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Conserved domains on  [gi|755537500|ref|XP_011247070|]
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keratin, type I cytoskeletal 10 isoform X1 [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;
134-443 7.70e-131

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 7.70e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  134 NEKVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQReprDYSKYYKTIEDLKGQILTLTTDNANVLLQI 213
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR---LYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  214 DNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQN-VSTGDVN 292
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  293 VEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQL 372
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537500  373 ALKQSLEASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
134-443 7.70e-131

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 7.70e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  134 NEKVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQReprDYSKYYKTIEDLKGQILTLTTDNANVLLQI 213
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR---LYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  214 DNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQN-VSTGDVN 292
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  293 VEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQL 372
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537500  373 ALKQSLEASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-443 1.41e-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: 58.14  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   190 KTIEDLKGQILTLTTDNANVLLQIDNARLAaddfrlkyenevtlRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEEL 269
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLE--------------VSELEEEIEELQKELYALANEISRLEQQKQILRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   270 AYLKKNHEEEMRDLQNVSTGDVNVEMNAApgvDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSK---------ELTTEI 340
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRleeleeqleTLRSKV 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   341 DSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRYC-VQLSQIQSQISALEEQLQQIRAETECQNA 419
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELRE 468

                          250       260
                   ....*....|....*....|....
gi 755537500   420 EYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLD 492
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
251-443 1.68e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 251 LTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQN--VSTGDVNVEMNAApgvDLTQLLNNMRNQYEQlAEKNRKDAEEW 328
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAK---LLLQQLSELESQLAE-ARAELAEAEAR 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 329 FNQKSKELTTEID-----SNIEQMSSHKSEITELRRTVQGLE----------IELQSQLA-LKQSLEASLAETEGRYCVQ 392
Cdd:COG3206  242 LAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAaLRAQLQQEAQRILASLEAE 321

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537500 393 LSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:COG3206  322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
46 PHA02562
endonuclease subunit; Provisional
 226-438 1.63e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 226 KYENEvtLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNaapgVDLTQ 305
Cdd:PHA02562 202 KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSK----IEQFQ 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 306 LLNNMRNQY-------EQLAEKNRKDAEewFNQKSKELTT---EIDSNIEQMSSHKSEITELRRTVQgleiELQSQLA-L 374
Cdd:PHA02562 276 KVIKMYEKGgvcptctQQISEGPDRITK--IKDKLKELQHsleKLDTAIDELEEIMDEFNEQSKKLL----ELKNKIStN 349

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537500 375 KQSLEASLAetegrycvQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTY 438
Cdd:PHA02562 350 KQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 243-359 2.26e-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: 40.39  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   243 GLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVStgDVNVEMNAAPGVDLTQLLNNMRNQYEQLAEKNR 322
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK--QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK 225

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755537500   323 KDAEewFNQKSKELTTEIDSNIEQMSSHKSEITELRR 359
Cdd:smart00787 226 KLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEK 260
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
134-443 7.70e-131

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.81  E-value: 7.70e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  134 NEKVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQReprDYSKYYKTIEDLKGQILTLTTDNANVLLQI 213
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSR---LYSLYEKEIEDLRRQLDTLTVERARLQLEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  214 DNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQN-VSTGDVN 292
Cdd:pfam00038  78 DNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAqVSDTQVN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  293 VEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQL 372
Cdd:pfam00038 158 VEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755537500  373 ALKQSLEASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-443 1.41e-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: 58.14  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   190 KTIEDLKGQILTLTTDNANVLLQIDNARLAaddfrlkyenevtlRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEEL 269
Cdd:TIGR02168  246 EELKEAEEELEELTAELQELEEKLEELRLE--------------VSELEEEIEELQKELYALANEISRLEQQKQILRERL 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   270 AYLKKNHEEEMRDLQNVSTGDVNVEMNAApgvDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSK---------ELTTEI 340
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRleeleeqleTLRSKV 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   341 DSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRYC-VQLSQIQSQISALEEQLQQIRAETECQNA 419
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqAELEELEEELEELQEELERLEEALEELRE 468

                          250       260
                   ....*....|....*....|....
gi 755537500   420 EYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:TIGR02168  469 ELEEAEQALDAAERELAQLQARLD 492
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
251-443 1.68e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.17  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 251 LTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQN--VSTGDVNVEMNAApgvDLTQLLNNMRNQYEQlAEKNRKDAEEW 328
Cdd:COG3206  166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAK---LLLQQLSELESQLAE-ARAELAEAEAR 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 329 FNQKSKELTTEID-----SNIEQMSSHKSEITELRRTVQGLE----------IELQSQLA-LKQSLEASLAETEGRYCVQ 392
Cdd:COG3206  242 LAALRAQLGSGPDalpelLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAaLRAQLQQEAQRILASLEAE 321

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755537500 393 LSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:COG3206  322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 236-443 3.27e-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: 46.98  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   236 SVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVStgdVNVEMNAAPGVDLTQLLNNMRNQYE 315
Cdd:TIGR02169  298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER---KRRDKLTEEYAELKEELEDLRAELE 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   316 QLAEKNRkdaeEWFnQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRycvqLSQ 395
Cdd:TIGR02169  375 EVDKEFA----ETR-DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE----KED 445

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 755537500   396 IQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:TIGR02169  446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 190-437 5.20e-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: 46.59  E-value: 5.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   190 KTIEDLKGQILTLTTDNANVLLQIDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEEL 269
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   270 AYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWfNQKSKELTTEIDSNIEQMSS 349
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-ERRLEDLEEQIEELSEDIES 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   350 HKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRYcvqlSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKT 429
Cdd:TIGR02168  857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   ....*...
gi 755537500   430 RLENEIQT 437
Cdd:TIGR02168  933 GLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-443 1.85e-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: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 225 LKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPgvdLT 304
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR---LE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 305 QLLNNMRNQYEQLAEKNRKDAEEwfNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAE 384
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755537500 385 TEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLE 443
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 212-440 5.60e-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: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 212 QIDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNV----- 286
Cdd:COG4942   35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlraly 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 287 STGDVNVEMNAAPGVDLTQLLNNMRNqYEQLAEKNRKDAEEWfnqkskeltteidsnieqmsshKSEITELRRTVQGLEI 366
Cdd:COG4942  115 RLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEEL----------------------RADLAELAALRAELEA 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537500 367 ELQSQLALKQSLEASLAETEgrycVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRS 440
Cdd:COG4942  172 ERAELEALLAELEEERAALE----ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 184-441 1.58e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  184 DYSKYYKTIEDLKGQILTLTTDNANVLLQIDNARLAaddfRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIE 263
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK----LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIE 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  264 SLNEELAYLK---KNHEEEMRDLQNVSTGDVN--------VEMNAAPGVDLTQLLNNMRNQYEQLaeKNRKDA------- 325
Cdd:TIGR04523 236 KKQQEINEKTteiSNTQTQLNQLKDEQNKIKKqlsekqkeLEQNNKKIKELEKQLNQLKSEISDL--NNQKEQdwnkelk 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500  326 EEWFNQKSK--ELTTEIDSNIEQMSSHKSEITELRRTVQGLE---IELQSQLALKQSLEASLAETEGRYCVQLSQIQSQI 400
Cdd:TIGR04523 314 SELKNQEKKleEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 755537500  401 SALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSL 441
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
46 PHA02562
endonuclease subunit; Provisional
 226-438 1.63e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 226 KYENEvtLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNaapgVDLTQ 305
Cdd:PHA02562 202 KNIEE--QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSK----IEQFQ 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 306 LLNNMRNQY-------EQLAEKNRKDAEewFNQKSKELTT---EIDSNIEQMSSHKSEITELRRTVQgleiELQSQLA-L 374
Cdd:PHA02562 276 KVIKMYEKGgvcptctQQISEGPDRITK--IKDKLKELQHsleKLDTAIDELEEIMDEFNEQSKKLL----ELKNKIStN 349

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755537500 375 KQSLEASLAetegrycvQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTY 438
Cdd:PHA02562 350 KQSLITLVD--------KAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 346-441 1.67e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 346 QMSSHKSEITELRRTVQGLEIELQsqlALKQSLEASLAEtegrycvQLSQIQSQISALEEQLQQIRAETECQNAEYQQLL 425
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKE---ALKKEQDEASFE-------RLAELRDELAELEEELEALKARWEAEKELIEEIQ 474

                         90
                 ....*....|....*.
gi 755537500 426 DIKTRLENEIQTYRSL 441
Cdd:COG0542  475 ELKEELEQRYGKIPEL 490
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 135-440 2.11e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 41.26  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   135 EKVTMQN----LNDRLASYMDKVRALEESNYEL-------EGKIKEWY-----EKHGNSSQREPR----DYSKYYKTIED 194
Cdd:pfam15921  487 KKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQhlkneGDHLRNVQTECEalklQMAEKDKVIEI 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   195 LKGQILTLTT-----DNANVLLQIDNARLAAD--DFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLemqIESLNE 267
Cdd:pfam15921  567 LRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEinDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSE 643

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   268 ELAYLKKNHEEEMRDLQNVSTGDVNvemnaapgvdltqlLNNMRNQYEQLAEKnrkdaeewFNQKSKELTTEIDSNIEQM 347
Cdd:pfam15921  644 RLRAVKDIKQERDQLLNEVKTSRNE--------------LNSLSEDYEVLKRN--------FRNKSEEMETTTNKLKMQL 701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   348 SSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGrycvQLSQIQSQISALEEQLQQIRAE----TECQNAEYQQ 423
Cdd:pfam15921  702 KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG----QIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQE 777

                          330       340
                   ....*....|....*....|
gi 755537500   424 LLDI---KTRLENEIQTYRS 440
Cdd:pfam15921  778 LSTVateKNKMAGELEVLRS 797
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 235-423 2.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 235 QSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKN----------HEEEMRDL------QNVSTGDVNVEMNAA 298
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaeaeieeRREELGERaralyrSGGSVSYLDVLLGSE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 299 pgvDLTQLLNNMrNQYEQLAEKNRKDAEEwfnqkSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSL 378
Cdd:COG3883  113 ---SFSDFLDRL-SALSKIADADADLLEE-----LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755537500 379 EASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQ 423
Cdd:COG3883  184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 243-359 2.26e-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: 40.39  E-value: 2.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   243 GLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVStgDVNVEMNAAPGVDLTQLLNNMRNQYEQLAEKNR 322
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK--QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK 225

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755537500   323 KDAEewFNQKSKELTTEIDSNIEQMSSHKSEITELRR 359
Cdd:smart00787 226 KLEE--LEEELQELESKIEDLTNKKSELNTEIAEAEK 260
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 302-437 2.79e-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: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500   302 DLTQLLNNMRNQYEQLAEKnrkdaEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEAS 381
Cdd:TIGR02169  713 DASRKIGEIEKEIEQLEQE-----EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755537500   382 LAETegrycvQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQT 437
Cdd:TIGR02169  788 LSHS------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 330-425 5.09e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755537500 330 NQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGrycvQLSQIQSQISALEEQLQQ 409
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ----ELAALEAELAELEKEIAE 94

                         90
                 ....*....|....*.
gi 755537500 410 IRAETECQNAEYQQLL 425
Cdd:COG4942   95 LRAELEAQKEELAELL 110
 
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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