQLDHLAKNISEEKAsLKSREhdKFHHIldavKEELNRERKQRhRAEMmnSKLLNDLSEMELA 288
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAKE--EIHKL----RNEFEKELRER-RNEL--QKLEKRLLQKEEN 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1162495507 289 AKRYSRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDEL-----EEEKKML--QMAEVWREERVHM 358
Cdd:PRK12704   98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaEEAKEILleKVEEEARHEAAVL 174
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 179-346 4.18e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 179 KASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREhdkfhhilDAVK 258
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR--------EELG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 259 EELNRERKQRHRAEM----MNSKLLND-LSEMELAAKRYSRDYEkerkarvLMEEVcDELAKEITEDRAEVEAMRSESMK 333
Cdd:COG3883    90 ERARALYRSGGSVSYldvlLGSESFSDfLDRLSALSKIADADAD-------LLEEL-KADKAELEAKKAELEAKLAELEA 161

                         170
                  ....*....|...
gi 1162495507 334 IRDELEEEKKMLQ 346
Cdd:COG3883   162 LKAELEAAKAELE 174
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-346 4.21e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  179 KASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKfhhilDAVK 258
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI-----EELE 909

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  259 EELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLmEEVCDELAKEIT----------EDRAEVEAMR 328
Cdd:TIGR02169  910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRalepvnmlaiQEYEEVLKRL 988

                          170
                   ....*....|....*...
gi 1162495507  329 SESMKIRDELEEEKKMLQ 346
Cdd:TIGR02169  989 DELKEKRAKLEEERKAIL 1006
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 166-382 4.63e-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: 40.09  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 166 ETEMATKWNHQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEekaslksr 245
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE-------- 612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 246 ehdkFHHILDAVKEELNRERKQRHRAEMMNSKLLNDLSEMELAAKRYSRDYEKERKARVLMEEvcdELAKEITEDRAEVE 325
Cdd:pfam05483 613 ----LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE---KLLEEVEKAKAIAD 685

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1162495507 326 amrsESMKIRDELEE--EKKMLQM-AEVWREERVHMKLV---DAKLTL-ENKYSQLSMLQNELE 382
Cdd:pfam05483 686 ----EAVKLQKEIDKrcQHKIAEMvALMEKHKHQYDKIIeerDSELGLyKNKEQEQSSAKAALE 745
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 203-386 5.86e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  203 LREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLK--SREHDKFHHILDAVKEELNRERKQ----RHRAEMMNS 276
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdaSRKIGEIEKEIEQLEQEEEKLKERleelEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  277 KLLNDLSEMELAAKRYSRDYEKERKARVLMEEVCDELA----KEITEDRAEVEAMRSESMKIRDELEEEKKMLQMAEVWR 352
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1162495507  353 EERVHMKLVDAKLTLENKYS---QLSMLQNELEDFLR 386
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSiekEIENLNGKKEELEE 868
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 157-267 7.81e-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: 38.37  E-value: 7.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507 157 EAHSAVRQIETEMAT------KWNHQFMKASLSADYDYIERKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDH 230
Cdd:COG1579    56 DLEKEIKRLELEIEEvearikKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAE 135

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1162495507 231 LAKNISEEKASLKSREHDkfhhiLDAVKEELNRERKQ 267
Cdd:COG1579   136 LEAELEEKKAELDEELAE-----LEAELEELEAEREE 167
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 191-382 8.78e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.57  E-value: 8.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  191 RKQRDAGREIYTLREELVVAQDRIHELEAECRSTKKQLDHLAKNISEEKASLKSREHDKFHHILDAVKEELNR-ERKQRH 269
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLlQELLRD 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162495507  270 RAEMMNSKLLNDLSEMELAAKRySRDYEKERKARVLMEEVCDELAKEITEDRAEVEAMRSESMKIRDELEEEKKM----- 344
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQV-LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEkkkae 327

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1162495507  345 --LQMAEVWREERVHMK--LVDAKLTLENKYSQLSMLQNELE 382
Cdd:pfam02463  328 keLKKEKEEIEELEKELkeLEIKREAEEEEEEELEKLQEKLE 369
 
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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