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Conserved domains on  [gi|1622879458|ref|XP_014975079|]
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keratin, type I cytoskeletal 10 [Macaca mulatta]

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;
134-443 3.92e-124

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 367.32  E-value: 3.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 134 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGQPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 213
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 214 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 292
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 293 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQL 372
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622879458 373 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
134-443 3.92e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 367.32  E-value: 3.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 134 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGQPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 213
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 214 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 292
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 293 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQL 372
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622879458 373 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-436 3.46e-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: 50.06  E-value: 3.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  152 KVRALEESNYELEGKIKEWYEKHGNSHQgqprDYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEV 231
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEE----ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  232 ALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTG----DVNVEMNAAPGVDLTQLL 307
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  308 NNMRSQYEQLAEQ------NRKDAEAWFNEKSKEL---TTEIDSNIEQMSSHKSEITELRRTVQALE---IELQSQLALK 375
Cdd:TIGR02168  841 EDLEEQIEELSEDieslaaEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELEskrSELRRELEEL 920
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622879458  376 QSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKI-RLENEIQ 436
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLkRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
225-443 5.95e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 225 LKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPgvdLT 304
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 305 QLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASLAE 384
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622879458 385 TEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
46 PHA02562
endonuclease subunit; Provisional
195-438 1.93e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 195 LKNQILNLTTDNANILLQIDNARLAADDFRlKYENEvaLRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKK 274
Cdd:PHA02562  172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYN-KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 275 NHEEEMKDLRNVSTGDVNVEMNaapgVDLTQLLNNMRSQY-------EQLAEQNRKDAEAwfNEKSKELTT---EIDSNI 344
Cdd:PHA02562  249 DIEDPSAALNKLNTAAAKIKSK----IEQFQKVIKMYEKGgvcptctQQISEGPDRITKI--KDKLKELQHsleKLDTAI 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 345 EQMSSHKSEITELRRTVQaleiELQSQLA-LKQSLEASLAetegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 423
Cdd:PHA02562  323 DELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
                         250
                  ....*....|....*
gi 1622879458 424 LLDIKIRLENEIQTY 438
Cdd:PHA02562  391 IVKTKSELVKEKYHR 405
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
134-443 3.92e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 367.32  E-value: 3.92e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 134 NEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHgnsHQGQPRDYSKYYKTIDDLKNQILNLTTDNANILLQI 213
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK---GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 214 DNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRN-VSTGDVN 292
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 293 VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQL 372
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622879458 373 ALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-436 3.46e-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: 50.06  E-value: 3.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  152 KVRALEESNYELEGKIKEWYEKHGNSHQgqprDYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEV 231
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEE----ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  232 ALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTG----DVNVEMNAAPGVDLTQLL 307
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERLESLERRIAATERRL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  308 NNMRSQYEQLAEQ------NRKDAEAWFNEKSKEL---TTEIDSNIEQMSSHKSEITELRRTVQALE---IELQSQLALK 375
Cdd:TIGR02168  841 EDLEEQIEELSEDieslaaEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELEskrSELRRELEEL 920
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622879458  376 QSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKI-RLENEIQ 436
Cdd:TIGR02168  921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLkRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
225-443 5.95e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 225 LKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPgvdLT 304
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 305 QLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASLAE 384
Cdd:COG1196   309 ERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622879458 385 TEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-437 1.22e-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: 48.51  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  190 KTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEEL 269
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  270 AYLKKNHEEEMKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWfNEKSKELTTEIDSNIEQMSS 349
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  350 HKSEITELRRTVQALEIELQSQLALKQSLEASLAETEGRYcvqlSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKI 429
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELEELREKLAQLELRLE 932

                   ....*...
gi 1622879458  430 RLENEIQT 437
Cdd:TIGR02168  933 GLEVRIDN 940
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
245-443 1.43e-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: 48.13  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  245 RRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNV----------------------EMNAAPGVD 302
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELsrqisalrkdlarleaeveqleERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  303 LTQLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASL 382
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622879458  383 AETEGRYCV---QLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:TIGR02168  834 AATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
244-443 1.84e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 244 LRRVLDELTLTKADLEMQIESLTEELAylkkNHEEEMKDLRNvSTGDVNVEMNAApgvDLTQLLNNMRSQYEQlAEQNRK 323
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQ-KNGLVDLSEEAK---LLLQQLSELESQLAE-ARAELA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 324 DAEAWFNEKSKELTTEIDSNIEQMSShkSEITELRRTVQALE-----------------IELQSQLA-LKQSLEASLAET 385
Cdd:COG3206   237 EAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEaelaelsarytpnhpdvIALRAQIAaLRAQLQQEAQRI 314
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622879458 386 EGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
190-443 1.45e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 190 KTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYE----NEVALRQSVEADINGLRRV----------LDELTLTK 255
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaEEYELLAELARLEQDIARLeerrreleerLEELEEEL 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 256 ADLEMQIESLTEELAYLKKNHEEEMKDLRnvstgdvnvemnaapgvDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKE 335
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELE-----------------EAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 336 LT---------TEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASLAETEGRycvqLSQIQAQISALEEQ 406
Cdd:COG1196   389 LEalraaaelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE----EAELEEEEEALLEL 464
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622879458 407 LQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
301-443 3.67e-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: 43.51  E-value: 3.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  301 VDLTQLLNNMRSQYEQLAEQNRKDAEAwfNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEA 380
Cdd:TIGR02168  225 LELALLVLRLEELREELEELQEELKEA--EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622879458  381 SLAETEgrycVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLE 443
Cdd:TIGR02168  303 QKQILR----ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
346-441 8.97e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.38  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 346 QMSSHKSEITELRRTVQALEIELQsqlALKQSLEASLAEtegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQLL 425
Cdd:COG0542   405 EIDSKPEELDELERRLEQLEIEKE---ALKKEQDEASFE-------RLAELRDELAELEEELEALKARWEAEKELIEEIQ 474
                          90
                  ....*....|....*.
gi 1622879458 426 DIKIRLENEIQTYRSL 441
Cdd:COG0542   475 ELKEELEQRYGKIPEL 490
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
197-440 9.59e-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: 41.67  E-value: 9.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 197 NQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNH 276
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 277 EEEMKDLRNV-----STGDVNVEMNAAPGVDLTQLLNNMRSqYEQLAEQNRKDAEawfnekskeltteidsnieqmsshk 351
Cdd:COG4942   100 EAQKEELAELlralyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAE------------------------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 352 sEITELRRTVQALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRL 431
Cdd:COG4942   154 -ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232

                  ....*....
gi 1622879458 432 ENEIQTYRS 440
Cdd:COG4942   233 EAEAAAAAE 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
235-413 1.57e-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: 40.29  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 235 QSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAApgvdltqllnnmRSQY 314
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK------------KYEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 315 EQLAEQNRKDAEAwfnekskeLTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASLAETEGRYCVQLS 394
Cdd:COG1579    81 QLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
                         170
                  ....*....|....*....
gi 1622879458 395 QIQAQISALEEQLQQIRAE 413
Cdd:COG1579   153 ELEAELEELEAEREELAAK 171
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
302-437 1.66e-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: 41.59  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  302 DLTQLLNNMRSQYEQLAEQNRKdaeawFNEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEAS 381
Cdd:TIGR02169  713 DASRKIGEIEKEIEQLEQEEEK-----LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622879458  382 LAETegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQT 437
Cdd:TIGR02169  788 LSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
46 PHA02562
endonuclease subunit; Provisional
195-438 1.93e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 195 LKNQILNLTTDNANILLQIDNARLAADDFRlKYENEvaLRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKK 274
Cdd:PHA02562  172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYN-KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 275 NHEEEMKDLRNVSTGDVNVEMNaapgVDLTQLLNNMRSQY-------EQLAEQNRKDAEAwfNEKSKELTT---EIDSNI 344
Cdd:PHA02562  249 DIEDPSAALNKLNTAAAKIKSK----IEQFQKVIKMYEKGgvcptctQQISEGPDRITKI--KDKLKELQHsleKLDTAI 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 345 EQMSSHKSEITELRRTVQaleiELQSQLA-LKQSLEASLAetegrycvQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 423
Cdd:PHA02562  323 DELEEIMDEFNEQSKKLL----ELKNKIStNKQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
                         250
                  ....*....|....*
gi 1622879458 424 LLDIKIRLENEIQTY 438
Cdd:PHA02562  391 IVKTKSELVKEKYHR 405
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
184-441 3.94e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 184 DYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAaddfRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIE 263
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK----LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 264 SLTEELAYLK---KNHEEEMKDLRNVSTGDVN--------VEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNE- 331
Cdd:TIGR04523 236 KKQQEINEKTteiSNTQTQLNQLKDEQNKIKKqlsekqkeLEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSe 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 332 ------KSKELTTEIDSNIEQMSSHKSEITELRRTVQALE---IELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISA 402
Cdd:TIGR04523 316 lknqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622879458 403 LEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSL 441
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
234-432 4.33e-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: 40.04  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  234 RQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMkdlrnvstgdvnvemnaapgvdlTQLLNNMRSQ 313
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-----------------------AQLEELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  314 YEQLAEQNRKDaeawfnEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSqlalkqsLEASLAETEGrycvQL 393
Cdd:TIGR02168  333 DELAEELAELE------EKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-------LRSKVAQLEL----QI 395
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1622879458  394 SQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLE 432
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
235-423 4.45e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  235 QSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEmKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQY 314
Cdd:COG4913    606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELEAELERLDASS 684
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  315 EQLAEQNRKDAEAWfnEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQS-----QLALKQSLEASLAE--TEG 387
Cdd:COG4913    685 DDLAALEEQLEELE--AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELRALLEERFAAalGDA 762
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1622879458  388 RYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQ 423
Cdd:COG4913    763 VERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
330-425 5.40e-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: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 330 NEKSKELTTEIDSNIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASLAETEGrycvQLSQIQAQISALEEQLQQ 409
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAE 94
                          90
                  ....*....|....*.
gi 1622879458 410 IRAETECQNTEYQQLL 425
Cdd:COG4942    95 LRAELEAQKEELAELL 110
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
190-440 6.09e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  190 KTIDDLKNQILNLTT-----DNANILLQIDNARLAAD--DFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLemqI 262
Cdd:pfam15921  562 KVIEILRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEinDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---V 638
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  263 ESLTEELAYLKKNHEEEMKDLRNVSTGDVNvemnaapgvdltqlLNNMRSQYEQLAEQnrkdaeawFNEKSKELTTEIDS 342
Cdd:pfam15921  639 NAGSERLRAVKDIKQERDQLLNEVKTSRNE--------------LNSLSEDYEVLKRN--------FRNKSEEMETTTNK 696
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458  343 NIEQMSSHKSEITELRRTVQALEIELQSQLALKQSLEASLAETEGrycvQLSQIQAQISALEEQLQQIRAE----TECQN 418
Cdd:pfam15921  697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKIQFLEEAMTNANKEkhflKEEKN 772
                          250       260
                   ....*....|....*....|....*
gi 1622879458  419 TEYQQLLDI---KIRLENEIQTYRS 440
Cdd:pfam15921  773 KLSQELSTVateKNKMAGELEVLRS 797
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
212-415 8.75e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 212 QIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNV----- 286
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622879458 287 ----STGDVNVEMNAApgvDLTQLLNNMrSQYEQLAEQNRKDAEAwfnekSKELTTEIDSNIEQMSSHKSEITELRRTVQ 362
Cdd:COG3883    97 rsggSVSYLDVLLGSE---SFSDFLDRL-SALSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELE 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622879458 363 ALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETE 415
Cdd:COG3883   168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
 
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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