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Conserved domains on  [gi|2462513918|ref|XP_054194867|]
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syncoilin isoform X3 [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 705869)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882
PubMed:  2183847|12596228|28101862

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
82-368 6.38e-14

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 71.88  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 221
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 222 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 301
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513918 302 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-368 6.38e-14

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 71.88  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 221
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 222 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 301
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513918 302 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-359 2.18e-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: 59.30  E-value: 2.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   96 QAVAQLEEERDQLIHELVLLRepalQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 175
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  176 QQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 255
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  256 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 335
Cdd:TIGR02168  827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260
                   ....*....|....*....|....
gi 2462513918  336 LRNGVQLQQQKNKEMEQLRLSLAE 359
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQ 926
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 131-368 7.99e-08

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: 53.61  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 131 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFQEVLTTRATQLSEELAQL 203
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 204 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 283
Cdd:COG4942    96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 284 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250


                  ....*
gi 2462513918 364 YKAML 368
Cdd:COG4942   251 LKGKL 255
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 73-368 1.23e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 47.36  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   73 PSVEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 152
Cdd:PRK10929    96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  153 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFQEVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 227
Cdd:PRK10929   160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  228 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 297
Cdd:PRK10929   234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  298 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRNGVQLQQQkNKEMEQLRLsLAEELSTYKA 366
Cdd:PRK10929   313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLRQIRQADGQ-PLTAEQNRI-LDAQLRTQRE 390


                   ..
gi 2462513918  367 ML 368
Cdd:PRK10929   391 LL 392
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
 240-369 5.78e-03

Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.


Pssm-ID: 341051 [Multi-domain]  Cd Length: 653  Bit Score: 38.98  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 240 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 303
Cdd:cd06456     7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462513918 304 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:cd06456    87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-368 6.38e-14

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 71.88  E-value: 6.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 221
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 222 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 301
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513918 302 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-359 2.18e-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: 59.30  E-value: 2.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   96 QAVAQLEEERDQLIHELVLLRepalQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 175
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  176 QQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 255
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  256 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 335
Cdd:TIGR02168  827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260
                   ....*....|....*....|....
gi 2462513918  336 LRNGVQLQQQKNKEMEQLRLSLAE 359
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQ 926
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 131-368 7.99e-08

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: 53.61  E-value: 7.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 131 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFQEVLTTRATQLSEELAQL 203
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 204 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 283
Cdd:COG4942    96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 284 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250


                  ....*
gi 2462513918 364 YKAML 368
Cdd:COG4942   251 LKGKL 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-368 1.93e-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: 53.14  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   83 DLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREpalqEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVT 162
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  163 KECVAYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFEN 242
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAE-----LEELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  243 LMAESRQDLEEEYEPQFLRLLErkeagtkaLQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKR-DEEVQQ 321
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEE 444

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2462513918  322 YREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
76-328 2.64e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 2.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   76 EENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHelvllrepaLQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVK 155
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEL---------LEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  156 QKLfkvtkecvaYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQ----KQKEQLRQQLEAPPSQRDghflq 231
Cdd:COG4913    290 LEL---------LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE----- 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  232 ESRRLSAQFENLMAesrqDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALV 311
Cdd:COG4913    356 ERERRRARLEALLA----ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431

                          250       260
                   ....*....|....*....|
gi 2462513918  312 RQKR---DEEVQQYREQLEE 328
Cdd:COG4913    432 ERRKsniPARLLALRDALAE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-363 7.13e-07

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: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 135 KLHAQAE--LERDGLREEIRLVKQKLfkvtkecvaYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLrdayQKQKE 212
Cdd:COG1196   204 PLERQAEkaERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAEL----EAELE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 213 QLRQQLEAppsqrdghFLQESRRLSAQFENLMAEsrqdlEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA 292
Cdd:COG1196   271 ELRLELEE--------LELELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462513918 293 EARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 122-364 6.25e-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: 48.53  E-value: 6.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  122 EVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFQEVLTTRATQLSEELA 201
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  202 QLRD----------AYQKQKEQLRQQLEAPPSQRDGHFLQES-----------RRLSAQFENLMAE-SRQDLEEEYEPQF 259
Cdd:TIGR02169  755 NVKSelkelearieELEEDLHKLEEALNDLEARLSHSRIPEIqaelskleeevSRIEARLREIEQKlNRLTLEKEYLEKE 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  260 LRLLERKEAGTKALQRT-QAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYReqleEMEERQRQLRN 338
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR----ELERKIEELEA 910

                          250       260
                   ....*....|....*....|....*.
gi 2462513918  339 GVQLQQQKNKEMEQLRLSLAEELSTY 364
Cdd:TIGR02169  911 QIEKKRKRLSELKAKLEALEEELSEI 936
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 73-368 1.23e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 47.36  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   73 PSVEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 152
Cdd:PRK10929    96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  153 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFQEVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 227
Cdd:PRK10929   160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  228 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 297
Cdd:PRK10929   234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  298 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRNGVQLQQQkNKEMEQLRLsLAEELSTYKA 366
Cdd:PRK10929   313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLRQIRQADGQ-PLTAEQNRI-LDAQLRTQRE 390


                   ..
gi 2462513918  367 ML 368
Cdd:PRK10929   391 LL 392
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
138-358 5.56e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 138 AQAELERDGLREEIRLVKQKLFKVTKECVAY--QYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLR 215
Cdd:COG3206   171 EEARKALEFLEEQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 216 QQLEAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYePQFLRLLERKEAGTKALQrtqaeiQEMKEALRPLQAEAR 295
Cdd:COG3206   251 SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNH-PDVIALRAQIAALRAQLQ------QEAQRILASLEAELE 323

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462513918 296 QLRLQNRNLEDQIALVRQKrdeeVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 358
Cdd:COG3206   324 ALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 186-354 7.35e-05

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: 45.05  E-value: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  186 QEVLTTRATQLSEELAQL-RDAYQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFENLMAESRQDLEEeYEPQFLRLLE 264
Cdd:TIGR02168  208 QAEKAERYKELKAELRELeLALLVLRLEELREELEELQEE-----LKEAEEELEELTAELQELEEKLEE-LRLEVSELEE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  265 RKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEevqqYREQLEEMEERQRQLRNGVQLQQ 344
Cdd:TIGR02168  282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE----LAEELAELEEKLEELKEELESLE 357

                          170
                   ....*....|
gi 2462513918  345 QKNKEMEQLR 354
Cdd:TIGR02168  358 AELEELEAEL 367
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-393 3.26e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  101 LEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTK--------ECVAYQYQL 172
Cdd:TIGR02169  217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKI 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  173 ECRQQDVAQFADFQEVLTTRATQLSEELAQL---RDAYQKQKEQLRQQLEAPPSQRDghflqesrRLSAQFENL---MAE 246
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRRD--------KLTEEYAELkeeLED 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  247 SRQDLEEEyEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVqqyreql 326
Cdd:TIGR02169  369 LRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE------- 440

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462513918  327 EEMEERQRQLR----NGVQLQQQKNKEMEQLRlSLAEELSTYKAMLLPKSLEQADAPTSQAGGMETQSQGA 393
Cdd:TIGR02169  441 EEKEDKALEIKkqewKLEQLAADLSKYEQELY-DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 199-366 3.51e-04

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: 42.80  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 199 ELAQLRDAYQKQKEQLRQQLEAPPSQRDGHflQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQA 278
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILE--EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQ 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 279 EIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQyreqleEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 358
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIY 530


                  ....*...
gi 2462513918 359 EELSTYKA 366
Cdd:pfam17380 531 EEERRREA 538
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
187-335 5.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 5.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  187 EVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLmAESRQDLeeeyePQFLRLLERK 266
Cdd:COG4913    613 AALEAELAELEEELAEA----EERLEALEAELDA---------LQERREALQRLAEY-SWDEIDV-----ASAEREIAEL 673

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462513918  267 EAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRD---EEVQQYREQLEEMEERQRQ 335
Cdd:COG4913    674 EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeEELDELQDRLEAAEDLARL 745
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 231-368 8.68e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 231 QESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIAL 310
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462513918 311 VRQKRD---EEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:COG1196   300 LEQDIArleERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
169-359 9.22e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 9.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 169 QYQLECRQQDVAQFADFqevLTTRATQLSEELAQLRDAYQKQKEQlrQQLEAPPSQRDGhFLQESRRLSAQFENLMAEsR 248
Cdd:COG3206   163 EQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKL-LLQQLSELESQLAEARAE-L 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 249 QDLEEEYepQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN-------RNLEDQIALVRQKRDEEVQQ 321
Cdd:COG3206   236 AEAEARL--AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR 313

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462513918 322 YRE----QLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAE 359
Cdd:COG3206   314 ILAsleaELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-378 1.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 169 QYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQqLEAppsqrdghflqESRRLSAQFENLMAESR 248
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEA-----------ELEELRLELEELELELE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 249 QDLEEEYEpqflrLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQ 325
Cdd:COG1196   285 EAQAEEYE-----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAE 359

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462513918 326 LEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADA 378
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 264-369 2.02e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.13  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 264 ERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQLEEMEERQRQLRNgv 340
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRA-- 97

                          90       100
                  ....*....|....*....|....*....
gi 2462513918 341 QLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLL 126
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-367 2.04e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  191 TRATQLSEELAQLRDAYQkQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLMAESR--QDLEEEYEPQFLRllERKEA 268
Cdd:COG4913    225 EAADALVEHFDDLERAHE-ALEDAREQIEL---------LEPIRELAERYAAARERLAelEYLRAALRLWFAQ--RRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  269 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIalvRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKnk 348
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEAL-- 367

                          170
                   ....*....|....*....
gi 2462513918  349 eMEQLRLSLAEELSTYKAM 367
Cdd:COG4913    368 -LAALGLPLPASAEEFAAL 385
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 125-336 3.34e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  125 QVHQDILAayKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQleCRQQDVAQFADFQEVLTTrATQLSEELAQLR 204
Cdd:pfam15921  263 QQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ--ARNQNSMYMRQLSDLEST-VSQLRSELREAK 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  205 DAYQKQKEQLRQQLEAPPS-------QRDgHFLQESRRLSAQFENLMA-----ESRQDLEEEyepQFLRLLERKEAGTKA 272
Cdd:pfam15921  338 RMYEDKIEELEKQLVLANSelteartERD-QFSQESGNLDDQLQKLLAdlhkrEKELSLEKE---QNKRLWDRDTGNSIT 413

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513918  273 LQRTQAEIQEMKEALRPLQAEARQLRLQNR-NLEDQIALVRQKRD--EEVQQYREQLEEMEERQRQL 336
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKV 480
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-394 5.08e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 138 AQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFQEVLTTRATQLSEELAQLRDAYQKQKEQLRQQ 217
Cdd:COG3883    12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 218 LEAppSQRDGH------FLQESRRLSAQFENL-----MAESRQDLEEEYEpqflRLLERKEAGTKALQRTQAEIQEMKEA 286
Cdd:COG3883    92 ARA--LYRSGGsvsyldVLLGSESFSDFLDRLsalskIADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 287 LRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKA 366
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245

                         250       260
                  ....*....|....*....|....*...
gi 2462513918 367 MLLPKSLEQADAPTSQAGGMETQSQGAV 394
Cdd:COG3883   246 AAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
 240-369 5.78e-03

Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.


Pssm-ID: 341051 [Multi-domain]  Cd Length: 653  Bit Score: 38.98  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 240 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 303
Cdd:cd06456     7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462513918 304 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:cd06456    87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-362 6.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  171 QLECRQQDVAQFADFQEVLTTRATQlsEELAQLRDAYQKQKEQ--LRQQLEAPPSQRDGHfLQESRRLSAQFENLmAESR 248
Cdd:COG4913    250 QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLelLEAELEELRAELARL-EAELERLEARLDAL-REEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  249 QDLEEEYEPQFLRLLERKEagtKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEE 328
Cdd:COG4913    326 DELEAQIRGNGGDRLEQLE---REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462513918  329 MEERQRQLRNGVQ---------------LQQQKN---KEMEQLRLSLAEELS 362
Cdd:COG4913    403 LEEALAEAEAALRdlrrelreleaeiasLERRKSnipARLLALRDALAEALG 454
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-332 7.20e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918   81 IEDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLR---------------EPALQEVQQVHQDILAAYKLHAQAELERD 145
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeidvasaEREIAELEAELERLDASSDDLAALEEQLE 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  146 GLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFAD--------------------FQEVLTTRAT-QLSEELAQLR 204
Cdd:COG4913    696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedlarlelralleerFAAALGDAVErELRENLEERI 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  205 DAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLSA------QFENLMAESRQDLEEEYEPQFLRLLERKEAGTKA--LQRT 276
Cdd:COG4913    776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdleslpEYLALLDRLEEDGLPEYEERFKELLNENSIEFVAdlLSKL 855

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462513918  277 QAEIQEMKEALRPLQAEARQLRLqnrNLEDQIAL-VRQKRDEEVQQYREQLEEMEER 332
Cdd:COG4913    856 RRAIREIKERIDPLNDSLKRIPF---GPGRYLRLeARPRPDPEVREFRQELRAVTSG 909
DUF4175 pfam13779
Domain of unknown function (DUF4175);
201-350 7.27e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 38.43  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 201 AQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLS--------AQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKA 272
Cdd:pfam13779 516 QELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTqqdlqrmlDRIEELARSGRRAEAQQMLSQLQQMLENLQAGQPQ 595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 273 LQRTQAeIQEMKEALRPLQAEAR---QLR----------------------LQNRNLEDQIALVRQKRDEEVQQYREQLE 327
Cdd:pfam13779 596 QQQQQG-QSEMQQAMDELGDLLReqqQLLdetfrqlqqqggqqqgqpgqqgQQGQGQQPGQGGQQPGAQMPPQGGAEALG 674

                         170       180
                  ....*....|....*....|...
gi 2462513918 328 EMEERQRQLRNGVQLQQQKNKEM 350
Cdd:pfam13779 675 DLAERQQALRRRLEELQDELKEL 697
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
241-360 7.51e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918 241 ENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQ------- 313
Cdd:COG2433   383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeerreir 462

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462513918 314 ------KRDEEVQQYREQLEEMEERQRQLRngvqlqqQKNKEMEQLRLSLAEE 360
Cdd:COG2433   463 kdreisRLDREIERLERELEEERERIEELK-------RKLERLKELWKLEHSG 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-366 7.51e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  171 QLECRQQDVAQFADFQEVLTTRATQLSEELAQL---RDAYQKQKEQLRQQLEAPPSQRdghflqESRRLSAQFENLMAES 247
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALqerREALQRLAEYSWDEIDVASAER------EIAELEAELERLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  248 RQdleeeyepqfLRLLERKeagtkaLQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE----EVQQYR 323
Cdd:COG4913    685 DD----------LAALEEQ------LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlARLELR 748

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462513918  324 EQLEEM------EERQRQLRNGVQLQQQK-NKEMEQLRLSLAEELSTYKA 366
Cdd:COG4913    749 ALLEERfaaalgDAVERELRENLEERIDAlRARLNRAEEELERAMRAFNR 798
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 189-357 8.79e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.39  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  189 LTTRATQLSEELAQLRDAYQKQKEQLRQQLEAppsqrdghfLQESRRLSAQFENL----MAESRQDLEEE---------Y 255
Cdd:COG3096    841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQ---------LQLLNKLLPQANLLadetLADRLEELREEldaaqeaqaF 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513918  256 EPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLR---------LQNR---NLEDQIALVRQKRDEeVQQYR 323
Cdd:COG3096    912 IQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKqqifalsevVQRRphfSYEDAVGLLGENSDL-NEKLR 990

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462513918  324 EQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSL 357
Cdd:COG3096    991 ARLEQAEEARREAREQLRQAQAQYSQYNQVLASL 1024
 
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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