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Conserved domains on  [gi|119581082|gb|EAW60678|]
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keratin 25C [Homo sapiens]

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;
83-396 1.52e-120

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 354.23  E-value: 1.52e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   83 NEKVTMQNLNDRLASYLENVRALEEANADLEQKIKGWYEKFGPGSCRgldhDYSRYFPIIDELKNQIISATTSNAHVVLQ 162
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  163 NDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQC-AAGGNV 241
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119581082  322 LATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIETYCLLIDGED 396
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
83-396 1.52e-120

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 354.23  E-value: 1.52e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   83 NEKVTMQNLNDRLASYLENVRALEEANADLEQKIKGWYEKFGPGSCRgldhDYSRYFPIIDELKNQIISATTSNAHVVLQ 162
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  163 NDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQC-AAGGNV 241
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119581082  322 LATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIETYCLLIDGED 396
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 142-386 3.99e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 142 IDELKNQIISATTSNAHVVLQNDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAY 221
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 222 LKKNHEEEMKALQCAAGGNVNVEMNAApgvDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQisddaGATTSAR 301
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELE---EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----RAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 302 NELTEMKRTLQTLEIELQSLLATKHSLEcsltetesnycAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHL 381
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEELE-----------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                 ....*
gi 119581082 382 EKEIE 386
Cdd:COG1196  469 LEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-376 1.85e-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: 50.44  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   142 IDELKNQIISATTSNAHVVLQNDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAY 221
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   222 L---KKNHEEEMKALQcaagGNVNVEMNAApgVDLTVLLNNMRAEYEAL----------AEQNRRDAEAWfnEKSAS-LQ 287
Cdd:TIGR02168  773 AeeeLAEAEAEIEELE----AQIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT--ERRLEdLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   288 QQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQ----------AQIGALEEQL 357
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELReleskrselrRELEELREKL 924

                          250
                   ....*....|....*....
gi 119581082   358 HQVRTETEGQKLEYEQLLD 376
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQE 943
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
87-387 4.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  87 TMQNLNDRLASY---LENVRALEEANADLEQKIKGWYEKFgpgscrgldhdysryfpiiDELKNQIISATTSNAHVVLQN 163
Cdd:PRK02224 235 TRDEADEVLEEHeerREELETLEAEIEDLRETIAETERER-------------------EELAEEVRDLRERLEELEEER 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 164 DNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELaylkKNHEEEMKALQCAAGgNVNV 243
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREEAA-ELES 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 244 EMNAApgvdlTVLLNNMRAEYEALAEQnRRDAEAWFN------EKSASLQQQISDDAGAttsARNELTEMKRTLQTLE-- 315
Cdd:PRK02224 371 ELEEA-----REAVEDRREEIEELEEE-IEELRERFGdapvdlGNAEDFLEELREERDE---LREREAELEATLRTARer 441

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119581082 316 -IELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIkVHLEKEIET 387
Cdd:PRK02224 442 vEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIER 513
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 178-375 9.36e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 37.43  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 178 ENELALHQSVEADINGLRRVLDeltlcrtDLEIQLETLSEELAYLKKNHEEEMKALqcaaggNVNVEMNAAPGVDLTVLL 257
Cdd:cd00176   36 EALLKKHEALEAELAAHEERVE-------ALNELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 258 NNMRAEYEALAEQnrRDAEAWFNEKSASLQQQ-ISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLEcsltetE 336
Cdd:cd00176  103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119581082 337 SNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLL 375
Cdd:cd00176  175 EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
83-396 1.52e-120

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 354.23  E-value: 1.52e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   83 NEKVTMQNLNDRLASYLENVRALEEANADLEQKIKGWYEKFGPGSCRgldhDYSRYFPIIDELKNQIISATTSNAHVVLQ 162
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  163 NDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQC-AAGGNV 241
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119581082  322 LATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIETYCLLIDGED 396
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEE 311
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 142-386 3.99e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 142 IDELKNQIISATTSNAHVVLQNDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAY 221
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 222 LKKNHEEEMKALQCAAGGNVNVEMNAApgvDLTVLLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQisddaGATTSAR 301
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELE---EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-----RAAAELA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 302 NELTEMKRTLQTLEIELQSLLATKHSLEcsltetesnycAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHL 381
Cdd:COG1196  400 AQLEELEEAEEALLERLERLEEELEELE-----------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468


                 ....*
gi 119581082 382 EKEIE 386
Cdd:COG1196  469 LEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 142-376 1.85e-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: 50.44  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   142 IDELKNQIISATTSNAHVVLQNDNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAY 221
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   222 L---KKNHEEEMKALQcaagGNVNVEMNAApgVDLTVLLNNMRAEYEAL----------AEQNRRDAEAWfnEKSAS-LQ 287
Cdd:TIGR02168  773 AeeeLAEAEAEIEELE----AQIEQLKEEL--KALREALDELRAELTLLneeaanlrerLESLERRIAAT--ERRLEdLE 844

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   288 QQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESNYCAQLAQIQ----------AQIGALEEQL 357
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELReleskrselrRELEELREKL 924

                          250
                   ....*....|....*....
gi 119581082   358 HQVRTETEGQKLEYEQLLD 376
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQE 943
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 185-368 2.33e-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: 46.30  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 185 QSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALqcAAGGNVNVEMNAAPGvdLTVLLNN----- 259
Cdd:COG4942   58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--AELLRALYRLGRQPP--LALLLSPedfld 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 260 --MRAEY-EALAEQNRRDAEAwFNEKSASLQQQISddagATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETE 336
Cdd:COG4942  134 avRRLQYlKYLAPARREQAEE-LRADLAELAALRA----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119581082 337 SNYCAQLAQIQAQIGALEEQLHQVRTETEGQK 368
Cdd:COG4942  209 AELAAELAELQQEAEELEALIARLEAEAAAAA 240
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 178-386 5.02e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 178 ENELALHQ--SVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQcAAGGNVNVEMNAAPGV--DL 253
Cdd:COG1196  226 EAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-EAQAEEYELLAELARLeqDI 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 254 TVLLNNMRAEYEALAEQNRRDAEAwfNEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLEcslt 333
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAEL--EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---- 378

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119581082 334 ETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIE 386
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
206-375 5.57e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 206 TDLEIQLETLSEELAylkknheeEMKALQCAAGGNVNVEMNAAPGVDLTVLLNNMRAEYEALaEQNRRDAEAWFNEKS-- 283
Cdd:COG3206  222 SELESQLAEARAELA--------EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHpd 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 284 -ASLQQQISDdagattsARNEL-TEMKRTLQTLEIELQSLLATKHSLECSLTETESNYcAQLAQIQAQIGALEEQLhQVR 361
Cdd:COG3206  293 vIALRAQIAA-------LRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREV-EVA 363

                        170
                 ....*....|....
gi 119581082 362 TETegqkleYEQLL 375
Cdd:COG3206  364 REL------YESLL 371
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 142-386 5.77e-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: 45.83  E-value: 5.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   142 IDELKNQI--ISATTSNAHVVLQNDNARLTA--DDFRLKFENELAlhqSVEADINGLRRVLDELTLCRTDLEIQLETLSE 217
Cdd:TIGR02169  253 LEKLTEEIseLEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIG---ELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   218 ELAYLKKNHEEEMKALQcaaggNVNVEMNAapgvdLTVLLNNMRAEYEAL---AEQNRRDAEAWFnEKSASLQQQISDda 294
Cdd:TIGR02169  330 EIDKLLAEIEELEREIE-----EERKRRDK-----LTEEYAELKEELEDLraeLEEVDKEFAETR-DELKDYREKLEK-- 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   295 gattsARNELTEMKRTLQTLEIELQsllatkhslecSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQL 374
Cdd:TIGR02169  397 -----LKREINELKRELDRLQEELQ-----------RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460

                          250
                   ....*....|..
gi 119581082   375 LDIKVHLEKEIE 386
Cdd:TIGR02169  461 AADLSKYEQELY 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 195-387 1.08e-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: 45.05  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   195 RRVLDELTLCRTDLEIQLETLSEELAYLKKNHEE--------------------EMKALQCAAGGNVN--VEMNAAPGVD 252
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkeleelsrqisALRKDLARLEAEVEqlEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   253 LTVLLNNMRAEYEALAEQNRRDAEAwfNEKSASLQQQISDDAGATT-------SARNELTEMKRTLQTLEIELQSLLATK 325
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKalrealdELRAELTLLNEEAANLRERLESLERRI 833

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119581082   326 HSLECSLTETEsnycAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIET 387
Cdd:TIGR02168  834 AATERRLEDLE----EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
256-374 1.49e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 43.69  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 256 LLNNM--RAEYEAL--AEQNRRDAEAWFNEKSASL-----QQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATkh 326
Cdd:COG3524  166 LVNQLseRAREDAVrfAEEEVERAEERLRDAREALlafrnRNGILDPEATAEALLQLIATLEGQLAELEAELAALRSY-- 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119581082 327 slecsltETESNycAQLAQIQAQIGALEEQLHQVRTE----TEGQKL-----EYEQL 374
Cdd:COG3524  244 -------LSPNS--PQVRQLRRRIAALEKQIAAERARltgaSGGDSLasllaEYERL 291
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 129-452 3.12e-04

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: 43.57  E-value: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   129 RGLDHDYS----RYFPIIDELKnQIISATTSNAHVVLQNDNARLtaddfrlkfENELALHqsvEADINGLRRVLDELTLC 204
Cdd:pfam15921  227 RELDTEISylkgRIFPVEDQLE-ALKSESQNKIELLLQQHQDRI---------EQLISEH---EVEITGLTEKASSARSQ 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   205 RTDLEIQLETLSEELaylKKNHEEEMKALQcaaggnvnvemnaapgvDLTVLLNNMRAEYealaeqnrRDAEAWFNEKSA 284
Cdd:pfam15921  294 ANSIQSQLEIIQEQA---RNQNSMYMRQLS-----------------DLESTVSQLRSEL--------REAKRMYEDKIE 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   285 SLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLT-ETESNycaqlAQIQAQIGALEEQLHQVRTE 363
Cdd:pfam15921  346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlEKEQN-----KRLWDRDTGNSITIDHLRRE 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   364 TEGQKLEYEQ----LLDIKVHLEKEIETYCLLIDGEDGSCSKSKGYGGPGNQTKDsskttIVKTVVEEIDPRGKVLSSRV 439
Cdd:pfam15921  421 LDDRNMEVQRlealLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE-----MLRKVVEELTAKKMTLESSE 495

                          330
                   ....*....|...
gi 119581082   440 HTVEEKSTKVNNK 452
Cdd:pfam15921  496 RTVSDLTASLQEK 508
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 292-384 5.25e-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: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 292 DDAGA-----TTSARNELTEMKRTLQTLEIELQSLLAtkhslecsltETESNYCAQLAQIQAQIGALEEQLHQVRTETEG 366
Cdd:COG0542  396 DEAAArvrmeIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEA 465

                         90
                 ....*....|....*...
gi 119581082 367 QKLEYEQLLDIKVHLEKE 384
Cdd:COG0542  466 EKELIEEIQELKEELEQR 483
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 185-368 6.11e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 185 QSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKN---HEEEMKALQCAAGGNVNVE-MNAAPGVDLTVLLNN- 259
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGSe 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 260 ------MRAEY-EALAEQNRRDAEAwfnekSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSL 332
Cdd:COG3883  113 sfsdflDRLSAlSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 119581082 333 TETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQK 368
Cdd:COG3883  188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-368 7.43e-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: 7.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   176 KFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQCAAGGNVNVE---MNAAPGVD 252
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVA 389

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   253 LTV----LLNNMRAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSL 328
Cdd:TIGR02168  390 QLElqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 119581082   329 ECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQK 368
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
252-386 1.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  252 DLTVLLNNMRAEYEALAEQnRRDAEawfnEKSASLQQQISDDAGAT-TSARNELTEMKRTLQTLEIELQSLLATKHSLEC 330
Cdd:COG4913   299 ELRAELARLEAELERLEAR-LDALR----EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGL 373

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 119581082  331 SLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIE 386
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 184-384 1.22e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   184 HQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHEEEMKALQcaaggnvnvemnaapgvdltvLLNNMRAE 263
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---------------------ELESKLDE 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   264 YEALAEQNRrdaeawfnEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLEcsltetesnycAQL 343
Cdd:TIGR02168  335 LAEELAELE--------EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE-----------LQI 395

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 119581082   344 AQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKE 384
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 280-375 1.50e-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: 40.52  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 280 NEKSASLQQQISDdagattsARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETE---SNYCAQLAQIQAQIGALEEQ 356
Cdd:COG4942   19 ADAAAEAEAELEQ-------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALArriRALEQELAALEAELAELEKE 91

                         90
                 ....*....|....*....
gi 119581082 357 LHQVRTETEGQKLEYEQLL 375
Cdd:COG4942   92 IAELRAELEAQKEELAELL 110
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 176-386 2.14e-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: 40.82  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   176 KFENELAlhqSVEADINGLRRVLDELTLCRTDLEIQLETLSEELAYLKKNHE---EEMKALQC------AAGGNVNVEM- 245
Cdd:TIGR02169  685 GLKRELS---SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkERLEELEEdlssleQEIENVKSELk 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082   246 -NAAPGVDLTVLLNNMRaeyEALAEQNRRDAEAWFNEKSASLQQQisddagattsaRNELTEMKRTLQTLEIELQSLLAT 324
Cdd:TIGR02169  762 eLEARIEELEEDLHKLE---EALNDLEARLSHSRIPEIQAELSKL-----------EEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119581082   325 KHSLECSLTETES--NYC-AQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIE 386
Cdd:TIGR02169  828 KEYLEKEIQELQEqrIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 261-387 3.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 261 RAEYEALAEQNRRDAEAWFNEKSASLQQQISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLECSLTETESN-- 338
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119581082 339 -YCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIKVHLEKEIET 387
Cdd:COG1196  306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
87-387 4.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082  87 TMQNLNDRLASY---LENVRALEEANADLEQKIKGWYEKFgpgscrgldhdysryfpiiDELKNQIISATTSNAHVVLQN 163
Cdd:PRK02224 235 TRDEADEVLEEHeerREELETLEAEIEDLRETIAETERER-------------------EELAEEVRDLRERLEELEEER 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 164 DNARLTADDFRLKFENELALHQSVEADINGLRRVLDELTLCRTDLEIQLETLSEELaylkKNHEEEMKALQCAAGgNVNV 243
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----DDLEERAEELREEAA-ELES 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 244 EMNAApgvdlTVLLNNMRAEYEALAEQnRRDAEAWFN------EKSASLQQQISDDAGAttsARNELTEMKRTLQTLE-- 315
Cdd:PRK02224 371 ELEEA-----REAVEDRREEIEELEEE-IEELRERFGdapvdlGNAEDFLEELREERDE---LREREAELEATLRTARer 441

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119581082 316 -IELQSLLATKHSLECSLTETESNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLLDIkVHLEKEIET 387
Cdd:PRK02224 442 vEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIER 513
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
208-374 4.30e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 208 LEIQLETLSEELAylkkNHEEEMKALQcAAGGNVNVEMNAAPGVDLTVLLNNMRAEyealAEQNRRDAEAwfneKSASLQ 287
Cdd:COG3206  180 LEEQLPELRKELE----EAEAALEEFR-QKNGLVDLSEEAKLLLQQLSELESQLAE----ARAELAEAEA----RLAALR 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 288 QQISDDAGATTSARN--ELTEMKRTLQTLEIELQSLLAT------------------KHSLECSLTETESNYCAQLAQIQ 347
Cdd:COG3206  247 AQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARytpnhpdvialraqiaalRAQLQQEAQRILASLEAELEALQ 326

                        170       180       190
                 ....*....|....*....|....*....|
gi 119581082 348 AQIGALEEQLHQVRTETEG---QKLEYEQL 374
Cdd:COG3206  327 AREASLQAQLAQLEARLAElpeLEAELRRL 356
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 178-375 9.36e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 37.43  E-value: 9.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 178 ENELALHQSVEADINGLRRVLDeltlcrtDLEIQLETLSEELAYLKKNHEEEMKALqcaaggNVNVEMNAAPGVDLTVLL 257
Cdd:cd00176   36 EALLKKHEALEAELAAHEERVE-------ALNELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119581082 258 NNMRAEYEALAEQnrRDAEAWFNEKSASLQQQ-ISDDAGATTSARNELTEMKRTLQTLEIELQSLLATKHSLEcsltetE 336
Cdd:cd00176  103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 119581082 337 SNYCAQLAQIQAQIGALEEQLHQVRTETEGQKLEYEQLL 375
Cdd:cd00176  175 EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
 
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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