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Conserved domains on  [gi|131888757|ref|NP_001076574|]
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keratin, type I cytoskeletal 17 [Danio rerio]

Protein Classification

intermediate filament family protein( domain architecture ID 11981676)

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 pfam00038
Intermediate filament protein;
72-380 1.92e-120

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.69  E-value: 1.92e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   72 NEKATMQNLNDRLASYLEKVRILEKENADLELKIRQFLDSKATPNARDYSAYYATISDLQAKILHATGVNAGIYLHIDNA 151
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  152 KLAADDFKVKFDNEQSMRHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEEELLAARTQMG-GQVNVEV 230
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  231 DAAPQEDLTKIIADIREHYEAVSAKYQKDFEQWFQSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMK 310
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  311 ASLEGTLADTQARYANMLNGYQLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLLDGE 380
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
72-380 1.92e-120

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.69  E-value: 1.92e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   72 NEKATMQNLNDRLASYLEKVRILEKENADLELKIRQFLDSKATPNARDYSAYYATISDLQAKILHATGVNAGIYLHIDNA 151
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  152 KLAADDFKVKFDNEQSMRHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEEELLAARTQMG-GQVNVEV 230
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  231 DAAPQEDLTKIIADIREHYEAVSAKYQKDFEQWFQSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMK 310
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  311 ASLEGTLADTQARYANMLNGYQLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLLDGE 380
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
169-378 1.17e-06

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: 50.83  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   169 RHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEEelLAARTQMGGQVNVEvDAAPQEDLTKIIADIREH 248
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE--LEAQLEELESKLDE-LAEELAELEEKLEELKEE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   249 YEAVSAKYQKDFEQWFQSKSESLNKEVAastetLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQAR----- 323
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEieell 427
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 131888757   324 ---YANMLNGYQLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLLD 378
Cdd:TIGR02168  428 kklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
148-355 3.29e-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: 45.91  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 148 IDNAKLAADDFKVKFDNEQSMRHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEE------ELLAARTQ 221
Cdd:COG4942   36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqkeelaELLRALYR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 222 MGGQVNVEVDAAPQEdltkiIADIrehyeAVSAKYQKDFEQWFQSKSESLN---KEVAASTETLQSSRSEFTELKRTLQS 298
Cdd:COG4942  116 LGRQPPLALLLSPED-----FLDA-----VRRLQYLKYLAPARREQAEELRadlAELAALRAELEAERAELEALLAELEE 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 131888757 299 LQIELQSQLSMKASLEGTLADTQARYANMLNGYQLQVGSLEEQLVHLRGDLERQRQE 355
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
172-378 1.04e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 172 VEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLkknhEEELLAARTQMG-GQVNVEVDAAPQEDLTKIIADIREHYE 250
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEEL----EEERDDLLAEAGlDDADAEAVEARREELEDRDEELRDRLE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 251 AVSAKYQKdfeqwFQSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQARYANMlng 330
Cdd:PRK02224 332 ECRVAAQA-----HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA--- 403
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 131888757 331 yQLQVGSLEEQLVHLRGDLERQRQEYQML-LDIKTrLEMEIAEYRRLLD 378
Cdd:PRK02224 404 -PVDLGNAEDFLEELREERDELREREAELeATLRT-ARERVEEAEALLE 450
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
72-380 1.92e-120

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 352.69  E-value: 1.92e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   72 NEKATMQNLNDRLASYLEKVRILEKENADLELKIRQFLDSKATPNARDYSAYYATISDLQAKILHATGVNAGIYLHIDNA 151
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  152 KLAADDFKVKFDNEQSMRHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEEELLAARTQMG-GQVNVEV 230
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  231 DAAPQEDLTKIIADIREHYEAVSAKYQKDFEQWFQSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMK 310
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  311 ASLEGTLADTQARYANMLNGYQLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLLDGE 380
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGE 310
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
169-378 1.17e-06

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: 50.83  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   169 RHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEEelLAARTQMGGQVNVEvDAAPQEDLTKIIADIREH 248
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE--LEAQLEELESKLDE-LAEELAELEEKLEELKEE 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   249 YEAVSAKYQKDFEQWFQSKSESLNKEVAastetLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQAR----- 323
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEieell 427
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 131888757   324 ---YANMLNGYQLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLLD 378
Cdd:TIGR02168  428 kklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
148-355 3.29e-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: 45.91  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 148 IDNAKLAADDFKVKFDNEQSMRHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEE------ELLAARTQ 221
Cdd:COG4942   36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqkeelaELLRALYR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 222 MGGQVNVEVDAAPQEdltkiIADIrehyeAVSAKYQKDFEQWFQSKSESLN---KEVAASTETLQSSRSEFTELKRTLQS 298
Cdd:COG4942  116 LGRQPPLALLLSPED-----FLDA-----VRRLQYLKYLAPARREQAEELRadlAELAALRAELEAERAELEALLAELEE 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 131888757 299 LQIELQSQLSMKASLEGTLADTQARYANMLNGYQLQVGSLEEQLVHLRGDLERQRQE 355
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
171-407 5.88e-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: 45.44  E-value: 5.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   171 AVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFL----KKNHEEELLAARTQMGG--------QVNVEVDAAPQEDL 238
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGEleaeiaslERSIAEKERELEDA 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   239 TKIIADIREHYEAVSAK----------YQKDFEQW-------------FQSKSESLNKEVAASTETLQSSRSEFTELKRT 295
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEieelereieeERKRRDKLteeyaelkeeledLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   296 LQSLQIELQSQLSMKASLEGTLADTQARYANMLNGY----------QLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTR 365
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneleeekedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 131888757   366 LEMEIAEYRRLLDGEATSVSTSSSKTSTTRKVVTIVEEVVDG 407
Cdd:TIGR02169  481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
169-398 3.77e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 169 RHAVEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLKKNHEEELLAArTQMGGQVNVEVDAAPQEDLTKIIADIR-E 247
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERrR 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 248 HYEAVSAKYQKDFEQWfQSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQARYANM 327
Cdd:COG1196  313 ELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 131888757 328 LNG---YQLQVGSLEEQLVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLLDGEATSVSTSSSKTSTTRKVV 398
Cdd:COG1196  392 LRAaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-377 5.79e-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: 42.35  E-value: 5.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   265 QSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQARYANMLNG---YQLQVGSLEEQ 341
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESK 331
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 131888757   342 LVHLRGDLERQRQEYQMLLDIKTRLEMEIAEYRRLL 377
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
172-378 1.04e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 172 VEADISGLRKVLDELTMTRSDLEMQIEGLKEELVFLkknhEEELLAARTQMG-GQVNVEVDAAPQEDLTKIIADIREHYE 250
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEEL----EEERDDLLAEAGlDDADAEAVEARREELEDRDEELRDRLE 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757 251 AVSAKYQKdfeqwFQSKSESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQARYANMlng 330
Cdd:PRK02224 332 ECRVAAQA-----HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA--- 403
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 131888757 331 yQLQVGSLEEQLVHLRGDLERQRQEYQML-LDIKTrLEMEIAEYRRLLD 378
Cdd:PRK02224 404 -PVDLGNAEDFLEELREERDELREREAELeATLRT-ARERVEEAEALLE 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
274-378 1.14e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757  274 EVAASTETLQSSRSEFTELKRTLQSLQiELQSQLSMKASLEGTLADTQARYANMLNGyQLQVGSLEEQLVHLRGDLERQR 353
Cdd:COG4913   628 EAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELEAELERLDAS-SDDLAALEEQLEELEAELEELE 705
                          90       100
                  ....*....|....*....|....*
gi 131888757  354 QEYQMLLDIKTRLEMEIAEYRRLLD 378
Cdd:COG4913   706 EELDELKGEIGRLEKELEQAEEELD 730
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
177-378 8.24e-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: 38.56  E-value: 8.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   177 SGLRKVLDELTMTRSDL-------EMQIEGLKEE----LVFLKKNHEEELlaarTQMGGQVNVEVDAapqedLTKIIADI 245
Cdd:pfam15921  220 SAISKILRELDTEISYLkgrifpvEDQLEALKSEsqnkIELLLQQHQDRI----EQLISEHEVEITG-----LTEKASSA 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   246 REHYEAVSAKYQKDFEQWFQSKSESLnKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMkASLEGTLADTQArya 325
Cdd:pfam15921  291 RSQANSIQSQLEIIQEQARNQNSMYM-RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL-ANSELTEARTER--- 365
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   326 nmlNGYQLQVGSLEEQLVHLRGDLERQRQEYQM-------LLDIKTRLEMEIAEYRRLLD 378
Cdd:pfam15921  366 ---DQFSQESGNLDDQLQKLLADLHKREKELSLekeqnkrLWDRDTGNSITIDHLRRELD 422
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
102-381 9.78e-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: 38.23  E-value: 9.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   102 ELKIRQFLDSKATPNARDYSAYYATISDLQAKILHATGVNAGIYLHIDNAKLAADDFKVKFDNEQSMRHAVEADISGLRK 181
Cdd:pfam01576  199 EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   182 VLDELTMTRSDLEMQIEGLKEELVFLKKNHEEEL--LAARTQMGGQVNVEVDAAPQ--EDLTKI----IADIREHYEAVS 253
Cdd:pfam01576  279 DLESERAARNKAEKQRRDLGEELEALKTELEDTLdtTAAQQELRSKREQEVTELKKalEEETRSheaqLQEMRQKHTQAL 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   254 AKYQKDFEQWFQSKS---------ESLNKEVAASTETLQSSRSEFTELKRTLQSLQIELQSQLSMKASLEGTLADTQARY 324
Cdd:pfam01576  359 EELTEQLEQAKRNKAnlekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888757   325 ANMLNGYQLQVGSLEEQLVHLRGD---LERQRQEYQMLLDIKTRLEMEIAEYRRLLDGEA 381
Cdd:pfam01576  439 QSELESVSSLLNEAEGKNIKLSKDvssLESQLQDTQELLQEETRQKLNLSTRLRQLEDER 498
 
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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