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Conserved domains on  [gi|198278448|ref|NP_081850|]
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keratin, type I cytoskeletal 28 [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;
83-397 7.20e-121

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 355.38  E-value: 7.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   83 NEKVTMQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYGPGSCRgldrDYSKYHLTIEDLKSKIISSTAANANIILQ 162
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  163 IDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAG-GNV 241
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198278448  322 SATKHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETYCRLIDGDEN 397
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEEC 312
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
83-397 7.20e-121

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 355.38  E-value: 7.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   83 NEKVTMQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYGPGSCRgldrDYSKYHLTIEDLKSKIISSTAANANIILQ 162
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  163 IDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAG-GNV 241
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198278448  322 SATKHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETYCRLIDGDEN 397
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEEC 312
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 188-387 1.18e-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: 57.76  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   188 EADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHE-EEMKVLQCAaggnvnvEMNAAPGVDLTVLLNNMRAEYEA 266
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLE-------ERIAQLSKELTELEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   267 LAEQNRRDAEAwfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETE---GNYCSQL 343
Cdd:TIGR02168  770 LEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrlEDLEEQI 847

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 198278448   344 AQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 302-384 4.38e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.84  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 302 TELTELKRSLQTLEIELQSLSAtkhslecslaETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHL 381
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480


                 ...
gi 198278448 382 EKE 384
Cdd:COG0542  481 EQR 483
PTZ00491 PTZ00491
major vault protein; Provisional
 272-393 1.69e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.77  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 272 RRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGNYcsQLAQIQA--- 348
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAEV--EQAELRAkal 746

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198278448 349 QISAlEEQLHQVRTETEgQKLEHEQLLD------IKAHLEKEIETYCRLID 393
Cdd:PTZ00491 747 RIEA-EAELEKLRKRQE-LELEYEQAQNeleiakAKELADIEATKFERIVE 795
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 178-372 2.47e-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: 39.35  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 178 ENELTLHQNVEADINGLRRVLDELtlcrtdqELQYESLSEEMTYLKKNHEEEMKVLqcaaggNVNVEMNAAPGVDLTVLL 257
Cdd:cd00176   36 EALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 258 NNMRAEYEALAEQnrRDAEAWFQEKSATLQQQ-ISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLEcslaetE 336
Cdd:cd00176  103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 198278448 337 GNYCSQLAQIQAQISALEEQLHQVRTETE--GQKLEHE 372
Cdd:cd00176  175 EGHPDADEEIEEKLEELNERWEELLELAEerQKKLEEA 212
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 138-364 5.84e-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: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   138 YHLTIEDLKSKIISSTAANANIILQI--DNARL------AADDFRLKYENELTL---HQNVEAD----------INGLRR 196
Cdd:smart00787  68 YQFSCKELKKYISEGRDLFKEIEEETliNNPPLfkeyfsASPDVKLLMDKQFQLvktFARLEAKkmwyewrmklLEGLKE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   197 VLDE-LTLCRTDQEL--QYE----SLSEEMTYLKKNHEEEMKVLQcaaggNVNVEMNAAPGVDLTVLlnnmraeyealae 269
Cdd:smart00787 148 GLDEnLEGLKEDYKLlmKELellnSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRA------------- 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   270 qnrrdaeawfQEKSATLQQQISNDlgaatsaRTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQA- 348
Cdd:smart00787 210 ----------KEKLKKLLQEIMIK-------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAE----KKLEQCRGf 268

                          250
                   ....*....|....*....
gi 198278448   349 ---QISALEEQLHQVRTET 364
Cdd:smart00787 269 tfkEIEKLKEQLKLLQSLT 287
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
83-397 7.20e-121

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 355.38  E-value: 7.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   83 NEKVTMQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYGPGSCRgldrDYSKYHLTIEDLKSKIISSTAANANIILQ 162
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR----LYSLYEKEIEDLRRQLDTLTVERARLQLE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  163 IDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAG-GNV 241
Cdd:pfam00038  77 LDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  242 NVEMNAAPGVDLTVLLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSL 321
Cdd:pfam00038 157 NVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 198278448  322 SATKHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETYCRLIDGDEN 397
Cdd:pfam00038 237 KKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEEC 312
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 188-387 1.18e-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: 57.76  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   188 EADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHE-EEMKVLQCAaggnvnvEMNAAPGVDLTVLLNNMRAEYEA 266
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLE-------ERIAQLSKELTELEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   267 LAEQNRRDAEAwfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETE---GNYCSQL 343
Cdd:TIGR02168  770 LEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErrlEDLEEQI 847

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 198278448   344 AQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 94-368 8.70e-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: 48.51  E-value: 8.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448    94 RLASYLDNVKALEEANSELERKIKTWHEKygpgsCRGLDRDYSKYHLTIEDLKSKI---------ISSTAANANIILQID 164
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEE-----LEELTAELQELEEKLEELRLEVseleeeieeLQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   165 NARLAADDFRLKY-ENELtlhQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAGGNVNV 243
Cdd:TIGR02168  301 EQQKQILRERLANlERQL---EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   244 E---MNAAPGVDLTV----LLNNMRAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAAtsaRTELTELKRSLQTLEI 316
Cdd:TIGR02168  378 EeqlETLRSKVAQLElqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL---QAELEELEEELEELQE 454

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 198278448   317 ELQSLSATKHSLECSLAETEGNYCS---QLAQIQAQISALEEQLHQVRTETEGQK 368
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAaerELAQLQARLDSLERLQENLEGFSEGVK 509
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 261-458 3.63e-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: 46.21  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   261 RAEYEALAEQnrrdaEAWFQEKSATLQQQISndlgaatSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGNYC 340
Cdd:TIGR02169  722 EKEIEQLEQE-----EEKLKERLEELEEDLS-------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   341 -SQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETY-CRLIDGDENSCSVSKGFEsgtSGNSPKDVS 418
Cdd:TIGR02169  790 hSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELqEQRIDLKEQIKSIEKEIE---NLNGKKEEL 866

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 198278448   419 KTTLVKT--VVEEIDQRGKVLSSRIHSIEEKMSKMSNGKAEQ 458
Cdd:TIGR02169  867 EEELEELeaALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 141-374 4.10e-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: 46.20  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   141 TIEDLKSKIISSTAANANIILQIDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMT 220
Cdd:TIGR02168  685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   221 YLKKNHEEEMKVLQCAAGGNVNVEMNAAPGVDLTVL----LNNMRAEYEAL----------AEQNRRDAEAWfqEKSAT- 285
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreaLDELRAELTLLneeaanlrerLESLERRIAAT--ERRLEd 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   286 LQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQAQISALEEQLHQVRTETE 365
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR----SELEELSEELRELESKRSELRRELE 918


                   ....*....
gi 198278448   366 GQKLEHEQL 374
Cdd:TIGR02168  919 ELREKLAQL 927
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 302-384 4.38e-05

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.84  E-value: 4.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 302 TELTELKRSLQTLEIELQSLSAtkhslecslaETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHL 381
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480


                 ...
gi 198278448 382 EKE 384
Cdd:COG0542  481 EQR 483
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
261-386 8.43e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 8.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  261 RAEYEALAEQNRR--DAEAWFQEKSATLQQQI-SNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEG 337
Cdd:COG4913   301 RAELARLEAELERleARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 198278448  338 NYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIE 386
Cdd:COG4913   381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 144-430 1.17e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 44.71  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  144 DLKSKIISSTAANANIILQIDNARLAADdFRLK--YENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLS--EEM 219
Cdd:pfam05483 187 DLNNNIEKMILAFEELRVQAENARLEMH-FKLKedHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTflLEE 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  220 TYLKKNHEEEMKVLQcaaggNVNVEMNAAPGVDLTVLLNNMRAEYEalaeqnrrdaeawfqeKSATLQQQISNDLGAATS 299
Cdd:pfam05483 266 SRDKANQLEEKTKLQ-----DENLKELIEKKDHLTKELEDIKMSLQ----------------RSMSTQKALEEDLQIATK 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  300 ARTELTELKRSlqtlEIELQSLSATKHSLecSLAETEGNYCSQ---LAQIQAQISALEEQLHQVRTETEGQKLEHEQLLD 376
Cdd:pfam05483 325 TICQLTEEKEA----QMEELNKAKAAHSF--VVTEFEATTCSLeelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 198278448  377 IKAHLEKEIETYCRLIDGDENSCSVSKGFESGTSGNSPKDVSKTTLVKTVVEEI 430
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 261-387 1.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 261 RAEYEALAEQNRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGN-- 338
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDia 305

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 198278448 339 -YCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:COG1196  306 rLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 88-339 3.18e-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: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448    88 MQNLNNRLASYLDNVKALEEANSELERKIKTWHEKYgpgscRGLDRDYSKYHLTIEDLKSKII---SSTAANANIILQ-- 162
Cdd:TIGR02168  276 VSELEEEIEELQKELYALANEISRLEQQKQILRERL-----ANLERQLEELEAQLEELESKLDelaEELAELEEKLEElk 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   163 --IDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEemkvlqcaaggn 240
Cdd:TIGR02168  351 eeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER------------ 418

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   241 vnvemnaapgvdltvLLNNMRAEYEALAEQNRRDAEAWFQEKS---ATLQQQISNDLGAATSARTELTELKRSLQTLEIE 317
Cdd:TIGR02168  419 ---------------LQQEIEELLKKLEEAELKELQAELEELEeelEELQEELERLEEALEELREELEEAEQALDAAERE 483

                          250       260
                   ....*....|....*....|..
gi 198278448   318 LQSLSATKHSLECSLAETEGNY 339
Cdd:TIGR02168  484 LAQLQARLDSLERLQENLEGFS 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 93-386 3.23e-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: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448    93 NRLASYLDNVKALEEANSELERKIKTWH------EKYgpgscRGLDRDYSKYHLTI-----EDLKSKI--ISSTAANANI 159
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKSLErqaekaERY-----KELKAELRELELALlvlrlEELREELeeLQEELKEAEE 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   160 ILQIDNARLAADDFRLkyeNELTL-HQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEemkvlqcaag 238
Cdd:TIGR02168  254 ELEELTAELQELEEKL---EELRLeVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE---------- 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   239 gnvnvemnaapgvdltvlLNNMRAEYEALAEQNRRDAEAWfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIEL 318
Cdd:TIGR02168  321 ------------------LEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198278448   319 QSLSATKHSLEcslaetegnycSQLAQIQAQISALEEQLHQV---------RTETEGQKLEHEQLLDIKAHLEKEIE 386
Cdd:TIGR02168  382 ETLRSKVAQLE-----------LQIASLNNEIERLEARLERLedrrerlqqEIEELLKKLEEAELKELQAELEELEE 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 162-368 3.85e-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: 42.44  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 162 QIDNARLAADDFRLKYENELTLHQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLqcAAGGNV 241
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--AELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 242 NVEMNAAPGvdLTVLLNN-------MRAEY-EALAEQNRRDAEAwFQEKSATLQQQISndlgAATSARTELTELKRSLQT 313
Cdd:COG4942  113 LYRLGRQPP--LALLLSPedfldavRRLQYlKYLAPARREQAEE-LRADLAELAALRA----ELEAERAELEALLAELEE 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 198278448 314 LEIELQSLSATKHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQK 368
Cdd:COG4942  186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
261-390 4.62e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 261 RAEYEALAEQNRRDAEAwfQEKSATLQQQISNDLGA--ATSARTELTELKRSLQTLEIELQSLSAtkhslecslaetegn 338
Cdd:COG4717  384 EEELRAALEQAEEYQEL--KEELEELEEQLEELLGEleELLEALDEEELEEELEELEEELEELEE--------------- 446

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 198278448 339 ycsQLAQIQAQISALEEQLHQVRTETEGQKLEHEQlldikAHLEKEIETYCR 390
Cdd:COG4717  447 ---ELEELREELAELEAELEQLEEDGELAELLQEL-----EELKAELRELAE 490
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-448 5.18e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 5.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  265 EALAEQNRRDAEAwfQEKSATLQQQIS--NDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLEcSLAEtegnycsQ 342
Cdd:COG4913   624 EELAEAEERLEAL--EAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLA-ALEE-------Q 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  343 LAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIETYCRLIDGDENSCsvskgFEsgtsgNSPKDVSKTTL 422
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-----LE-----ERFAAALGDAV 763

                         170       180
                  ....*....|....*....|....*.
gi 198278448  423 VKTVVEEIDQRGKVLSSRIHSIEEKM 448
Cdd:COG4913   764 ERELRENLEERIDALRARLNRAEEEL 789
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 165-386 6.05e-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: 42.36  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   165 NARLAADDFRLKYENELtlhQNVEADINGLRRVLDELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQCAAGG-NVNV 243
Cdd:TIGR02169  660 RAPRGGILFSRSEPAEL---QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEeEKLK 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   244 EMNAAPGVDLTVL---LNNMRAEYEALA---EQNRRDAEAwFQEKSATL-----QQQISNDLGAATSARTELTELKRSLQ 312
Cdd:TIGR02169  737 ERLEELEEDLSSLeqeIENVKSELKELEariEELEEDLHK-LEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLR 815

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 198278448   313 TLEIELQSLSATKHSLECSLAETEG--NYC-SQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDIKAHLEKEIE 386
Cdd:TIGR02169  816 EIEQKLNRLTLEKEYLEKEIQELQEqrIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD 892
PTZ00491 PTZ00491
major vault protein; Provisional
 272-393 1.69e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.77  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 272 RRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEGNYcsQLAQIQA--- 348
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAEAEV--EQAELRAkal 746

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 198278448 349 QISAlEEQLHQVRTETEgQKLEHEQLLD------IKAHLEKEIETYCRLID 393
Cdd:PTZ00491 747 RIEA-EAELEKLRKRQE-LELEYEQAQNeleiakAKELADIEATKFERIVE 795
Gp58 pfam07902
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ...
 257-351 1.76e-03

gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.


Pssm-ID: 369586 [Multi-domain]  Cd Length: 594  Bit Score: 40.71  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448  257 LNNMRAEYEALAEQNRRDAE-------AWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLE 329
Cdd:pfam07902 229 LDDLRAEFTRSNQGMRTELEskisglqSTQQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQDAEKNYSSLTQTVKGLQ 308

                          90       100
                  ....*....|....*....|..
gi 198278448  330 CSLAETEGNYCSQLAQIQAQIS 351
Cdd:pfam07902 309 STVSDPNSKLESRITQLAGLIE 330
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 176-387 1.83e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   176 KYENELTLHQNVEADINGLRRVL------DELTLCRTDQELQYESLSEEMTYLKKNHEEEMKVLQcaaggnvnvemNAAP 249
Cdd:TIGR00618  271 ELRAQEAVLEETQERINRARKAAplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK-----------QQSS 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   250 GVDLTVLLNNMRAEYEALAEQNrrDAEAWFQEKSA----------TLQQQISNDLGAATSARTELTELKRSLQTLEIELQ 319
Cdd:TIGR00618  340 IEEQRRLLQTLHSQEIHIRDAH--EVATSIREISCqqhtltqhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS 417

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 198278448   320 SLSATKHSL-----ECSLAETEGNYCSQLAQIQAQISALEEQlHQVRTEtEGQKLEHEQLLDIKAHLEKEIET 387
Cdd:TIGR00618  418 AFRDLQGQLahakkQQELQQRYAELCAAAITCTAQCEKLEKI-HLQESA-QSLKEREQQLQTKEQIHLQETRK 488
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 266-363 2.06e-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: 40.13  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 266 ALAEQNRRDAEawfQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQ 345
Cdd:COG4942   15 AAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----AELAE 87

                         90
                 ....*....|....*...
gi 198278448 346 IQAQISALEEQLHQVRTE 363
Cdd:COG4942   88 LEKEIAELRAELEAQKEE 105
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 296-460 2.41e-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: 40.13  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 296 AATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLl 375
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELAELEKEIAEL- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 376 diKAHLEKEIETYCRLIDGDENSCSVSKgFESGTSGNSPKDVSKT-TLVKTVVEEIDQRGKVLSSRIHSIEEKMSKMSNG 454
Cdd:COG4942   96 --RAELEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRlQYLKYLAPARREQAEELRADLAELAALRAELEAE 172


                 ....*.
gi 198278448 455 KAEQRV 460
Cdd:COG4942  173 RAELEA 178
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 178-372 2.47e-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: 39.35  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 178 ENELTLHQNVEADINGLRRVLDELtlcrtdqELQYESLSEEMTYLKKNHEEEMKVLqcaaggNVNVEMNAAPGVDLTVLL 257
Cdd:cd00176   36 EALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEIQERLEEL------NQRWEELRELAEERRQRL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 258 NNMRAEYEALAEQnrRDAEAWFQEKSATLQQQ-ISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLEcslaetE 336
Cdd:cd00176  103 EEALDLQQFFRDA--DDLEQWLEEKEAALASEdLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELL------E 174

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 198278448 337 GNYCSQLAQIQAQISALEEQLHQVRTETE--GQKLEHE 372
Cdd:cd00176  175 EGHPDADEEIEEKLEELNERWEELLELAEerQKKLEEA 212
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
256-363 2.61e-03

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


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 39.83  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 256 LLNNM--RAEYEAL--AEQNRRDAEAWFQEKSATL-----QQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATkh 326
Cdd:COG3524  166 LVNQLseRAREDAVrfAEEEVERAEERLRDAREALlafrnRNGILDPEATAEALLQLIATLEGQLAELEAELAALRSY-- 243

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 198278448 327 slecsLAETEgnycSQLAQIQAQISALEEQLHQVRTE 363
Cdd:COG3524  244 -----LSPNS----PQVRQLRRRIAALEKQIAAERAR 271
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
289-394 3.52e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 289 QISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQAQISALEEQLHQVrTETEGQK 368
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE----ERIEELKKEIEELEEKVKEL-KELKEKA 292

                         90       100       110
                 ....*....|....*....|....*....|...
gi 198278448 369 LEHEQL-------LDIKAHLEKEIETYCRLIDG 394
Cdd:PRK03918 293 EEYIKLsefyeeyLDELREIEKRLSRLEEEING 325
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 138-364 5.84e-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: 5.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   138 YHLTIEDLKSKIISSTAANANIILQI--DNARL------AADDFRLKYENELTL---HQNVEAD----------INGLRR 196
Cdd:smart00787  68 YQFSCKELKKYISEGRDLFKEIEEETliNNPPLfkeyfsASPDVKLLMDKQFQLvktFARLEAKkmwyewrmklLEGLKE 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   197 VLDE-LTLCRTDQEL--QYE----SLSEEMTYLKKNHEEEMKVLQcaaggNVNVEMNAAPGVDLTVLlnnmraeyealae 269
Cdd:smart00787 148 GLDEnLEGLKEDYKLlmKELellnSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRA------------- 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448   270 qnrrdaeawfQEKSATLQQQISNDlgaatsaRTELTELKRSLQTLEIELQSLSATKHSLECSLAETEgnycSQLAQIQA- 348
Cdd:smart00787 210 ----------KEKLKKLLQEIMIK-------VKKLEELEEELQELESKIEDLTNKKSELNTEIAEAE----KKLEQCRGf 268

                          250
                   ....*....|....*....
gi 198278448   349 ---QISALEEQLHQVRTET 364
Cdd:smart00787 269 tfkEIEKLKEQLKLLQSLT 287
PLN02939 PLN02939
transferase, transferring glycosyl groups
 141-448 6.95e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.11  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 141 TIEDLKSKIISSTAANANIILQIDNARLAADDFRL------------KYENELTLHQNVEADI---NGLR-RVLDELTLC 204
Cdd:PLN02939  82 TVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQtnskdgeqlsdfQLEDLVGMIQNAEKNIlllNQARlQALEDLEKI 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 205 RTDQElqyeSLSEEMTYLKKNHEEEMKVLQCAAGGNVNVEMNAApgvdltvLLNNMRAEYEALAEQNRRDAEAWFQEKSA 284
Cdd:PLN02939 162 LTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEE-------QLEKLRNELLIRGATEGLCVHSLSKELDV 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 285 TLQQQIS--NDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLECSLAETegnycsqlaqiQAQISaleeQLHQVRT 362
Cdd:PLN02939 231 LKEENMLlkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVA-----------QEDVS----KLSPLQY 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 363 ETEGQKLEHEQLLDIKAhlEKEIETYCRLIDGDEN-SCSVSKGFESGTSGNspkdVSKTTLVKtvVEEIDQRGKVLSSRI 441
Cdd:PLN02939 296 DCWWEKVENLQDLLDRA--TNQVEKAALVLDQNQDlRDKVDKLEASLKEAN----VSKFSSYK--VELLQQKLKLLEERL 367


                 ....*..
gi 198278448 442 HSIEEKM 448
Cdd:PLN02939 368 QASDHEI 374
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
252-388 7.53e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 252 DLTVLLNNMRAEYEALAEQ--NRRDAEAWFQEKSATLQQQISNDLGAATSARTELTELKRSLQTLEIELQSLSATKHSLE 329
Cdd:COG4372   49 QLREELEQAREELEQLEEEleQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 198278448 330 CSLAETEGNY---CSQLAQIQAQISALEEQLHQVRTETEgqKLEHEQLLDIKAHLEKEIETY 388
Cdd:COG4372  129 QQRKQLEAQIaelQSEIAEREEELKELEEQLESLQEELA--ALEQELQALSEAEAEQALDEL 188
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
257-387 8.97e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 8.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 257 LNNMRAEYEAlAEQNRRDAEAwfqeKSATLQQQISNDLGAATSART--ELTELKRSLQTLEIELQSLSAT---------- 324
Cdd:COG3206  221 LSELESQLAE-ARAELAEAEA----RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARytpnhpdvia 295

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 198278448 325 --------KHSLECSLAETEGNYCSQLAQIQAQISALEEQLHQVRTETEGQKLEHEQLLDikahLEKEIET 387
Cdd:COG3206  296 lraqiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEV 362
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 257-386 9.35e-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: 37.60  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 198278448 257 LNNMRAEYEALAEQNRRdaeawFQEKSATLQQQISND---LGAATSAR------TELTELKRSLQTLEIELQSLSATKHS 327
Cdd:COG1579   47 LEAAKTELEDLEKEIKR-----LELEIEEVEARIKKYeeqLGNVRNNKeyealqKEIESLKRRISDLEDEILELMERIEE 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 198278448 328 LECSLAETEgnycSQLAQIQAQISALEEQLHQVRTETEGqklEHEQLLDIKAHLEKEIE 386
Cdd:COG1579  122 LEEELAELE----AELAELEAELEEKKAELDEELAELEA---ELEELEAEREELAAKIP 173
 
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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