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Conserved domains on  [gi|122425580|ref|NP_083669|]
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keratin, type I cytoskeletal 24 [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;
140-450 8.88e-128

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 374.64  E-value: 8.88e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  140 SEKQTMQDLNDRLANYLDKVRALEEANTDLECKIKDWYGKHGSvkgGSGRDYSQYYSIIEDLKKQILSATCENARMTLQI 219
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA---EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  220 DNARLAADDFRMKYEHELCLRECLEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEEMKCMQGS-SGGDVT 298
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  299 VEMNAAPGVDLTKLLNDMRAQYEAMAEQNRQEAERQFNERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQL 378
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122425580  379 ALKCSLEGTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLLNG 450
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
140-450 8.88e-128

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 374.64  E-value: 8.88e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  140 SEKQTMQDLNDRLANYLDKVRALEEANTDLECKIKDWYGKHGSvkgGSGRDYSQYYSIIEDLKKQILSATCENARMTLQI 219
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA---EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  220 DNARLAADDFRMKYEHELCLRECLEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEEMKCMQGS-SGGDVT 298
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  299 VEMNAAPGVDLTKLLNDMRAQYEAMAEQNRQEAERQFNERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQL 378
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122425580  379 ALKCSLEGTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLLNG 450
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
307-449 7.06e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 307 VDLTKLLNDMRAQYeAMAEQNRQEAERQFNERSASLQAQISSDAGEAncARSEVMELKRTVQTLE----------IELQS 376
Cdd:COG3206  222 SELESQLAEARAEL-AEAEARLAALRAQLGSGPDALPELLQSPVIQQ--LRAQLAELEAELAELSarytpnhpdvIALRA 298

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122425580 377 QLA-LKCSLEGTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQC---QSAEYecllnikTRLEQEIETYRRLLN 449
Cdd:COG3206  299 QIAaLRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeLEAEL-------RRLEREVEVARELYE 368
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-448 1.81e-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: 41.20  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   243 LEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEemkcmqgssggdvtVEMNAApgvDLTKLLNDMRAQYEA 322
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIE---ELQKELYALANEISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   323 MAEQNR--QEAERQFNERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQLALKCSLEGTLADTEAGYVAQLS 400
Cdd:TIGR02168  300 LEQQKQilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 122425580   401 GIQAQ---ISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLL 448
Cdd:TIGR02168  380 QLETLrskVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
140-450 8.88e-128

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 374.64  E-value: 8.88e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  140 SEKQTMQDLNDRLANYLDKVRALEEANTDLECKIKDWYGKHGSvkgGSGRDYSQYYSIIEDLKKQILSATCENARMTLQI 219
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGA---EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  220 DNARLAADDFRMKYEHELCLRECLEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEEMKCMQGS-SGGDVT 298
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQvSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  299 VEMNAAPGVDLTKLLNDMRAQYEAMAEQNRQEAERQFNERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQL 378
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 122425580  379 ALKCSLEGTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLLNG 450
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
307-449 7.06e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.86  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 307 VDLTKLLNDMRAQYeAMAEQNRQEAERQFNERSASLQAQISSDAGEAncARSEVMELKRTVQTLE----------IELQS 376
Cdd:COG3206  222 SELESQLAEARAEL-AEAEARLAALRAQLGSGPDALPELLQSPVIQQ--LRAQLAELEAELAELSarytpnhpdvIALRA 298

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122425580 377 QLA-LKCSLEGTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQC---QSAEYecllnikTRLEQEIETYRRLLN 449
Cdd:COG3206  299 QIAaLRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeLEAEL-------RRLEREVEVARELYE 368
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 131-424 2.78e-05

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: 47.04  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   131 GYDGGLLSGSEKQTMQDLNDR---------LANYLD-KVRALEEANTDLECKikdwygKHGSVKGGSGRdysqyYSIIED 200
Cdd:pfam15921  582 GRTAGAMQVEKAQLEKEINDRrlelqefkiLKDKKDaKIRELEARVSDLELE------KVKLVNAGSER-----LRAVKD 650

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   201 LKKqilsatcENARMTLQIDNARLAADDFRMKYEhelCLREcleadinGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRK 280
Cdd:pfam15921  651 IKQ-------ERDQLLNEVKTSRNELNSLSEDYE---VLKR-------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   281 NheeeMKCMQGSSGGDVTVEMNAAPGV-----DLTKLLNDMRAQYEAMAEQNRQ-----EAERQFNERSASLQAQISSDA 350
Cdd:pfam15921  714 T----LKSMEGSDGHAMKVAMGMQKQItakrgQIDALQSKIQFLEEAMTNANKEkhflkEEKNKLSQELSTVATEKNKMA 789

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   351 GEANCARSEVMELKRTVQTLEIEL----------------QSQLALKCSLEGTLADTE---AGYVAQlsgiqaqiSSLEE 411
Cdd:pfam15921  790 GELEVLRSQERRLKEKVANMEVALdkaslqfaecqdiiqrQEQESVRLKLQHTLDVKElqgPGYTSN--------SSMKP 861

                          330
                   ....*....|...
gi 122425580   412 QLSQIRAETQCQS 424
Cdd:pfam15921  862 RLLQPASFTRTHS 874
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
189-421 3.84e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  189 RDYSQYYSIIEDLKKQI-----LSATCEN-ARMTLQIDNARLAADDFRMkYEHELCLREcLEADINGLRKVLDEmtmtrc 262
Cdd:COG4913   235 DDLERAHEALEDAREQIellepIRELAERyAAARERLAELEYLRAALRL-WFAQRRLEL-LEAELEELRAELAR------ 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  263 dLEMQIEGLTEELVFLRKNHEEemkcmqgssggdVTVEMNAAPGVDLTKLLNDMRAqyeAMAEQNRQEAER-QFNERSAS 341
Cdd:COG4913   307 -LEAELERLEARLDALREELDE------------LEAQIRGNGGDRLEQLEREIER---LERELEERERRRaRLEALLAA 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  342 LQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQLAlkcslegTLADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQ 421
Cdd:COG4913   371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA-------EAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
312-419 4.31e-04

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


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 42.53  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 312 LLNDM--RAQYEAM--AEQNRQEAERQFNErsaslqaqissdageancARSEVMELKRTVQTL--EIELQSQLALKCSLE 385
Cdd:COG3524  166 LVNQLseRAREDAVrfAEEEVERAEERLRD------------------AREALLAFRNRNGILdpEATAEALLQLIATLE 227

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 122425580 386 GTLADTEAGYVA----------QLSGIQAQISSLEEQLSQIRAE 419
Cdd:COG3524  228 GQLAELEAELAAlrsylspnspQVRQLRRRIAALEKQIAAERAR 271
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 356-449 1.29e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  356 ARSEVMELKRTVQTLEIELQSQLALKCSLEGtLADTEAGYVAQLSGIQAQISSLEEQLSQIRAetqcQSAEYECLLNIKT 435
Cdd:pfam00529  63 AEAQLAKAQAQVARLQAELDRLQALESELAI-SRQDYDGATAQLRAAQAAVKAAQAQLAQAQI----DLARRRVLAPIGG 137

                          90
                  ....*....|....
gi 122425580  436 RLEQEIETYRRLLN 449
Cdd:pfam00529 138 ISRESLVTAGALVA 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 243-448 1.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 243 LEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEemkcmqgssggdvtvemnaapgvdLTKLLNDMRAQ-YE 321
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE------------------------LELELEEAQAEeYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 322 AMAEQNRQEAERQFN-ERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQLALKCSLEGTLADTEAGYVAQLS 400
Cdd:COG1196  293 LLAELARLEQDIARLeERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 122425580 401 GIQAQISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLL 448
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-448 1.81e-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: 41.20  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   243 LEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVFLRKNHEEemkcmqgssggdvtVEMNAApgvDLTKLLNDMRAQYEA 322
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIE---ELQKELYALANEISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   323 MAEQNR--QEAERQFNERSASLQAQISSDAGEANCARSEVMELKRTVQTLEIELQSQLALKCSLEGTLADTEAGYVAQLS 400
Cdd:TIGR02168  300 LEQQKQilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 122425580   401 GIQAQ---ISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLL 448
Cdd:TIGR02168  380 QLETLrskVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 243-426 3.17e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 243 LEADINGLRKVLDEmtmtrcdLEMQIEGLTEELVFLRKNHEEEMKCMQGSSGGD-VTVEMNAAPGVDLTKLLNDMRAQYE 321
Cdd:COG4942   74 LEQELAALEAELAE-------LEKEIAELRAELEAQKEELAELLRALYRLGRQPpLALLLSPEDFLDAVRRLQYLKYLAP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 322 AMAEQNRQEAERQfnERSASLQAQISSdageancARSEVMELKRTVQTLEIELQSQLALKCSLEGTLADTEAGYVAQLSG 401
Cdd:COG4942  147 ARREQAEELRADL--AELAALRAELEA-------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217

                        170       180
                 ....*....|....*....|....*
gi 122425580 402 IQAQISSLEEQLSQIRAETQCQSAE 426
Cdd:COG4942  218 LQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 321-449 4.08e-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: 40.05  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580   321 EAMAEQNR-QEAERQFNERSASLQAQISSdageancARSEVMELKRTVQTLEIELQSQLALKCSLEGTLADTEAGYV-AQ 398
Cdd:TIGR02169  720 EIEKEIEQlEQEEEKLKERLEELEEDLSS-------LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShSR 792

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 122425580   399 LSGIQAQISSLEEQLSQIRAETQCQSAEYECLLNIKTRLEQEIETYRRLLN 449
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 352-440 5.03e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580 352 EAnCAR---------SEVMELKRTVQTLEIELQsqlALKcslegtlADTEAGYVAQLSGIQAQISSLEEQLSQIRAETQC 422
Cdd:COG0542  397 EA-AARvrmeidskpEELDELERRLEQLEIEKE---ALK-------KEQDEASFERLAELRDELAELEEELEALKARWEA 465

                         90
                 ....*....|....*...
gi 122425580 423 QSAEYECLLNIKTRLEQE 440
Cdd:COG0542  466 EKELIEEIQELKEELEQR 483
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 200-451 9.36e-03

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: 38.93  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  200 DLKKQILSATCENARMTLQIDNARLAADdFRMKYEHELC--LRECLEADINGLRKVLDEMTMTRCDLEMQIEGLTEELVF 277
Cdd:pfam05483 187 DLNNNIEKMILAFEELRVQAENARLEMH-FKLKEDHEKIqhLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEE 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  278 LRK--NHEEEMKCMQgssggDVTVEMNAAPGVDLTKLLNDMRAQYE-AMAEQNRQEAERQFNERS-ASLQAQISSDAGEA 353
Cdd:pfam05483 266 SRDkaNQLEEKTKLQ-----DENLKELIEKKDHLTKELEDIKMSLQrSMSTQKALEEDLQIATKTiCQLTEEKEAQMEEL 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122425580  354 NCARSE----VMELKRTVQTLEIELQSQlalkcslegtladteagyvaqlsgiQAQISSLEEQLSQIRAETQCQSAEYEC 429
Cdd:pfam05483 341 NKAKAAhsfvVTEFEATTCSLEELLRTE-------------------------QQRLEKNEDQLKIITMELQKKSSELEE 395

                         250       260
                  ....*....|....*....|..
gi 122425580  430 LLNIKTRLEQEIETYRRLLNGD 451
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAED 417
 
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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