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Conserved domains on  [gi|2024337526|ref|XP_040562978|]
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myb/SANT-like DNA-binding domain-containing protein 4 [Gallus gallus]

Protein Classification

SANT/Myb-like DNA-binding domain-containing protein( domain architecture ID 10620601)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein may bind DNA and function as a transcription factor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 8-85 1.01e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT like DNA binding domains. This family is greatly expanded in arthropods and higher eukaryotes.


:

Pssm-ID: 433544  Cd Length: 78  Bit Score: 79.25  E-value: 1.01e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526   8 RKSNFSVQETQTLLKEIRKRREVLFSKQLNTTINEMKRKAWEEIAECVNAVGEGeQRTGTEVKRRYLDWRALMKRKRL 85
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGKKSDAATWKAKNRAWKEIAARVNAIGGV-HRTAEELKKKWRDLKRRTKRKLA 77
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 187-340 1.45e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 187 NLSSAQARLAYEDSHLLINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEK----ERLQIEREK 262
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELE 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526 263 LRLETLRAEKPALENDLTQSEKpiiqplDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:COG1196   316 ERLEELEEELAELEEELEELEE------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
 
Name Accession Description Interval E-value
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 8-85 1.01e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT like DNA binding domains. This family is greatly expanded in arthropods and higher eukaryotes.


Pssm-ID: 433544  Cd Length: 78  Bit Score: 79.25  E-value: 1.01e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526   8 RKSNFSVQETQTLLKEIRKRREVLFSKQLNTTINEMKRKAWEEIAECVNAVGEGeQRTGTEVKRRYLDWRALMKRKRL 85
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGKKSDAATWKAKNRAWKEIAARVNAIGGV-HRTAEELKKKWRDLKRRTKRKLA 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 187-340 1.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 187 NLSSAQARLAYEDSHLLINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEK----ERLQIEREK 262
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELE 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526 263 LRLETLRAEKPALENDLTQSEKpiiqplDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:COG1196   316 ERLEELEEELAELEEELEELEE------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 206-340 1.30e-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: 43.90  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  206 LEKQKVELEKQRLDIEAERLQVEK--ERLQIEKERLRHIDLEHERLQLEKERLQIEREKL--RLETLRAEKPALENDLTQ 281
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKERELEDaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteEYAELKEELEDLRAELEE 375

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024337526  282 SEKpiiqpldleteKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:TIGR02169  376 VDK-----------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 206-285 3.24e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 39.34  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  206 LEKQKVE-LEKQRLD-IEAERLQ-VEKERLQ---IEKERLRHIDLEHERL-QLEKERL-QIEREklRLETLRAEK---PA 274
Cdd:PTZ00266   455 LEKKRIErLEREERErLERERMErIERERLErerLERERLERDRLERDRLdRLERERVdRLERD--RLEKARRNSyflKG 532

                           90
                   ....*....|.
gi 2024337526  275 LENDLTQSEKP 285
Cdd:PTZ00266   533 MENGLSAGGGP 543
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 200-340 3.29e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 200 SHLLINLEKQKVELEKQRLD----IEAERLQVEKERLQIEKERLRHIDLEHERLQ----------LEKERLQIEREKlRL 265
Cdd:pfam17380 272 NQLLHIVQHQKAVSERQQQEkfekMEQERLRQEKEEKAREVERRRKLEEAEKARQaemdrqaaiyAEQERMAMERER-EL 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 266 ETLRAEKPALENDLTQSEKPIIQPLDL-ETEKLKLEK----ERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMrELERLQMERqqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE 430
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 198-308 4.77e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 38.43  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 198 EDSHLLINLEKQKV-----ELEKQRLDIEAERL----QVEKERLQIEKERLRHIDleherlQLEKErLQIEREKLRL--E 266
Cdd:cd03406   174 EKTKLLIAEQHQKVvekeaETERKRAVIEAEKDaevaKIQMQQKIMEKEAEKKIS------EIEDE-MHLAREKARAdaE 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2024337526 267 TLRAEKPAlendltqsekpiiqpldlETEKLKLEKERLQLEK 308
Cdd:cd03406   247 YYRALREA------------------EANKLKLTPEYLELKK 270
 
Name Accession Description Interval E-value
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 8-85 1.01e-18

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT like DNA binding domains. This family is greatly expanded in arthropods and higher eukaryotes.


Pssm-ID: 433544  Cd Length: 78  Bit Score: 79.25  E-value: 1.01e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526   8 RKSNFSVQETQTLLKEIRKRREVLFSKQLNTTINEMKRKAWEEIAECVNAVGEGeQRTGTEVKRRYLDWRALMKRKRL 85
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGKKSDAATWKAKNRAWKEIAARVNAIGGV-HRTAEELKKKWRDLKRRTKRKLA 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 187-340 1.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 187 NLSSAQARLAYEDSHLLINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEK----ERLQIEREK 262
Cdd:COG1196   236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELE 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526 263 LRLETLRAEKPALENDLTQSEKpiiqplDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:COG1196   316 ERLEELEEELAELEEELEELEE------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 207-344 1.67e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 207 EKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEKERLQIEREKLRLETLRAEKPALENDLTQSEKPI 286
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024337526 287 IQPLDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQREGLLQ 344
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 183-344 1.89e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 183 EEFGNLSSAQARLAYEDSHL---LINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERlrhIDLEHERLQLEKERLQIE 259
Cdd:COG1196   288 AEEYELLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEEL---EEAEEELEEAEAELAEAE 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 260 REKLRLETLRAEKPALENDLTQSEkpiiqpLDLETEKLKLEKERLQLEKERLQFLKfESEKLQIEKERLQVEKERLRIQR 339
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEEL------LEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEE 437


                  ....*
gi 2024337526 340 EGLLQ 344
Cdd:COG1196   438 EEEEE 442
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 203-344 2.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 203 LINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRhidLEHERLQLEKERLQIEREKLRLETLRAEKPALENDLTQS 282
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE---LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024337526 283 EKPIIQPLDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQREGLLQ 344
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 206-344 8.44e-05

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: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 206 LEKQKVELEKQRLDIEA---------ERLQVEKERLQIEKERLRHIDLEHERLQLEKERL--QIEREKLRLETLRAEKPA 274
Cdd:COG1196   269 LEELRLELEELELELEEaqaeeyellAELARLEQDIARLEERRRELEERLEELEEELAELeeELEELEEELEELEEELEE 348

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 275 LENDLTQSEKPIIQpldLETEKLKLEKERLQLEKERLQFLKFESEKLQiEKERLQVEKERLRIQREGLLQ 344
Cdd:COG1196   349 AEEELEEAEAELAE---AEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLE 414
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 206-340 1.30e-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: 43.90  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  206 LEKQKVELEKQRLDIEAERLQVEK--ERLQIEKERLRHIDLEHERLQLEKERLQIEREKL--RLETLRAEKPALENDLTQ 281
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKERELEDaeERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteEYAELKEELEDLRAELEE 375

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024337526  282 SEKpiiqpldleteKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:TIGR02169  376 VDK-----------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 205-343 1.50e-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: 43.52  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  205 NLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHI-DLEHERLQLEKERLQIEREKLRLETLRAEKPALENDLTQSE 283
Cdd:TIGR02169  858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024337526  284 KPIIQPL-----DLETEKLKLEKERLQLEKERLQFLKF----ESEKLQIEKERLQVEKERLRIQREGLL 343
Cdd:TIGR02169  938 DPKGEDEeipeeELSLEDVQAELQRVEEEIRALEPVNMlaiqEYEEVLKRLDELKEKRAKLEEERKAIL 1006
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 186-329 3.86e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 186 GNLSSAQARLAYEDSHLLINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEKERLQIEREKLRL 265
Cdd:COG1196   656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 266 ETLRAEKPALENDLTQSEKPIIQPLDLETEKLKLEKERLQLE----------------KERLQFLKFESEKLQIEKERLQ 329
Cdd:COG1196   736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEalgpvnllaieeyeelEERYDFLSEQREDLEEARETLE 815
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 208-340 6.26e-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: 41.59  E-value: 6.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  208 KQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEKERLQIEREKL--RLETLRAEKPALENDLTQSEKp 285
Cdd:TIGR02169  363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLseELADLNAAIAGIEAKINELEE- 441

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024337526  286 iiqplDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:TIGR02169  442 -----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-344 8.80e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 8.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  180 THIEEFGNLSSAQARLAYEDSHLLINLEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRhiDLEHERLQLEKERLQIE 259
Cdd:COG4913    259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD--ALREELDELEAQIRGNG 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  260 REklRLETLRAEKPALENDLTQSEKPI------IQPLDLETEKLKLEKERLQLE-KERLQFLKFESEKLQIEKERLQVEK 332
Cdd:COG4913    337 GD--RLEQLEREIERLERELEERERRRarlealLAALGLPLPASAEEFAALRAEaAALLEALEEELEALEEALAEAEAAL 414

                          170
                   ....*....|..
gi 2024337526  333 ERLRIQREGLLQ 344
Cdd:COG4913    415 RDLRRELRELEA 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-344 1.06e-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: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  207 EKQKVELEKQRLDIEAERLQVEKERLQIEKERL-RHIDLEHERLQLEKERL-----QIEREKLRLETLRAEKPALENDLT 280
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELeSKLDELAEELAELEEKLeelkeELESLEAELEELEAELEELESRLE 375

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024337526  281 QSEKpiiqplDLETEKLKLEKERLQLEKERLQFlkfesEKLQIEKERLQVEKERLRIQREGLLQ 344
Cdd:TIGR02168  376 ELEE------QLETLRSKVAQLELQIASLNNEI-----ERLEARLERLEDRRERLQQEIEELLK 428
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 206-285 3.24e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 39.34  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  206 LEKQKVE-LEKQRLD-IEAERLQ-VEKERLQ---IEKERLRHIDLEHERL-QLEKERL-QIEREklRLETLRAEK---PA 274
Cdd:PTZ00266   455 LEKKRIErLEREERErLERERMErIERERLErerLERERLERDRLERDRLdRLERERVdRLERD--RLEKARRNSyflKG 532

                           90
                   ....*....|.
gi 2024337526  275 LENDLTQSEKP 285
Cdd:PTZ00266   533 MENGLSAGGGP 543
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 200-340 3.29e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 200 SHLLINLEKQKVELEKQRLD----IEAERLQVEKERLQIEKERLRHIDLEHERLQ----------LEKERLQIEREKlRL 265
Cdd:pfam17380 272 NQLLHIVQHQKAVSERQQQEkfekMEQERLRQEKEEKAREVERRRKLEEAEKARQaemdrqaaiyAEQERMAMERER-EL 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 266 ETLRAEKPALENDLTQSEKPIIQPLDL-ETEKLKLEK----ERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQRE 340
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMrELERLQMERqqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE 430
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
222-342 3.48e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 222 AERLQVEKERLQIEKERLRHIDLEHERLQLEKERLQIEREKLRLETLRAEKPALENDLTQSEKpIIQPLDLETEKLKLEk 301
Cdd:COG2433   379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-RIERLERELSEARSE- 456

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2024337526 302 ERLQLEKERlqflkfESEKLQIEKERLQVEKERLRIQREGL 342
Cdd:COG2433   457 ERREIRKDR------EISRLDREIERLERELEEERERIEEL 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
206-336 3.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  206 LEKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERLQLEKERLQIEREKL--RLETLRAEKPALENDLTQse 283
Cdd:COG4913    307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLeaLLAALGLPLPASAEEFAA-- 384

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024337526  284 kpIIQPLDLETEKLKLEKERLQLEKERlqfLKFESEKLQIEKERLQVEKERLR 336
Cdd:COG4913    385 --LRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAEIASLE 432
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 230-339 3.82e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 39.34  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  230 ERLQIEKERLRHIDLEHErlQLEKERLQ-IEREKL-RLETLRAEKpalendltqsekpiiqpldleTEKLKLEKERLqlE 307
Cdd:PTZ00266   436 ERARIEKENAHRKALEMK--ILEKKRIErLEREEReRLERERMER---------------------IERERLERERL--E 490

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2024337526  308 KERLQFLKFESEKL-QIEKERL-QVEKERLRIQR 339
Cdd:PTZ00266   491 RERLERDRLERDRLdRLERERVdRLERDRLEKAR 524
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
207-344 3.93e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526  207 EKQKVELEKQRLDIEAERLQVEKERLQIEKERLRHID-----------LEHERLQLEKERLQIEREKLRLETLRAEKPAL 275
Cdd:COG4913    618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvasAEREIAELEAELERLDASSDDLAALEEQLEEL 697

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024337526  276 ENDLTQSEKPIIQpLDLETEKLKLEKERLQLEKERLQFLKFESEKLQIEKERLQVEKERLRIQREGLLQ 344
Cdd:COG4913    698 EAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 198-308 4.77e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 38.43  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 198 EDSHLLINLEKQKV-----ELEKQRLDIEAERL----QVEKERLQIEKERLRHIDleherlQLEKErLQIEREKLRL--E 266
Cdd:cd03406   174 EKTKLLIAEQHQKVvekeaETERKRAVIEAEKDaevaKIQMQQKIMEKEAEKKIS------EIEDE-MHLAREKARAdaE 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2024337526 267 TLRAEKPAlendltqsekpiiqpldlETEKLKLEKERLQLEK 308
Cdd:cd03406   247 YYRALREA------------------EANKLKLTPEYLELKK 270
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 190-340 5.50e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 190 SAQARLAYEDSHLLINLEKQKVELEKQRL-------DIEAERLQVEKERLQIEKERLRhidlEHERLQLEKERlQIEREK 262
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQERMAMERERElerirqeERKRELERIRQEEIAMEISRMR----ELERLQMERQQ-KNERVR 395

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024337526 263 LRLETLRAEKPALENDLTQSEKPIIQPLDLETEKLKLEKERLQ-LEKERLQflkfESEKLQIEKERLQVEKERLRIQRE 340
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrLEEERAR----EMERVRLEEQERQQQVERLRQQEE 470
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 191-302 8.14e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.14  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024337526 191 AQARLAYEDSHLLINLEkqkvELEKQRLDIEAERLQVEKERLQIEKERLRHIDLEHERL--QLEKERLQIEREKLRLETL 268
Cdd:COG0542   398 AAARVRMEIDSKPEELD----ELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELeeELEALKARWEAEKELIEEI 473

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024337526 269 RAEKPALEN---DLTQSEKPIIQPLDLETEKLKLEKE 302
Cdd:COG0542   474 QELKEELEQrygKIPELEKELAELEEELAELAPLLRE 510
 
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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