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Conserved domains on  [gi|118130981|ref|NP_034791|]
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keratin, type I cytoskeletal 12 [Mus musculus]

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
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 pfam00038
Intermediate filament protein;
118-428 5.26e-127

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 371.95  E-value: 5.26e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  118 SEKETMQNLNDRLASYLGKVRSLEEANAELENKIREWYETRRtrdAGSQSDYSKYYPLIEDLKNKIVSARVSNAQLLLQI 197
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG---AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  198 DNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAG-GPGEVN 276
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  277 VEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEAWFLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQL 356
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118130981  357 AMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEG 428
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
118-428 5.26e-127

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 371.95  E-value: 5.26e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  118 SEKETMQNLNDRLASYLGKVRSLEEANAELENKIREWYETRRtrdAGSQSDYSKYYPLIEDLKNKIVSARVSNAQLLLQI 197
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG---AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  198 DNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAG-GPGEVN 276
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  277 VEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEAWFLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQL 356
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118130981  357 AMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEG 428
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-421 9.90e-09

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: 58.14  E-value: 9.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   176 IEDLKNKIVSARVSNAQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELA- 254
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEe 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   255 --YMKKNHEEELQSFQAggpgEVNVEMDAApgVDLTKVLNEMRAQYEAM----------AEQNRKDAEAWfLEKSRELRK 322
Cdd:TIGR02168  773 aeEELAEAEAEIEELEA----QIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT-ERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   323 EISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGgyccQLSQVQQLIGSLEEQLQQVRADAERQN 402
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS----ELEELSEELRELESKRSELRRELEELR 921

                          250
                   ....*....|....*....
gi 118130981   403 ADHQRLLGVKARLEMEIET 421
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 191-401 4.12e-07

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: 52.07  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 191 AQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQ----- 265
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelael 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 266 ---SFQAGGPGEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQnrkdaeawfLEKSRELRKEISSNTEQLQSSKSEVTDLK 342
Cdd:COG4942  110 lraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ---------AEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118130981 343 RMVQNLEIELQSQLAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQ 401
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
46 PHA02562
endonuclease subunit; Provisional
 137-351 1.89e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 137 VRSLEEANAELENKIREWYETRRTRDAGSQSDYSKyyplIEDLKNKIVSARVSNAQlllqidnarlAAEDFRMKYENELA 216
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQ----IKTYNKNIEEQRKKNGE----------NIARKQNKYDELVE 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 217 LRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHE---EELQSFQAGG----------PGEVNVEMDAAP 283
Cdd:PHA02562 228 EAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqKVIKMYEKGGvcptctqqisEGPDRITKIKDK 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118130981 284 GVDLTKVLNEMRAQYEAMAEQNRKDAEAwfLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIE 351
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQ--SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 189-343 5.35e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   189 SNAQLLLQIDNARLAAE----DFRMKYENelALRQTVEADINGLRRVLDELTltraDLEAQLETLTEELAYMKKNHEEEL 264
Cdd:smart00787 115 MDKQFQLVKTFARLEAKkmwyEWRMKLLE--GLKEGLDENLEGLKEDYKLLM----KELELLNSIKPKLRDRKDALEEEL 188

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118130981   265 QSFQaggpgEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEawFLEKSRELRKEISSNTEQLQSSKSEVTDLKR 343
Cdd:smart00787 189 RQLK-----QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEK 260
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
118-428 5.26e-127

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 371.95  E-value: 5.26e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  118 SEKETMQNLNDRLASYLGKVRSLEEANAELENKIREWYETRRtrdAGSQSDYSKYYPLIEDLKNKIVSARVSNAQLLLQI 197
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKG---AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  198 DNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAG-GPGEVN 276
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  277 VEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEAWFLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQL 356
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118130981  357 AMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEG 428
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-421 9.90e-09

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: 58.14  E-value: 9.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   176 IEDLKNKIVSARVSNAQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELA- 254
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEe 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   255 --YMKKNHEEELQSFQAggpgEVNVEMDAApgVDLTKVLNEMRAQYEAM----------AEQNRKDAEAWfLEKSRELRK 322
Cdd:TIGR02168  773 aeEELAEAEAEIEELEA----QIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT-ERRLEDLEE 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   323 EISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGgyccQLSQVQQLIGSLEEQLQQVRADAERQN 402
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS----ELEELSEELRELESKRSELRRELEELR 921

                          250
                   ....*....|....*....
gi 118130981   403 ADHQRLLGVKARLEMEIET 421
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDN 940
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-349 3.55e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 3.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   123 MQNLNDRLASYLGKVRSLEEANAELENKIREwyetRRTRDAGSQSDYSKYYPLIEDLKNKIV-----SARVSN--AQLLL 195
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQI----LRERLANLERQLEELEAQLEELESKLDelaeeLAELEEklEELKE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   196 QIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAGGPGEV 275
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118130981   276 NVEMDAAPG--VDLTKVLNEMRAQYEAMAEQNRKDAEAwflekSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLE 349
Cdd:TIGR02168  432 EAELKELQAelEELEEELEELQEELERLEEALEELREE-----LEEAEQALDAAERELAQLQARLDSLERLQENLE 502
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 191-401 4.12e-07

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: 52.07  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 191 AQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQ----- 265
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelael 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 266 ---SFQAGGPGEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQnrkdaeawfLEKSRELRKEISSNTEQLQSSKSEVTDLK 342
Cdd:COG4942  110 lraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ---------AEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118130981 343 RMVQNLEIELQSQLAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQ 401
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 210-427 8.47e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 8.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 210 KYENELAL--RQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAGGPGEVNVEMDAAPGVDL 287
Cdd:COG1196  224 ELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 288 TKVLNEMRAQYEAMAEQNRKDAEAWfLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLA 367
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 368 ETEGgyccQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLE 427
Cdd:COG1196  383 ELAE----ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 129-432 4.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 129 RLASYLGKVRSLEEANAELENKIREWYETRRTRDAGsqsdyskyyplIEDLKNKIVSARVSNAQLLLQIDNARLAAEDFR 208
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLELEELELELEEAQAEEYELLAELARLE 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 209 MKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQaggpgEVNVEMDAApgvdlt 288
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-----EAEEALLEA------ 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 289 kvLNEMRAQYEAMAEQNRKDAEAwfLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAE 368
Cdd:COG1196  371 --EAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118130981 369 TEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETyRRLLEGDSQG 432
Cdd:COG1196  447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEG 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 120-432 5.03e-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: 49.28  E-value: 5.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   120 KETMQNLNDRLASYLGKVRSLE------EANAELENKIREW--------YETRRTRDAGSQSDYSKYYPLIEDLKNKIVS 185
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELelallvlrLEELREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   186 ARVSNAQLLLQIDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETL---TEELAYMKKNHEE 262
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELAELEE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   263 ELQSFQaggpgeVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQ--NRKDAEAWFLEKSRELRKEISSNTEQLQSSKSEVTD 340
Cdd:TIGR02168  345 KLEELK------EELESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   341 LKRMVQNLEIELQSqlAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMeIE 420
Cdd:TIGR02168  419 LQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LE 495

                          330
                   ....*....|..
gi 118130981   421 TYRRLLEGDSQG 432
Cdd:TIGR02168  496 RLQENLEGFSEG 507
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 229-428 2.93e-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: 46.97  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   229 RRVLDELTLTRADLEAQLETLTEELAYMKKNHEEelqsfqaggpGEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKD 308
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEE----------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   309 AEAW---------FLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGGYCCQLSQ 379
Cdd:TIGR02168  746 EERIaqlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 118130981   380 VQQL---IGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLEG 428
Cdd:TIGR02168  826 LESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
228-427 4.04e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 228 LRRVLDELTLTRADLEAQLETLTEELAymkkNHEEELQSFQAGGpGEVNVEMDAApgvDLTKVLNEMRAQYEAmAEQNRK 307
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKN-GLVDLSEEAK---LLLQQLSELESQLAE-ARAELA 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 308 DAEAWFLEKSRELRKEISSNTEQLQSS-----KSEVTDLKRMVQNLE----------IELQSQLA-MKSSLEGSLAETEG 371
Cdd:COG3206  237 EAEARLAALRAQLGSGPDALPELLQSPviqqlRAQLAELEAELAELSarytpnhpdvIALRAQIAaLRAQLQQEAQRILA 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118130981 372 GYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLlgvkARLEMEIETYRRLLE 427
Cdd:COG3206  317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARELYE 368
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 119-427 2.16e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   119 EKETMQNLNDRLASYLGK--VRSLEEANAELENKIREWYETRRTRDagsqsdysKYYPLIEDLKNKIVSARVSNAQLLLQ 196
Cdd:TIGR02169  209 KAERYQALLKEKREYEGYelLKEKEALERQKEAIERQLASLEEELE--------KLTEEISELEKRLEEIEQLLEELNKK 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   197 IDnarlaaedfRMKYENELALRQT---VEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEelqsfQAGGPG 273
Cdd:TIGR02169  281 IK---------DLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-----LEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   274 EVNVEMDAapgvdLTKVLNEMRAQYEAM---AEQNRKDAEAWFlEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEI 350
Cdd:TIGR02169  347 EERKRRDK-----LTEEYAELKEELEDLraeLEEVDKEFAETR-DELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118130981   351 ELQSQLAMKSSLEGSLAETEGgyccQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIETYRRLLE 427
Cdd:TIGR02169  421 ELADLNAAIAGIEAKINELEE----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 198-343 1.74e-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: 40.93  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   198 DNARLAAEDFRMKYENELALRQTvEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEELQSFQAGGPGEVNV 277
Cdd:pfam01576  472 DTQELLQEETRQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118130981   278 EMDAApgvDLTKVLNEMRAQYEAmaeqnrkdaeawfLEKSRE-LRKEISSNTEQLQSSKSEVTDLKR 343
Cdd:pfam01576  551 QRELE---ALTQQLEEKAAAYDK-------------LEKTKNrLQQELDDLLVDLDHQRQLVSNLEK 601
46 PHA02562
endonuclease subunit; Provisional
 137-351 1.89e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 137 VRSLEEANAELENKIREWYETRRTRDAGSQSDYSKyyplIEDLKNKIVSARVSNAQlllqidnarlAAEDFRMKYENELA 216
Cdd:PHA02562 162 ISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQ----IKTYNKNIEEQRKKNGE----------NIARKQNKYDELVE 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 217 LRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHE---EELQSFQAGG----------PGEVNVEMDAAP 283
Cdd:PHA02562 228 EAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqKVIKMYEKGGvcptctqqisEGPDRITKIKDK 307

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118130981 284 GVDLTKVLNEMRAQYEAMAEQNRKDAEAwfLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIE 351
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQ--SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 216-394 2.91e-03

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: 40.26  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  216 ALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEelqsfqaggpgevnvemdaapgvdLTKVLNEMR 295
Cdd:pfam07888  52 AANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEE------------------------LEEKYKELS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  296 AQYEAMAEQNRK--DAEAWFLEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEGGY 373
Cdd:pfam07888 108 ASSEELSEEKDAllAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187

                         170       180
                  ....*....|....*....|.
gi 118130981  374 CCQLSQVQQLIGSLEEQLQQV 394
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQV 208
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 219-420 3.61e-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: 39.14  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 219 QTVEADINGLRRVLDELTLTRADLEAQLETLTEELAYMKKNHEEelqsfqaggpgevnvemdaapgvdltkvLNEMRAQY 298
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED----------------------------LEKEIKRL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 299 EAMAEQNRKDaeawfLEKSRELRKEISSNtEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETEggyccqlS 378
Cdd:COG1579   65 ELEIEEVEAR-----IKKYEEQLGNVRNN-KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE-------A 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 118130981 379 QVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKARLEMEIE 420
Cdd:COG1579  132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 189-343 5.35e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.85  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   189 SNAQLLLQIDNARLAAE----DFRMKYENelALRQTVEADINGLRRVLDELTltraDLEAQLETLTEELAYMKKNHEEEL 264
Cdd:smart00787 115 MDKQFQLVKTFARLEAKkmwyEWRMKLLE--GLKEGLDENLEGLKEDYKLLM----KELELLNSIKPKLRDRKDALEEEL 188

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118130981   265 QSFQaggpgEVNVEMDAAPGVDLTKVLNEMRAQYEAMAEQNRKDAEawFLEKSRELRKEISSNTEQLQSSKSEVTDLKR 343
Cdd:smart00787 189 RQLK-----QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEK 260
PRK11281 PRK11281
mechanosensitive channel MscK;
238-431 7.60e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  238 TRADLEAQLETLTEelaymKKNHEEELQSFQAggpgevnvemdaapgvDLTKVLnemraQYEAMAEQNRKDAEAwfleks 317
Cdd:PRK11281   37 TEADVQAQLDALNK-----QKLLEAEDKLVQQ----------------DLEQTL-----ALLDKIDRQKEETEQ------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981  318 reLRKEISSNTEQLQSSKSEVTDLKRMVQ--------NLEI-ELQSQLAMKSSLEGSLAETEGGYCCQLS-------QVQ 381
Cdd:PRK11281   85 --LKQQLAQAPAKLRQAQAELEALKDDNDeetretlsTLSLrQLESRLAQTLDQLQNAQNDLAEYNSQLVslqtqpeRAQ 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 118130981  382 QLIGSLEEQLQQVR-------ADAERQNADHQRLLGVK-ARLEMEIETYRRLLEGDSQ 431
Cdd:PRK11281  163 AALYANSQRLQQIRnllkggkVGGKALRPSQRVLLQAEqALLNAQNDLQRKSLEGNTQ 220
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 241-427 8.58e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 8.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   241 DLEAQLETLTEELAYMKKNHEEELQSFQaggpgevnvemdaapgvDLTKVLNEMRAQYEAMAEQNRKdaeawFLEKSREL 320
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELS-----------------DASRKIGEIEKEIEQLEQEEEK-----LKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981   321 RKEISSNTEQLQSSKSEVTDLKRMVQNLEIELQSQLAMKSSLEGSLAETeggyccQLSQVQQLIGSLEEQLQQVRADAER 400
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS------RIPEIQAELSKLEEEVSRIEARLRE 816

                          170       180       190
                   ....*....|....*....|....*....|
gi 118130981   401 QNADHQRLLGVKARLEMEIET---YRRLLE 427
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQElqeQRIDLK 846
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
120-423 9.93e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 9.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 120 KETMQNLNDRLASYLGK---VRSLEEANAELENKIREwyeTRRTRdagsqsdyskyypliEDLKNKIVSARVSNAQLLLQ 196
Cdd:PRK02224 233 RETRDEADEVLEEHEERreeLETLEAEIEDLRETIAE---TERER---------------EELAEEVRDLRERLEELEEE 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 197 IDNARLAAEDFRMKYENELALRQTVEADINGLRRVLDELTLTRADLEAQLETLTEELaymkKNHEEELQSFQAGGpGEVN 276
Cdd:PRK02224 295 RDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREEA-AELE 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118130981 277 VEMDAApgvdlTKVLNEMRAQYEAMAEQNRkDAEAWF------LEKSRELRKEISSNTEQLQSSKSEVTDLKRMVQNLEI 350
Cdd:PRK02224 370 SELEEA-----REAVEDRREEIEELEEEIE-ELRERFgdapvdLGNAEDFLEELREERDELREREAELEATLRTARERVE 443

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118130981 351 ELQSQLAMKSSLEGSLAETEGGYCCQLSQVQQLIGSLEEQLQQVRADAERQNADHQRLLGVKArLEMEIETYR 423
Cdd:PRK02224 444 EAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLE 515
 
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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