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Conserved domains on  [gi|300669677|sp|Q9H7C4|]
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RecName: Full=Syncoilin; AltName: Full=Syncoilin intermediate filament 1; AltName: Full=Syncoilin-1

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

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List of domain hits

 Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
170-456 2.48e-15

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 76.50  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  170 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 238
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  239 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 309
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  310 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 389
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669677  390 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 456
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
170-456 2.48e-15

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 76.50  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  170 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 238
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  239 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 309
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  310 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 389
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669677  390 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 456
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-447 3.47e-10

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: 62.77  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   184 QAVAQLEEERDQLIHELVLLRepalQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 263
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   264 QQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 343
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   344 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 423
Cdd:TIGR02168  827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260
                   ....*....|....*....|....
gi 300669677   424 LRNGVQLQQQKNKEMEQLRLSLAE 447
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQ 926
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 219-456 2.60e-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: 55.93  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 219 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFREVLTTRATQLSEELAQL 291
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 292 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 371
Cdd:COG4942   96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 372 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 451
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250


                 ....*
gi 300669677 452 YKAML 456
Cdd:COG4942  251 LKGKL 255
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 161-456 1.56e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 47.74  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  161 PSMEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 240
Cdd:PRK10929   96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  241 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFREVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 315
Cdd:PRK10929  160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  316 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 385
Cdd:PRK10929  234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  386 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRngvQLQQQKNKEM--EQLRLsLAEELSTY 452
Cdd:PRK10929  313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLR---QIRQADGQPLtaEQNRI-LDAQLRTQ 388


                  ....
gi 300669677  453 KAML 456
Cdd:PRK10929  389 RELL 392
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
 328-457 8.21e-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: 38.59  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 328 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 391
Cdd:cd06456    7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300669677 392 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 457
Cdd:cd06456   87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
170-456 2.48e-15

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 76.50  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  170 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 238
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  239 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 309
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  310 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 389
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669677  390 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 456
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-447 3.47e-10

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: 62.77  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   184 QAVAQLEEERDQLIHELVLLRepalQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 263
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   264 QQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 343
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   344 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 423
Cdd:TIGR02168  827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260
                   ....*....|....*....|....
gi 300669677   424 LRNGVQLQQQKNKEMEQLRLSLAE 447
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQ 926
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 219-456 2.60e-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: 55.93  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 219 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFREVLTTRATQLSEELAQL 291
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 292 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 371
Cdd:COG4942   96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 372 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 451
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250


                 ....*
gi 300669677 452 YKAML 456
Cdd:COG4942  251 LKGKL 255
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-456 5.80e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 5.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   171 DLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREpalqEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVT 250
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   251 KECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFEN 330
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAE-----LEELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   331 LMAESRQDLEEEYEPQFLRLLErkeagtkaLQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKR-DEEVQQ 409
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEE 444

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 300669677   410 YREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 456
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
164-416 8.13e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.92  E-value: 8.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  164 EENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHelvllrepaLQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVK 243
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEL---------LEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  244 QKLfkvtkecvaYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQ----KQKEQLRQQLEAPPSQRDghflq 319
Cdd:COG4913   290 LEL---------LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE----- 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  320 ESRRLSAQFENLMAesrqDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALV 399
Cdd:COG4913   356 ERERRRARLEALLA----ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431

                         250       260
                  ....*....|....*....|
gi 300669677  400 RQKR---DEEVQQYREQLEE 416
Cdd:COG4913   432 ERRKsniPARLLALRDALAE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-451 3.30e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 3.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 223 KLHAQAE--LERDGLREEIRLVKQKLfkvtkecvaYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLrdayQKQKE 300
Cdd:COG1196  204 PLERQAEkaERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAEL----EAELE 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 301 QLRQQLEAppsqrdghFLQESRRLSAQFENLMAEsrqdlEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA 380
Cdd:COG1196  271 ELRLELEE--------LELELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300669677 381 EARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELST 451
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 229-452 7.33e-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: 48.91  E-value: 7.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   229 ELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDA-------------- 294
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienvkselkelear 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   295 ---YQKQKEQLRQQLEAPPSQRDGHFLQES-----------RRLSAQFENLMAE-SRQDLEEEYEPQFLRLLERKEAGTK 359
Cdd:TIGR02169  767 ieeLEEDLHKLEEALNDLEARLSHSRIPEIqaelskleeevSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLK 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   360 ALQRT-QAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYReqleEMEERQRQLRNGVQLQQQKNKEM 438
Cdd:TIGR02169  847 EQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR----ELERKIEELEAQIEKKRKRLSEL 922

                          250
                   ....*....|....
gi 300669677   439 EQLRLSLAEELSTY 452
Cdd:TIGR02169  923 KAKLEALEEELSEI 936
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 161-456 1.56e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 47.74  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  161 PSMEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 240
Cdd:PRK10929   96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  241 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFREVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 315
Cdd:PRK10929  160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  316 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 385
Cdd:PRK10929  234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  386 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRngvQLQQQKNKEM--EQLRLsLAEELSTY 452
Cdd:PRK10929  313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLR---QIRQADGQPLtaEQNRI-LDAQLRTQ 388


                  ....
gi 300669677  453 KAML 456
Cdd:PRK10929  389 RELL 392
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
226-446 3.74e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 226 AQAELERDGLREEIRLVKQKLFKVTKECVAYQyqlecRQQDVAQFADFREVLTTRATQLSEELAQLRDAY---QKQKEQL 302
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELaeaEARLAAL 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 303 RQQL----EAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYePQFLRLLERKEAGTKALQrtqaeiQEMKEALRPL 378
Cdd:COG3206  246 RAQLgsgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNH-PDVIALRAQIAALRAQLQ------QEAQRILASL 318

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300669677 379 QAEARQLRLQNRNLEDQIALVRQKrdeeVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 446
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-442 7.87e-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: 45.43  E-value: 7.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   278 TTRATQLSEELAQL-RDAYQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFENLMAESRQDLEEeYEPQFLRLLERKEA 356
Cdd:TIGR02168  212 AERYKELKAELRELeLALLVLRLEELREELEELQEE-----LKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   357 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEevqqYREQLEEMEERQRQLRNGVQLQQQKNK 436
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE----LAEELAELEEKLEELKEELESLEAELE 361


                   ....*.
gi 300669677   437 EMEQLR 442
Cdd:TIGR02168  362 ELEAEL 367
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 287-454 1.22e-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: 44.73  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  287 ELAQLRDAYQKQKEQLRQQLEAPPSQRDGHflQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQA 366
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILE--EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQ 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  367 EIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQyreqleEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 446
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIY 530


                  ....*...
gi 300669677  447 EELSTYKA 454
Cdd:pfam17380 531 EEERRREA 538
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-420 1.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  186 VAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQ 265
Cdd:COG4913   663 VASAEREIAELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  266 DVAQF------ADFREVLTTRAT-QLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLSA------QFENLM 332
Cdd:COG4913   742 LARLElralleERFAAALGDAVErELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdleslpEYLALL 821

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  333 AESRQDLEEEYEPQFLRLLERKEAGTKA--LQRTQAEIQEMKEALRPLQAEARQLRLqnrNLEDQIAL-VRQKRDEEVQQ 409
Cdd:COG4913   822 DRLEEDGLPEYEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDPLNDSLKRIPF---GPGRYLRLeARPRPDPEVRE 898

                         250
                  ....*....|.
gi 300669677  410 YREQLEEMEER 420
Cdd:COG4913   899 FRQELRAVTSG 909
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
274-423 2.32e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  274 REVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLmAESRQDLeeeyePQFLRLLER 353
Cdd:COG4913   612 LAALEAELAELEEELAEA----EERLEALEAELDA---------LQERREALQRLAEY-SWDEIDV-----ASAEREIAE 672

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300669677  354 KEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRD---EEVQQYREQLEEMEERQRQ 423
Cdd:COG4913   673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeEELDELQDRLEAAEDLARL 745
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 257-466 3.66e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 257 QYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQqLEAppsqrdghflqESRRLSAQFENLMAESR 336
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEA-----------ELEELRLELEELELELE 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 337 QDLEEEYEpqflrLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQ 413
Cdd:COG1196  285 EAQAEEYE-----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAE 359

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 300669677 414 LEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADA 466
Cdd:COG1196  360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
PTZ00121 PTZ00121
MAEBL; Provisional
 12-437 3.97e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   12 GAAQAARKTRVEANSPLPKNSGSLNEAEALNpevtlSSEGSLNLEDILYLEDTGDLDETLYVQETEKAEEALYIEEAMQP 91
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAEEAKKKAEDAR-----KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA 1172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   92 DEALHVEEPGNPEETVCVEETTEPDRIQFVEGPVEPGKPTSPEHV-----VYEGETVTRAE--KSNPEESLRAEQSPSME 164
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEArkaedAKKAEAVKKAEeaKKDAEEAKKAEEERNNE 1252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  165 ENLSIEdlellEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELER--DGLREEIRLV 242
Cdd:PTZ00121 1253 EIRKFE-----EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEA 1327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  243 KQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRA---TQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQ 319
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  320 ESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALV 399
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 300669677  400 RQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKE 437
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 189-481 4.31e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   189 LEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTK--------ECVAYQYQL 260
Cdd:TIGR02169  217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKI 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   261 ECRQQDVAQFADFREVLTTRATQLSEELAQL---RDAYQKQKEQLRQQLEAPPSQRDghflqesrRLSAQFENL---MAE 334
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRRD--------KLTEEYAELkeeLED 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   335 SRQDLEEEyEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVqqyreql 414
Cdd:TIGR02169  369 LRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE------- 440

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300669677   415 EEMEERQRQLR----NGVQLQQQKNKEMEQLRlSLAEELSTYKAMLLPKSLEQADAPTSQAGGMETQSQGA 481
Cdd:TIGR02169  441 EEKEDKALEIKkqewKLEQLAADLSKYEQELY-DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
257-447 5.78e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 257 QYQLECRQQDVAQFADFrevLTTRATQLSEELAQLRDAYQKQKEQlrQQLEAPPSQRDGhFLQESRRLSAQFENLMAEsR 336
Cdd:COG3206  163 EQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKL-LLQQLSELESQLAEARAE-L 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 337 QDLEEEYepQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN-------RNLEDQIALVRQKRDEEVQQ 409
Cdd:COG3206  236 AEAEARL--AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR 313

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 300669677 410 YRE----QLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAE 447
Cdd:COG3206  314 ILAsleaELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 352-464 8.48e-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: 41.67  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 352 ERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQLEEMEERQRQLRNgv 428
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRA-- 97

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 300669677 429 QLQQQKNKEMEQLR-LSLAEELSTYKAMLLPKSLEQA 464
Cdd:COG4942   98 ELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDA 134
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
279-455 1.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  279 TRATQLSEELAQLRDAYQkQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLMAESR--QDLEEEYEPQFLRllERKEA 356
Cdd:COG4913   225 EAADALVEHFDDLERAHE-ALEDAREQIEL---------LEPIRELAERYAAARERLAelEYLRAALRLWFAQ--RRLEL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  357 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIalvRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKnk 436
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEAL-- 367

                         170
                  ....*....|....*....
gi 300669677  437 eMEQLRLSLAEELSTYKAM 455
Cdd:COG4913   368 -LAALGLPLPASAEEFAAL 385
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 213-424 1.27e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.64  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   213 QVHQDILAayKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQleCRQQDVAQFADFREVLTTrATQLSEELAQLR 292
Cdd:pfam15921  263 QQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ--ARNQNSMYMRQLSDLEST-VSQLRSELREAK 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   293 DAYQKQKEQLRQQLEAPPS-------QRDgHFLQESRRLSAQFENLMA-----ESRQDLEEEyepQFLRLLERKEAGTKA 360
Cdd:pfam15921  338 RMYEDKIEELEKQLVLANSelteartERD-QFSQESGNLDDQLQKLLAdlhkrEKELSLEKE---QNKRLWDRDTGNSIT 413

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300669677   361 LQRTQAEIQEMKEALRPLQAEARQLRLQNR-NLEDQIALVRQKRD--EEVQQYREQLEEMEERQRQL 424
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKV 480
PTZ00121 PTZ00121
MAEBL; Provisional
 54-449 1.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   54 NLEDILYLEDTGDLDETlYVQETEKAEEALYIEEAMQ-PDEALHVEEPGNPEETVCVEET--TEPDRIQFVEGPVEPGKP 130
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEA-KKTETGKAEEARKAEEAKKkAEDARKAEEARKAEDARKAEEArkAEDAKRVEIARKAEDARK 1165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  131 TSPEHVVYEGETVTRAEKSnpEESLRAEQSPSMEENLSIEDLELLEGrfQQCVQAVAQLEEERdqlihelvllREPALQE 210
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKA--EEVRKAEELRKAEDARKAEAARKAEE--ERKAEEARKAEDAK----------KAEAVKK 1231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  211 VQQVHQDILAAYKlhaqAELERDglREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADfrEVLTTRATQLSEELAQ 290
Cdd:PTZ00121 1232 AEEAKKDAEEAKK----AEEERN--NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE--EKKKADEAKKAEEKKK 1303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  291 LRDAyQKQKEQLRQQLEAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQE 370
Cdd:PTZ00121 1304 ADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  371 MK----EALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRlslA 446
Cdd:PTZ00121 1383 AKkkaeEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK---A 1459


                  ...
gi 300669677  447 EEL 449
Cdd:PTZ00121 1460 EEA 1462
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 170-428 2.68e-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: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   170 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQ-QVH---------QDILAAYKLHAQ-AELERDGLREE 238
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGeleaeiaslERSIAEKERELEdAEERLAKLEAE 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   239 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRD---AYQKQKEQLRQQLEapPSQRDG 315
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelkDYREKLEKLKREIN--ELKREL 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   316 HFLQE-SRRLSAQFENLMAESrqdleEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLED 394
Cdd:TIGR02169  409 DRLQEeLQRLSEELADLNAAI-----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          250       260       270
                   ....*....|....*....|....*....|....
gi 300669677   395 qialvrqkrdeEVQQYREQLEEMEERQRQLRNGV 428
Cdd:TIGR02169  484 -----------ELSKLQRELAEAEAQARASEERV 506
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 186-445 2.74e-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: 40.32  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  186 VAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGlREEIRLVKQKLFKVTKECVAYQYQLecrQQ 265
Cdd:COG3096   787 LEELRAERDELAEQYAKASF-DVQKLQRLHQAFSQFVGGHLAVAFAPDP-EAELAALRQRRSELERELAQHRAQE---QQ 861

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  266 DVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQFENLMAESRQDLEeeyep 345
Cdd:COG3096   862 LRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDA--AQEAQAFIQQHGKALAQLEPLVAVLQSDPE----- 934

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  346 QFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA----EARQLRLQNRNLEDQIalvrqkrdeevqqyREQLEEMEERQ 421
Cdd:COG3096   935 QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyeDAVGLLGENSDLNEKL--------------RARLEQAEEAR 1000

                         250       260
                  ....*....|....*....|....
gi 300669677  422 RQLRNGVQLQQQKNKEMEQLRLSL 445
Cdd:COG3096  1001 REAREQLRQAQAQYSQYNQVLASL 1024
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
259-450 4.23e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  259 QLECRQQDVAQFADFREVLTTRATQlsEELAQLRDAYQKQKEQ--LRQQLEAPPSQRDGHfLQESRRLSAQFENLmAESR 336
Cdd:COG4913   250 QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLelLEAELEELRAELARL-EAELERLEARLDAL-REEL 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  337 QDLEEEYEPQFLRLLERKEagtKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEE 416
Cdd:COG4913   326 DELEAQIRGNGGDRLEQLE---REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300669677  417 MEERQRQLRNGVQ---------------LQQQKN---KEMEQLRLSLAEELS 450
Cdd:COG4913   403 LEEALAEAEAALRdlrrelreleaeiasLERRKSnipARLLALRDALAEALG 454
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 226-482 4.42e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 226 AQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQ 305
Cdd:COG3883   12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 306 LEAppSQRDGH------FLQESRRLSAQFENL-----MAESRQDLEEEYEpqflRLLERKEAGTKALQRTQAEIQEMKEA 374
Cdd:COG3883   92 ARA--LYRSGGsvsyldVLLGSESFSDFLDRLsalskIADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 375 LRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKA 454
Cdd:COG3883  166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245

                        250       260
                 ....*....|....*....|....*...
gi 300669677 455 MLLPKSLEQADAPTSQAGGMETQSQGAV 482
Cdd:COG3883  246 AAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
DUF4175 pfam13779
Domain of unknown function (DUF4175);
289-438 5.65e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 39.20  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  289 AQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLS--------AQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKA 360
Cdd:pfam13779 516 QELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTqqdlqrmlDRIEELARSGRRAEAQQMLSQLQQMLENLQAGQPQ 595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  361 LQRTQAeIQEMKEALRPLQAEAR---QLR----------------------LQNRNLEDQIALVRQKRDEEVQQYREQLE 415
Cdd:pfam13779 596 QQQQQG-QSEMQQAMDELGDLLReqqQLLdetfrqlqqqggqqqgqpgqqgQQGQGQQPGQGGQQPGAQMPPQGGAEALG 674

                         170       180
                  ....*....|....*....|...
gi 300669677  416 EMEERQRQLRNGVQLQQQKNKEM 438
Cdd:pfam13779 675 DLAERQQALRRRLEELQDELKEL 697
PTZ00121 PTZ00121
MAEBL; Provisional
 74-471 6.63e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   74 QETEKAEEALY--IEEAMQPDEALHVEEPGNPEETVCVEETTEPDRIQFVEgpvEPGKPTSPEHVVYEGETVTRAEKSNP 151
Cdd:PTZ00121 1325 EEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKADAAKKKAEEKKKADEAKKKAE 1401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  152 EESLRAEQ-SPSMEENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAEL 230
Cdd:PTZ00121 1402 EDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  231 ER--DGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFAD-------FREVLTTRATQLSEELAQLRDAYQ-KQKE 300
Cdd:PTZ00121 1482 AKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeakkaeeAKKADEAKKAEEKKKADELKKAEElKKAE 1561

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  301 QLRQQLEAPPSQRDGHFLQESRRLSAQFENLMAESRQDL-EEEYEPQFLRLLERKEAGTKALQ-RTQAEIQEMKEALRPL 378
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKK 1641

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677  379 QAEARQLRLQNRNLEDQIALVRQ---KRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELStyKAM 455
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAeeaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK--KAE 1719

                         410
                  ....*....|....*.
gi 300669677  456 LLPKSLEQADAPTSQA 471
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEA 1735
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 223-482 7.90e-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: 38.88  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   223 KLHAQAELERD--GLREEIRLVKQKLFkvTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKE 300
Cdd:TIGR02168  204 SLERQAEKAERykELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   301 QLRQQleappSQRDGHFLQESRRLSAQFENLmAESRQDLE---EEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRP 377
Cdd:TIGR02168  282 EIEEL-----QKELYALANEISRLEQQKQIL-RERLANLErqlEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677   378 LQAEARQLRLQNRNLEDQIalvrQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 457
Cdd:TIGR02168  356 LEAELEELEAELEELESRL----EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          250       260
                   ....*....|....*....|....*
gi 300669677   458 PKSLEQADAPTSQAGGMETQSQGAV 482
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQEEL 456
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
 328-457 8.21e-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: 38.59  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300669677 328 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 391
Cdd:cd06456    7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300669677 392 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 457
Cdd:cd06456   87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
 
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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