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Conserved domains on  [gi|767994715|ref|XP_011523088|]
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keratin, type I cuticular Ha3-I isoform X1 [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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament super family cl25641
Intermediate filament protein;
37-207 7.79e-66

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 206.69  E-value: 7.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   37 EEVNTLRCQLGD-RLNVEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQWFATQTEELNKQVVSSSEQLQSYQAEIIE 115
Cdd:pfam00038 142 EEVRELQAQVSDtQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITE 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  116 LRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEIN 195
Cdd:pfam00038 222 LRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301
                         170
                  ....*....|..
gi 767994715  196 TYRSLLESEDCK 207
Cdd:pfam00038 302 TYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
37-207 7.79e-66

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 206.69  E-value: 7.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   37 EEVNTLRCQLGD-RLNVEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQWFATQTEELNKQVVSSSEQLQSYQAEIIE 115
Cdd:pfam00038 142 EEVRELQAQVSDtQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITE 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  116 LRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEIN 195
Cdd:pfam00038 222 LRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301
                         170
                  ....*....|..
gi 767994715  196 TYRSLLESEDCK 207
Cdd:pfam00038 302 TYRKLLEGEECR 313
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
60-203 3.95e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.40  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  60 VDLNQVLNETRSQYEALvETNRREVEQWFATQTEELNKqvVSSSEQLQSYQAEIIELRRTVNALEIELQAQH----NLRD 135
Cdd:COG3206  222 SELESQLAEARAELAEA-EARLAALRAQLGSGPDALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRA 298
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767994715 136 SLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRA---RLECEINTYRSLLES 203
Cdd:COG3206  299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAelrRLEREVEVARELYES 369
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-210 1.10e-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: 46.20  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    34 ADFEEVNTLRCQLGDRLnvEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQWfatqtEELNKQVVSSSEQLQSYQAEI 113
Cdd:TIGR02168  316 RQLEELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAEL-----EELESRLEELEEQLETLRSKV 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   114 IELRRTVNALEIEL--------QAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLD 185
Cdd:TIGR02168  389 AQLELQIASLNNEIerlearleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
                          170       180
                   ....*....|....*....|....*
gi 767994715   186 VRARLECEINTYRSLLESEDCKLPS 210
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDS 493
PRK11281 PRK11281
mechanosensitive channel MscK;
62-181 7.85e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 37.20  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   62 LNQVLNETRSQYEALVETNRReveqwfatqTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDsLENTL 141
Cdd:PRK11281   61 VQQDLEQTLALLDKIDRQKEE---------TEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ-LESRL 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767994715  142 TESearySSQLSQVQRLITNVESQLAEIRSDLER-QNQEYQ 181
Cdd:PRK11281  131 AQT----LDQLQNAQNDLAEYNSQLVSLQTQPERaQAALYA 167
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
37-207 7.79e-66

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 206.69  E-value: 7.79e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   37 EEVNTLRCQLGD-RLNVEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQWFATQTEELNKQVVSSSEQLQSYQAEIIE 115
Cdd:pfam00038 142 EEVRELQAQVSDtQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITE 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  116 LRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEIN 195
Cdd:pfam00038 222 LRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIA 301
                         170
                  ....*....|..
gi 767994715  196 TYRSLLESEDCK 207
Cdd:pfam00038 302 TYRKLLEGEECR 313
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
60-203 3.95e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.40  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  60 VDLNQVLNETRSQYEALvETNRREVEQWFATQTEELNKqvVSSSEQLQSYQAEIIELRRTVNALEIELQAQH----NLRD 135
Cdd:COG3206  222 SELESQLAEARAELAEA-EARLAALRAQLGSGPDALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRA 298
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767994715 136 SLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRA---RLECEINTYRSLLES 203
Cdd:COG3206  299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAelrRLEREVEVARELYES 369
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
34-191 1.58e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  34 ADFEEVNTLRCQLGDRLNVEVDAAPTVDLNQVLNETRSQYEALvetnRREVEQWFATQTEElNKQVVSSSEQLQSYQAEI 113
Cdd:COG3206  233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL----EAELAELSARYTPN-HPDVIALRAQIAALRAQL 307
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767994715 114 -IELRRTVNALEIELQAQHNLRDSLENTLTESEARYSSqlsqvqrlITNVESQLAEIRSDLERQNQEYQVLLdvrARLE 191
Cdd:COG3206  308 qQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLL---QRLE 375
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
64-204 2.22e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  64 QVLNETRSQY-EALVETNRREVEQ---WFATQTEELNKQV----------------VSSSEQLQSYQAEIIELRRTVNAL 123
Cdd:COG3206  152 AVANALAEAYlEQNLELRREEARKaleFLEEQLPELRKELeeaeaaleefrqknglVDLSEEAKLLLQQLSELESQLAEA 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715 124 EIELQAQHNLRDSLENTL-----TESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLL----DVRARLECEI 194
Cdd:COG3206  232 RAELAEAEARLAALRAQLgsgpdALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRaqiaALRAQLQQEA 311
                        170
                 ....*....|
gi 767994715 195 NTYRSLLESE 204
Cdd:COG3206  312 QRILASLEAE 321
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-210 1.10e-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: 46.20  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    34 ADFEEVNTLRCQLGDRLnvEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQWfatqtEELNKQVVSSSEQLQSYQAEI 113
Cdd:TIGR02168  316 RQLEELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAEL-----EELESRLEELEEQLETLRSKV 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   114 IELRRTVNALEIEL--------QAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLD 185
Cdd:TIGR02168  389 AQLELQIASLNNEIerlearleRLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
                          170       180
                   ....*....|....*....|....*
gi 767994715   186 VRARLECEINTYRSLLESEDCKLPS 210
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLDS 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-208 1.15e-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: 46.20  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    61 DLNQVLNETRSQYEALVETNRREVEQWFAT------QTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLR 134
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEElaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767994715   135 DSLENTLTESEARY---SSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCKL 208
Cdd:TIGR02168  827 ESLERRIAATERRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
62-199 1.85e-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: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    62 LNQVLNETRSQYEALvETNRREVEqwfaTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTL 141
Cdd:TIGR02168  244 LQEELKEAEEELEEL-TAELQELE----EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767994715   142 TESEAR----------YSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRS 199
Cdd:TIGR02168  319 EELEAQleeleskldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
99-205 2.29e-05

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: 44.75  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  99 VVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEAR----------YSSQLSQVQRLITNVESQLAE 168
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalarriraLEQELAALEAELAELEKEIAE 94
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767994715 169 IRSDLERQNQEYQVLLDVRARLEcEINTYRSLLESED 205
Cdd:COG4942   95 LRAELEAQKEELAELLRALYRLG-RQPPLALLLSPED 130
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
62-191 4.56e-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: 44.28  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    62 LNQVLNETRSQYEALVETNRREVEQWFATQT--EELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLEN 139
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767994715   140 TLTESEARYSSQLSQVQrlitNVESQLAEIRSDLERQNQEyqvLLDVRARLE 191
Cdd:TIGR02168  888 ALALLRSELEELSEELR----ELESKRSELRRELEELREK---LAQLELRLE 932
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
68-203 9.30e-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: 43.13  E-value: 9.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    68 ETRSQYEALvETNRREVEQW--------FATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELqAQHNLRdslEN 139
Cdd:TIGR02169  208 EKAERYQAL-LKEKREYEGYellkekeaLERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL-EELNKK---IK 282
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767994715   140 TLTESEARyssqlsQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLES 203
Cdd:TIGR02169  283 DLGEEEQL------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
93-205 2.21e-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: 41.97  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    93 EELNKQVVSSSEQLQSYQAEIIELR----------RTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQRLITNV 162
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRkeleeleeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 767994715   163 ESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESED 205
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
66-179 2.28e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  66 LNETRSQYEALVETNRREVEQWfatqTEELNKqvVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESE 145
Cdd:COG1579   57 LEKEIKRLELEIEEVEARIKKY----EEQLGN--VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE 130
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767994715 146 ARYSSQLSQVQRLITNVESQLAEIRSDLERQNQE 179
Cdd:COG1579  131 AELAELEAELEEKKAELDEELAELEAELEELEAE 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-191 2.52e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  37 EEVNTLRCQLgDRLNVEVDAAptvdlNQVLNETRSQYEALVETNRREVEQW--FATQTEELNKQVVSSSEQLQSYQAEII 114
Cdd:COG1196  267 AELEELRLEL-EELELELEEA-----QAEEYELLAELARLEQDIARLEERRreLEERLEELEEELAELEEELEELEEELE 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715 115 ELRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQRL---ITNVESQLAEIRSDLERQNQEYQVLLDVRARLE 191
Cdd:COG1196  341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaeeLLEALRAAAELAAQLEELEEAEEALLERLERLE 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-183 2.58e-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: 41.97  E-value: 2.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    61 DLNQVLNETRSQYEALvETNRREVEQwfatQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENT 140
Cdd:TIGR02168  695 ELEKALAELRKELEEL-EEELEQLRK----ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767994715   141 LTESE---ARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVL 183
Cdd:TIGR02168  770 LEEAEeelAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
61-191 4.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  61 DLNQVLNETRSQYEALVETNRREVEQWFATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENT 140
Cdd:COG1196  217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767994715 141 LTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLE 191
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
61-158 9.00e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 9.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  61 DLNQVLNETRSQYEALvETNRREVEQwfatQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAqhnlrdsLENT 140
Cdd:COG4942   31 QLQQEIAELEKELAAL-KKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIAE-------LRAE 98
                         90
                 ....*....|....*...
gi 767994715 141 LTESEARYSSQLSQVQRL 158
Cdd:COG4942   99 LEAQKEELAELLRALYRL 116
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
62-173 1.34e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    62 LNQVLNETRSQYEALvETNRREVEQWFATQTEELNKQVVSSSEQLQSYQAE---IIELRRTvnaleiELQAQHNLRDSLE 138
Cdd:pfam15921   76 IERVLEEYSHQVKDL-QRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR------ESQSQEDLRNQLQ 148
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 767994715   139 NTLTESEA----------RYSSQLSQVQRLITNVESQLAEIRSDL 173
Cdd:pfam15921  149 NTVHELEAakclkedmleDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
86-194 1.35e-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: 39.36  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  86 QWFATQTEELNKQVvsssEQLQSYQAEIIELRRtvnaleiELQAQHNLRDSLENTLTESEARYSSQLSQVQRLITNVESQ 165
Cdd:COG4942  139 QYLKYLAPARREQA----EELRADLAELAALRA-------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
                         90       100
                 ....*....|....*....|....*....
gi 767994715 166 LAEIRSDLERQNQEYQVLLDVRARLECEI 194
Cdd:COG4942  208 LAELAAELAELQQEAEELEALIARLEAEA 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
105-208 1.64e-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: 39.27  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   105 QLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEarysSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLL 184
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELE----EELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100
                   ....*....|....*....|....
gi 767994715   185 DVRARLECEINTYRSLLESEDCKL 208
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERL 770
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
61-189 1.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  61 DLNQVLNETRSQYEALVEtnrrEVEQWfATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENT 140
Cdd:COG4372   63 QLEEELEQARSELEQLEE----ELEEL-NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767994715 141 LTESEARYSSQLSQVQRLitnvESQLAEIRSDLERQNQEYQVLLDVRAR 189
Cdd:COG4372  138 IAELQSEIAEREEELKEL----EEQLESLQEELAALEQELQALSEAEAE 182
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
104-205 1.79e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715 104 EQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESE---ARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEY 180
Cdd:COG4372   45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
                         90       100
                 ....*....|....*....|....*
gi 767994715 181 QVLLDVRARLECEINTYRSLLESED 205
Cdd:COG4372  125 QDLEQQRKQLEAQIAELQSEIAERE 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
61-218 2.30e-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: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    61 DLNQVLNETRSQYEALVETNRReveqwFATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENT 140
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEE-----LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767994715   141 LTESEAryssQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCKLPSNPCATTNA 218
Cdd:TIGR02168  374 LEELEE----QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
34-199 3.06e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   34 ADFEEVNTLRcQLGDRLNVEVDAAPTVDLNQVLNETRSQYEALvETNRREVEQwfatQTEELNKQVVSSSEQLQSYQAEI 113
Cdd:COG4913   266 AARERLAELE-YLRAALRLWFAQRRLELLEAELEELRAELARL-EAELERLEA----RLDALREELDELEAQIRGNGGDR 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  114 IE-LRRTVNALEIELQAQHNLRDSLENTLT-------ESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLD 185
Cdd:COG4913   340 LEqLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
                         170
                  ....*....|....
gi 767994715  186 VRARLECEINTYRS 199
Cdd:COG4913   420 ELRELEAEIASLER 433
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
51-203 3.20e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  51 NVEVDAAPTVDLNQVLNETRSQYEALVETNRREVEQ--------WFATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNA 122
Cdd:COG3206  165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715 123 LEIELQAQHNL----------------RDSLENTLTESEARYSSQLSQVQRL---ITNVESQL-AEIRSDLERQNQEYQV 182
Cdd:COG3206  245 LRAQLGSGPDAlpellqspviqqlraqLAELEAELAELSARYTPNHPDVIALraqIAALRAQLqQEAQRILASLEAELEA 324
                        170       180
                 ....*....|....*....|.
gi 767994715 183 LLDVRARLECEINTYRSLLES 203
Cdd:COG3206  325 LQAREASLQAQLAQLEARLAE 345
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
77-202 3.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  77 VETNRREVEQWFATQTE--ELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNL--RDSLENTLTESEARYSS-- 150
Cdd:COG4717   73 LKELEEELKEAEEKEEEyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqeLEALEAELAELPERLEEle 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767994715 151 ----QLSQVQRLITNVESQLAEIRSDLERQNQeyQVLLDVRARLECEINTYRSLLE 202
Cdd:COG4717  153 erleELRELEEELEELEAELAELQEELEELLE--QLSLATEEELQDLAEELEELQQ 206
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
62-191 3.59e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715  62 LNQVLNETRSQYEAL---VETNRREVEQWFATQT-EELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSL 137
Cdd:COG4717  100 LEEELEELEAELEELreeLEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767994715 138 ENTLTESEARYSSQLSQVQRLITNVESQLAEIRSDLERQNQEYQVLLDVRARLE 191
Cdd:COG4717  180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
62-203 4.00e-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: 38.11  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715    62 LNQVLNETRSQYEAL------------VETNRREVEQW-FATQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQ 128
Cdd:TIGR02168  191 LEDILNELERQLKSLerqaekaerykeLKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767994715   129 aQHNLRDS-LENTLTESEARYSSQLSQVQRLitnvESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLES 203
Cdd:TIGR02168  271 -ELRLEVSeLEEEIEELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
61-204 6.28e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 37.69  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   61 DLNQVLNETRSQYEALvETNRREVEQwfatQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENT 140
Cdd:TIGR04523 339 QLNEQISQLKKELTNS-ESENSEKQR----ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767994715  141 LTESEARYSSQLSQVQRLITNVESQLAEIrSDLERQNQEYQVLLDVRARLECEINTYRSLLESE 204
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEI-KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
PRK11281 PRK11281
mechanosensitive channel MscK;
62-181 7.85e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 37.20  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994715   62 LNQVLNETRSQYEALVETNRReveqwfatqTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDsLENTL 141
Cdd:PRK11281   61 VQQDLEQTLALLDKIDRQKEE---------TEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ-LESRL 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767994715  142 TESearySSQLSQVQRLITNVESQLAEIRSDLER-QNQEYQ 181
Cdd:PRK11281  131 AQT----LDQLQNAQNDLAEYNSQLVSLQTQPERaQAALYA 167
 
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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