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Conserved domains on  [gi|664806102|ref|NP_001287739|]
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keratin, type II cuticular Hb5 isoform 2 [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;
18-221 1.08e-85

Intermediate filament protein;


The actual alignment was detected with superfamily member pfam00038:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 259.08  E-value: 1.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   18 QDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAE 97
Cdd:pfam00038 110 KDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   98 AESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELE 177
Cdd:pfam00038 190 AEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELE 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 664806102  178 GALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 221
Cdd:pfam00038 270 AELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
18-221 1.08e-85

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 259.08  E-value: 1.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   18 QDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAE 97
Cdd:pfam00038 110 KDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   98 AESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELE 177
Cdd:pfam00038 190 AEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELE 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 664806102  178 GALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 221
Cdd:pfam00038 270 AELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-194 5.83e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102    28 SDLEANVEAL---VEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAEAESWYRS 104
Cdd:TIGR02169  304 ASLERSIAEKereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   105 KCEEMKATvirhgETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQ---QGEAALSDARCKLAELEGALQ 181
Cdd:TIGR02169  384 RDELKDYR-----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLE 458

                          170
                   ....*....|...
gi 664806102   182 KAKQDMACLLKEY 194
Cdd:TIGR02169  459 QLAADLSKYEQEL 471
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 120-200 1.05e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102 120 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALSDARCKLAELEGALQKAKQDMACLLKEYQE 196
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108


                 ....
gi 664806102 197 VMNS 200
Cdd:COG4942  109 LLRA 112
PRK11281 PRK11281
mechanosensitive channel MscK;
81-188 1.41e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.36  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   81 AEIKAQYDDVASRSRAEAESwyrskceemKATVIRHGETLR------RTKEEINELNRMIQRLTAEIENAKCQRAKLEAA 154
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 664806102  155 VAEAEQQGEAALSDARC--KLAELEGALQKAKQDMA 188
Cdd:PRK11281  110 NDEETRETLSTLSLRQLesRLAQTLDQLQNAQNDLA 145
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
18-221 1.08e-85

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 259.08  E-value: 1.08e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   18 QDVDCAYLRKSDLEANVEALVEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAE 97
Cdd:pfam00038 110 KDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   98 AESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELE 177
Cdd:pfam00038 190 AEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELE 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 664806102  178 GALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 221
Cdd:pfam00038 270 AELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 28-194 5.83e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102    28 SDLEANVEAL---VEESSFLRRLYEEEIRVLQAHISDTSVIVKMDNSRDLNMDCIIAEIKAQYDDVASRSRAEAESWYRS 104
Cdd:TIGR02169  304 ASLERSIAEKereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   105 KCEEMKATvirhgETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQ---QGEAALSDARCKLAELEGALQ 181
Cdd:TIGR02169  384 RDELKDYR-----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLE 458

                          170
                   ....*....|...
gi 664806102   182 KAKQDMACLLKEY 194
Cdd:TIGR02169  459 QLAADLSKYEQEL 471
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 120-200 1.05e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102 120 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALSDARCKLAELEGALQKAKQDMACLLKEYQE 196
Cdd:COG4942   29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108


                 ....
gi 664806102 197 VMNS 200
Cdd:COG4942  109 LLRA 112
PRK11281 PRK11281
mechanosensitive channel MscK;
81-188 1.41e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 43.36  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   81 AEIKAQYDDVASRSRAEAESwyrskceemKATVIRHGETLR------RTKEEINELNRMIQRLTAEIENAKCQRAKLEAA 154
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 664806102  155 VAEAEQQGEAALSDARC--KLAELEGALQKAKQDMA 188
Cdd:PRK11281  110 NDEETRETLSTLSLRQLesRLAQTLDQLQNAQNDLA 145
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 108-198 1.62e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102  108 EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKA 183
Cdd:pfam07888 297 EGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVA 376

                          90
                  ....*....|....*
gi 664806102  184 KQDMACLLKEYQEVM 198
Cdd:pfam07888 377 QKEKEQLQAEKQELL 391
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
80-184 4.00e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102  80 IAEIKAQYDDVASRSRAEAESWYRSKCEEMKATVIRHGETLRRTKE-EINELNRM--IQRLTAEIEnakcQRAKLEAAVA 156
Cdd:COG2268  246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEreEAELEADVR----KPAEAEKQAA 321

                         90       100
                 ....*....|....*....|....*...
gi 664806102 157 EAEQQGEAALSDARCKlAELEGALQKAK 184
Cdd:COG2268  322 EAEAEAEAEAIRAKGL-AEAEGKRALAE 348
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-222 4.63e-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: 41.58  E-value: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102    48 YEEEIRVLQAHISDTSVIVKMDNSRDLNMdcIIAEIKAQYDDVASRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKE 125
Cdd:TIGR02168  218 LKAELRELELALLVLRLEELREELEELQE--ELKEAEEELEELTAELQELEEKLeeLRLEVSELEEEIEELQKELYALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   126 EINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGE---AALSDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKL 202
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375

                          170       180
                   ....*....|....*....|
gi 664806102   203 GLDIEIATYRRLLEGEEHRL 222
Cdd:TIGR02168  376 ELEEQLETLRSKVAQLELQI 395
PRK12704 PRK12704
phosphodiesterase; Provisional
 82-196 5.65e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102  82 EIKAQYDDVASRSRAEAESWYRSKCEEMKAT---VIRHGETLRRTKEEI----NELNRMIQRLTAEIENAKCQRAKLEAA 154
Cdd:PRK12704  57 EALLEAKEEIHKLRNEFEKELRERRNELQKLekrLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEEL 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 664806102 155 VAEAEQQGE--AALS--DARCKLaeLEGALQKAKQDMACLLKEYQE 196
Cdd:PRK12704 137 IEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 80-222 5.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102  80 IAEIKAQYDDVASRSRAEAESWYrskceEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAE 159
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEY-----ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806102 160 QQG----------EAALSDARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHRL 222
Cdd:COG1196  344 EELeeaeeeleeaEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 118-196 1.71e-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: 1.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806102 118 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLSDARCKLAELEGALQKAKQDMACLLKEYQE 196
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAE 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 103-213 2.22e-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: 39.65  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   103 RSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQ---QGEAALSDARCKLAELEGA 179
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNeraSLEEALALLRSELEELSEE 902

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 664806102   180 LQKAKQDMACLLKEYQEVMN--SKLGLDIEIATYRR 213
Cdd:TIGR02168  903 LRELESKRSELRRELEELREklAQLELRLEGLEVRI 938
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-222 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: 39.65  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102    26 RKSDLEANVEALVEESSFLRR---LYEEEIRVLQAHISDTSVIVKMdnsrdlnMDCIIAEIKAQYDDVASRSRAEAESWy 102
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERqleELEAQLEELESKLDELAEELAE-------LEEKLEELKEELESLEAELEELEAEL- 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   103 rskcEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDA-RCKLAELEGALQ 181
Cdd:TIGR02168  368 ----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELE 443

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 664806102   182 KAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLL---EGEEHRL 222
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALdaaERELAQL 487
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 124-204 3.07e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102 124 KEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKAKQDMAC--------LLKEYQ 195
Cdd:COG1579  102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREElaakippeLLALYE 181


                 ....*....
gi 664806102 196 EVMNSKLGL 204
Cdd:COG1579  182 RIRKRKNGL 190
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 26-186 7.72e-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: 37.44  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102  26 RKSDLEANVEALVEESSFLRRLYEEEIRVLQAH--ISDTSVIVKMDNSRDlnmdciiAEIKAQYDDVASRSRAEaeswyr 103
Cdd:COG4942   84 ELAELEKEIAELRAELEAQKEELAELLRALYRLgrQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------ 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102 104 skceemkatvirHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALSDARCKLAELEGALQKA 183
Cdd:COG4942  151 ------------QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218


                 ...
gi 664806102 184 KQD 186
Cdd:COG4942  219 QQE 221
TMCO5 pfam14992
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ...
 28-218 7.80e-03

TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.


Pssm-ID: 464427 [Multi-domain]  Cd Length: 278  Bit Score: 37.39  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102   28 SDLEANVEALVEES-SFLRRLY--EEEIRVLQAHISDTSVIVKMDNSRDLNmdCIIAEikaqyddvasRSRAEAEswyrs 104
Cdd:pfam14992   6 SDLEKDLQRLDEANqVLLLKIQekEEEIQSLEREITLTRSLAEDEEREELN--FTIME----------KEDALQE----- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102  105 kCEEMKATVIRHGETLRRtkeEINELNRMIQRltAEIENAKCQRAKLEAAVAEAE---QQGEAALSDARCKLAELEGALQ 181
Cdd:pfam14992  69 -LELETAKLEKKNEILVK---SVMELQRKLSR--KSDKNTGLEQETLKQMLEELKvklQQSEESCADQEKELAKVESDYQ 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 664806102  182 KAKQ---DMACLLKEYQEVMNSklgldIEIATYRRLLEGE 218
Cdd:pfam14992 143 SVHQlceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 27-183 8.68e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 37.85  E-value: 8.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102    27 KSDLEANVEALVEESSFLRRLYEEEIRvLQAHISDtsVIVKMDNSRDL---------NMDCIIAE---IKAQYDDvaSRS 94
Cdd:pfam01576  551 QRELEALTQQLEEKAAAYDKLEKTKNR-LQQELDD--LLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERD 625

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102    95 RAEAESwyRSKceEMKA-TVIRHGETLRRTKEEINELNRMiqrLTAEIENAKCQRAKLEAAVAEAEQQG---EAALSDAR 170
Cdd:pfam01576  626 RAEAEA--REK--ETRAlSLARALEEALEAKEELERTNKQ---LRAEMEDLVSSKDDVGKNVHELERSKralEQQVEEMK 698

                          170
                   ....*....|...
gi 664806102   171 CKLAELEGALQKA 183
Cdd:pfam01576  699 TQLEELEDELQAT 711
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
120-222 9.00e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.19  E-value: 9.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806102 120 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALSDARCKLAELEGALQKAKQDMACLLKEYQE 196
Cdd:COG4372   47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                         90       100
                 ....*....|....*....|....*.
gi 664806102 197 VMNSKLGLDIEIATYRRLLEGEEHRL 222
Cdd:COG4372  127 LEQQRKQLEAQIAELQSEIAEREEEL 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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