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Conserved domains on  [gi|2217271138|ref|XP_047287186|]
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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 1.43e-14

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 73.80  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 221
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 222 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 301
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217271138 302 RNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLL 307
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-368 1.43e-14

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 73.80  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 221
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 222 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 301
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217271138 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 6.62e-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: 61.23  E-value: 6.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   96 QAVAQLEEERDQLIHELVLLRepalQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 175
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  176 QQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 255
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  256 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 335
Cdd:TIGR02168  827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260
                   ....*....|....*....|....
gi 2217271138  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 8.36e-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: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 131 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFREVLTTRATQLSEELAQL 203
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 204 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 283
Cdd:COG4942    96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 284 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250


                  ....*
gi 2217271138 364 YKAML 368
Cdd:COG4942   251 LKGKL 255
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 73-368 3.49e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.20  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   73 PSMEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 152
Cdd:PRK10929    96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  153 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFREVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 227
Cdd:PRK10929   160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  228 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 297
Cdd:PRK10929   234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  298 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRNGVQLQQQkNKEMEQLRLsLAEELSTYKA 366
Cdd:PRK10929   313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLRQIRQADGQ-PLTAEQNRI-LDAQLRTQRE 390


                   ..
gi 2217271138  367 ML 368
Cdd:PRK10929   391 LL 392
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
 240-369 6.04e-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: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 240 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 303
Cdd:cd06456     7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217271138 304 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:cd06456    87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
82-368 1.43e-14

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 73.80  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQQVHQ-----------DILAAYKLHAQAELERDGLREE 150
Cdd:pfam00038   4 EQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSlyekeiedlrrQLDTLTVERARLQLELDNLRLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQL---------EAP 221
Cdd:pfam00038  84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdtqvnvemDAA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 222 PSQRDGHFLQESRrlsAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN 301
Cdd:pfam00038 164 RKLDLTSALAEIR---AQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217271138 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 6.62e-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: 61.23  E-value: 6.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   96 QAVAQLEEERDQLIHELVLLRepalQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECR 175
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  176 QQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRdghflQESRRLSAQFENLmAESRQDLEEEY 255
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-----EALDELRAELTLL-NEEAANLRERL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  256 EpqflRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQ 335
Cdd:TIGR02168  827 E----SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260
                   ....*....|....*....|....
gi 2217271138  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 8.36e-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: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 131 LAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLE-------CRQQDVAQFADFREVLTTRATQLSEELAQL 203
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalerriaALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 204 RDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQfENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEM 283
Cdd:COG4942    96 RAELEAQKEELAELLRA--LYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 284 KEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNgvQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA--LIARLEAEAAAAAERTPAAGFAA 250


                  ....*
gi 2217271138 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 1.26e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   83 DLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREpalqEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVT 162
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTA----ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  163 KECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFEN 242
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELESLEAE-----LEELEAELEELES 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  243 LMAESRQDLEEEYEPQFLRLLErkeagtkaLQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKR-DEEVQQ 321
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEE 444

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2217271138  322 YREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAML 368
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
76-328 2.04e-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: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   76 EENLSIEDLELLEGRFQQCVQAVAQLEEERDQLIHelvllrepaLQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVK 155
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEL---------LEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  156 QKLfkvtkecvaYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQ----KQKEQLRQQLEAPPSQRDghflq 231
Cdd:COG4913    290 LEL---------LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE----- 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  232 ESRRLSAQFENLMAesrqDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALV 311
Cdd:COG4913    356 ERERRRARLEALLA----ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431

                          250       260
                   ....*....|....*....|
gi 2217271138  312 RQKR---DEEVQQYREQLEE 328
Cdd:COG4913    432 ERRKsniPARLLALRDALAE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 135-363 6.04e-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: 6.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 135 KLHAQAE--LERDGLREEIRLVKQKLfkvtkecvaYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLrdayQKQKE 212
Cdd:COG1196   204 PLERQAEkaERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAEL----EAELE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 213 QLRQQLEAppsqrdghFLQESRRLSAQFENLMAEsrqdlEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA 292
Cdd:COG1196   271 ELRLELEE--------LELELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217271138 293 EARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELST 363
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 141-364 1.64e-05

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: 46.98  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  141 ELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDA-------------- 206
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienvkselkelear 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  207 ---YQKQKEQLRQQLEAPPSQRDGHFLQES-----------RRLSAQFENLMAE-SRQDLEEEYEPQFLRLLERKEAGTK 271
Cdd:TIGR02169  767 ieeLEEDLHKLEEALNDLEARLSHSRIPEIqaelskleeevSRIEARLREIEQKlNRLTLEKEYLEKEIQELQEQRIDLK 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  272 ALQRT-QAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYReqleEMEERQRQLRNGVQLQQQKNKEM 350
Cdd:TIGR02169  847 EQIKSiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR----ELERKIEELEAQIEKKRKRLSEL 922

                          250
                   ....*....|....
gi 2217271138  351 EQLRLSLAEELSTY 364
Cdd:TIGR02169  923 KAKLEALEEELSEI 936
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 73-368 3.49e-05

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.20  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   73 PSMEENLSIEDLEllegrfQQCVQAVAQLEEERDQLIHELVLLREPAlQEVQQVHQDILAAYKlhAQAELERdglreeiR 152
Cdd:PRK10929    96 RSVPPNMSTDALE------QEILQVSSQLLEKSRQAQQEQDRAREIS-DSLSQLPQQQTEARR--QLNEIER-------R 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  153 LVKQKlfkvTKECVAYQYQLECRQQDVAqfADFREVLTTRATQLS----EELAQLR-DAYQKQKEQLRQQLEAPPSQRDG 227
Cdd:PRK10929   160 LQTLG----TPNTPLAQAQLTALQAESA--ALKALVDELELAQLSannrQELARLRsELAKKRSQQLDAYLQALRNQLNS 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  228 HFLQESRRLSAQFEnLMAESRQDLEEEYEPQFLRLLERKEAGTKALQR----------TQAEIQEMKEALRPLQAEARQL 297
Cdd:PRK10929   234 QRQREAERALESTE-LLAEQSGDLPKSIVAQFKINRELSQALNQQAQRmdliasqqrqAASQTLQVRQALNTLREQSQWL 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  298 RLQN---RNLEDQIALV-----RQKRDEEVQQYREQ---LEEMEERQRQLRNGVQLQQQkNKEMEQLRLsLAEELSTYKA 366
Cdd:PRK10929   313 GVSNalgEALRAQVARLpempkPQQLDTEMAQLRVQrlrYEDLLNKQPQLRQIRQADGQ-PLTAEQNRI-LDAQLRTQRE 390


                   ..
gi 2217271138  367 ML 368
Cdd:PRK10929   391 LL 392
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
138-358 5.51e-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: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 138 AQAELERDGLREEIRLVKQKLFKVTKECVAY--QYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLR 215
Cdd:COG3206   171 EEARKALEFLEEQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 216 QQLEAPPSQRDGHFLQESRRLSAQFENLMAESRQDLEEEYePQFLRLLERKEAGTKALQrtqaeiQEMKEALRPLQAEAR 295
Cdd:COG3206   251 SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNH-PDVIALRAQIAALRAQLQ------QEAQRILASLEAELE 323

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217271138 296 QLRLQNRNLEDQIALVRQKrdeeVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 358
Cdd:COG3206   324 ALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-354 1.36e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  190 TTRATQLSEELAQL-RDAYQKQKEQLRQQLEAPPSQrdghfLQESRRLSAQFENLMAESRQDLEEeYEPQFLRLLERKEA 268
Cdd:TIGR02168  212 AERYKELKAELRELeLALLVLRLEELREELEELQEE-----LKEAEEELEELTAELQELEEKLEE-LRLEVSELEEEIEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  269 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEevqqYREQLEEMEERQRQLRNGVQLQQQKNK 348
Cdd:TIGR02168  286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE----LAEELAELEEKLEELKEELESLEAELE 361


                   ....*.
gi 2217271138  349 EMEQLR 354
Cdd:TIGR02168  362 ELEAEL 367
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-332 2.62e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   98 VAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQ 177
Cdd:COG4913    663 VASAEREIAELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  178 DVAQFADFR-------EVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLSA------QFENLM 244
Cdd:COG4913    742 LARLELRALleerfaaALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDAdleslpEYLALL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  245 AESRQDLEEEYEPQFLRLLERKEAGTKA--LQRTQAEIQEMKEALRPLQAEARQLRLqnrNLEDQIAL-VRQKRDEEVQQ 321
Cdd:COG4913    822 DRLEEDGLPEYEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDPLNDSLKRIPF---GPGRYLRLeARPRPDPEVRE 898

                          250
                   ....*....|.
gi 2217271138  322 YREQLEEMEER 332
Cdd:COG4913    899 FRQELRAVTSG 909
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 199-366 4.07e-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: 42.42  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 199 ELAQLRDAYQKQKEQLRQQLEAPPSQRDGHflQESRRLSAQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQA 278
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILE--EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQ 456

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 279 EIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQyreqleEMEERQRQLRNGVQLQQQKNKEMEQLRLSLA 358
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIY 530


                  ....*...
gi 2217271138 359 EELSTYKA 366
Cdd:pfam17380 531 EEERRREA 538
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
186-335 4.60e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 4.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  186 REVLTTRATQLSEELAQLrdayQKQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLmAESRQDLeeeyePQFLRLLER 265
Cdd:COG4913    612 LAALEAELAELEEELAEA----EERLEALEAELDA---------LQERREALQRLAEY-SWDEIDV-----ASAEREIAE 672

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217271138  266 KEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRD---EEVQQYREQLEEMEERQRQ 335
Cdd:COG4913    673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeEELDELQDRLEAAEDLARL 745
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 169-378 5.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 169 QYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQqLEAppsqrdghflqESRRLSAQFENLMAESR 248
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-LEA-----------ELEELRLELEELELELE 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 249 QDLEEEYEpqflrLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQ 325
Cdd:COG1196   285 EAQAEEYE-----LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAE 359

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217271138 326 LEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLLPKSLEQADA 378
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
169-359 8.45e-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: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 169 QYQLECRQQDVAQFADFrevLTTRATQLSEELAQLRDAYQKQKEQlrQQLEAPPSQRDGhFLQESRRLSAQFENLMAEsR 248
Cdd:COG3206   163 EQNLELRREEARKALEF---LEEQLPELRKELEEAEAALEEFRQK--NGLVDLSEEAKL-LLQQLSELESQLAEARAE-L 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 249 QDLEEEYepQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQN-------RNLEDQIALVRQKRDEEVQQ 321
Cdd:COG3206   236 AEAEARL--AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQR 313

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217271138 322 YRE----QLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAE 359
Cdd:COG3206   314 ILAsleaELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 101-393 9.52e-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: 41.59  E-value: 9.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  101 LEEERDQLIHELVLLREPALQEVQQVHQDILAAYKLHAQAELERDGLREEIRLVKQKLFKVTK--------ECVAYQYQL 172
Cdd:TIGR02169  217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKI 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  173 ECRQQDVAQFADFREVLTTRATQLSEELAQL---RDAYQKQKEQLRQQLEAPPSQRDghflqesrRLSAQFENL---MAE 246
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRRD--------KLTEEYAELkeeLED 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  247 SRQDLEEEyEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVqqyreql 326
Cdd:TIGR02169  369 LRAELEEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE------- 440

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217271138  327 EEMEERQRQLR----NGVQLQQQKNKEMEQLRlSLAEELSTYKAMLLPKSLEQADAPTSQAGGMETQSQGA 393
Cdd:TIGR02169  441 EEKEDKALEIKkqewKLEQLAADLSKYEQELY-DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 264-369 1.85e-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: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 264 ERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDE---EVQQYREQLEEMEERQRQLRNgv 340
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRA-- 97

                          90       100
                  ....*....|....*....|....*....
gi 2217271138 341 QLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQPPLALLL 126
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-367 2.06e-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: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  191 TRATQLSEELAQLRDAYQkQKEQLRQQLEAppsqrdghfLQESRRLSAQFENLMAESR--QDLEEEYEPQFLRllERKEA 268
Cdd:COG4913    225 EAADALVEHFDDLERAHE-ALEDAREQIEL---------LEPIRELAERYAAARERLAelEYLRAALRLWFAQ--RRLEL 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  269 GTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIalvRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKnk 348
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEAL-- 367

                          170
                   ....*....|....*....
gi 2217271138  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 3.61e-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: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  125 QVHQDILAayKLHAQAELERDGLREEIRLVKQKLFKVTKECVAYQYQleCRQQDVAQFADFREVLTTrATQLSEELAQLR 204
Cdd:pfam15921  263 QQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ--ARNQNSMYMRQLSDLEST-VSQLRSELREAK 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  205 DAYQKQKEQLRQQLEAPPS-------QRDgHFLQESRRLSAQFENLMA-----ESRQDLEEEyepQFLRLLERKEAGTKA 272
Cdd:pfam15921  338 RMYEDKIEELEKQLVLANSelteartERD-QFSQESGNLDDQLQKLLAdlhkrEKELSLEKE---QNKRLWDRDTGNSIT 413

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217271138  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 4.74e-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: 4.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 138 AQAELERDGLREEIRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQ 217
Cdd:COG3883    12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 218 LEAppSQRDGH------FLQESRRLSAQFENL-----MAESRQDLEEEYEpqflRLLERKEAGTKALQRTQAEIQEMKEA 286
Cdd:COG3883    92 ARA--LYRSGGsvsyldVLLGSESFSDFLDRLsalskIADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 287 LRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEEMEERQRQLRNGVQLQQQKNKEMEQLRLSLAEELSTYKA 366
Cdd:COG3883   166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245

                         250       260
                  ....*....|....*....|....*...
gi 2217271138 367 MLLPKSLEQADAPTSQAGGMETQSQGAV 394
Cdd:COG3883   246 AAGAGAAGAAGAAAGSAGAAGAAAGAAG 273
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-340 5.59e-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: 38.90  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   82 EDLELLEGRFQQCVQAVAQLEEERDQLIHELVLLREPALQEVQ-QVH---------QDILAAYKLHAQ-AELERDGLREE 150
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGeleaeiaslERSIAEKERELEdAEERLAKLEAE 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  151 IRLVKQKLFKVTKECVAYQYQLECRQQDVAQFADFREVLTTRATQLSEELAQLRD---AYQKQKEQLRQQLEapPSQRDG 227
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelkDYREKLEKLKREIN--ELKREL 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  228 HFLQE-SRRLSAQFENLMAESrqdleEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLED 306
Cdd:TIGR02169  409 DRLQEeLQRLSEELADLNAAI-----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2217271138  307 qialvrqkrdeEVQQYREQLEEMEERQRQLRNGV 340
Cdd:TIGR02169  484 -----------ELSKLQRELAEAEAQARASEERV 506
M3A_DCP cd06456
Peptidase family M3, dipeptidyl carboxypeptidase (DCP); Peptidase family M3 dipeptidyl ...
 240-369 6.04e-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: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 240 FENLMAESRQDLEE----EYEPQFLRLLERKEAGTKALQRTQA------------EIQEMKEALRPLQAEARQLRLQNRN 303
Cdd:cd06456     7 IEEAIAEQRAEIEAieanPEPPTFENTIEPLERAGEPLDRVWGvfshlnsvnnsdELRAAYEEVLPLLSAHSDAIGQNEA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217271138 304 LedqialvrQKRDEEVQQYREQLEEMEERQRQL--------RNGVQLQQQKNKEMEQLRLSLAEELSTYKAMLL 369
Cdd:cd06456    87 L--------FARVKALYDSREALGLDPEQKRLLektlrdfvLSGAALSEEKKERLAEINEELSELSTKFSQNVL 152
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 98-357 7.52e-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: 38.78  E-value: 7.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138   98 VAQLEEERDQLIHELVLLREpALQEVQQVHQDILAAYKLHAQAELERDGlREEIRLVKQKLFKVTKECVAYQYQLecrQQ 177
Cdd:COG3096    787 LEELRAERDELAEQYAKASF-DVQKLQRLHQAFSQFVGGHLAVAFAPDP-EAELAALRQRRSELERELAQHRAQE---QQ 861

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  178 DVAQFADFREVLTTRATQLSEELAQLRDAYQKQKEQLRQQLEAppSQRDGHFLQESRRLSAQFENLMAESRQDLEeeyep 257
Cdd:COG3096    862 LRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDA--AQEAQAFIQQHGKALAQLEPLVAVLQSDPE----- 934

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  258 QFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQA----EARQLRLQNRNLEDQIalvrqkrdeevqqyREQLEEMEERQ 333
Cdd:COG3096    935 QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyeDAVGLLGENSDLNEKL--------------RARLEQAEEAR 1000

                          250       260
                   ....*....|....*....|....
gi 2217271138  334 RQLRNGVQLQQQKNKEMEQLRLSL 357
Cdd:COG3096   1001 REAREQLRQAQAQYSQYNQVLASL 1024
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
241-360 7.71e-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: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 241 ENLMAESRQDLEEEYEPQFLRLLERKEAGTKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQ------- 313
Cdd:COG2433   383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeerreir 462

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217271138 314 ------KRDEEVQQYREQLEEMEERQRQLRngvqlqqQKNKEMEQLRLSLAEE 360
Cdd:COG2433   463 kdreisRLDREIERLERELEEERERIEELK-------RKLERLKELWKLEHSG 508
DUF4175 pfam13779
Domain of unknown function (DUF4175);
201-350 8.06e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 38.43  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 201 AQLRDAYQKQKEQLRQQLEAPPSQRDGHFLQESRRLS--------AQFENLMAESRQDLEEEYEPQFLRLLERKEAGTKA 272
Cdd:pfam13779 516 QELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTqqdlqrmlDRIEELARSGRRAEAQQMLSQLQQMLENLQAGQPQ 595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138 273 LQRTQAeIQEMKEALRPLQAEAR---QLR----------------------LQNRNLEDQIALVRQKRDEEVQQYREQLE 327
Cdd:pfam13779 596 QQQQQG-QSEMQQAMDELGDLLReqqQLLdetfrqlqqqggqqqgqpgqqgQQGQGQQPGQGGQQPGAQMPPQGGAEALG 674

                         170       180
                  ....*....|....*....|...
gi 2217271138 328 EMEERQRQLRNGVQLQQQKNKEM 350
Cdd:pfam13779 675 DLAERQQALRRRLEELQDELKEL 697
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
171-362 8.85e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 8.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  171 QLECRQQDVAQFADFREVLTTRATQlsEELAQLRDAYQKQKEQ--LRQQLEAPPSQRDGHfLQESRRLSAQFENLmAESR 248
Cdd:COG4913    250 QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLelLEAELEELRAELARL-EAELERLEARLDAL-REEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271138  249 QDLEEEYEPQFLRLLERKEagtKALQRTQAEIQEMKEALRPLQAEARQLRLQNRNLEDQIALVRQKRDEEVQQYREQLEE 328
Cdd:COG4913    326 DELEAQIRGNGGDRLEQLE---REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA 402

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217271138  329 MEERQRQLRNGVQ---------------LQQQKN---KEMEQLRLSLAEELS 362
Cdd:COG4913    403 LEEALAEAEAALRdlrrelreleaeiasLERRKSnipARLLALRDALAEALG 454
 
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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